|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1588-4084 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 1465.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1588 REDARAIEHAFPLTPL-QRGVLLESLRGDGAD------------------PYFQQ------------------TVAELDG 1630
Cdd:PRK12316 3 AEDSLKLARRFIELPLeKRRVFLATLRGEGVDfslfpipagvssaerdrlSYAQQrmwflwqlepqsgaynlpSAVRLNG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1631 EIDAAALAQAWQQTVRRQPMLRTAIVWEGlSVPHQIVLADAAAPWQTLDWSALDDAAQDAQLQRWLADDAAQGVDFAHAP 1710
Cdd:PRK12316 83 PLDRQALERAFASLVQRHETLRTVFPRGA-DDSLAQVPLDRPLEVEFEDCSGLPEAEQEARLRDEAQRESLQPFDLCEGP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1711 LARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGATLRLPPAPgfQAYLD-------WRERQDLARQ 1783
Cdd:PRK12316 162 LLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALP--IQYADyalwqrsWLEAGEQERQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1784 RGWWRERLSGyagtaalpapvaaaHHPVQREECER--------RLSAHD-------SERLRAFCRERGCTLSDLIAMVWG 1848
Cdd:PRK12316 240 LEYWRAQLGE--------------EHPVLELPTDHprpavpsyRGSRYEfsidpalAEALRGTARRQGLTLFMLLLGAFN 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1849 LANARYGNHDDVVLGATRSGRppELAGVESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAEN---------EAV 1919
Cdd:PRK12316 306 VLLHRYSGQTDIRVGVPIANR--NRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHqdlpferlvEAL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1920 GLGEILADSGLDADRLFASLLVVENFPAMAPAQLPFALRVRETRAAnHYALTLRVSERECVRLEALLDAARVDRAAVAAM 1999
Cdd:PRK12316 384 KVERSLSHSPLFQVMYNHQPLVADIEALDTVAGLEFGQLEWKSRTT-QFDLTLDTYEKGGRLHAALTYATDLFEARTVER 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2000 LDLAVAGLLR-LLQRPDCRVAEL-----------LGGDDAVQAPQPQRASSATaqslLWQMPAQ----AVAVEEGAASWT 2063
Cdd:PRK12316 463 MARHWQNLLRgMVENPQARVDELpmldaeergqlVEGWNATAAEYPLQRGVHR----LFEEQVErtpeAPALAFGEETLD 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2064 YAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGWGAA 2143
Cdd:PRK12316 539 YAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHL 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2144 PAWVP--ASVRWLDAESVLDVVSAY-EEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDAS 2220
Cdd:PRK12316 619 GRKLPlaAGVQVLDLDRPAAWLEGYsEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDT 698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2221 LATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPRECLVTG 2300
Cdd:PRK12316 699 VLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRRIVCS 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2301 GEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPEEwpVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYL 2380
Cdd:PRK12316 779 GEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEE--GGDSVPIGRPIANLACYILDANLEPVPVGVLGELYL 856
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2381 GGGNLSLGYWQRAEQTAERFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEV 2460
Cdd:PRK12316 857 AGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVRE 936
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2461 AAVLALPGAN--GVLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALAdllQQDDADSSAE-A 2537
Cdd:PRK12316 937 AAVLAVDGKQlvGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALP---APEASVAQQGyV 1013
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2538 IDETPVNEVLRELWQKLLGREHIGAHDNFFALGGDSILSLQLVARARQAGLALMPRQLYDHPTLAGLsaqVQASSPAPAT 2617
Cdd:PRK12316 1014 APRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQAGIQLSPRDLFQHQTIRSL---ALVAKAGQAT 1090
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2618 IKPATEAEQSFGLTPIQHWFFEQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARFqRDAAGQWQQTLGD 2697
Cdd:PRK12316 1091 AADQGPASGEVALAPVQRWFFEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRF-REEDGGWQQAYAA 1169
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2698 WQADRFAHREaDAGQREDLLA---QWQAGLSFD-GALLRVLaLPDPQDGDTRVLFAAHHLLVDAVSWGIIVDDLQHAYAE 2773
Cdd:PRK12316 1170 PQAGEVLWQR-QAASEEELLAlceEAQRSLDLEqGPLLRAL-LVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYAD 1247
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2774 RRAgrspALAAEACGFGAWqAALRQLSAATLDGWRSYWRaQAADAEAIALPWQDSD----NRYADTVHLhdRFERDWTER 2849
Cdd:PRK12316 1248 LDA----DLPARTSSYQAW-ARRLHEHAGARAEELDYWQ-AQLEDAPHELPCENPDgaleNRHERKLEL--RLDAERTRQ 1319
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2850 LLTQTARAYGNEPQEVLLTALALAL-RDGGDAATLwVEMEGHGRDDLGAGLDLSRTVGWFTARYPLALHlPAGeDLGAAL 2928
Cdd:PRK12316 1320 LLQEAPAAYRTQVNDLLLTALARVTcRWSGQASVL-VQLEGHGREDLFEDIDLSRTVGWFTSLFPVRLT-PAA-DLGESI 1396
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2929 RSTKDRMRAVPDRGLGFGVLRYLHGE-----LAELPVPQVCFNYLGQLRaGERDGWALCE---EPDGGGRAGGNRRRHLL 3000
Cdd:PRK12316 1397 KAIKEQLRAVPDKGIGYGLLRYLAGEeaaarLAALPQPRITFNYLGQFD-RQFDEAALFVpatESAGAAQDPCAPLANWL 1475
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3001 DVNAMLVDGELRLDWAWPQDAASREAMQALSRRYLAVLRELIA-CVQTAEPRPTLADLPLAGLDNAPLDALLSQHPQTQD 3079
Cdd:PRK12316 1476 SIEGQVYGGELSLHWSFSREMFAEATVQRLADDYARELQALIEhCCDERNRGVTPSDFPLAGLSQAQLDALPLPAGEIAD 1555
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3080 VYPLAPLQEGLLFHSLLNAEADPYINQTTVALHGaLDREAFAAAWQQALERHPILRSGFAVQ-GLPSPRQLPHRQVSLPL 3158
Cdd:PRK12316 1556 IYPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFLWQdGLEQPLQVIHKQVELPF 1634
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3159 AEQDWSGLEPAQArsRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAAlr 3238
Cdd:PRK12316 1635 AELDWRGREDLGQ--ALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYAG-- 1710
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3239 esrtpQLPAAP--PFRDYLHWLRGQDEAAARAFWREQLTGL-EPAALPEA---TEPAEGYASSTRRFD---LAAASAWAQ 3309
Cdd:PRK12316 1711 -----QPVAAPggRYRDYIAWLQRQDAAASEAFWKEQLAALeEPTRLAQAartEDGQVGYGDHQQLLDpaqTRALAEFAR 1785
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3310 SHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRPPELAGVERMLGVFINSVPLRVTPAGEATPAPWLQALQQRNLDL 3389
Cdd:PRK12316 1786 AQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLAL 1865
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3390 RTHGYLPLAQIQRAGAADAVSPFDVLLVFENLP-TESREERS--GMRIEELDHRAHSNYPLMLtAIPDAGGLRIEAALDR 3466
Cdd:PRK12316 1866 REHEHTPLYDIQRWAGQGGEALFDSLLVFENYPvAEALKQGApaGLVFGRVSNHEQTNYPLTL-AVTLGETLSLQYSYDR 1944
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3467 SKLDGWLVEQMLDDLDFVLQQ--VPALQRFDALPLLPSQTRS---AAWTSRERYACTGNLV-SRFAEIARRYPARIAVSA 3540
Cdd:PRK12316 1945 GHFDAAAIERLDRHLLHLLEQmaEDAQAALGELALLDAGERQrilADWDRTPEAYPRGPGVhQRIAEQAARAPEAIAVVF 2024
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3541 EDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVCLS 3620
Cdd:PRK12316 2025 GDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALL 2104
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3621 VSQRALAVELPGTAlclddpfTRAQLDAVEPGELPEVPTEAP---------AYLIYTSGSTGTPKGVVVTHRNVERLFTA 3691
Cdd:PRK12316 2105 LTQRHLLERLPLPA-------GVARLPLDRDAEWADYPDTAPavqlagenlAYVIYTSGSTGLPKGVAVSHGALVAHCQA 2177
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3692 ATQtgRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRaVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQA 3771
Cdd:PRK12316 2178 AGE--RYELSPADCELQFMSFSFDGAHEQWFHPLLNGAR-VLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHA 2254
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3772 MRRELALNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQ-SPTSRIGSALPDLAVHVLD 3850
Cdd:PRK12316 2255 ERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCgAAYVPIGRALGNRRAYILD 2334
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3851 AAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFV----ERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRI 3926
Cdd:PRK12316 2335 ADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVpdpfSASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRI 2414
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3927 EPGEIAAKIASLPQVSDAAVTVEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLD 4006
Cdd:PRK12316 2415 ELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLD 2494
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 4007 RKALPKPETQDRDEGVLESAS--ERRLAELWRQLLGGELPGRGAHFFARGGHSLLVVRLAEAIRAEFAIAVPLKSLFEQP 4084
Cdd:PRK12316 2495 RKALPKPDVSQLRQAYVAPQEglEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERP 2574
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1628-4084 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 1404.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1628 LDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGLSVPHQIvlaDAAAPWQTLDWSALDDAAQDAQLQRWLADDAAQGVDFA 1707
Cdd:PRK12467 1147 LKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVI---HPVGSLTLEEPLLLAADKDEAQLKVYVEAEARQPFDLE 1223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1708 HAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGATLRLPPAPgfQAYLD-------WRERQDL 1780
Cdd:PRK12467 1224 QGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALP--IQYADyavwqrqWMDAGER 1301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1781 ARQRGWWRERLSGyagtaalpapvaaaHHPVQREECERRLSAHDSER---------------LRAFCRERGCTLSDLIAM 1845
Cdd:PRK12467 1302 ARQLAYWKAQLGG--------------EQPVLELPTDRPRPAVQSHRgarlafelppalaegLRALARREGVTLFMLLLA 1367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1846 VWGLANARYGNHDDVVLGATRSGRppELAGVESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAENEAVGLgEIL 1925
Cdd:PRK12467 1368 SFQTLLHRYSGQDDIRVGVPIANR--NRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPF-EQL 1444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1926 ADSgLDADR------LFASLLVVENFPAMAPAQLPfALRVR----ETRAAnHYALTLRVSEREcvrlEALLDAARVDRAA 1995
Cdd:PRK12467 1445 VEA-LQPERslshspLFQVMFNHQRDDHQAQAQLP-GLSVEslswESQTA-QFDLTLDTYESS----EGLQASLTYATDL 1517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1996 VAAMLDLAVAG-LLRLLQ----RPDCRVAE--LLGGDDAVQAPQPQRASSA--TAQSLLWQMPA-------QAVAVEEGA 2059
Cdd:PRK12467 1518 FEASTIERLAGhWLNLLQglvaDPERRLGEldLLDEAERRQILEGWNATHTgyPLARLVHQLIEdqaaatpEAVALVFGE 1597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2060 ASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIG 2139
Cdd:PRK12467 1598 QELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLT 1677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2140 WGAAPAWVPA--SVRWLDAESVLDVVSAY-EEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLG 2216
Cdd:PRK12467 1678 QSHLQARLPLpdGLRSLVLDQEDDWLEGYsDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLS 1757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2217 EDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAG-LLAAAGGTAVLPRE 2295
Cdd:PRK12467 1758 AADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQlLQMDEQVEHPLSLR 1837
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2296 CLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPEEWPVEQG-VPVGHPLAGNEAWVLDRFGLPAPVGV 2374
Cdd:PRK12467 1838 RVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCRRKDLEGRDsVPIGQPIANLSTYILDASLNPVPIGV 1917
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2375 AGELYLGGGNLSLGYWQRAEQTAERFVAHPLA-PDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLA 2453
Cdd:PRK12467 1918 AGELYLGGVGLARGYLNRPALTAERFVADPFGtVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLR 1997
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2454 QLPGVEVAAVLALPGANG-------------VLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQ 2520
Cdd:PRK12467 1998 EQGGVREAVVIAQDGANGkqlvayvvptdpgLVDDDEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRK 2077
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2521 AL----ADLLQQDDADSSAEAidetpvNEVLRELWQKLLGREHIGAHDNFFALGGDSILSLQLVARARQAGLALMPRQLY 2596
Cdd:PRK12467 2078 ALpapdASELQQAYVAPQSEL------EQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLF 2151
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2597 DHPTLAGLSAQVQASSPAPATIKPATEAEQSfgLTPIQHWFFEQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAH 2676
Cdd:PRK12467 2152 QHQTVQSLAAVAQEGDGTVSIDQGPVTGDLP--LLPIQQMFFADDIPERHHWNQSVLLEPREALDAELLEAALQALLVHH 2229
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2677 PMLRARFqRDAAGQWQQTLGDWQADR----FAHREADAGQREDLLAQWQAGLSF-DGALLRVLALPDPqDGDTRVLFAAH 2751
Cdd:PRK12467 2230 DALRLGF-VQEDGGWSAMHRAPEQERrpllWQVVVADKEELEALCEQAQRSLDLeEGPLLRAVLATLP-DGSQRLLLVIH 2307
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2752 HLLVDAVSWGIIVDDLQHAYAERRAGRSPALAAEACGFGAWQAALRQLSA-ATLDGWRSYWRAQAADAEAIaLPWQDSD- 2829
Cdd:PRK12467 2308 HLVVDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAAsAALADELGYWQAQLQGASTE-LPCDHPQg 2386
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2830 ---NRYADTVHLHdrFERDWTERLLTQTARAYGNEPQEVLLTALALA-LRDGGDAATLwVEMEGHGRDDLGAGLDLSRTV 2905
Cdd:PRK12467 2387 glqRRHAASVTTH--LDSEWTRRLLQEAPAAYRTQVNDLLLTALARViARWTGQASTL-IQLEGHGREDLFDEIDLTRTV 2463
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2906 GWFTARYPLALHLPAgeDLGAALRSTKDRMRAVPDRGLGFGVLRYLHGE-----LAELPVPQVCFNYLGQLRAG-ERDGW 2979
Cdd:PRK12467 2464 GWFTSLYPVKLSPTA--SLATSIKTIKEQLRAVPNKGLGFGVLRYLGSEaarqtLQALPVPRITFNYLGQFDGSfDAEKQ 2541
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2980 AL---CEEPDGGGRAGGNRRRHLLDVNAMLVDGELRLDWAWPQDAASREAMQALSRRYLAVLRELIA-CVQTAEPRPTLA 3055
Cdd:PRK12467 2542 ALfvpSGEFSGAEQSEEAPLGNWLSINGQVYGGELNLGWTFSQEMFDEATIQRLADAYAEELRALIEhCCSNDQRGVTPS 2621
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3056 DLPLAGLDNAPLDALLSQHPQTQDVYPLAPLQEGLLFHSLLNAEADPYINQTTVALHGaLDREAFAAAWQQALERHPILR 3135
Cdd:PRK12467 2622 DFPLAGLSQEQLDRLPVAVGDIEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILR 2700
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3136 SGFAVQG-LPSPRQLPHRQVSLPLAEQDWSglEPAQARSRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRH 3214
Cdd:PRK12467 2701 SGFLWDGeLEEPLQVVYKQARLPFSRLDWR--DRADLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNH 2778
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3215 HLIVDGWSSALLLDEVWRLYAAlresrtpQLPAAPP--FRDYLHWLRGQDEAAARAFWREQL------TGLEPAALPEAT 3286
Cdd:PRK12467 2779 HILMDGWSGSQLLGEVLQRYFG-------QPPPAREgrYRDYIAWLQAQDAEASEAFWKEQLaaleepTRLARALYPAPA 2851
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3287 EPAEGYASSTRRFD---LAAASAWAQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRPPELAGVERMLGVFINSV 3363
Cdd:PRK12467 2852 EAVAGHGAHYLHLDatqTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTL 2931
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3364 PLRVTPAGEATPAPWLQALQQRNLDLRTHGYLPLAQIQRAGAADAVSPFDVLLVFENLPTESREER---SGMRIEELDHR 3440
Cdd:PRK12467 2932 PVIASPRAEQTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQGGEALFDSILVFENYPISEALKQgapSGLRFGAVSSR 3011
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3441 AHSNYPLMLtAIPDAGGLRIEAALDRSKLDGWLVEQMLDDLDFVLQQ--VPALQRFDALPLL----PSQTRSAAWTSRER 3514
Cdd:PRK12467 3012 EQTNYPLTL-AVGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAmlNNPAARLGELPTLaaheRRQVLHAWNATAAA 3090
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3515 YACTGNLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGA 3594
Cdd:PRK12467 3091 YPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGG 3170
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3595 AYVPVDPHAPAARRGFILEDSGVCLSVSQRALAVELP----GTALCLDDpftraqldAVEPGELPEVPT-----EAPAYL 3665
Cdd:PRK12467 3171 AYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPapagDTALTLDR--------LDLNGYSENNPStrvmgENLAYV 3242
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3666 IYTSGSTGTPKGVVVTHRNVERLFTAATQTgrFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVcRQPDAF 3745
Cdd:PRK12467 3243 IYTSGSTGKPKGVGVRHGALANHLCWIAEA--YELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDL-WDPEEL 3319
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3746 LDLLAEYGVTVLNQTPSAFYALQSQAMRRELAlNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVhVSFHRL 3825
Cdd:PRK12467 3320 WQAIHAHRISIACFPPAYLQQFAEDAGGADCA-SLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVV-TVTLWK 3397
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3826 SDEDLQ--SPTSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFV----ERGGQRFYRSGD 3899
Cdd:PRK12467 3398 CGGDAVceAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVadpfSGSGGRLYRTGD 3477
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3900 LGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEGAWLMAYAVAADGAEPDPQSLREALR 3979
Cdd:PRK12467 3478 LARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVPADPQGDWRETLRDHLA 3557
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3980 ALLPDYMLPRLIQLLPALPLTANGKLDRKALPKPETQDRDEGVL-ESASERRLAELWRQLLGGELPGRGAHFFARGGHSL 4058
Cdd:PRK12467 3558 ASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSREYVApRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSL 3637
|
2570 2580
....*....|....*....|....*.
gi 1246793773 4059 LVVRLAEAIRAEFAIAVPLKSLFEQP 4084
Cdd:PRK12467 3638 LALQVLSRIRQSLGLKLSLRDLMSAP 3663
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1573-4084 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 1387.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1573 PQARLQADEFALLAAREDARAIEHAFPLTPLQRGVLLESLRGD-----------GADPYFQQTVAELDGEIDAAALAQAW 1641
Cdd:PRK12316 2567 LRILFERPTLAAFAASLESGQTSRAPVLQKVTRVQPLPLSHAQqrqwflwqlepESAAYHLPSALHLRGVLDQAALEQAF 2646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1642 QQTVRRQPMLRTAIVWEGLSVPHQIVLADAAAPWQTLDWSALDDAAQDAqlqrwLADDAAQGVDFAHAPLARMSLIGRGG 1721
Cdd:PRK12316 2647 DALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLEDCAGVADAAIRQR-----VAEEIQRPFDLARGPLLRVRLLALDG 2721
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1722 GRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGATLRLPPAPGFQA-----YLDWRERQDLARQRGWWRERLSGYAG 1796
Cdd:PRK12316 2722 QEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYAdyaawQRAWMDSGEGARQLDYWRERLGGEQP 2801
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1797 TAALPAPVAAAHHPVQREECER-RLSAHDSERLRAFCRERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRppELAG 1875
Cdd:PRK12316 2802 VLELPLDRPRPALQSHRGARLDvALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANR--NRAE 2879
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1876 VESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAENEAVGLGEILA----DSGLDADRLFASLLVVENFPAMAPA 1951
Cdd:PRK12316 2880 TERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEalqpERSLSHSPLFQVMYNHQSGERAAAQ 2959
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1952 Q-LPFALRVRETRAANHYALTLRVSERECVRLEALLDAARVDRAAVAAMLDLAVAGLLRLLQRPDCRVAELLGGDDAVQA 2030
Cdd:PRK12316 2960 LpGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEER 3039
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2031 PQPQRASSATA----------QSLLWQMPAQ--AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFA 2098
Cdd:PRK12316 3040 GQLLEAWNATAaeyplergvhRLFEEQVERTpdAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLE 3119
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2099 QLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGWGAAPAWVPASVRWLDAESVLDvvSAYEEPPRVDVDADT 2178
Cdd:PRK12316 3120 MVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDE--NYAEANPAIRTMPEN 3197
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2179 PAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQ 2258
Cdd:PRK12316 3198 LAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPA 3277
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2259 ALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPRECLVTGGEALTGALVQQVRALAPTLrivNHYGPTETTVGILTCT 2338
Cdd:PRK12316 3278 LLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLPLY---NLYGPTEATITVTHWQ 3354
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2339 VPEEWPVEqgVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPDRLLYRSGDLA 2418
Cdd:PRK12316 3355 CVEEGKDA--VPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLA 3432
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2419 RLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQGS--LEGVAEALAQRLPE 2496
Cdd:PRK12316 3433 RYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQLVAYVVPEDEAGdlREALKAHLKASLPE 3512
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2497 YLCPSRWRAVESMPRLGNGKIDRQAL----ADLLQQDDAdssaeaideTPVNEVLREL---WQKLLGREHIGAHDNFFAL 2569
Cdd:PRK12316 3513 YMVPAHLLFLERMPLTPNGKLDRKALprpdAALLQQDYV---------APVNELERRLaaiWADVLKLEQVGLTDNFFEL 3583
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2570 GGDSILSLQLVARARQAGLALMPRQLYDHPTLAGLSAQVQASSPAPATIKPATEAEQsfgLTPIQHWFFEQALDQPAHWN 2649
Cdd:PRK12316 3584 GGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQGLARVARVGGGVAVDQGPVSGETL---LLPIQQQFFEEPVPERHHWN 3660
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2650 MSLYLKLPGALDTAAFAAALADVAAAHPMLRARFQRDAAGQWQQTLG-------DWQADRfahreADAGQREDLLAQWQA 2722
Cdd:PRK12316 3661 QSLLLKPREALDAAALEAALQALVEHHDALRLRFVEDAGGWTAEHLPvelggalLWRAEL-----DDAEELERLGEEAQR 3735
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2723 GLSF-DGALLRVLaLPDPQDGDTRVLFAAHHLLVDAVSWGIIVDDLQHAYAERRAGRSPALAAEACGFGAWQAALRQ-LS 2800
Cdd:PRK12316 3736 SLDLaDGPLLRAL-LATLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLPAKTSSFKAWAERLQEhAR 3814
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2801 AATLDGWRSYWRAQ---AADAEAIALPWQDSDNRYADTVHlhDRFERDWTERLLTQTARAYGNEPQEVLLTALALAL-RD 2876
Cdd:PRK12316 3815 GEALKAELAYWQEQlqgVSSELPCDHPQGALQNRHAASVQ--TRLDRELTRRLLQQAPAAYRTQVNDLLLTALARVVcRW 3892
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2877 GGDAATLwVEMEGHGRDDLGAGLDLSRTVGWFTARYPLalHLPAGEDLGAALRSTKDRMRAVPDRGLGFGVLRYLHGE-- 2954
Cdd:PRK12316 3893 TGEASAL-VQLEGHGREDLFADIDLSRTVGWFTSLFPV--RLSPVEDLGASIKAIKEQLRAIPNKGIGFGLLRYLGDEes 3969
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2955 ---LAELPVPQVCFNYLGQLRAGERDGWAL---CEEPDGGGRAGGNRRRHLLDVNAMLVDGELRLDWAWPQDAASREAMQ 3028
Cdd:PRK12316 3970 rrtLAGLPVPRITFNYLGQFDGSFDEEMALfvpAGESAGAEQSPDAPLDNWLSLNGRVYGGELSLDWTFSREMFEEATIQ 4049
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3029 ALSRRYLAVLRELIA-CVQTAEPRPTLADLPLAGLDNAPLDALLSQHPQTQDVYPLAPLQEGLLFHSLLNAEADPYINQT 3107
Cdd:PRK12316 4050 RLADDYAAELTALVEhCCDAERHGVTPSDFPLAGLDQARLDALPLPLGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQM 4129
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3108 TVALHGaLDREAFAAAWQQALERHPILRSGFAVQG-LPSPRQLPHRQVSLPLAEQDWSGLEPAQARsrLSELQAQQCEAG 3186
Cdd:PRK12316 4130 RVDVQG-LDVERFRAAWQAALDRHDVLRSGFVWQGeLGRPLQVVHKQVSLPFAELDWRGRADLQAA--LDALAAAERERG 4206
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3187 FDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAAlresRTPQLPAAPpFRDYLHWLRGQDEAAA 3266
Cdd:PRK12316 4207 FDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERYSG----RPPAQPGGR-YRDYIAWLQRQDAAAS 4281
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3267 RAFWREQLTGL-EPAALPEATE-----PAEGYASSTRRFD---LAAASAWAQSHGLTASSLLQGALALVLQRYYGRDDFA 3337
Cdd:PRK12316 4282 EAFWREQLAALdEPTRLAQAIAradlrSANGYGEHVRELDataTARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVA 4361
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3338 LGITIAGRPPELAGVERMLGVFINSVPLRVTPAGEATPAPWLQALQQRNLDLRTHGYLPLAQIQRAGAADAVSPFDVLLV 3417
Cdd:PRK12316 4362 FGATVAGRPAELPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEIQRWAGQGGEALFDSLLV 4441
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3418 FENLPTESREER---SGMRIEELDHRAHSNYPLMLtAIPDAGGLRIEAALDRSKLDGWLVEQMLDDLDFVLQQVPA--LQ 3492
Cdd:PRK12316 4442 FENYPVSEALQQgapGGLRFGEVTNHEQTNYPLTL-AVGLGETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEdpQR 4520
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3493 RFDALPLLPSQTRSAA---WTSRE-RYACTGNLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGP 3568
Cdd:PRK12316 4521 RLGELQLLEKAEQQRIvalWNRTDaGYPATRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGP 4600
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3569 GQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVCLSVSQRALAVELPGTA----LCLDdpftRA 3644
Cdd:PRK12316 4601 EVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDglasLALD----RD 4676
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3645 QLDAVEPGELPEVPTEAP--AYLIYTSGSTGTPKGVVVTHRNVERLFTAATQtgRFSFDEHDVWSLFHSHAFDFAVWELW 3722
Cdd:PRK12316 4677 EDWEGFPAHDPAVRLHPDnlAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGE--RYELTPDDRVLQFMSFSFDGSHEGLY 4754
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3723 GAWLYGGRaVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALNVRAVVFGGEALEPSRLQPWRERY 3802
Cdd:PRK12316 4755 HPLINGAS-VVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLAWRAL 4833
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3803 PQAELVNMYGITETTVHVSFHRLSDEDLQSPTS-RIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPEL 3881
Cdd:PRK12316 4834 KPVYLFNGYGPTETTVTVLLWKARDGDACGAAYmPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPAL 4913
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3882 TAERFV----ERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEGAWL 3957
Cdd:PRK12316 4914 TAERFVpdpfGAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQL 4993
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3958 MAYAVAADGAEPDP--------QSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKALPKPET--QDRDEGVLESAS 4027
Cdd:PRK12316 4994 VGYVVPQDPALADAdeaqaelrDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDAslLQQAYVAPRSEL 5073
|
2570 2580 2590 2600 2610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 4028 ERRLAELWRQLLGGELPGRGAHFFARGGHSLLVVRLAEAIRAEFAIAVPLKSLFEQP 4084
Cdd:PRK12316 5074 EQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTP 5130
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
87-2812 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 1352.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 87 PAPLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQGEDS-----VAAGGGAAVES 161
Cdd:PRK12316 49 RDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADdslaqVPLDRPLEVEF 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 162 ADLRGRGQDEIDALVE----GFRLRPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSLGLLTQDLSRAYR 237
Cdd:PRK12316 129 EDCSGLPEAEQEARLRdeaqRESLQPFDLCEGPLLRVRLLRLGEE-----EHVLLLTLHHIVSDGWSMNVLIEEFSRFYS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 238 VECGLAAEPAPPLPCQYGDYARWQRDTLD--RLDASLRHHVEALSGAPHLHELPLDHERPAVLGQSGAKLRLAFPPGLSE 315
Cdd:PRK12316 204 AYATGAEPGLPALPIQYADYALWQRSWLEagEQERQLEYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAE 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 316 RVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDDPDFASLVARCRD 395
Cdd:PRK12316 284 ALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKD 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 396 HQLAALEHQALPLERVIETLQVERSSRHAPLFQLMF---ALRHDADLALDLHGVQAHALTLPEDVAKHELTLEVLVGAGG 472
Cdd:PRK12316 364 TVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYnhqPLVADIEALDTVAGLEFGQLEWKSRTTQFDLTLDTYEKGGR 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 473 MSAVWEYNTALWNPATVARWAERYFVALAAMLENPHEPALSWPW-PADELAL-------DDKREPAPRTVGNVVDAIARA 544
Cdd:PRK12316 444 LHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMlDAEERGQlvegwnaTAAEYPLQRGVHRLFEEQVER 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 545 AdefPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARR 624
Cdd:PRK12316 524 T---PEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERL 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 625 AEVVAASGCDAVLTDaQGLAGFAPsVAIAVDELKLDGAG-------ENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHA 697
Cdd:PRK12316 601 AYMLEDSGVQLLLSQ-SHLGRKLP-LAAGVQVLDLDRPAawlegysEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHR 678
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 698 ALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGA-CVVARPDELLEPQRFLAFLSERAITVTDLAPAYAN 776
Cdd:PRK12316 679 ALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGArLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQ 758
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 777 ELVRAsvADDWRDLALRCLVVGGDVLPVALAQRWFelGLDRRCALINAYGPTEATIS-SHYHRVQAidASRPVPLGQLLP 855
Cdd:PRK12316 759 AFLQD--EDVASCTSLRRIVCSGEALPADAQEQVF--AKLPQAGLYNLYGPTEAAIDvTHWTCVEE--GGDSVPIGRPIA 832
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 856 GRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGEslRMYRSGDRVRLLDDGELQFLGRADF 935
Cdd:PRK12316 833 NLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGE--RMYRTGDLARYRADGVIEYAGRIDH 910
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 936 QVKLRGYRIELEEIEHCLGQLPQVRAAAAGVVGegaAQRLVAWVECAGEDGFGQADLNQtdsdqteserwhrALCERLPA 1015
Cdd:PRK12316 911 QVKLRGLRIELGEIEARLLEHPWVREAAVLAVD---GKQLVGYVVLESEGGDWREALKA-------------HLAASLPE 974
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1016 YMVPTQFVALPRLPRNASGKIDRRALPAPPV-LAQAERTPPRTAEESALCEVWAEVLQCE-VGIHDSFFRLGGDSIRSLQ 1093
Cdd:PRK12316 975 YMVPAQWLALERLPLTPNGKLDRKALPAPEAsVAQQGYVAPRNALERTLAAIWQDVLGVErVGLDDNFFELGGDSIVSIQ 1054
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1094 VVARLRERGYAVTPKLMYQYQSAAELAPQLIALQAAPAEAAPLVGEVGLSPIQRWFFDSAPAQPDRYHQYVALRLKQPLD 1173
Cdd:PRK12316 1055 VVSRARQAGIQLSPRDLFQHQTIRSLALVAKAGQATAADQGPASGEVALAPVQRWFFEQAIPQRQHWNQSLLLQARQPLD 1134
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1174 AQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPAIQAQDWRGAADLDSRVDAAfarmQEATPLA-GPLV-ALT 1251
Cdd:PRK12316 1135 PDRLGRALERLVAHHDALRLRFREEDGGWQQAYAAPQAGEVLWQRQAASEEELLALCEEA----QRSLDLEqGPLLrALL 1210
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1252 HAHCDDGERLLICAHHLIVDAVSWRLLLGELfdgLAALARGEAWTPsARGASYADYVEALREADDAQRFDAGFWRELAAQ 1331
Cdd:PRK12316 1211 VDMADGSQRLLLVIHHLVVDGVSWRILLEDL---QRAYADLDADLP-ARTSSYQAWARRLHEHAGARAEELDYWQAQLED 1286
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1332 PMQALPQDRPVALADARQSNvgRIVQTLDAGLTADLLERAGEAYRCRTDEVLLIALARALATRTGRNRLWLDRERHGR-D 1410
Cdd:PRK12316 1287 APHELPCENPDGALENRHER--KLELRLDAERTRQLLQEAPAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGHGReD 1364
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1411 VLDGRDWSSVLGWYTAVHPLPLDlGVADGPAQIGALKEQIRALARRGLDYMPLV------ASARIPALPAGQLLFNYHGV 1484
Cdd:PRK12316 1365 LFEDIDLSRTVGWFTSLFPVRLT-PAADLGESIKAIKEQLRAVPDKGIGYGLLRylageeAAARLAALPQPRITFNYLGQ 1443
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1485 VDAGAHPAFEVEPRTLASGNGADN--PPGALVEINARVQAGRLGLVWNYAGEAYDAATIEAWSQAFAAELAALVAHCLQP 1562
Cdd:PRK12316 1444 FDRQFDEAALFVPATESAGAAQDPcaPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLADDYARELQALIEHCCDE 1523
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1563 GSGALTASDLPQARL---QADEFALlaareDARAIEHAFPLTPLQRGVLLESLRGDGADPYFQQTVAELDGeIDAAALAQ 1639
Cdd:PRK12316 1524 RNRGVTPSDFPLAGLsqaQLDALPL-----PAGEIADIYPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG-LDPDRFRA 1597
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1640 AWQQTVRRQPMLRTAIVWE-GLSVPHQIVLADAAAPWQTLDWSALDDAAQDaqLQRWLADDAAQGVDFAHAPLARMSLIG 1718
Cdd:PRK12316 1598 AWQATVDRHEILRSGFLWQdGLEQPLQVIHKQVELPFAELDWRGREDLGQA--LDALAQAERQKGFDLTRAPLLRLVLVR 1675
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1719 RGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAgaqgatlRLPPAPG--FQAYLDWRERQDLARQRGWWRERLSGYAG 1796
Cdd:PRK12316 1676 TGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYAG-------QPVAAPGgrYRDYIAWLQRQDAAASEAFWKEQLAALEE 1748
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1797 TAALPAPVAAAHHPVQREECERRLSAHDSERLRAFCRERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPPELAGV 1876
Cdd:PRK12316 1749 PTRLAQAARTEDGQVGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGI 1828
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1877 ESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAENEAVGLGEILADSGLDADRLFASLLVVENFPAM------AP 1950
Cdd:PRK12316 1829 EQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWAGQGGEALFDSLLVFENYPVAealkqgAP 1908
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1951 AQLPFA-LRVRETraaNHYALTLRVSERECVRLE-----------ALLDAARVDRAAVAAMLDLAVAGL--LRLLQRPDC 2016
Cdd:PRK12316 1909 AGLVFGrVSNHEQ---TNYPLTLAVTLGETLSLQysydrghfdaaAIERLDRHLLHLLEQMAEDAQAALgeLALLDAGER 1985
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2017 RvaELLGGDDAVQAPQPQRASSATAQSLLWQMPAQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRT 2096
Cdd:PRK12316 1986 Q--RILADWDRTPEAYPRGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERS 2063
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2097 FAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGWG--AAPAWVPASVRWLDAESVLDVVSAYEEPPRVDV 2174
Cdd:PRK12316 2064 FELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRhlLERLPLPAGVARLPLDRDAEWADYPDTAPAVQL 2143
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2175 DADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELa 2254
Cdd:PRK12316 2144 AGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDEL- 2222
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2255 FDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLP--RECLVtGGEALTGALVQQVRALAPTLRIVNHYGPTETTV 2332
Cdd:PRK12316 2223 WDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPavRVYCF-GGEAVPAASLRLAWEALRPVYLFNGYGPTEAVV 2301
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2333 GILTCTV-PEEWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPL-APDRL 2410
Cdd:PRK12316 2302 TPLLWKCrPQDPCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsASGER 2381
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2411 LYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI-----QGSLEG 2485
Cdd:PRK12316 2382 LYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVpddaaEDLLAE 2461
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2486 VAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL----ADLLQQddadssAEAIDETPVNEVLRELWQKLLGREHIG 2561
Cdd:PRK12316 2462 LRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALpkpdVSQLRQ------AYVAPQEGLEQRLAAIWQAVLKVEQVG 2535
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2562 AHDNFFALGGDSILSLQLVARARQA-GLALMPRQLYDHPTLAGLSA--QVQASSPAPATIKPATEAEQSFGLTPIQHWFF 2638
Cdd:PRK12316 2536 LDDHFFELGGHSLLATQVVSRVRQDlGLEVPLRILFERPTLAAFAAslESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFL 2615
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2639 EQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARFQRDAAGQWQQTLGDWQADRF---AHREADAGQRED 2715
Cdd:PRK12316 2616 WQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVledCAGVADAAIRQR 2695
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2716 LLAQWQAGLSFDGALLRVLALPDPQDGDTRVLFAAHHLLVDAVSWGIIVDDLQHAYAERRAGRSPALAAEACGFGAWQAA 2795
Cdd:PRK12316 2696 VAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYADYAAW 2775
|
2810
....*....|....*...
gi 1246793773 2796 LRQ-LSAATLDGWRSYWR 2812
Cdd:PRK12316 2776 QRAwMDSGEGARQLDYWR 2793
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
69-2628 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 1339.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 69 TQDADWRAQSIERAPAGTPAPLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQGE 148
Cdd:PRK12467 1098 AAQQQGAQPALPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQE 1177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 149 DS-----VAAGGGAAVESADLRGRGQDE--IDALVEGFRLRPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACD 221
Cdd:PRK12467 1178 DGrtrqvIHPVGSLTLEEPLLLAADKDEaqLKVYVEAEARQPFDLEQGPLLRVGLLRLAAD-----EHVLVLTLHHIVSD 1252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 222 GVSLGLLTQDLSRAYRVECGLAAEPAPPLPCQYGDYARWQRDTLD--RLDASLRHHVEALSGAPHLHELPLDHERPAVLG 299
Cdd:PRK12467 1253 GWSMQVLVDELVALYAAYSQGQSLQLPALPIQYADYAVWQRQWMDagERARQLAYWKAQLGGEQPVLELPTDRPRPAVQS 1332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 300 QSGAKLRLAFPPGLSERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQ 379
Cdd:PRK12467 1333 HRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAE 1412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 380 LHDDPDFASLVARCRDHQLAALEHQALPLERVIETLQVERSSRHAPLFQLMFALRHDADLAL-DLHGVQAHALTLPEDVA 458
Cdd:PRK12467 1413 VDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQaQLPGLSVESLSWESQTA 1492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 459 KHELTLEVLVGAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENPHEP--ALSWPWPADELAL------DDKREPA 530
Cdd:PRK12467 1493 QFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRlgELDLLDEAERRQIlegwnaTHTGYPL 1572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 531 PRTVGNVvdaIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGL 610
Cdd:PRK12467 1573 ARLVHQL---IEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGG 1649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 611 SVIPLDTEWPQARRAEVVAASGCDAVLTDAQGLAGFA-----PSVAIAVDELKLDGAGENGSGENAAPNQLAYILYTSGS 685
Cdd:PRK12467 1650 AYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPlpdglRSLVLDQEDDWLEGYSDSNPAVNLAPQNLAYVIYTSGS 1729
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 686 TGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGA-CVVARPDELLEPQRFLAFLSERA 764
Cdd:PRK12467 1730 TGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGArLVIAPPGAHRDPEQLIQLIERQQ 1809
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 765 ITVTDLAPAYANELVRAsVADDWRDLALRCLVVGGDVLPVALAQRWFELGLDRrcALINAYGPTEATISSHYHRVQAID- 843
Cdd:PRK12467 1810 VTTLHFVPSMLQQLLQM-DEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDT--GLFNLYGPTETAVDVTHWTCRRKDl 1886
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 844 -ASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGESlRMYRSGDRVRLL 922
Cdd:PRK12467 1887 eGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGTVGS-RLYRTGDLARYR 1965
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 923 DDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAAGVVGEGAAQRLVAWVECAGEDGfgqadLNQTDSDQTES 1002
Cdd:PRK12467 1966 ADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGANGKQLVAYVVPTDPGL-----VDDDEAQVALR 2040
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1003 ERWHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRALPAP-PVLAQAERTPPRTAEESALCEVWAEVLQCE-VGIHDS 1080
Cdd:PRK12467 2041 AILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPdASELQQAYVAPQSELEQRLAAIWQDVLGLEqVGLHDN 2120
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1081 FFRLGGDSIRSLQVVARLRERGYAVTPKLMYQYQSAAELAPQLIALQAAPAEAAPLV-GEVGLSPIQRWFFDSAPAQPDR 1159
Cdd:PRK12467 2121 FFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLAAVAQEGDGTVSIDQGPVtGDLPLLPIQQMFFADDIPERHH 2200
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1160 YHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPaiQAQDWRGAADLDSRVDAAFARMQE 1239
Cdd:PRK12467 2201 WNQSVLLEPREALDAELLEAALQALLVHHDALRLGFVQEDGGWSAMHRAPEQER--RPLLWQVVVADKEELEALCEQAQR 2278
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1240 ATPLA-GPLVALTHAHCDDGE-RLLICAHHLIVDAVSWRLLLGELFDGLAALARGEAWTPSARGASYADYVEALRE--AD 1315
Cdd:PRK12467 2279 SLDLEeGPLLRAVLATLPDGSqRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTyaAS 2358
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1316 DAQRFDAGFWRelaAQpMQALPQDRPVALADARQSN--VGRIVQTLDAGLTADLLERAGEAYRCRTDEVLLIALARALAT 1393
Cdd:PRK12467 2359 AALADELGYWQ---AQ-LQGASTELPCDHPQGGLQRrhAASVTTHLDSEWTRRLLQEAPAAYRTQVNDLLLTALARVIAR 2434
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1394 RTGRNRLWLDRERHGR-DVLDGRDWSSVLGWYTAVHPLPLDlGVADGPAQIGALKEQIRALARRGLDYMPL------VAS 1466
Cdd:PRK12467 2435 WTGQASTLIQLEGHGReDLFDEIDLTRTVGWFTSLYPVKLS-PTASLATSIKTIKEQLRAVPNKGLGFGVLrylgseAAR 2513
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1467 ARIPALPAGQLLFNYHGVVD----AGAHPAFEVEPRTLASGNGADNPPGALVEINARVQAGRLGLVWNYAGEAYDAATIE 1542
Cdd:PRK12467 2514 QTLQALPVPRITFNYLGQFDgsfdAEKQALFVPSGEFSGAEQSEEAPLGNWLSINGQVYGGELNLGWTFSQEMFDEATIQ 2593
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1543 AWSQAFAAELAALVAHCLQPGSGALTASDLPQARL-QADEFALLAAREDaraIEHAFPLTPLQRGVLLESLRGDGADPYF 1621
Cdd:PRK12467 2594 RLADAYAEELRALIEHCCSNDQRGVTPSDFPLAGLsQEQLDRLPVAVGD---IEDIYPLSPMQQGMLFHTLYEGGAGDYI 2670
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1622 QQTVAELDGeIDAAALAQAWQQTVRRQPMLRTAIVWEG-LSVPHQIVLADAAAPWQTLDWSALDDAAQDaqLQRWLADDA 1700
Cdd:PRK12467 2671 NQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFLWDGeLEEPLQVVYKQARLPFSRLDWRDRADLEQA--LDALAAADR 2747
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1701 AQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAgaqgatlRLPPAPG--FQAYLDWRERQ 1778
Cdd:PRK12467 2748 QQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRYFG-------QPPPAREgrYRDYIAWLQAQ 2820
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1779 DLARQRGWWRERLSGYAGTAALPAPVAAAHHPVQREECERRL--SAHDSERLRAFCRERGCTLSDLIAMVWGLANARYGN 1856
Cdd:PRK12467 2821 DAEASEAFWKEQLAALEEPTRLARALYPAPAEAVAGHGAHYLhlDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTG 2900
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1857 HDDVVLGATRSGRPPELAGVESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAENEAVGLGEILADSGLDADRLF 1936
Cdd:PRK12467 2901 QDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPRAEQTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQGGEALF 2980
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1937 ASLLVVENFPA------MAPAQLPF-ALRVRETraaNHYALTLRVSERECVRLEaLLDAARVDRAAVAAMLDLAVAGLLR 2009
Cdd:PRK12467 2981 DSILVFENYPIsealkqGAPSGLRFgAVSSREQ---TNYPLTLAVGLGDTLELE-FSYDRQHFDAAAIERLAESFDRLLQ 3056
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2010 -LLQRPDCRVAEL--LGGDDAVQAPQPQRASSAT--AQSLLWQM-------PAQAVAVEEGAASWTYAQLRAAAGRIAGA 2077
Cdd:PRK12467 3057 aMLNNPAARLGELptLAAHERRQVLHAWNATAAAypSERLVHQLieaqvarTPEAPALVFGDQQLSYAELNRRANRLAHR 3136
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2078 LDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGWGAAPAWVP--ASVRWLD 2155
Cdd:PRK12467 3137 LIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPapAGDTALT 3216
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2156 AESvLDVVSAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFTA 2235
Cdd:PRK12467 3217 LDR-LDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQER 3295
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2236 LFGALLSGRRVRLLPAELaFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPRECLVTGGEALTGALVQQVRAL 2315
Cdd:PRK12467 3296 FLWTLICGGCLVVRDNDL-WDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGADCASLDIYVFGGEAVPPAAFEQVKRK 3374
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2316 APTLRIVNHYGPTETTVGILTCTVP-EEWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAE 2394
Cdd:PRK12467 3375 LKPRGLTNGYGPTEAVVTVTLWKCGgDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPS 3454
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2395 QTAERFVAHPL--APDRlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANG- 2471
Cdd:PRK12467 3455 LTAERFVADPFsgSGGR-LYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGk 3533
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2472 ----VLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLlqqdDADSSAEAIdeTPVNEVL 2547
Cdd:PRK12467 3534 qlvaYVVPADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDP----DAKGSREYV--APRSEVE 3607
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2548 REL---WQKLLGREHIGAHDNFFALGGDSILSLQLVARARQA-GLALMPRQLYDHPTLAGLSAQVQASSPAPATIKPATE 2623
Cdd:PRK12467 3608 QQLaaiWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSlGLKLSLRDLMSAPTIAELAGYSPLGDVPVNLLLDLNR 3687
|
....*
gi 1246793773 2624 AEQSF 2628
Cdd:PRK12467 3688 LETGF 3692
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
75-2617 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 1237.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 75 RAQSIERAPAGTPAPLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQGEDS---- 150
Cdd:PRK12316 2590 RAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEqtrq 2669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 151 -VAAGGGAAVESADLRGRGQDEIDALVEGFRLRPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSLGLLT 229
Cdd:PRK12316 2670 vILPNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQ-----EHVLVITQHHIVSDGWSMQVMV 2744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 230 QDLSRAYRVECGLAAEPAPPLPCQYGDYARWQRDTLD--RLDASLRHHVEALSGAPHLHELPLDHERPAVLGQSGAKLRL 307
Cdd:PRK12316 2745 DELVQAYAGARRGEQPTLPPLPLQYADYAAWQRAWMDsgEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHRGARLDV 2824
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 308 AFPPGLSERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDDPDFA 387
Cdd:PRK12316 2825 ALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFR 2904
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 388 SLVARCRDHQLAALEHQALPLERVIETLQVERSSRHAPLFQLMFALRHDADLALDLHGVQAHALTLPEDVAKHELTLEVL 467
Cdd:PRK12316 2905 DLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERAAAQLPGLHIESFAWDGAATQFDLALDTW 2984
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 468 VGAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENPHEPALSWPW---PADELALDD-----KREPAPRTVGNVVD 539
Cdd:PRK12316 2985 ESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMldaEERGQLLEAwnataAEYPLERGVHRLFE 3064
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 540 AIARAAdefPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEW 619
Cdd:PRK12316 3065 EQVERT---PDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEY 3141
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 620 PQARRAEVVAASGCDAVLTDAQGLAGFAPSVAIAVDELKLDGAGENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHAAL 699
Cdd:PRK12316 3142 PEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSAL 3221
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 700 AAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARPDELLEPQRFLAFLSERaiTVTDLAPAYANELV 779
Cdd:PRK12316 3222 SNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINS--EGVDVLHAYPSMLQ 3299
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 780 RASVADDWRDL-ALRCLVVGGDVLPVALAQRWFELGldrrcALINAYGPTEATISSHYHRVQAIDASRPvPLGQLLPGRI 858
Cdd:PRK12316 3300 AFLEEEDAHRCtSLKRIVCGGEALPADLQQQVFAGL-----PLYNLYGPTEATITVTHWQCVEEGKDAV-PIGRPIANRA 3373
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 859 AAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGEslRMYRSGDRVRLLDDGELQFLGRADFQVK 938
Cdd:PRK12316 3374 CYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGE--RLYRTGDLARYRADGVIEYIGRVDHQVK 3451
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 939 LRGYRIELEEIEHCLGQLPQVRAAaagVVGEGAAQRLVAWVEcagedgfgqadlnQTDSDQTESERWHRALCERLPAYMV 1018
Cdd:PRK12316 3452 IRGFRIELGEIEARLLEHPWVREA---VVLAVDGRQLVAYVV-------------PEDEAGDLREALKAHLKASLPEYMV 3515
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1019 PTQFVALPRLPRNASGKIDRRALPAPPV-LAQAERTPPRTAEESALCEVWAEVLQCE-VGIHDSFFRLGGDSIRSLQVVA 1096
Cdd:PRK12316 3516 PAHLLFLERMPLTPNGKLDRKALPRPDAaLLQQDYVAPVNELERRLAAIWADVLKLEqVGLTDNFFELGGDSIISLQVVS 3595
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1097 RLRERGYAVTPKLMYQYQSAAELAPQLIALQAAPAEAAPLVGEVGLSPIQRWFFDSAPAQPDRYHQYVALRLKQPLDAQH 1176
Cdd:PRK12316 3596 RARQAGIRFTPKDLFQHQTIQGLARVARVGGGVAVDQGPVSGETLLLPIQQQFFEEPVPERHHWNQSLLLKPREALDAAA 3675
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1177 LAQVWDALWRRHDLLRASFERADGQWRqqvAAPGPAPAIQAQDWRGAADLDSRVDAAFARMQEATPLA-GPLV-ALTHAH 1254
Cdd:PRK12316 3676 LEAALQALVEHHDALRLRFVEDAGGWT---AEHLPVELGGALLWRAELDDAEELERLGEEAQRSLDLAdGPLLrALLATL 3752
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1255 CDDGERLLICAHHLIVDAVSWRLLLGELFDGLAALARGEAWTPSARGASYADYVEALRE--ADDAQRFDAGFWRELAAQP 1332
Cdd:PRK12316 3753 ADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLPAKTSSFKAWAERLQEhaRGEALKAELAYWQEQLQGV 3832
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1333 MQALPQDRPvalADARQSNVGRIVQT-LDAGLTADLLERAGEAYRCRTDEVLLIALARALATRTGRNRLWLDRERHGR-D 1410
Cdd:PRK12316 3833 SSELPCDHP---QGALQNRHAASVQTrLDRELTRRLLQQAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGReD 3909
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1411 VLDGRDWSSVLGWYTAVHPLPLDLGVADGpAQIGALKEQIRALARRGLDYMPL------VASARIPALPAGQLLFNYHGV 1484
Cdd:PRK12316 3910 LFADIDLSRTVGWFTSLFPVRLSPVEDLG-ASIKAIKEQLRAIPNKGIGFGLLrylgdeESRRTLAGLPVPRITFNYLGQ 3988
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1485 VDAgahpAFEVEPRTL---ASGNGADNPPGALVE----INARVQAGRLGLVWNYAGEAYDAATIEAWSQAFAAELAALVA 1557
Cdd:PRK12316 3989 FDG----SFDEEMALFvpaGESAGAEQSPDAPLDnwlsLNGRVYGGELSLDWTFSREMFEEATIQRLADDYAAELTALVE 4064
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1558 HCLQPGSGALTASDLPQARLqaDEFALLAAREDARAIEHAFPLTPLQRGVLLESLRGDGADPYFQQTVAELDGeIDAAAL 1637
Cdd:PRK12316 4065 HCCDAERHGVTPSDFPLAGL--DQARLDALPLPLGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERF 4141
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1638 AQAWQQTVRRQPMLRTAIVWEG-LSVPHQIVLADAAAPWQTLDWSALDDaaQDAQLQRWLADDAAQGVDFAHAPLARMSL 1716
Cdd:PRK12316 4142 RAAWQAALDRHDVLRSGFVWQGeLGRPLQVVHKQVSLPFAELDWRGRAD--LQAALDALAAAERERGFDLQRAPLLRLVL 4219
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1717 IGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGatlrlPPAPGFQAYLDWRERQDLARQRGWWRERLSGY-A 1795
Cdd:PRK12316 4220 VRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERYSGRPPA-----QPGGRYRDYIAWLQRQDAAASEAFWREQLAALdE 4294
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1796 GTAALPAPVAAAHHPVQ-REECERRLSAHDSERLRAFCRERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPPELA 1874
Cdd:PRK12316 4295 PTRLAQAIARADLRSANgYGEHVRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELP 4374
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1875 GVESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAENEAVGLGEILADSGLDADRLFASLLVVENFPAMAPAQLP 1954
Cdd:PRK12316 4375 GIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEIQRWAGQGGEALFDSLLVFENYPVSEALQQG 4454
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1955 FALRVRETRAANH----YALTLRVSERECVRLEALLDAARVDRAAVAAMLDLAVAGLLRLLQRPDCRVAEL--LGGDDAV 2028
Cdd:PRK12316 4455 APGGLRFGEVTNHeqtnYPLTLAVGLGETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELqlLEKAEQQ 4534
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2029 QAPQPQRASSA--TAQSLLWQ-------MPAQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQ 2099
Cdd:PRK12316 4535 RIVALWNRTDAgyPATRCVHQlvaerarMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEM 4614
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2100 LAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVI--GWGAAPAWVPASVRWLDAESVLDVVSAYEEPPRVDVDAD 2177
Cdd:PRK12316 4615 MVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLtqSHLLQRLPIPDGLASLALDRDEDWEGFPAHDPAVRLHPD 4694
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2178 TPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELaFDA 2257
Cdd:PRK12316 4695 NLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSL-WDP 4773
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2258 QALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPR-ECLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVGILT 2336
Cdd:PRK12316 4774 ERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSlRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLL 4853
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2337 CTVPE-EWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPL-APDRLLYRS 2414
Cdd:PRK12316 4854 WKARDgDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGGRLYRT 4933
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2415 GDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVlQLGACIQGSLEGVAE------ 2488
Cdd:PRK12316 4934 GDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGK-QLVGYVVPQDPALADadeaqa 5012
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2489 --------ALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL----ADLLQQddadssAEAIDETPVNEVLRELWQKLLG 2556
Cdd:PRK12316 5013 elrdelkaALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALpqpdASLLQQ------AYVAPRSELEQQVAAIWAEVLQ 5086
|
2570 2580 2590 2600 2610 2620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 2557 REHIGAHDNFFALGGDSILSLQLVARAR-QAGLALMPRQLYDHPTLAGLSAQVQASSPAPAT 2617
Cdd:PRK12316 5087 LERVGLDDNFFELGGHSLLAIQVTSRIQlELGLELPLRELFQTPTLAAFVELAAAAGSGDDE 5148
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1625-4082 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 1207.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1625 VAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGlSVPHQIVLADAAAPWQTLDWSALDDAAQDAQLQRWLADDAAQGV 1704
Cdd:PRK05691 1756 MARLSGVLDVDRFEAALQALILRHETLRTTFPSVD-GVPVQQVAEDSGLRMDWQDFSALPADARQQRLQQLADSEAHQPF 1834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1705 DFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGATLRLPPAPgfQAYLD-------WRER 1777
Cdd:PRK05691 1835 DLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDRESPLEPLP--VQYLDysvwqrqWLES 1912
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1778 QDLARQRGWWRERLsgyaGTA--ALPAPVAAAHHPVQ--REECER-RLSAHDSERLRAFCRERGCTLSDLIAMVWGLANA 1852
Cdd:PRK05691 1913 GERQRQLDYWKAQL----GNEhpLLELPADRPRPPVQshRGELYRfDLSPELAARVRAFNAQRGLTLFMTMTATLAALLY 1988
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1853 RYGNHDDVVLGATRSGR-PPElagVESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAENEAVGLGEILadSGLD 1931
Cdd:PRK05691 1989 RYSGQRDLRIGAPVANRiRPE---SEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLV--EALQ 2063
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1932 ADR------LFASLLVVENFPAMAPAQLP---FALRVRETRAANhYALTLRVSERE-----CVRLEALLDAARVDRAAVA 1997
Cdd:PRK05691 2064 PPRsaaynpLFQVMCNVQRWEFQQSRQLAgmtVEYLVNDARATK-FDLNLEVTDLDgrlgcCLTYSRDLFDEPRIARMAE 2142
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1998 AMLDLAVAgllrLLQRPDCRVAELLGGDDAVQ-------APQP-QRASSATAQSLLWQMPA---QAVAVEEGAASWTYAQ 2066
Cdd:PRK05691 2143 HWQNLLEA----LLGDPQQRLAELPLLAAAEQqqlldslAGEAgEARLDQTLHGLFAAQAArtpQAPALTFAGQTLSYAE 2218
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2067 LRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGWGA---A 2143
Cdd:PRK05691 2219 LDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRAlfeA 2298
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2144 PAWVPASV-RWL--DAESVLDVVSAyEEPPRVDVdADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDAS 2220
Cdd:PRK05691 2299 LGELPAGVaRWCleDDAAALAAYSD-APLPFLSL-PQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDC 2376
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2221 LATLSTVAADLGFTALFGALLSGRRVrLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLA-AAGGTAVLPRECLVT 2299
Cdd:PRK05691 2377 ELHFYSINFDAASERLLVPLLCGARV-VLRAQGQWGAEEICQLIREQQVSILGFTPSYGSQLAQwLAGQGEQLPVRMCIT 2455
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2300 GGEALTGALVQQVR-ALAPTLrIVNHYGPTETTVGILTCTVPEEWPVEQG-VPVGHPLAGNEAWVLDRFGLPAPVGVAGE 2377
Cdd:PRK05691 2456 GGEALTGEHLQRIRqAFAPQL-FFNAYGPTETVVMPLACLAPEQLEEGAAsVPIGRVVGARVAYILDADLALVPQGATGE 2534
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2378 LYLGGGNLSLGYWQRAEQTAERFVAHPLAPDR-LLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLP 2456
Cdd:PRK05691 2535 LYVGGAGLAQGYHDRPGLTAERFVADPFAADGgRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHP 2614
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2457 GVEVAAVLALPGANG----------VLQLGACIQGSL-EGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL-AD 2524
Cdd:PRK05691 2615 AVREAVVLALDTPSGkqlagylvsaVAGQDDEAQAALrEALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALpAP 2694
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2525 LLQQDDADSSAeaidetPVNEVLREL---WQKLLGREHIGAHDNFFALGGDSILSLQLVARARQAGLALMPRQLYDHPTL 2601
Cdd:PRK05691 2695 DPELNRQAYQA------PRSELEQQLaqiWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTV 2768
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2602 AGLSAQVQASSPAPATIKPATEAEqsfGLTPIQHWFFEQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRA 2681
Cdd:PRK05691 2769 QTLAAVATHSEAAQAEQGPLQGAS---GLTPIQHWFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRL 2845
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2682 RFqRDAAGQWQ---QTLGD----WQAdrfahREADAGQREDLLAQWQAGLSF-DGALLRVLALPDPQdGDTRVLFAAHHL 2753
Cdd:PRK05691 2846 RF-SQADGRWQaeyRAVTAqellWQV-----TVADFAECAALFADAQRSLDLqQGPLLRALLVDGPQ-GQQRLLLAIHHL 2918
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2754 LVDAVSWGIIVDDLQHAYAERRAGRSPALAAEACGFGAWQAALRQLSAA-TLDGWRSYWRAQAADAEAI---ALPWQDSD 2829
Cdd:PRK05691 2919 VVDGVSWRVLLEDLQALYRQLSAGAEPALPAKTSAFRDWAARLQAYAGSeSLREELGWWQAQLGGPRAElpcDRPQGGNL 2998
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2830 NRYADTVHLhdRFERDWTERLLTQTARAYGNEPQEVLLTALALAL-RDGGDAATLwVEMEGHGRDDLGAGLDLSRTVGWF 2908
Cdd:PRK05691 2999 NRHAQTVSV--RLDAERTRQLLQQAPAAYRTQVNDLLLTALARVLcRWSGQPSVL-VQLEGHGREALFDDIDLTRSVGWF 3075
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2909 TARYPLAL--HLPAGEDLGAALRSTKDRMRAVPDRGLGFGVLRYLHGE-----LAELPVPQVCFNYLGQLRAG-ERDG-W 2979
Cdd:PRK05691 3076 TSAYPLRLtpAPGDDAARGESIKAIKEQLRAVPHKGLGYGVLRYLADAavreaMAALPQAPITFNYLGQFDQSfASDAlF 3155
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2980 ALCEEPDGGGRAGGNRRRHLLDVNAMLVDGELRLDWAWPQDAASREAMQALSRRYLAVLRELIA-CVQTAEPRPTLADLP 3058
Cdd:PRK05691 3156 RPLDEPAGPAHDPDAPLPNELSVDGQVYGGELVLRWTYSAERYDEQTIAELAEAYLAELQALIAhCLADGAGGLTPSDFP 3235
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3059 LAGLDNAPLDALLSQHPQTQDVYPLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGF 3138
Cdd:PRK05691 3236 LAQLTQAQLDALPVPAAEIEDVYPLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASF 3315
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3139 AVQGLPSPRQLPHRQVSLPLAEQDWSGLEPAQARSRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIV 3218
Cdd:PRK05691 3316 SWNAGETMLQVIHKPGRTPIDYLDWRGLPEDGQEQRLQALHKQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILI 3395
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3219 DGWSSALLLDEVWRLYAALRESRTPQLPAAPPFRDYLHWLRGQDEAAARAFWREQLTGLE-PAALP-------EATEPAE 3290
Cdd:PRK05691 3396 DAWCRSLLMNDFFEIYTALGEGREAQLPVPPRYRDYIGWLQRQDLAQARQWWQDNLRGFErPTPIPsdrpflrEHAGDSG 3475
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3291 GYASSTRRFDLAAASA-----WAQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRPPELAGVERMLGVFINSVPL 3365
Cdd:PRK05691 3476 GMVVGDCYTRLDAADGarlreLAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPVSMPQMQRTVGLFINSIAL 3555
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3366 RV---TPAGEATPAPWLQALQQRNLDLRTHGYLPLAQIQRAGAADAVSP-FDVLLVFENLPTESR--EERSGMRIEELDH 3439
Cdd:PRK05691 3556 RVqlpAAGQRCSVRQWLQGLLDSNMELREYEYLPLVAIQECSELPKGQPlFDSLFVFENAPVEVSvlDRAQSLNASSDSG 3635
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3440 RAHSNYPLMLTAIP-DAGGLRIeaALDRSKLDGWLVEQMLDDLDFVLqqVPALQRFD----ALPLLPSQTRS----AAWT 3510
Cdd:PRK05691 3636 RTHTNFPLTAVCYPgDDLGLHL--SYDQRYFDAPTVERLLGEFKRLL--LALVQGFHgdlsELPLLGEQERDflldGCNR 3711
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3511 SRERYACTGNLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAIL 3590
Cdd:PRK05691 3712 SERDYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSF 3791
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3591 KTGAAYVPVDPHAPAARRGFILEDSG----VClSVSQRALAVELPGTALCLDDPftraQLDAVEPGELPEVPTEAP---- 3662
Cdd:PRK05691 3792 KAGAGYLPLDPGLPAQRLQRIIELSRtpvlVC-SAACREQARALLDELGCANRP----RLLVWEEVQAGEVASHNPgiys 3866
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3663 -----AYLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEA 3737
Cdd:PRK05691 3867 gpdnlAYVIYTSGSTGLPKGVMVEQRGM--LNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNA 3944
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3738 VCRQPDAFLDLLAEYGVTVLNQTPSafyALQSQAMRRELALN-VRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITET 3816
Cdd:PRK05691 3945 IAHDPQGLLAHVQAQGITVLESVPS---LIQGMLAEDRQALDgLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAEC 4021
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3817 TVHVSFHRLSDEDLQSPTSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVER----GGQ 3892
Cdd:PRK05691 4022 SDDVAFFRVDLASTRGSYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHpfgaPGE 4101
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3893 RFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEGAWLMAYAVAADGAEPDPQ 3972
Cdd:PRK05691 4102 RLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNGKHLVGYLVPHQTVLAQGA 4181
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3973 SL---REALRALLPDYMLPRLIQLLPALPLTANGKLDRKALPKPE---TQDRDEGVLESASERRLAELWRQLLGGELPGR 4046
Cdd:PRK05691 4182 LLeriKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDigqLQSQAYLAPRNELEQTLATIWADVLKVERVGV 4261
|
2570 2580 2590
....*....|....*....|....*....|....*.
gi 1246793773 4047 GAHFFARGGHSLLVVRLAEAIRAEFAIAVPLKSLFE 4082
Cdd:PRK05691 4262 HDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFE 4297
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
75-2609 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 1082.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 75 RAQSIERAPAGTPAPLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQGEDS---- 150
Cdd:PRK05691 1716 SQGAIARVDRSQPVPLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGvpvq 1795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 151 -VAAGGGAAVE----SADLRGRGQDEIDALVEGFRLRPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSL 225
Cdd:PRK05691 1796 qVAEDSGLRMDwqdfSALPADARQQRLQQLADSEAHQPFDLERGPLLRACLVKAAER-----EHYFVLTLHHIVTEGWAM 1870
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 226 GLLTQDLSRAYrvECGLAAEPAP--PLPCQYGDYARWQRDTLDRLDAS--LRHHVEALSGAPHLHELPLDHERPAVLGQS 301
Cdd:PRK05691 1871 DIFARELGALY--EAFLDDRESPlePLPVQYLDYSVWQRQWLESGERQrqLDYWKAQLGNEHPLLELPADRPRPPVQSHR 1948
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 302 GAKLRLAFPPGLSERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLH 381
Cdd:PRK05691 1949 GELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQLD 2028
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 382 DDPDFASLVARCRDHQLAALEHQALPLERVIETLQVERSSRHAPLFQLMFAL-RHDADLALDLHGVQAHALTLPEDVAKH 460
Cdd:PRK05691 2029 GQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVqRWEFQQSRQLAGMTVEYLVNDARATKF 2108
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 461 ELTLEVLVGAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENPHEPALSWPW--PADELALDDKREPAP---RTVG 535
Cdd:PRK05691 2109 DLNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLlaAAEQQQLLDSLAGEAgeaRLDQ 2188
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 536 NVVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPL 615
Cdd:PRK05691 2189 TLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPL 2268
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 616 DTEWPQARRAEVVAASGCDAVLTDA---QGLAGFAPSVA---IAVDELKLDGAGENGSGENAAPNQLAYILYTSGSTGIP 689
Cdd:PRK05691 2269 DPEYPLERLHYMIEDSGIGLLLSDRalfEALGELPAGVArwcLEDDAAALAAYSDAPLPFLSLPQHQAYLIYTSGSTGKP 2348
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 690 KGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARPDELLEPQRFLAFLSERAITVTD 769
Cdd:PRK05691 2349 KGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQGQWGAEEICQLIREQQVSILG 2428
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 770 LAPAYANELVRAsVADDWRDLALRCLVVGGDVLPVALAQRWfelgldRRC----ALINAYGPTEATI----SSHYHRVQA 841
Cdd:PRK05691 2429 FTPSYGSQLAQW-LAGQGEQLPVRMCITGGEALTGEHLQRI------RQAfapqLFFNAYGPTETVVmplaCLAPEQLEE 2501
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 842 IDASrpVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLpSGESLRMYRSGDRVRL 921
Cdd:PRK05691 2502 GAAS--VPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPF-AADGGRLYRTGDLVRL 2578
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 922 LDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAAGVVGEGAAQRLVAWVEC--AGEDGFGQADLNqtdsdq 999
Cdd:PRK05691 2579 RADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLVSavAGQDDEAQAALR------ 2652
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1000 tesERWHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRALPAP-PVLAQAERTPPRTAEESALCEVWAEVLQCE-VGI 1077
Cdd:PRK05691 2653 ---EALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPdPELNRQAYQAPRSELEQQLAQIWREVLNVErVGL 2729
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1078 HDSFFRLGGDSIRSLQVVARLRERGYAVTPKLMYQYQSAAELAPQLIALQAAPAEAAPLVGEVGLSPIQRWFFDSAPAQP 1157
Cdd:PRK05691 2730 GDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQTLAAVATHSEAAQAEQGPLQGASGLTPIQHWFFDSPVPQP 2809
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1158 DRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPA-IQAQdwrgAADLDSRvDAAFAR 1236
Cdd:PRK05691 2810 QHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGRWQAEYRAVTAQELlWQVT----VADFAEC-AALFAD 2884
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1237 MQEATPLA-GPLV-ALTHAHCDDGERLLICAHHLIVDAVSWRLLLGELFDGLAALARGEAWTPSARGASYADYVEALRE- 1313
Cdd:PRK05691 2885 AQRSLDLQqGPLLrALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAGAEPALPAKTSAFRDWAARLQAy 2964
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1314 -ADDAQRFDAGFWRELAAQPMQALPQDRPVALADARQSNVGRIvqTLDAGLTADLLERAGEAYRCRTDEVLLIALARALA 1392
Cdd:PRK05691 2965 aGSESLREELGWWQAQLGGPRAELPCDRPQGGNLNRHAQTVSV--RLDAERTRQLLQQAPAAYRTQVNDLLLTALARVLC 3042
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1393 TRTGRNRLWLDRERHGRDVL-DGRDWSSVLGWYTAVHPL---PLDLGVADGPAQIGALKEQIRALARRGLDYMPL----- 1463
Cdd:PRK05691 3043 RWSGQPSVLVQLEGHGREALfDDIDLTRSVGWFTSAYPLrltPAPGDDAARGESIKAIKEQLRAVPHKGLGYGVLrylad 3122
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1464 -VASARIPALPAGQLLFNYHGVVDAGAHPAFEVEPRTLASGnGADNPPGAL---VEINARVQAGRLGLVWNYAGEAYDAA 1539
Cdd:PRK05691 3123 aAVREAMAALPQAPITFNYLGQFDQSFASDALFRPLDEPAG-PAHDPDAPLpneLSVDGQVYGGELVLRWTYSAERYDEQ 3201
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1540 TIEAWSQAFAAELAALVAHCLQPGSGALTASDLPQARLQADEFALLAAreDARAIEHAFPLTPLQRGVLLESLRGDGADP 1619
Cdd:PRK05691 3202 TIAELAEAYLAELQALIAHCLADGAGGLTPSDFPLAQLTQAQLDALPV--PAAEIEDVYPLTPMQEGLLLHTLLEPGTGL 3279
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1620 YFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGLSVPHQIVLADAAAPWQTLDWSALDDAAQDAQLQRWLADD 1699
Cdd:PRK05691 3280 YYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGETMLQVIHKPGRTPIDYLDWRGLPEDGQEQRLQALHKQE 3359
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1700 AAQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGATLRLPPAPGFQAYLDWRERQD 1779
Cdd:PRK05691 3360 REAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYTALGEGREAQLPVPPRYRDYIGWLQRQD 3439
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1780 LARQRGWWRERLSGYAGTaalpaPVAAAHHPVQRE-----------ECERRLSAHDSERLRAFCRERGCTLSDLIAMVWG 1848
Cdd:PRK05691 3440 LAQARQWWQDNLRGFERP-----TPIPSDRPFLREhagdsggmvvgDCYTRLDAADGARLRELAQAHQLTVNTFAQAAWA 3514
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1849 LANARYGNHDDVVLGATRSGRPPELAGVESMVGVFINTLPLRLRI-DAGQPAL--DLLSALRSQSLEVAENEAVGLGEIL 1925
Cdd:PRK05691 3515 LVLRRYSGDRDVLFGVTVAGRPVSMPQMQRTVGLFINSIALRVQLpAAGQRCSvrQWLQGLLDSNMELREYEYLPLVAIQ 3594
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1926 ADSGL-DADRLFASLLVVENfpamAPAQLPFALRVRETRAAN-------HYALTLRVSERECVRLEALLDAARVDRAAVA 1997
Cdd:PRK05691 3595 ECSELpKGQPLFDSLFVFEN----APVEVSVLDRAQSLNASSdsgrthtNFPLTAVCYPGDDLGLHLSYDQRYFDAPTVE 3670
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1998 AMLDLAVAGLLRLLQRPDCRVAE--LLGGDDA---VQAPQPQRASSATAQSLLWQMPAQAVAVEEGAA------SWTYAQ 2066
Cdd:PRK05691 3671 RLLGEFKRLLLALVQGFHGDLSElpLLGEQERdflLDGCNRSERDYPLEQSYVRLFEAQVAAHPQRIAascldqQWSYAE 3750
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2067 LRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGWGAAPAW 2146
Cdd:PRK05691 3751 LNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACREQ 3830
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2147 VPASVRWLDAES-----VLDVVSAYEEP---PRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGED 2218
Cdd:PRK05691 3831 ARALLDELGCANrprllVWEEVQAGEVAshnPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEA 3910
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2219 ASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPRECLV 2298
Cdd:PRK05691 3911 DVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQALDGLRWMLP 3990
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2299 TgGEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPEEWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGEL 2378
Cdd:PRK05691 3991 T-GEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFFRVDLASTRGSYLPIGSPTDNNRLYLLDEALELVPLGAVGEL 4069
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2379 YLGGGNLSLGYWQRAEQTAERFVAHPL-APDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPG 2457
Cdd:PRK05691 4070 CVAGTGVGRGYVGDPLRTALAFVPHPFgAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAE 4149
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2458 VEVAAVLALPGANGVLQLGACIQGS--------LEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALA--DLLQ 2527
Cdd:PRK05691 4150 VREAAVAVQEGVNGKHLVGYLVPHQtvlaqgalLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPalDIGQ 4229
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2528 QDDADSSAEaidETPVNEVLRELWQKLLGREHIGAHDNFFALGGDSILSLQLVARARQAGLALMP-RQLYDHPTLAGLSA 2606
Cdd:PRK05691 4230 LQSQAYLAP---RNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPlRAMFECSTVEELAE 4306
|
...
gi 1246793773 2607 QVQ 2609
Cdd:PRK05691 4307 YIE 4309
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
3065-4084 |
0e+00 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 741.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3065 APLDALLSQHPQTQDVYPLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFAVQgLP 3144
Cdd:COG1020 2 AAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTR-AG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3145 SPRQLPHRQVSLPLAEQDWSGLEPAQARSRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSA 3224
Cdd:COG1020 81 RPVQVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3225 LLLDEVWRLYAALRESRTPQLPAAPP-----FRDYLHWLRGQDEAAARAFWREQLTGLEPA-ALPE--ATEPAEGYASST 3296
Cdd:COG1020 161 LLLAELLRLYLAAYAGAPLPLPPLPIqyadyALWQREWLQGEELARQLAYWRQQLAGLPPLlELPTdrPRPAVQSYRGAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3297 RRFDLAAA-----SAWAQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRPpeLAGVERMLGVFINSVPLRVTPAG 3371
Cdd:COG1020 241 VSFRLPAEltaalRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRP--RPELEGLVGFFVNTLPLRVDLSG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3372 EATPAPWLQALQQRNLDLRTHGYLPLAQIQRA---GAADAVSP-FDVLLVFENLPTESREeRSGMRIEELD-HRAHSNYP 3446
Cdd:COG1020 319 DPSFAELLARVRETLLAAYAHQDLPFERLVEElqpERDLSRNPlFQVMFVLQNAPADELE-LPGLTLEPLElDSGTAKFD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3447 LMLTAIPDAGGLRIEAALDRSKLDGWLVEQMLDDLDFVLQQVPAL--QRFDALPLLPSQTRS---AAWTSRER-YACTGN 3520
Cdd:COG1020 398 LTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADpdQPLGDLPLLTAAERQqllAEWNATAApYPADAT 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3521 LVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVD 3600
Cdd:COG1020 478 LHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLD 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3601 PHAPAARRGFILEDSGVCLSVSQRALAVELPGTA---LCLDDPFTRAQldavePGELPEVPT--EAPAYLIYTSGSTGTP 3675
Cdd:COG1020 558 PAYPAERLAYMLEDAGARLVLTQSALAARLPELGvpvLALDALALAAE-----PATNPPVPVtpDDLAYVIYTSGSTGRP 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3676 KGVVVTHRNVERLFTAATQtgRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVT 3755
Cdd:COG1020 633 KGVMVEHRALVNLLAWMQR--RYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVT 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3756 VLNQTPSAFYALQSQAMRRELALnvRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQSPTS 3835
Cdd:COG1020 711 VLNLTPSLLRALLDAAPEALPSL--RLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADGGSV 788
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3836 RIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE----RGGQRFYRSGDLGRYRADGSLEY 3911
Cdd:COG1020 789 PIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVAdpfgFPGARLYRTGDLARWLPDGNLEF 868
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3912 RGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTV-EGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRL 3990
Cdd:COG1020 869 LGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVArEDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAA 948
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3991 IQLLPALPLTANGKLDRKALPKPETQDRDEGVLESASERR--LAELWRQLLGGELPGRGAHFFARGGHSLLVVRLAEAIR 4068
Cdd:COG1020 949 VVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEeeAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAAR 1028
|
1050
....*....|....*.
gi 1246793773 4069 AEFAIAVPLKSLFEQP 4084
Cdd:COG1020 1029 LLLLLLLLLLLFLAAA 1044
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3075-4085 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 676.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3075 PQTQDVY---PLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFAVQGlPSPRQLPH 3151
Cdd:PRK12467 41 PQVRSAFeriPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDE-EGFRQVID 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3152 RQVSLPLAEQDWSGLEPAQARSRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVW 3231
Cdd:PRK12467 120 ASLSLTIPLDDLANEQGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3232 RLYAALRESRTPQLPAAP-PFRDYLHWLRGQDEAAARA----FWREQLTGLEPA-ALP-EATEPA-EGYASSTRRFDL-- 3301
Cdd:PRK12467 200 QLYSAYSQGREPSLPALPiQYADYAIWQRSWLEAGERErqlaYWQEQLGGEHTVlELPtDRPRPAvPSYRGARLRVDLpq 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3302 ---AAASAWAQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRPPElaGVERMLGVFINSVPLRVTPAGEATPAPW 3378
Cdd:PRK12467 280 alsAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRV--ETERLIGFFVNTQVLKAEVDPQASFLEL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3379 LQALQQRNLDLRTHGYLPLAQIqragaADAVSP---------FDVLLVFENLPTESRE----ERSGMRIEELDHRAHS-N 3444
Cdd:PRK12467 358 LQQVKRTALGAQAHQDLPFEQL-----VEALQPerslshsplFQVMFNHQNTATGGRDregaQLPGLTVEELSWARHTaQ 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3445 YPLMLTAIPDAGGLRIEAALDRSKLDGWLVEQMLDDLDFVLQQVPA--LQRFDALPLLPSQTRSA---AWTSRERYACTG 3519
Cdd:PRK12467 433 FDLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAepRRRLGELPLLDAEERARelvRWNAPATEYAPD 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPV 3599
Cdd:PRK12467 513 CVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPL 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3600 DPHAPAARRGFILEDSGVCLSVSQRALAVELPG----TALCLDDPftrAQLDAVEPGELPEVPTEAP--AYLIYTSGSTG 3673
Cdd:PRK12467 593 DPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVpaglRSLCLDEP---ADLLCGYSGHNPEVALDPDnlAYVIYTSGSTG 669
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3674 TPKGVVVTHRNVERLFTAATQtgRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYG 3753
Cdd:PRK12467 670 QPKGVAISHGALANYVCVIAE--RLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQG 747
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3754 VTVLNQTPSAFYALQsQAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQSP 3833
Cdd:PRK12467 748 VTVLKIVPSHLQALL-QASRVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYELSDEERDFG 826
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3834 TSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE----RGGQRFYRSGDLGRYRADGSL 3909
Cdd:PRK12467 827 NVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPdpfgADGGRLYRTGDLARYRADGVI 906
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3910 EYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEGAWLMAYAVAADGAEPDPQS-----LREALRALLPD 3984
Cdd:PRK12467 907 EYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVPAAVADGAEHQatrdeLKAQLRQVLPD 986
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3985 YMLPRLIQLLPALPLTANGKLDRKALPKPETQDRDEGVLESAS--ERRLAELWRQLLGGELPGRGAHFFARGGHSLLVVR 4062
Cdd:PRK12467 987 YMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTelEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQ 1066
|
1050 1060
....*....|....*....|...
gi 1246793773 4063 LAEAIRAEFAIAVPLKSLFEQPR 4085
Cdd:PRK12467 1067 VISRVRQRLGIQVPLRTLFEHQT 1089
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
84-1371 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 664.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 84 AGTPAPLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVL--------DRCIQGEDSVAAGG 155
Cdd:PRK12467 46 AFERIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLrtrfvqdeEGFRQVIDASLSLT 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 156 GAAVESADLRGRGQDE-IDALVEGFRLRPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSLGLLTQDLSR 234
Cdd:PRK12467 126 IPLDDLANEQGRARESqIEAYINEEVARPFDLANGPLLRVRLLRLADD-----EHVLVVTLHHIISDGWSMRVLVEELVQ 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 235 AYRVECGLAAEPAPPLPCQYGDYARWQRDTLD--RLDASLRHHVEALSGAPHLHELPLDHERPAVLGQSGAKLRLAFPPG 312
Cdd:PRK12467 201 LYSAYSQGREPSLPALPIQYADYAIWQRSWLEagERERQLAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 313 LSERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDDPDFASLVAR 392
Cdd:PRK12467 281 LSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQ 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 393 CRDHQLAALEHQALPLERVIETLQVERSSRHAPLFQLMFALRHDA-----DLALDLHGVQAHALTLPEDVAKHELTLEVL 467
Cdd:PRK12467 361 VKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQNTAtggrdREGAQLPGLTVEELSWARHTAQFDLALDTY 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 468 VGAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENPHEPALSWP-WPADELALDDKREPAPRTV---GNVVDAIAR 543
Cdd:PRK12467 441 ESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPlLDAEERARELVRWNAPATEyapDCVHQLIEA 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 544 AADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQAR 623
Cdd:PRK12467 521 QARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDR 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 624 RAEVVAASGCDAVLTDAQGLAGFA-----PSVAIAVDELKLDGAGENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHAA 698
Cdd:PRK12467 601 LAYMLDDSGVRLLLTQSHLLAQLPvpaglRSLCLDEPADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGA 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 699 LAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARP-DELLEPQRFLAFLSERAITVTDLAPAYANE 777
Cdd:PRK12467 681 LANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPpDCARDAEAFAALMADQGVTVLKIVPSHLQA 760
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 778 LVRASVADDwrDLALRCLVVGGDVLPVALAQRWFELGLDrrCALINAYGPTEATISSHYHRVQAIDA-SRPVPLGQLLPG 856
Cdd:PRK12467 761 LLQASRVAL--PRPQRALVCGGEALQVDLLARVRALGPG--ARLINHYGPTETTVGVSTYELSDEERdFGNVPIGQPLAN 836
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 857 RIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPlrLPSG-ESLRMYRSGDRVRLLDDGELQFLGRADF 935
Cdd:PRK12467 837 LGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVP--DPFGaDGGRLYRTGDLARYRADGVIEYLGRMDH 914
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 936 QVKLRGYRIELEEIEHCLGQLPQVRAAAAGVVGEGAAQRLVAW-VECAGEDGFGQADLNQTdsdqteserWHRALCERLP 1014
Cdd:PRK12467 915 QVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYlVPAAVADGAEHQATRDE---------LKAQLRQVLP 985
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1015 AYMVPTQFVALPRLPRNASGKIDRRALPAPPVLA-QAERTPPRTAEESALCEVWAEVLQCE-VGIHDSFFRLGGDSIRSL 1092
Cdd:PRK12467 986 DYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAvQATFVAPQTELEKRLAAIWADVLKVErVGLTDNFFELGGHSLLAT 1065
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1093 QVVARLRER-GYAVTPKLMYQYQSAAELAPQLIALQAAPAEAAPLVGE---VGLSPIQ--RWFFDSAPAQPDRYHQYVAL 1166
Cdd:PRK12467 1066 QVISRVRQRlGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDRdqpLPLSYAQerQWFLWQLEPGSAAYHIPQAL 1145
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1167 RLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPAIQAQDWRGAAD---LDSRVDAAFARMQEATpl 1243
Cdd:PRK12467 1146 RLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLTLEEPLLLAADKDeaqLKVYVEAEARQPFDLE-- 1223
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1244 AGPLVALTHAHCDDGERLLICA-HHLIVDAVSWRLLLGELFDGLAALARGEAWTPSARGASYADYVEALReaddaQRFDA 1322
Cdd:PRK12467 1224 QGPLLRVGLLRLAADEHVLVLTlHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALPIQYADYAVWQR-----QWMDA 1298
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 1323 G-------FWREL--AAQPMQALPQDRPvalADARQSNVG-RIVQTLDAGLTADLLERA 1371
Cdd:PRK12467 1299 GerarqlaYWKAQlgGEQPVLELPTDRP---RPAVQSHRGaRLAFELPPALAEGLRALA 1354
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
75-1374 |
0e+00 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 655.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 75 RAQSIERAPAGTPAPLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCI--------- 145
Cdd:COG1020 5 AAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLrtragrpvq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 146 QGEDSVAAGGGAAVESADLRGRGQDEIDALVEGFRLRPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSL 225
Cdd:COG1020 85 VIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLL-----LLLLLLALHHIISDGLSD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 226 GLLTQDLSRAYRVECGLAAEPAPPLPCQYGDYARWQRDTL--DRLDASLRHHVEALSGAPHLHELPLDHERPAVLGQSGA 303
Cdd:COG1020 160 GLLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLqgEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 304 KLRLAFPPGLSERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDD 383
Cdd:COG1020 240 RVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 384 PDFASLVARCRDHQLAALEHQALPLERVIETLQVERSSRHAPLFQLMFALRHDADLALDLHGVQAHALTLPEDVAKHELT 463
Cdd:COG1020 320 PSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 464 LEVLVGAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENPHEPALSWPW-PADELAL-----DDKREPAPRTVGnV 537
Cdd:COG1020 400 LTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLlTAAERQQllaewNATAAPYPADAT-L 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 538 VDAIARAADEFPERAALETAQGRLSYRELLtaadaraaalrrrlgaqARS-----------------VALCLPRGLDWYC 600
Cdd:COG1020 479 HELFEAQAARTPDAVAVVFGDQSLTYAELN-----------------ARAnrlahhlralgvgpgdlVGVCLERSLEMVV 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 601 LLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQGLAGFAPSVA--IAVDELKLDGAGENGSGENAAPNQLAY 678
Cdd:COG1020 542 ALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGVpvLALDALALAAEPATNPPVPVTPDDLAY 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 679 ILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGAC-VVARPDELLEPQRFL 757
Cdd:COG1020 622 VIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATlVLAPPEARRDPAALA 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 758 AFLSERAITVTDLAPAYANELVRASVADdwrDLALRCLVVGGDVLPVALAQRWFELGLDRRcaLINAYGPTEATISSHYH 837
Cdd:COG1020 702 ELLARHRVTVLNLTPSLLRALLDAAPEA---LPSLRLVLVGGEALPPELVRRWRARLPGAR--LVNLYGPTETTVDSTYY 776
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 838 RVQAIDA-SRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGESlRMYRSG 916
Cdd:COG1020 777 EVTPPDAdGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGA-RLYRTG 855
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 917 DRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAAGVVGEGAAQRLVAWVECAGEDgfgqadlnqtd 996
Cdd:COG1020 856 DLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAG----------- 924
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 997 sDQTESERWHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRALPAPPVL-AQAERTPPRTAEESALCEVWAEVLQCEV 1075
Cdd:COG1020 925 -AAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAaAAAAAAPPAEEEEEEAALALLLLLVVVV 1003
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1076 GIHDSFFRLGGDSIRSLQVVARLRERGYAVTPKLMYQYQSAAELAPQLIALQAAPAEAAPLVGEVGLSPI------QRWF 1149
Cdd:COG1020 1004 GDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPplllslLALL 1083
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1150 FDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPAIQAQDWRGAADLDSR 1229
Cdd:COG1020 1084 LALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAA 1163
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1230 VDAAFARMQEATPLAGPLVALTHAHCDDGERLLICAHHLIVDAVSWRLLLGELfDGLAALARGEAWTPSARGASYADYVE 1309
Cdd:COG1020 1164 AAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL-LLLLLLLLAAAAAALLALALLLALLA 1242
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 1310 ALREADDAQRFDAGFWRELAAQPMQALPQDRPVALADARQSNVGRIVQTLDAGLTADLLERAGEA 1374
Cdd:COG1020 1243 LAALLALAALAALAAALLALALALLALALLLLALALLLPALARARAARTARALALLLLLALLLLL 1307
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
3533-4010 |
0e+00 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 580.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3533 PARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFIL 3612
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3613 EDSGVclsvsqralavelpgtALCLDDPftraqldavepgelpevptEAPAYLIYTSGSTGTPKGVVVTHRNVERLFtAA 3692
Cdd:cd17643 81 ADSGP----------------SLLLTDP-------------------DDLAYVIYTSGSTGRPKGVVVSHANVLALF-AA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3693 TQTGrFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAM 3772
Cdd:cd17643 125 TQRW-FGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAAD 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3773 RR-ELALNVRAVVFGGEALEPSRLQPWRERY--PQAELVNMYGITETTVHVSFHRLSDEDLQSPT-SRIGSALPDLAVHV 3848
Cdd:cd17643 204 RDgRDPLALRYVIFGGEALEAAMLRPWAGRFglDRPQLVNMYGITETTVHVTFRPLDAADLPAAAaSPIGRPLPGLRVYV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3849 LDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE----RGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGY 3924
Cdd:cd17643 284 LDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVAnpfgGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGF 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3925 RIEPGEIAAKIASLPQVSDAAVTV-EGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANG 4003
Cdd:cd17643 364 RIELGEIEAALATHPSVRDAAVIVrEDEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNG 443
|
....*..
gi 1246793773 4004 KLDRKAL 4010
Cdd:cd17643 444 KLDRAAL 450
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1583-2887 |
1.22e-178 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 590.68 E-value: 1.22e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1583 ALLAAREDARAIEHAFPLTPLQRGVLLESLRGDGADPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGLSV 1662
Cdd:COG1020 4 AAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1663 PHQIVLADAAAPWQTLDWSALDDAAQDAQLQRWLADDAAQgvDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPL 1742
Cdd:COG1020 84 QVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPF--DLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1743 LVGEMLQRYTAGAQGATLRLPPAPG-----FQAYLDWRERQDLARQRGWWRERLSGYAGTAALPAPVAAAHHPVQR-EEC 1816
Cdd:COG1020 162 LLAELLRLYLAAYAGAPLPLPPLPIqyadyALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRgARV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1817 ERRLSAHDSERLRAFCRERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPpeLAGVESMVGVFINTLPLRLRIDAG 1896
Cdd:COG1020 242 SFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRP--RPELEGLVGFFVNTLPLRVDLSGD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1897 QPALDLLSALRSQSLEVAENEAVGLGEILADSGLDADR----LFASLLVVENFPaMAPAQLPfALRVRETRAAN---HYA 1969
Cdd:COG1020 320 PSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLsrnpLFQVMFVLQNAP-ADELELP-GLTLEPLELDSgtaKFD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1970 LTLRVSER-ECVRLEALLDAARVDRAAVAAMLDLAVAGLLRLLQRPDCRVAEL--LGGDDAVQ------APQPQRASSAT 2040
Cdd:COG1020 398 LTLTVVETgDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLplLTAAERQQllaewnATAAPYPADAT 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2041 AQSLLWQMPAQ---AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLD 2117
Cdd:COG1020 478 LHELFEAQAARtpdAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLD 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2118 PQHPDARQIAVLDDSGARIVIGWGAAPAWVPA-SVRWLDAESvLDVVSAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVV 2196
Cdd:COG1020 558 PAYPAERLAYMLEDAGARLVLTQSALAARLPElGVPVLALDA-LALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVM 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2197 VSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVP 2276
Cdd:COG1020 637 VEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTP 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2277 SHLAGLLAAAGGtAVLPRECLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPEEWPVEQGVPVGHPLA 2356
Cdd:COG1020 717 SLLRALLDAAPE-ALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADGGSVPIGRPIA 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2357 GNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPL-APDRLLYRSGDLARLDGEGRIVYLGRGDHQ 2435
Cdd:COG1020 796 NTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQ 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2436 VKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQGSLEGVAE------ALAQRLPEYLCPSRWRAVESM 2509
Cdd:COG1020 876 VKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAaallrlALALLLPPYMVPAAVVLLLPL 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2510 PRLGNGKIDRQALADLlqqDDADSSAEAIDETPVNEVLRELWQKLLGREHIGAHDNFFALGGDSILSLQLVARARQAGLA 2589
Cdd:COG1020 956 PLTGNGKLDRLALPAP---AAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLL 1032
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2590 LMPRQLYDHPTLAGLSAQVQASSPAPATIkPATEAEQSFGLTPIQHWFFEQALDQPAHWNMSLYLKLPGALDTAAFAAAL 2669
Cdd:COG1020 1033 LLLLLLLFLAAAAAAAAAAAAAAAAAAAA-PLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLAL 1111
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2670 ADVAAAHPMLRARFQRDAAGQWQQtlgDWQADRFAHREADAGQREDLLAQWQAGLSFDGALLRVLALPDPQDGDTRVLFA 2749
Cdd:COG1020 1112 LLLLALLLALLAALRARRAVRQEG---PRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLL 1188
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2750 AHHLLVDAVSWGIIVDDLQHAYAERRAGRSPALAAEACGFGAWQAALRQLSAATLDGWRSYWRAQAADAEAIALPWQDSD 2829
Cdd:COG1020 1189 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLA 1268
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 2830 NRYADTVHLHDRFERDWTERLLTQTARAYGNEPQEVLLTALALALRDGGDAATLWVEM 2887
Cdd:COG1020 1269 LALLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLL 1326
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3082-4081 |
4.39e-176 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 614.48 E-value: 4.39e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3082 PLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFaVQGLPSPRQLPHRQVSLPLAEQ 3161
Cdd:PRK12467 1118 PLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTF-VQEDGRTRQVIHPVGSLTLEEP 1196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3162 --DWSGLEPAQARSRLsELQAQQCeagFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAALRE 3239
Cdd:PRK12467 1197 llLAADKDEAQLKVYV-EAEARQP---FDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQ 1272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3240 SRTPQLPAAP-PFRDYLHWLRGQDEAAAR----AFWREQLTGLEPA-ALP-EATEPAEG-YASSTRRFDLAAA-----SA 3306
Cdd:PRK12467 1273 GQSLQLPALPiQYADYAVWQRQWMDAGERarqlAYWKAQLGGEQPVlELPtDRPRPAVQsHRGARLAFELPPAlaeglRA 1352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3307 WAQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRppELAGVERMLGVFINSVPLRVTPAGEATPAPWLQALQQRN 3386
Cdd:PRK12467 1353 LARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANR--NRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAA 1430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3387 LDLRTHGYLPLAQIqragaADAVSP---------FDVLLVFENLPTESREERSGMRIEEL--DHRaHSNYPLMLTAIPDA 3455
Cdd:PRK12467 1431 LEAQAHQDLPFEQL-----VEALQPerslshsplFQVMFNHQRDDHQAQAQLPGLSVESLswESQ-TAQFDLTLDTYESS 1504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3456 GGLRIEAALDRSKLDGWLVEQMLDDLDFVLQQVPA--LQRFDALPLLPSQTRSA---AWTSRERYACTGNLV-SRFAEIA 3529
Cdd:PRK12467 1505 EGLQASLTYATDLFEASTIERLAGHWLNLLQGLVAdpERRLGELDLLDEAERRQileGWNATHTGYPLARLVhQLIEDQA 1584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3530 RRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRG 3609
Cdd:PRK12467 1585 AATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLA 1664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3610 FILEDSGVCLSVSQRALAVELPGT----ALCLDdpftraQLDAVEPGELPEVPTEAP-----AYLIYTSGSTGTPKGVVV 3680
Cdd:PRK12467 1665 YMIEDSGIELLLTQSHLQARLPLPdglrSLVLD------QEDDWLEGYSDSNPAVNLapqnlAYVIYTSGSTGRPKGAGN 1738
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3681 THRNVERLFTAATQtgRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQT 3760
Cdd:PRK12467 1739 RHGALVNRLCATQE--AYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFV 1816
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3761 PSAFYALQSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQ-SPTSRIGS 3839
Cdd:PRK12467 1817 PSMLQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCRRKDLEgRDSVPIGQ 1896
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3840 ALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFV----ERGGQRFYRSGDLGRYRADGSLEYRGRG 3915
Cdd:PRK12467 1897 PIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVadpfGTVGSRLYRTGDLARYRADGVIEYLGRI 1976
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3916 DDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEGAWLMAYAVAADGAEPDP--------QSLREALRALLPDYML 3987
Cdd:PRK12467 1977 DHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGANGKQLVAYVVPTDPGLVDDdeaqvalrAILKNHLKASLPEYMV 2056
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3988 PRLIQLLPALPLTANGKLDRKALPKPETQDRDEGVLESAS--ERRLAELWRQLLGGELPGRGAHFFARGGHSLLVVRLAE 4065
Cdd:PRK12467 2057 PAHLVFLARMPLTPNGKLDRKALPAPDASELQQAYVAPQSelEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVS 2136
|
1050
....*....|....*.
gi 1246793773 4066 AIRAEfAIAVPLKSLF 4081
Cdd:PRK12467 2137 RARQA-GIRFTPKDLF 2151
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
3533-4010 |
7.44e-173 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 540.19 E-value: 7.44e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3533 PARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFIL 3612
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3613 EDSGVclsvsqralavelpgtALCLDDPftraqldavepgelpevptEAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAA 3692
Cdd:cd05930 81 EDSGA----------------KLVLTDP-------------------DDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWM 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3693 TQtgRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAFYALqSQAM 3772
Cdd:cd05930 126 QE--AYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLL-LQEL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3773 RRELALNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQSPTSRIGSALPDLAVHVLDAA 3852
Cdd:cd05930 203 ELAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDEEDGRVPIGRPIPNTRVYVLDEN 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3853 GQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE---RGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPG 3929
Cdd:cd05930 283 LRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPnpfGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3930 EIAAKIASLPQVSDAAVTVEGQGEG-AWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRK 4008
Cdd:cd05930 363 EIEAALLAHPGVREAAVVAREDGDGeKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRK 442
|
..
gi 1246793773 4009 AL 4010
Cdd:cd05930 443 AL 444
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1582-2812 |
4.73e-164 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 574.80 E-value: 4.73e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1582 FALLAAREDARAIEhAFPLTPLQ-RGVLLESLRGDGAdPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGL 1660
Cdd:PRK12467 35 FANLPIPQVRSAFE-RIPLSYAQeRQWFLWQLDPDSA-AYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1661 SVpHQIVLADAAAPWQTLDWSALDDAAQDAQLQRWLADDAAQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWST 1740
Cdd:PRK12467 113 GF-RQVIDASLSLTIPLDDLANEQGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSM 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1741 PLLVGEMLQRYTAGAQGATLRLPPAPgfQAYLD-------WRERQDLARQRGWWRERLSGYAGTAALPAPVAAAHHPVQR 1813
Cdd:PRK12467 192 RVLVEELVQLYSAYSQGREPSLPALP--IQYADyaiwqrsWLEAGERERQLAYWQEQLGGEHTVLELPTDRPRPAVPSYR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1814 -EECERRLSAHDSERLRAFCRERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPPElaGVESMVGVFINTLPLRLR 1892
Cdd:PRK12467 270 gARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRV--ETERLIGFFVNTQVLKAE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1893 IDAGQPALDLLSALRSQSLEVAEN---------EAVGLGEILADSGL-------------DADRLFASL--LVVENFP-A 1947
Cdd:PRK12467 348 VDPQASFLELLQQVKRTALGAQAHqdlpfeqlvEALQPERSLSHSPLfqvmfnhqntatgGRDREGAQLpgLTVEELSwA 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1948 MAPAQLPFALRVRETRAANHYALTLRVSERECVRLEALldaarvdraavaamldlaVAGLLRLLQR----PDCRVAELLG 2023
Cdd:PRK12467 428 RHTAQFDLALDTYESAQGLWAAFTYATDLFEATTIERL------------------ATHWRNLLEAivaePRRRLGELPL 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2024 GDDAVQAPQPQR----ASSATAQSL--LWQMPAQ----AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCL 2093
Cdd:PRK12467 490 LDAEERARELVRwnapATEYAPDCVhqLIEAQARqhpeRPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAV 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2094 PRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGW--GAAPAWVPASVRWLDAESVLDVVSAY-EEPP 2170
Cdd:PRK12467 570 ERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQshLLAQLPVPAGLRSLCLDEPADLLCGYsGHNP 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2171 RVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLP 2250
Cdd:PRK12467 650 EVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLP 729
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2251 AELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPRECLVTGGEALTGALVQQVRALAPTLRIVNHYGPTET 2330
Cdd:PRK12467 730 PDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTET 809
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2331 TVGILTCTVPEEWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPD-R 2409
Cdd:PRK12467 810 TVGVSTYELSDEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGADgG 889
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2410 LLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI---------- 2479
Cdd:PRK12467 890 RLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVpaavadgaeh 969
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2480 QGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALAdllqQDDADSSAEAID--ETPVNEVLRELWQKLLGR 2557
Cdd:PRK12467 970 QATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALP----KPDASAVQATFVapQTELEKRLAAIWADVLKV 1045
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2558 EHIGAHDNFFALGGDSILSLQLVARARQA-GLALMPRQLYDHPTLAGLSAQVQASSPAPATIKPATEAEQSFGLTPIQ-- 2634
Cdd:PRK12467 1046 ERVGLTDNFFELGGHSLLATQVISRVRQRlGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDRDQPLPLSYAQer 1125
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2635 HWFFEQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARFqRDAAGQWQQTLGDWQADRFAHREADAG--- 2711
Cdd:PRK12467 1126 QWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTF-VQEDGRTRQVIHPVGSLTLEEPLLLAAdkd 1204
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2712 -QREDLLAQWQAGLSFD---GALLRVLALPDPQDGDTRVLfAAHHLLVDAVSWGIIVDDLQHAYAERRAGRS---PALAA 2784
Cdd:PRK12467 1205 eAQLKVYVEAEARQPFDleqGPLLRVGLLRLAADEHVLVL-TLHHIVSDGWSMQVLVDELVALYAAYSQGQSlqlPALPI 1283
|
1290 1300
....*....|....*....|....*....
gi 1246793773 2785 EACGFGAWQaalRQ-LSAATLDGWRSYWR 2812
Cdd:PRK12467 1284 QYADYAVWQ---RQwMDAGERARQLAYWK 1309
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
3082-4085 |
9.66e-154 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 516.13 E-value: 9.66e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3082 PLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFaVQGLPSPRQLPHRQVSLPLAE- 3160
Cdd:PRK10252 9 PLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRF-TEDNGEVWQWVDPALTFPLPEi 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3161 QDWSGlEPAQARSRLSELQAqqceagfDLAAP-------PLMRLALLRrSADEHWLVWTR-HHLIVDGWSSALLLDEVWR 3232
Cdd:PRK10252 88 IDLRT-QPDPHAAAQALMQA-------DLQQDlrvdsgkPLVFHQLIQ-LGDNRWYWYQRyHHLLVDGFSFPAITRRIAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3233 LYAALRESRTPQLPAAPPFRD----YLHWLRGQDEAAARAFWREQLTGL-EPAALpeATEPAEGYASSTR------RFDL 3301
Cdd:PRK10252 159 IYCAWLRGEPTPASPFTPFADvveeYQRYRASEAWQRDAAFWAEQRRQLpPPASL--SPAPLPGRSASADilrlklEFTD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3302 AAASAW-AQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRPPELAGveRMLGVFINSVPLRVTPAGEATPAPWLQ 3380
Cdd:PRK10252 237 GAFRQLaAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAAL--TATGPVLNVLPLRVHIAAQETLPELAT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3381 ALQQRNLDLRTHGYLPLAQIQR-----AGAADAVSPFDVLLVFENLPtesreersgmRIEELDHRAH--SNYP---LMLT 3450
Cdd:PRK10252 315 RLAAQLKKMRRHQRYDAEQIVRdsgraAGDEPLFGPVLNIKVFDYQL----------DFPGVQAQTHtlATGPvndLELA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3451 AIPD-AGGLRIEAALDRSKLDGWLVEQMLDDLDFVLQQ---VPALQRFDALPLLPSQTRSAAWTSRERYAC-TGNLVSRF 3525
Cdd:PRK10252 385 LFPDeHGGLSIEILANPQRYDEATLIAHAERLKALIAQfaaDPALLCGDVDILLPGEYAQLAQVNATAVEIpETTLSALV 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3526 AEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPA 3605
Cdd:PRK10252 465 AQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPD 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3606 ARRGFILEDSGVCLSVSQRALAVELPG----TALCLDDPFTRAQldaVEPGELPEvpTEAPAYLIYTSGSTGTPKGVVVT 3681
Cdd:PRK10252 545 DRLKMMLEDARPSLLITTADQLPRFADvpdlTSLCYNAPLAPQG---AAPLQLSQ--PHHTAYIIFTSGSTGRPKGVMVG 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3682 HRN-VERLFTAATQTGrfsFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQT 3760
Cdd:PRK10252 620 QTAiVNRLLWMQNHYP---LTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFV 696
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3761 PS---AFYALQSQAMRRELALNVRAVVFGGEALEPSRLQPWrERYPQAELVNMYGITETTVHVSFHRLSDEDLQSPTSR- 3836
Cdd:PRK10252 697 PSmlaAFVASLTPEGARQSCASLRQVFCSGEALPADLCREW-QQLTGAPLHNLYGPTEAAVDVSWYPAFGEELAAVRGSs 775
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3837 --IGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE---RGGQRFYRSGDLGRYRADGSLEY 3911
Cdd:PRK10252 776 vpIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIAdpfAPGERMYRTGDVARWLDDGAVEY 855
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3912 RGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAV-------TVEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPD 3984
Cdd:PRK10252 856 LGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVThacvinqAAATGGDARQLVGYLVSQSGLPLDTSALQAQLRERLPP 935
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3985 YMLPRLIQLLPALPLTANGKLDRKALPKPETQDRDEG-VLESASERRLAELWRQLLGGELPGRGAHFFARGGHSLLVVRL 4063
Cdd:PRK10252 936 HMVPVVLLQLDQLPLSANGKLDRKALPLPELKAQVPGrAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKL 1015
|
1050 1060
....*....|....*....|..
gi 1246793773 4064 AEAIRAEFAIAVPLKSLFEQPR 4085
Cdd:PRK10252 1016 AAQLSRQFARQVTPGQVMVAST 1037
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
3524-4010 |
1.07e-149 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 475.54 E-value: 1.07e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3524 RFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHA 3603
Cdd:cd12117 2 LFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3604 PAARRGFILEDSGVCLSVSQRALAVELPGTALCLDdpfTRAQLDAVEPGELPEVPT-EAPAYLIYTSGSTGTPKGVVVTH 3682
Cdd:cd12117 82 PAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVV---IDEALDAGPAGNPAVPVSpDDLAYVMYTSGSTGRPKGVAVTH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3683 RNVERLftaATQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPS 3762
Cdd:cd12117 159 RGVVRL---VKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3763 AFYAL---QSQAMRrelalNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQSPTSRIGS 3839
Cdd:cd12117 236 LFNQLadeDPECFA-----GLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAGSIPIGR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3840 ALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE---RGGQRFYRSGDLGRYRADGSLEYRGRGD 3916
Cdd:cd12117 311 PIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVAdpfGPGERLYRTGDLARWLPDGRLEFLGRID 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3917 DQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEG-AWLMAYAVAAdgAEPDPQSLREALRALLPDYMLPRLIQLLP 3995
Cdd:cd12117 391 DQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGdKRLVAYVVAE--GALDAAELRAFLRERLPAYMVPAAFVVLD 468
|
490
....*....|....*
gi 1246793773 3996 ALPLTANGKLDRKAL 4010
Cdd:cd12117 469 ELPLTANGKVDRRAL 483
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
3082-4082 |
1.16e-146 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 517.80 E-value: 1.16e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3082 PLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFAVQ-GLPSPRQLPhrQVSLPLAE 3160
Cdd:PRK05691 677 PQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERdGVALQRIDA--QGEFALQR 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3161 QDWSGLEPAQARSRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAALRES 3240
Cdd:PRK05691 755 IDLSDLPEAEREARAAQIREEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQG 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3241 RTPQLPAAP-PFRDYLHWLR---GQDEAAA-RAFWREQLtGLEPAALPEATE-PAEGY-ASSTRRFDL-------AAASA 3306
Cdd:PRK05691 835 QTAELAPLPlGYADYGAWQRqwlAQGEAARqLAYWKAQL-GDEQPVLELATDhPRSARqAHSAARYSLrvdaslsEALRG 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3307 WAQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRP-PELAGverMLGVFINSVPLRVTPAGEATPAPWLQALQQR 3385
Cdd:PRK05691 914 LAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPrLETQG---LVGFFINTQVLRAQLDGRLPFTALLAQVRQA 990
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3386 NLDLRTHGYLPLAQIQRA-GAADAVSPFDVLLVFENLPTESREERSGMRIEELD-HRAHSNYPLMLTAIPDAGGlRIEAA 3463
Cdd:PRK05691 991 TLGAQAHQDLPFEQLVEAlPQAREQGLFQVMFNHQQRDLSALRRLPGLLAEELPwHSREAKFDLQLHSEEDRNG-RLTLS 1069
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3464 LDRSK--LDGWLVEQMLDDLDFVLQQV---PALQRFDaLPLL--PSQTRSAAWTSRERYACTGNLVSRFAEIARRYPARI 3536
Cdd:PRK05691 1070 FDYAAelFDAATIERLAEHFLALLEQVcedPQRALGD-VQLLdaAERAQLAQWGQAPCAPAQAWLPELLNEQARQTPERI 1148
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3537 AVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSG 3616
Cdd:PRK05691 1149 ALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSG 1228
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3617 VCLSVSQRALAVELPG----TALCLDdpftraQLdavepgELPEVPTEAP---------AYLIYTSGSTGTPKGVVVTHR 3683
Cdd:PRK05691 1229 VELLLTQSHLLERLPQaegvSAIALD------SL------HLDSWPSQAPglhlhgdnlAYVIYTSGSTGQPKGVGNTHA 1296
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3684 N-VERL-FTAATqtgrFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTP 3761
Cdd:PRK05691 1297 AlAERLqWMQAT----YALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVP 1372
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3762 SafyaLQSQAMRRELALN---VRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDED-LQSPtsrI 3837
Cdd:PRK05691 1373 P----LLQLFIDEPLAAActsLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVTHWQCQAEDgERSP---I 1445
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3838 GSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE----RGGQRFYRSGDLGRYRADGSLEYRG 3913
Cdd:PRK05691 1446 GRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPdplgEDGARLYRTGDRARWNADGALEYLG 1525
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3914 RGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQL 3993
Cdd:PRK05691 1526 RLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIR 1605
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3994 LPALPLTANGKLDRKALPKPETQDRDEGVLESASERRLAELWRQLLGgeLPGRGAH--FFARGGHSLLVVRLAEAIRAEF 4071
Cdd:PRK05691 1606 LDQMPLGPSGKLDRRALPEPVWQQREHVEPRTELQQQIAAIWREVLG--LPRVGLRddFFALGGHSLLATQIVSRTRQAC 1683
|
1050
....*....|.
gi 1246793773 4072 AIAVPLKSLFE 4082
Cdd:PRK05691 1684 DVELPLRALFE 1694
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
68-1341 |
1.36e-143 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 507.78 E-value: 1.36e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 68 QTQDADWRAQSIERAPAGTPAPLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQG 147
Cdd:PRK05691 656 QLAGGGAAQAAIARLPRGQALPQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYE 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 148 EDSVA-----AGGGAAVESADLRGRGQDEIDALVEGFR----LRPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHI 218
Cdd:PRK05691 736 RDGVAlqridAQGEFALQRIDLSDLPEAEREARAAQIReeeaRQPFDLEKGPLLRVTLVRLDDE-----EHQLLVTLHHI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 219 ACDGVSLGLLTQDLSRAYRVECGLAAEPAPPLPCQYGDYARWQRDTLD--RLDASLRHHVEALSGAPHLHELPLDHERPA 296
Cdd:PRK05691 811 VADGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGAWQRQWLAqgEAARQLAYWKAQLGDEQPVLELATDHPRSA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 297 VLGQSGAKLRLAFPPGLSERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVL 376
Cdd:PRK05691 891 RQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVL 970
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 377 RTQLHDDPDFASLVARCRDHQLAALEHQALPLERVIETLQVERSSrhaPLFQLMFALRH-DADLALDLHGVQAHALTLPE 455
Cdd:PRK05691 971 RAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAREQ---GLFQVMFNHQQrDLSALRRLPGLLAEELPWHS 1047
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 456 DVAKHELTLEVLVGAGG-MSAVWEYNTALWNPATVARWAERYFVALAAMLENPhEPALSwpwpadELALDDKRE------ 528
Cdd:PRK05691 1048 REAKFDLQLHSEEDRNGrLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDP-QRALG------DVQLLDAAEraqlaq 1120
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 529 ----PAPRTVGNVVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLG 604
Cdd:PRK05691 1121 wgqaPCAPAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLA 1200
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 605 AWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQGLAGFaPSV----AIAVDELKLDGAGENGSGENAAPNQLAYIL 680
Cdd:PRK05691 1201 ILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERL-PQAegvsAIALDSLHLDSWPSQAPGLHLHGDNLAYVI 1279
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 681 YTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGA-CVVARPDELLEPQRFLAF 759
Cdd:PRK05691 1280 YTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCrLVLAGPGEHRDPQRIAEL 1359
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 760 LSERAITVTDLAPAYANELVRASVADDWRdlALRCLVVGGDVLPVALAQRwfELGLDRRCALINAYGPTEATISSHYHRV 839
Cdd:PRK05691 1360 VQQYGVTTLHFVPPLLQLFIDEPLAAACT--SLRRLFSGGEALPAELRNR--VLQRLPQVQLHNRYGPTETAINVTHWQC 1435
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 840 QAIDASRpVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPlrLPSGES-LRMYRSGDR 918
Cdd:PRK05691 1436 QAEDGER-SPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVP--DPLGEDgARLYRTGDR 1512
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 919 VRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAAGVVGEGAAQRLVAWvecagedgfgqadLNQTDSD 998
Cdd:PRK05691 1513 ARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGY-------------YTGEAGQ 1579
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 999 QTESERWHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRALPApPVLAQAERTPPRTAEESALCEVWAEVL-QCEVGI 1077
Cdd:PRK05691 1580 EAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPE-PVWQQREHVEPRTELQQQIAAIWREVLgLPRVGL 1658
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1078 HDSFFRLGGDSIRSLQVVARLRERGYAVTP-KLMYQYQSAAELAPQLIALQAAPAEAAPLVGE-------VGLSPIQR-- 1147
Cdd:PRK05691 1659 RDDFFALGGHSLLATQIVSRTRQACDVELPlRALFEASELGAFAEQVARIQAAGERNSQGAIArvdrsqpVPLSYSQQrm 1738
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1148 WFFDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGpAPAIQAQDWRG-AADL 1226
Cdd:PRK05691 1739 WFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDS-GLRMDWQDFSAlPADA 1817
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1227 DSRVDAAFARMQEATPL---AGPLVALTHAHCDDGERLLICAHHLIVDAvSWRL-----LLGELFDGLAAlARGEAWTPS 1298
Cdd:PRK05691 1818 RQQRLQQLADSEAHQPFdleRGPLLRACLVKAAEREHYFVLTLHHIVTE-GWAMdifarELGALYEAFLD-DRESPLEPL 1895
|
1290 1300 1310 1320
....*....|....*....|....*....|....*....|....*...
gi 1246793773 1299 ArgASYADYVEALR---EADDAQRfDAGFWRELAA--QPMQALPQDRP 1341
Cdd:PRK05691 1896 P--VQYLDYSVWQRqwlESGERQR-QLDYWKAQLGneHPLLELPADRP 1940
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
3547-3946 |
1.44e-143 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 454.80 E-value: 1.44e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3547 YATLDRRSSQLATLLI-RQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVCLSVSQRA 3625
Cdd:TIGR01733 2 YRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3626 LAVELPGTALC--LDDPFTRAQLDAVEPGELPEVPTEA--PAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQtgRFSFD 3701
Cdd:TIGR01733 82 LASRLAGLVLPviLLDPLELAALDDAPAPPPPDAPSGPddLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLAR--RYGLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3702 EHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFL-DLLAEYGVTVLNQTPSAFYALQSQAmrRELALNV 3780
Cdd:TIGR01733 160 PDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLaALIAEHPVTVLNLTPSLLALLAAAL--PPALASL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3781 RAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQSPTSR-IGSALPDLAVHVLDAAGQPVPLG 3859
Cdd:TIGR01733 238 RLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRESPVpIGRPLANTRLYVLDDDLRPVPVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3860 VVGELVVEGDGVAQGYWQRPELTAERFVE-----RGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAK 3934
Cdd:TIGR01733 318 VVGELYIGGPGVARGYLNRPELTAERFVPdpfagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAA 397
|
410
....*....|..
gi 1246793773 3935 IASLPQVSDAAV 3946
Cdd:TIGR01733 398 LLRHPGVREAVV 409
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
3525-4010 |
2.27e-138 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 443.26 E-value: 2.27e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAP 3604
Cdd:cd17646 4 VAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3605 AARRGFILEDSGVCLSVSQRALAVELPGTAlclDDPFTRAQLDAVEPGELPEVPTE--APAYLIYTSGSTGTPKGVVVTH 3682
Cdd:cd17646 84 ADRLAYMLADAGPAVVLTTADLAARLPAGG---DVALLGDEALAAPPATPPLVPPRpdNLAYVIYTSGSTGRPKGVMVTH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3683 RN-VERLftaATQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTP 3761
Cdd:cd17646 161 AGiVNRL---LWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3762 SAFYALqSQAMRRELALNVRAVVFGGEALEPSRLQPWRERyPQAELVNMYGITETTVHVSFHRLSDEDLQSPTSrIGSAL 3841
Cdd:cd17646 238 SMLRVF-LAEPAAGSCASLRRVFCSGEALPPELAARFLAL-PGAELHNLYGPTEAAIDVTHWPVRGPAETPSVP-IGRPV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3842 PDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE---RGGQRFYRSGDLGRYRADGSLEYRGRGDDQ 3918
Cdd:cd17646 315 PNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPdpfGPGSRMYRTGDLARWRPDGALEFLGRSDDQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3919 VKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEGA-WLMAYAVAADGAE-PDPQSLREALRALLPDYMLPRLIQLLPA 3996
Cdd:cd17646 395 VKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAaRLVGYVVPAAGAAgPDTAALRAHLAERLPEYMVPAAFVVLDA 474
|
490
....*....|....
gi 1246793773 3997 LPLTANGKLDRKAL 4010
Cdd:cd17646 475 LPLTANGKLDRAAL 488
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
2050-2522 |
9.91e-138 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 439.27 E-value: 9.91e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2050 AQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVL 2129
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 DDSGARIVIgwgaapawvpasvrwldaesvldvvsayeepprvdVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGV 2209
Cdd:cd05930 81 EDSGAKLVL-----------------------------------TDPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWM 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2210 LPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGT 2289
Cdd:cd05930 126 QEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2290 AVLPRECLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPEEWPVEQGVPVGHPLAGNEAWVLDRFGLP 2369
Cdd:cd05930 206 ALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDEEDGRVPIGRPIPNTRVYVLDENLRP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2370 APVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVE 2449
Cdd:cd05930 286 VPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIE 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 2450 QVLAQLPGVEVAAVLALPGANGVLQLGACIQG------SLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:cd05930 366 AALLAHPGVREAAVVAREDGDGEKRLVAYVVPdeggelDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
3080-3488 |
9.93e-137 |
|
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380465 [Multi-domain] Cd Length: 423 Bit Score: 435.48 E-value: 9.93e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3080 VYPLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFAVQGLPSPRQLPHRQVSLPLA 3159
Cdd:cd19543 1 IYPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDRKLPWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3160 EQDWSGLEPAQARSRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAALRE 3239
Cdd:cd19543 81 ELDLSHLSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3240 SRTPQLPAAPPFRDYLHWLRGQDEAAARAFWREQLTGLE-PAALPEAT--EPAEGYASSTRRFDLAAA-----SAWAQSH 3311
Cdd:cd19543 161 GQPPSLPPVRPYRDYIAWLQRQDKEAAEAYWREYLAGFEePTPLPKELpaDADGSYEPGEVSFELSAEltarlQELARQH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3312 GLTASSLLQGALALVLQRYYGRDDFALGITIAGRPPELAGVERMLGVFINSVPLRVTPAGEATPAPWLQALQQRNLDLRT 3391
Cdd:cd19543 241 GVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQLELRE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3392 HGYLPLAQIQRAgAADAVSPFDVLLVFENLPT----ESREERSGMRIEELDHRAHSNYPLMLTAIPDaGGLRIEAALDRS 3467
Cdd:cd19543 321 HEYVPLYEIQAW-SEGKQALFDHLLVFENYPVdeslEEEQDEDGLRITDVSAEEQTNYPLTVVAIPG-EELTIKLSYDAE 398
|
410 420
....*....|....*....|.
gi 1246793773 3468 KLDGWLVEQMLDDLDFVLQQV 3488
Cdd:cd19543 399 VFDEATIERLLGHLRRVLEQV 419
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
3533-4010 |
1.15e-134 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 431.72 E-value: 1.15e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3533 PARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFIL 3612
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3613 EDSGVCLSVSQRALAVELPGTALCLDDPFTRAQLDAVEPGelPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAA 3692
Cdd:cd12116 81 EDAEPALVLTDDALPDRLPAGLPVLLLALAAAAAAPAAPR--TPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3693 TQtgRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPsAFYALQSQAM 3772
Cdd:cd12116 159 RE--RLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATP-ATWRMLLDAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3773 RRELAlNVRAVVfGGEALEPSRLQPWRERypQAELVNMYGITETTVHVSFHRLSDEDLQSPtsrIGSALPDLAVHVLDAA 3852
Cdd:cd12116 236 WQGRA-GLTALC-GGEALPPDLAARLLSR--VGSLWNLYGPTETTIWSTAARVTAAAGPIP---IGRPLANTQVYVLDAA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3853 GQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE----RGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEP 3928
Cdd:cd12116 309 LRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPdpfaGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIEL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3929 GEIAAKIASLPQVSDAAVTVEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRK 4008
Cdd:cd12116 389 GEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRK 468
|
..
gi 1246793773 4009 AL 4010
Cdd:cd12116 469 AL 470
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
3533-4011 |
3.41e-134 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 428.98 E-value: 3.41e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3533 PARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFIL 3612
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3613 EDSGVCLSVSQralavelpgtalclddpftraqldavepgelpevpTEAPAYLIYTSGSTGTPKGVVVTHRNVERLftAA 3692
Cdd:cd17652 81 ADARPALLLTT-----------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANL--AA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3693 TQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAM 3772
Cdd:cd17652 124 AQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPDDL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3773 rrelaLNVRAVVFGGEALEPSRLQPWReryPQAELVNMYGITETTVHVSFHRLsDEDLQSPTsrIGSALPDLAVHVLDAA 3852
Cdd:cd17652 204 -----PDLRTLVVAGEACPAELVDRWA---PGRRMINAYGPTETTVCATMAGP-LPGGGVPP--IGRPVPGTRVYVLDAR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3853 GQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE----RGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEP 3928
Cdd:cd17652 273 LRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVAdpfgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIEL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3929 GEIAAKIASLPQVSDAAVTVEGQGEG-AWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDR 4007
Cdd:cd17652 353 GEVEAALTEHPGVAEAVVVVRDDRPGdKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDR 432
|
....
gi 1246793773 4008 KALP 4011
Cdd:cd17652 433 RALP 436
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
3525-4011 |
7.11e-134 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 430.23 E-value: 7.11e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAP 3604
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3605 AARRGFILEDSGVCLSVSQRALAVELPGTA---LCLDDPFTRAQLDAVepgelPEVPTEA--PAYLIYTSGSTGTPKGVV 3679
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGELAVELvavTLLDQPGAAAGADAE-----PDPALDAddLAYVIYTSGSTGRPKGVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3680 VTHRNVERLftAATQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQ 3759
Cdd:cd17651 156 MPHRSLANL--VAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3760 TPSAFYALQSQAMRRELAL-NVRAVVFGGEALEP-SRLQPWRERYPQAELVNMYGITETTVhVSFHRLSDEDLQSP-TSR 3836
Cdd:cd17651 234 PTVALRALAEHGRPLGVRLaALRYLLTGGEQLVLtEDLREFCAGLPGLRLHNHYGPTETHV-VTALSLPGDPAAWPaPPP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3837 IGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE---RGGQRFYRSGDLGRYRADGSLEYRG 3913
Cdd:cd17651 313 IGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPdpfVPGARMYRTGDLARWLPDGELEFLG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3914 RGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTV-EGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQ 3992
Cdd:cd17651 393 RADDQVKIRGFRIELGEIEAALARHPGVREAVVLArEDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFV 472
|
490
....*....|....*....
gi 1246793773 3993 LLPALPLTANGKLDRKALP 4011
Cdd:cd17651 473 LLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
549-1041 |
8.79e-128 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 410.77 E-value: 8.79e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 549 PERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVV 628
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 629 AASGCDAVLTDaqglagfapsvaiavdelkldgagengsgenaaPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAE 708
Cdd:cd05930 81 EDSGAKLVLTD---------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 709 ALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARPDEL-LEPQRFLAFLSERAITVTDLAPAYANELVRAsvADDW 787
Cdd:cd05930 128 AYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVrKDPEALADLLAEEGITVLHLTPSLLRLLLQE--LELA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 788 RDLALRCLVVGGDVLPVALAQRWFELGldRRCALINAYGPTEATISSHYHRVQA-IDASRPVPLGQLLPGRIAAVLDAHG 866
Cdd:cd05930 206 ALPSLRLVLVGGEALPPDLVRRWRELL--PGARLVNLYGPTEATVDATYYRVPPdDEEDGRVPIGRPIPNTRVYVLDENL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 867 RIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGEslRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIEL 946
Cdd:cd05930 284 RPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGE--RMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIEL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 947 EEIEHCLGQLPQVRAAAAGVVGEGAA-QRLVAWVECAGEDGFGQADLNQtdsdqteserwhrALCERLPAYMVPTQFVAL 1025
Cdd:cd05930 362 GEIEAALLAHPGVREAAVVAREDGDGeKRLVAYVVPDEGGELDEEELRA-------------HLAERLPDYMVPSAFVVL 428
|
490
....*....|....*.
gi 1246793773 1026 PRLPRNASGKIDRRAL 1041
Cdd:cd05930 429 DALPLTPNGKVDRKAL 444
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
87-507 |
6.40e-127 |
|
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380454 [Multi-domain] Cd Length: 427 Bit Score: 407.51 E-value: 6.40e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 87 PAPLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQGED-----SVAAGGGAAVES 161
Cdd:cd19531 1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDgepvqVILPPLPLPLPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 162 ADLRGRG----QDEIDALVEGFRLRPFELQRQRPLRMQLLRLdgqgdGPVRHWLQVVVHHIACDGVSLGLLTQDLSRAYR 237
Cdd:cd19531 81 VDLSGLPeaerEAEAQRLAREEARRPFDLARGPLLRATLLRL-----GEDEHVLLLTMHHIVSDGWSMGVLLRELAALYA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 238 VECGLAAEPAPPLPCQYGDYARWQRDTL--DRLDASLRHHVEALSGAPHLHELPLDHERPAVLGQSGAKLRLAFPPGLSE 315
Cdd:cd19531 156 AFLAGRPSPLPPLPIQYADYAVWQREWLqgEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 316 RVAAYAQASRAT-------AFHVLQAafaallaRCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDDPDFAS 388
Cdd:cd19531 236 ALRALARREGATlfmtllaAFQVLLH-------RYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 389 LVARCRDHQLAALEHQALPLERVIETLQVERSSRHAPLFQLMFALRHDADLALDLHGVQAHALTLPEDVAKHELTLEVLV 468
Cdd:cd19531 309 LLARVRETALEAYAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTE 388
|
410 420 430
....*....|....*....|....*....|....*....
gi 1246793773 469 GAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENP 507
Cdd:cd19531 389 TDGGLRGSLEYNTDLFDAATIERMAGHFQTLLEAIVADP 427
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
3525-4010 |
1.29e-126 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 407.47 E-value: 1.29e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAP 3604
Cdd:cd12115 5 VEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3605 AARRGFILEDSGVCLSVSQRAlavelpgtalclddpftraqldavepgelpevpteAPAYLIYTSGSTGTPKGVVVTHRN 3684
Cdd:cd12115 85 PERLRFILEDAQARLVLTDPD-----------------------------------DLAYVIYTSGSTGRPKGVAIEHRN 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3685 -VERLFTAATQtgrFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVcrqpdAFLDLLAEYGVTVLNQTPSA 3763
Cdd:cd12115 130 aAAFLQWAAAA---FSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLADNVL-----ALPDLPAAAEVTLINTVPSA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3764 FYALQSQamrRELALNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQSPTsrIGSALPD 3843
Cdd:cd12115 202 AAELLRH---DALPASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPGASGEVS--IGRPLAN 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3844 LAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFV---ERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVK 3920
Cdd:cd12115 277 TQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLpdpFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVK 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3921 LRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEGA-WLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPL 3999
Cdd:cd12115 357 VRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGErRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPL 436
|
490
....*....|.
gi 1246793773 4000 TANGKLDRKAL 4010
Cdd:cd12115 437 TPNGKIDRSAL 447
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
3524-4014 |
3.17e-124 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 402.48 E-value: 3.17e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3524 RFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHA 3603
Cdd:cd17655 2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3604 PAARRGFILEDSGVCLSVSQRALAVELPGTALCLDDPFTRAQLDAVEPGELPEVPTEApAYLIYTSGSTGTPKGVVVTHR 3683
Cdd:cd17655 82 PEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDDL-AYVIYTSGSTGKPKGVMIEHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3684 NVERLFTAATQtgRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSA 3763
Cdd:cd17655 161 GVVNLVEWANK--VIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3764 FYALqsQAMRRELALNVRAVVFGGEALEPSRLQPWRERY-PQAELVNMYGITETTVHVSFHRLSDEDLQSPTSRIGSALP 3842
Cdd:cd17655 239 LKLL--DAADDSEGLSLKHLIVGGEALSTELAKKIIELFgTNPTITNAYGPTETTVDASIYQYEPETDQQVSVPIGKPLG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3843 DLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE---RGGQRFYRSGDLGRYRADGSLEYRGRGDDQV 3919
Cdd:cd17655 317 NTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDdpfVPGERMYRTGDLARWLPDGNIEFLGRIDHQV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3920 KLRGYRIEPGEIAAKIASLPQVSDAAVTV-EGQGEGAWLMAYAVAADgaEPDPQSLREALRALLPDYMLPRLIQLLPALP 3998
Cdd:cd17655 397 KIRGYRIELGEIEARLLQHPDIKEAVVIArKDEQGQNYLCAYIVSEK--ELPVAQLREFLARELPDYMIPSYFIKLDEIP 474
|
490
....*....|....*.
gi 1246793773 3999 LTANGKLDRKALPKPE 4014
Cdd:cd17655 475 LTPNGKVDRKALPEPD 490
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
3533-4011 |
3.18e-119 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 386.34 E-value: 3.18e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3533 PARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFIL 3612
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3613 EDSGVCLSVSQRAlavelpgtalclddpftraqldavepgelpevptEAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAA 3692
Cdd:cd17649 81 EDSGAGLLLTHHP----------------------------------RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQAT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3693 TqtGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAFY--ALQSQ 3770
Cdd:cd17649 127 A--ERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQqlAEEAD 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3771 AMRRELALNVRAVVFGGEALEPSRLQPWReryPQAE-LVNMYGITETTVHVS-FHRLSDEDLQSPTSRIGSALPDLAVHV 3848
Cdd:cd17649 205 RTGDGRPPSLRLYIFGGEALSPELLRRWL---KAPVrLFNAYGPTEATVTPLvWKCEAGAARAGASMPIGRPLGGRSAYI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3849 LDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVER----GGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGY 3924
Cdd:cd17649 282 LDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDpfgaPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGF 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3925 RIEPGEIAAKIASLPQVSDAAVTVEGQGEGAWLMAYAVAADGAEP--DPQSLREALRALLPDYMLPRLIQLLPALPLTAN 4002
Cdd:cd17649 362 RIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAAAQpeLRAQLRTALRASLPDYMVPAHLVFLARLPLTPN 441
|
....*....
gi 1246793773 4003 GKLDRKALP 4011
Cdd:cd17649 442 GKLDRKALP 450
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
3533-4010 |
1.99e-118 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 385.09 E-value: 1.99e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3533 PARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFIL 3612
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3613 EDSGVCLSVSQRALAVELPGTalclDDPFTRAQLDAVEPGELPEVPTE--APAYLIYTSGSTGTPKGVVVTHRNVerLFT 3690
Cdd:cd12114 81 ADAGARLVLTDGPDAQLDVAV----FDVLILDLDALAAPAPPPPVDVApdDLAYVIFTSGSTGTPKGVMISHRAA--LNT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3691 AATQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAF-----Y 3765
Cdd:cd12114 155 ILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLemlldV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3766 ALQSQAMRRELalnvRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQSPTSRIGSALPDLA 3845
Cdd:cd12114 235 LEAAQALLPSL----RLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEVPPDWRSIPYGRPLANQR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3846 VHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERG-GQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGY 3924
Cdd:cd12114 311 YRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHPdGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3925 RIEPGEIAAKIASLPQVSDAAVTVEGQGEGAWLMAYAVA-ADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANG 4003
Cdd:cd12114 391 RIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPdNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANG 470
|
....*..
gi 1246793773 4004 KLDRKAL 4010
Cdd:cd12114 471 KVDRAAL 477
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
2051-2522 |
2.77e-116 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 379.24 E-value: 2.77e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLD 2130
Cdd:cd12117 12 DAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2131 DSGARIVIGWGAAPAWVPASVRWLDAESVLDVVSAyeEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVl 2210
Cdd:cd12117 92 DAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPA--GNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNT- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2211 PVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIvpshlagllaaaggTA 2290
Cdd:cd12117 169 NYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWL--------------TA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2291 VLPRE-------------CLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPEEWPVEQGVPVGHPLAG 2357
Cdd:cd12117 235 ALFNQladedpecfaglrELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAGSIPIGRPIAN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2358 NEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVK 2437
Cdd:cd12117 315 TRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2438 IRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI----QGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLG 2513
Cdd:cd12117 395 IRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVvaegALDAAELRAFLRERLPAYMVPAAFVVLDELPLTA 474
|
....*....
gi 1246793773 2514 NGKIDRQAL 2522
Cdd:cd12117 475 NGKVDRRAL 483
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
3529-4010 |
5.19e-116 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 376.97 E-value: 5.19e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARr 3608
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAER- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3609 gfiledsgvclsvsqralavelpgtalclddpfTRAQLDAVEPGELPEVPTEaPAYLIYTSGSTGTPKGVVVTHRNVErL 3688
Cdd:cd05945 80 ---------------------------------IREILDAAKPALLIADGDD-NAYIIFTSGSTGRPKGVQISHDNLV-S 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3689 FTAATqTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPS-AFYAL 3767
Cdd:cd05945 125 FTNWM-LSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSfAAMCL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3768 QSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDL-QSPTSRIGSALPDLAV 3846
Cdd:cd05945 204 LSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIEVTPEVLdGYDRLPIGYAKPGAKL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3847 HVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRI 3926
Cdd:cd05945 284 VILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRI 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3927 EPGEIAAKIASLPQVSDAAVTVEGQGEGA-WLMAYAVAADGAE-PDPQSLREALRALLPDYMLPRLIQLLPALPLTANGK 4004
Cdd:cd05945 364 ELEEIEAALRQVPGVKEAVVVPKYKGEKVtELIAFVVPKPGAEaGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGK 443
|
....*.
gi 1246793773 4005 LDRKAL 4010
Cdd:cd05945 444 IDRKAL 449
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
3525-4011 |
8.09e-115 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 374.46 E-value: 8.09e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAP 3604
Cdd:cd17644 6 FEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3605 AARRGFILEDSGVCLSVSQralavelpgtalclddpftraqldavePGELpevpteapAYLIYTSGSTGTPKGVVVTHRN 3684
Cdd:cd17644 86 QERLTYILEDAQISVLLTQ---------------------------PENL--------AYVIYTSGSTGKPKGVMIEHQS 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3685 VERLFTAATQTgrFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAF 3764
Cdd:cd17644 131 LVNLSHGLIKE--YGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAYW 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3765 YALQSQAMRRELAL--NVRAVVFGGEALEPSRLQPWRE-RYPQAELVNMYGITETTVHVSFHRLSDEDLQSPTS-RIGSA 3840
Cdd:cd17644 209 HLLVLELLLSTIDLpsSLRLVIVGGEAVQPELVRQWQKnVGNFIQLINVYGPTEATIAATVCRLTQLTERNITSvPIGRP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3841 LPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFV-----ERGGQRFYRSGDLGRYRADGSLEYRGRG 3915
Cdd:cd17644 289 IANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFIshpfnSSESERLYKTGDLARYLPDGNIEYLGRI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3916 DDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTV-EGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLL 3994
Cdd:cd17644 369 DNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVrEDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVL 448
|
490
....*....|....*..
gi 1246793773 3995 PALPLTANGKLDRKALP 4011
Cdd:cd17644 449 EELPLTPNGKIDRRALP 465
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
3525-4010 |
3.22e-114 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 373.42 E-value: 3.22e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAP 3604
Cdd:cd05918 5 IEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3605 AARRGFILEDSGVCLSVSqralavelpgtalclDDPftraqldavepgelpevptEAPAYLIYTSGSTGTPKGVVVTHRN 3684
Cdd:cd05918 85 LQRLQEILQDTGAKVVLT---------------SSP-------------------SDAAYVIFTSGSTGKPKGVVIEHRA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3685 VerlFTAATQTGR-FSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRqpDAFLDLLAEYGVTVLNQTPSA 3763
Cdd:cd05918 131 L---STSALAHGRaLGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRL--NDLAGFINRLRVTWAFLTPSV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3764 fyalqSQAMRRELALNVRAVVFGGEALEPSRLQPWRERypqAELVNMYGITETTVHVSFHRLSDEdlqSPTSRIGSALPd 3843
Cdd:cd05918 206 -----ARLLDPEDVPSLRTLVLGGEALTQSDVDTWADR---VRLINAYGPAECTIAATVSPVVPS---TDPRNIGRPLG- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3844 LAVHVLDAA--GQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE----------RGGQRFYRSGDLGRYRADGSLEY 3911
Cdd:cd05918 274 ATCWVVDPDnhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEdpawlkqegsGRGRRLYRTGDLVRYNPDGSLEY 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3912 RGRGDDQVKLRGYRIEPGEIAAKI-ASLPQVSDAAVTV---EGQGEGAWLMAyAVAADGAEPD----------------- 3970
Cdd:cd05918 354 VGRKDTQVKIRGQRVELGEIEHHLrQSLPGAKEVVVEVvkpKDGSSSPQLVA-FVVLDGSSSGsgdgdslflepsdefra 432
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1246793773 3971 -PQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:cd05918 433 lVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
3521-4021 |
3.33e-114 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 372.22 E-value: 3.33e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3521 LVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVD 3600
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3601 PHAPAARRGFILEDSGVclsvsqRALAVelpgtalclddpftraqldavepgelpevpteapAYLIYTSGSTGTPKGVVV 3680
Cdd:COG0318 81 PRLTAEELAYILEDSGA------RALVT----------------------------------ALILYTSGTTGRPKGVML 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3681 THRNVerLFTAATQTGRFSFDEHDVW----SLFHSHAFdfaVWELWGAWLYGGRAVLVPEavcRQPDAFLDLLAEYGVTV 3756
Cdd:COG0318 121 THRNL--LANAAAIAAALGLTPGDVVlvalPLFHVFGL---TVGLLAPLLAGATLVLLPR---FDPERVLELIERERVTV 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3757 LNQTPSAFYALQSQAMRRELAL-NVRAVVFGGEALEPSRLQPWRERYpQAELVNMYGITETTVHVSFhRLSDEDLQSPTS 3835
Cdd:COG0318 193 LFGVPTMLARLLRHPEFARYDLsSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTV-NPEDPGERRPGS 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3836 rIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFveRGGqrFYRSGDLGRYRADGSLEYRGRG 3915
Cdd:COG0318 271 -VGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF--RDG--WLRTGDLGRLDEDGYLYIVGRK 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3916 DDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLL 3994
Cdd:COG0318 346 KDMIISGGENVYPAEVEEVLAAHPGVAEAAVVgVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFV 425
|
490 500
....*....|....*....|....*..
gi 1246793773 3995 PALPLTANGKLDRKALPKPETQDRDEG 4021
Cdd:COG0318 426 DELPRTASGKIDRRALRERYAAGALEA 452
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1628-2793 |
4.52e-112 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 403.78 E-value: 4.52e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1628 LDGEIDAAALAQAWQQTVRRQPMLRTAIvWEGLSVPHQIVLADAAAPWQTLDWSALDDAAQDAQLQRWLADDAAQGVDFA 1707
Cdd:PRK05691 706 LRGELDEAALRASFQRLVERHESLRTRF-YERDGVALQRIDAQGEFALQRIDLSDLPEAEREARAAQIREEEARQPFDLE 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1708 HAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGATLRLPPAP-GFQAYLDWrERQDLA----- 1781
Cdd:PRK05691 785 KGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPlGYADYGAW-QRQWLAqgeaa 863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1782 RQRGWWRERLSGYAGTAALPAPVAAAHHpvQREECER---RLSAHDSERLRAFCRERGCTLSDLIAMVWGLANARYGNHD 1858
Cdd:PRK05691 864 RQLAYWKAQLGDEQPVLELATDHPRSAR--QAHSAARyslRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQG 941
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1859 DVVLGATRSGRP-PELAGvesMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAENEAVGLGEILADSGLDADR-LF 1936
Cdd:PRK05691 942 DIRIGVPNANRPrLETQG---LVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAREQgLF 1018
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1937 A--------SLLVVENFPAMAPAQLPFalRVRETRaanhYALTLRVSERECVRLEalLDAARVDRAAVAAMLDLAVAGLL 2008
Cdd:PRK05691 1019 QvmfnhqqrDLSALRRLPGLLAEELPW--HSREAK----FDLQLHSEEDRNGRLT--LSFDYAAELFDAATIERLAEHFL 1090
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2009 RLLQ----RPDCRVAE--LLGGDDAVQAPQPQRASSATAQSLLWQM-------PAQAVAVEEGAASWTYAQLRAAAGRIA 2075
Cdd:PRK05691 1091 ALLEqvceDPQRALGDvqLLDAAERAQLAQWGQAPCAPAQAWLPELlneqarqTPERIALVWDGGSLDYAELHAQANRLA 1170
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2076 GALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGWGAAPAWVPAS--VRW 2153
Cdd:PRK05691 1171 HYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAegVSA 1250
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2154 LDAESvLDVVSAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGF 2233
Cdd:PRK05691 1251 IALDS-LHLDSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSV 1329
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2234 TALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPRECLVTGGEALTGALVQQVR 2313
Cdd:PRK05691 1330 WECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRLFSGGEALPAELRNRVL 1409
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2314 ALAPTLRIVNHYGPTETTVGIltctvpEEW--PVEQG--VPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGY 2389
Cdd:PRK05691 1410 QRLPQVQLHNRYGPTETAINV------THWqcQAEDGerSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGY 1483
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2390 WQRAEQTAERFVAHPLAPD-RLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPG 2468
Cdd:PRK05691 1484 LGRPALTAERFVPDPLGEDgARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREG 1563
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2469 ANGVLQLG-----ACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLLQQddadsSAEAID-ETP 2542
Cdd:PRK05691 1564 AAGAQLVGyytgeAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQ-----QREHVEpRTE 1638
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2543 VNEVLRELWQKLLGREHIGAHDNFFALGGDSILSLQLVARARQAGLALMP-RQLYDHPTLAGLSAQVQASSPAPAT-IKP 2620
Cdd:PRK05691 1639 LQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPlRALFEASELGAFAEQVARIQAAGERnSQG 1718
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2621 ATEA---EQSFGLTPIQH--WFFEQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARFQRDAAGQWQQTL 2695
Cdd:PRK05691 1719 AIARvdrSQPVPLSYSQQrmWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVA 1798
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2696 GD------WQadRFAHREADA-GQREDLLAQWQAGLSFD---GALLRVlALPDPQDGDTRVLFAAHHLLVDAVSWGIIVD 2765
Cdd:PRK05691 1799 EDsglrmdWQ--DFSALPADArQQRLQQLADSEAHQPFDlerGPLLRA-CLVKAAEREHYFVLTLHHIVTEGWAMDIFAR 1875
|
1210 1220 1230
....*....|....*....|....*....|.
gi 1246793773 2766 DLQHAYAERRAGR-SP--ALAAEACGFGAWQ 2793
Cdd:PRK05691 1876 ELGALYEAFLDDReSPlePLPVQYLDYSVWQ 1906
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
87-507 |
1.24e-109 |
|
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380463 [Multi-domain] Cd Length: 433 Bit Score: 358.27 E-value: 1.24e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 87 PAPLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLdRCIQGED------SVAAGGGAAVE 160
Cdd:cd19540 1 RIPLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESL-RTVFPEDdggpyqVVLPAAEARPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 161 sADLRGRGQDEIDALVEGFRLRPFELQRQRPLRMQLLRLdgqgdGPVRHWLQVVVHHIACDGVSLGLLTQDLSRAYRVEC 240
Cdd:cd19540 80 -LTVVDVTEDELAARLAEAARRGFDLTAELPLRARLFRL-----GPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 241 GlAAEPA-PPLPCQYGDYARWQRDTLD-------RLDASLRHHVEALSGAPHLHELPLDHERPAVLGQSGAKLRLAFPPG 312
Cdd:cd19540 154 A-GRAPDwAPLPVQYADYALWQRELLGdeddpdsLAARQLAYWRETLAGLPEELELPTDRPRPAVASYRGGTVEFTIDAE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 313 LSERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDDPDFASLVAR 392
Cdd:cd19540 233 LHARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLAR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 393 CRDHQLAALEHQALPLERVIETLQVERSSRHAPLFQLMFALRHDADLALDLHGVQAHALTLPEDVAKHELTLEV------ 466
Cdd:cd19540 313 VRETDLAAFAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVDTGVAKFDLSFTLterrda 392
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1246793773 467 LVGAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENP 507
Cdd:cd19540 393 DGAPAGLTGELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
2063-2463 |
2.45e-109 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 356.19 E-value: 2.45e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2063 TYAQLRAAAGRIAGAL-DAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVI--- 2138
Cdd:TIGR01733 1 TYRELDERANRLARHLrAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLtds 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2139 GWGAAPAWVPASVR-WLDAESVLDVVSAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGE 2217
Cdd:TIGR01733 81 ALASRLAGLVLPVIlLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2218 DASLATLSTVAADLGFTALFGALLSGRRVRLLP-AELAFDAQALAAHLQAHPVDCLKIVPSHLAG-LLAAAGGTAVLPRe 2295
Cdd:TIGR01733 161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPeDEERDDAALLAALIAEHPVTVLNLTPSLLALlAAALPPALASLRL- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2296 cLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVG--ILTCTVPEEwPVEQGVPVGHPLAGNEAWVLDRFGLPAPVG 2373
Cdd:TIGR01733 240 -VILGGEALTPALVDRWRARGPGARLINLYGPTETTVWstATLVDPDDA-PRESPVPIGRPLANTRLYVLDDDLRPVPVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2374 VAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPD--RLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQV 2451
Cdd:TIGR01733 318 VVGELYIGGPGVARGYLNRPELTAERFVPDPFAGGdgARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAA 397
|
410
....*....|..
gi 1246793773 2452 LAQLPGVEVAAV 2463
Cdd:TIGR01733 398 LLRHPGVREAVV 409
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
82-1120 |
3.55e-107 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 377.08 E-value: 3.55e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 82 APAGTPAPLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLD-RCIQGEDSV-----AAGG 155
Cdd:PRK10252 2 EPMSQHLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRmRFTEDNGEVwqwvdPALT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 156 GAAVESADLRgrgqDEID------ALVEGFRLRPFELQRQRPL-RMQLLRLdgqgdGPVRHWLQVVVHHIACDGVSLGLL 228
Cdd:PRK10252 82 FPLPEIIDLR----TQPDphaaaqALMQADLQQDLRVDSGKPLvFHQLIQL-----GDNRWYWYQRYHHLLVDGFSFPAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 229 TQDLSRAYRVECGLAAEPAPPLPCQYG---DYARWQRDTLDRLDASLRHhvEALSGAPHLHELPldhERPAVLGQSGAK- 304
Cdd:PRK10252 153 TRRIAAIYCAWLRGEPTPASPFTPFADvveEYQRYRASEAWQRDAAFWA--EQRRQLPPPASLS---PAPLPGRSASADi 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 305 LRLAFPPGLSERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDDP 384
Cdd:PRK10252 228 LRLKLEFTDGAFRQLAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 385 DFASLVARCRDHQLAALEHQALPLERVIETLQVERSSR--HAPLFQL-MFalrhdaDLALDLHGVQAHALTL---PEDva 458
Cdd:PRK10252 308 TLPELATRLAAQLKKMRRHQRYDAEQIVRDSGRAAGDEplFGPVLNIkVF------DYQLDFPGVQAQTHTLatgPVN-- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 459 khELTLEVLV-GAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENPH----EPALSWPWPADELA-LDDKREPAPR 532
Cdd:PRK10252 380 --DLELALFPdEHGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPAllcgDVDILLPGEYAQLAqVNATAVEIPE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 533 TvgNVVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSV 612
Cdd:PRK10252 458 T--TLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAW 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 613 IPLDTEWPQARRAEVVAASGCDAVLTDAQGLAGFA--PSVAIA-VDELKLDGAGEngSGENAAPNQLAYILYTSGSTGIP 689
Cdd:PRK10252 536 LPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFAdvPDLTSLcYNAPLAPQGAA--PLQLSQPHHTAYIIFTSGSTGRP 613
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 690 KGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGAC-VVARPDELLEPQRFLAFLSERAITVT 768
Cdd:PRK10252 614 KGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKlVMAEPEAHRDPLAMQQFFAEYGVTTT 693
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 769 DLAPAYANELVRASVADDWRD--LALRCLVVGGDVLPVALAQRWFELgldRRCALINAYGPTEATISSHYHRVQAID--- 843
Cdd:PRK10252 694 HFVPSMLAAFVASLTPEGARQscASLRQVFCSGEALPADLCREWQQL---TGAPLHNLYGPTEAAVDVSWYPAFGEElaa 770
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 844 -ASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGEslRMYRSGDRVRLL 922
Cdd:PRK10252 771 vRGSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGE--RMYRTGDVARWL 848
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 923 DDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA-------GVVGEGAAQRLVAWVECAGEDGFGQADLnqt 995
Cdd:PRK10252 849 DDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVThacvinqAAATGGDARQLVGYLVSQSGLPLDTSAL--- 925
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 996 dsdqteserwHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRALPAPPVLAQAERTPPRTAEESALCEVWAEVLQCEV 1075
Cdd:PRK10252 926 ----------QAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELKAQVPGRAPKTGTETIIAAAFSSLLGCDV 995
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*..
gi 1246793773 1076 -GIHDSFFRLGGDSIRSLQVVARL-RERGYAVTPKLMYQYQSAAELA 1120
Cdd:PRK10252 996 vDADADFFALGGHSLLAMKLAAQLsRQFARQVTPGQVMVASTVAKLA 1042
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
3525-3922 |
5.81e-107 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 349.69 E-value: 5.81e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPARIAVSAEDGE-LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHA 3603
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGRrLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3604 PAARRGFILEDSGVCLSVSQRAL----------AVELPGTALCLDDP--------FTRAQLDAVEPGELPEVPTEAPAYL 3665
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALkleellealgKLEVVKLVLVLDRDpvlkeeplPEEAKPADVPPPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3666 IYTSGSTGTPKGVVVTHRNVERLFTAA--TQTGRFSFDEHDVWSLFHSHAFDFAV-WELWGAWLYGGRAVLVPEAVCRQP 3742
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIkrVRPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3743 DAFLDLLAEYGVTVLNQTPSAFYAL-QSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAeLVNMYGITETTVHVS 3821
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLlEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTETTGVVT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3822 FHRLSDEDLQSPTSrIGSALPDLAVHVLDAA-GQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVErggQRFYRSGDL 3900
Cdd:pfam00501 320 TPLPLDEDLRSLGS-VGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE---DGWYRTGDL 395
|
410 420
....*....|....*....|..
gi 1246793773 3901 GRYRADGSLEYRGRGDDQVKLR 3922
Cdd:pfam00501 396 GRRDEDGYLEIVGRKKDQIKLG 417
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
3533-4010 |
2.72e-106 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 349.07 E-value: 2.72e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3533 PARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFIL 3612
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3613 EDSGVCLSVSQralavelpgtalclddpftraqldavepgelpevPTEaPAYLIYTSGSTGTPKGVVVTHRNVERLFTAA 3692
Cdd:cd17650 81 EDSGAKLLLTQ----------------------------------PED-LAYVIYTSGTTGKPKGVMVEHRNVAHAAHAW 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3693 TQtgRFSFDEHDVWSL-FHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQA 3771
Cdd:cd17650 126 RR--EYELDSFPVRLLqMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3772 MRRELALN-VRAVVFGGEALEPSRLQPWRERYPQA-ELVNMYGITETTVHVSFHRLSDEDL-QSPTSRIGSALPDLAVHV 3848
Cdd:cd17650 204 YRNGLDLSaMRLLIVGSDGCKAQDFKTLAARFGQGmRIINSYGVTEATIDSTYYEEGRDPLgDSANVPIGRPLPNTAMYV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3849 LDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVER---GGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYR 3925
Cdd:cd17650 284 LDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENpfaPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFR 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3926 IEPGEIAAKIASLPQVSDAAVTV-EGQGEGAWLMAYAVAAdgAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGK 4004
Cdd:cd17650 364 IELGEIESQLARHPAIDEAVVAVrEDKGGEARLCAYVVAA--ATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGK 441
|
....*.
gi 1246793773 4005 LDRKAL 4010
Cdd:cd17650 442 VDRRAL 447
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
1599-1978 |
6.97e-106 |
|
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380465 [Multi-domain] Cd Length: 423 Bit Score: 346.88 E-value: 6.97e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1599 PLTPLQRGVLLESLRGDGADPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGLSVPHQIVLADAAAPWQTL 1678
Cdd:cd19543 3 PLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDRKLPWREL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1679 DWSALDDAAQDAQLQRWLADDAAQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGA 1758
Cdd:cd19543 83 DLSHLSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGEGQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1759 TLRLPPAPGFQAYLDWRERQDLARQRGWWRERLSGY-AGTAALPAPVAAAHHPVQREECERRLSAHDSERLRAFCRERGC 1837
Cdd:cd19543 163 PPSLPPVRPYRDYIAWLQRQDKEAAEAYWREYLAGFeEPTPLPKELPADADGSYEPGEVSFELSAELTARLQELARQHGV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1838 TLSDLIAMVWGLANARYGNHDDVVLGATRSGRPPELAGVESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAENE 1917
Cdd:cd19543 243 TLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQLELREHE 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 1918 AVGLGEILADSGLDaDRLFASLLVVENFP---AMAPAQLPFALRVRETRAA--NHYALTLRVSERE 1978
Cdd:cd19543 323 YVPLYEIQAWSEGK-QALFDHLLVFENYPvdeSLEEEQDEDGLRITDVSAEeqTNYPLTVVAIPGE 387
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
3525-4010 |
5.01e-105 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 345.06 E-value: 5.01e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAP 3604
Cdd:cd17653 3 FERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3605 AARRGFILEDSGVCLsvsqralavelpgtALCLDDPftraqldavepgelpevptEAPAYLIYTSGSTGTPKGVVVTHRN 3684
Cdd:cd17653 83 SARIQAILRTSGATL--------------LLTTDSP-------------------DDLAYIIFTSGSTGIPKGVMVPHRG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3685 VerlfTAATQTGRFSFD--EHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLvpeavcRQPDA-FLDLLAEygVTVLNQTP 3761
Cdd:cd17653 130 V----LNYVSQPPARLDvgPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVL------ADPSDpFAHVART--VDALMSTP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3762 SAFYALQSQAMRrelalNVRAVVFGGEALEPSRLQPWRERypqAELVNMYGITETTVHVSFHRLSDEDlqsPTSrIGSAL 3841
Cdd:cd17653 198 SILSTLSPQDFP-----NLKTIFLGGEAVPPSLLDRWSPG---RRLYNAYGPTECTISSTMTELLPGQ---PVT-IGKPI 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3842 PDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE---RGGQRFYRSGDLGRYRADGSLEYRGRGDDQ 3918
Cdd:cd17653 266 PNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPdpfWPGSRMYRTGDYGRWTEDGGLEFLGREDNQ 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3919 VKLRGYRIEPGEIAAKIASL-PQVSDAAVTVEGQGegawLMAYAVAADgaePDPQSLREALRALLPDYMLPRLIQLLPAL 3997
Cdd:cd17653 346 VKVRGFRINLEEIEEVVLQSqPEVTQAAAIVVNGR----LVAFVTPET---VDVDGLRSELAKHLPSYAVPDRIIALDSF 418
|
490
....*....|...
gi 1246793773 3998 PLTANGKLDRKAL 4010
Cdd:cd17653 419 PLTANGKVDRKAL 431
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
542-1041 |
4.37e-104 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 344.18 E-value: 4.37e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 542 ARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQ 621
Cdd:cd12117 4 EEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 622 ARRAEVVAASGCDAVLTDAQGLAGFAPSVAIAVDELKLDGAGENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAA 701
Cdd:cd12117 84 ERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 702 HIDAAAEALALSaDDRVLHVAGLAVDTTLEQILAAWSRGA-CVVARPDELLEPQRFLAFLSERAITVTDLAPAYANELVR 780
Cdd:cd12117 164 LVKNTNYVTLGP-DDRVLQTSPLAFDASTFEIWGALLNGArLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALFNQLAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 781 ASVADdwrdLA-LRCLVVGGDVLPVALAQRWFelgldRRCA---LINAYGPTEATISSHYHRVQAIDAS-RPVPLGQLLP 855
Cdd:cd12117 243 EDPEC----FAgLRELLTGGEVVSPPHVRRVL-----AACPglrLVNGYGPTENTTFTTSHVVTELDEVaGSIPIGRPIA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 856 GRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGEslRMYRSGDRVRLLDDGELQFLGRADF 935
Cdd:cd12117 314 NTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGE--RLYRTGDLARWLPDGRLEFLGRIDD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 936 QVKLRGYRIELEEIEHCLGQLPQVRAAAAGVV-GEGAAQRLVAWVecAGEDGFGQADLnqtdsdqteserwhRALC-ERL 1013
Cdd:cd12117 392 QVKIRGFRIELGEIEAALRAHPGVREAVVVVReDAGGDKRLVAYV--VAEGALDAAEL--------------RAFLrERL 455
|
490 500
....*....|....*....|....*...
gi 1246793773 1014 PAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd12117 456 PAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
2052-2522 |
1.63e-103 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 341.96 E-value: 1.63e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDD 2131
Cdd:cd12116 3 ATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVIGWGAAPAWVPASVRWLDAESVLDVVSAyeEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLP 2211
Cdd:cd12116 83 AEPALVLTDDALPDRLPAGLPVLLLALAAAAAAP--AAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2212 VLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPShlagLLAAAGGTAV 2291
Cdd:cd12116 161 RLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPA----TWRMLLDAGW 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2292 LPRECL--VTGGEALTGALVQQVraLAPTLRIVNHYGPTETTVGILTCTVPEEWPveqGVPVGHPLAGNEAWVLDRFGLP 2369
Cdd:cd12116 237 QGRAGLtaLCGGEALPPDLAARL--LSRVGSLWNLYGPTETTIWSTAARVTAAAG---PIPIGRPLANTQVYVLDAALRP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2370 APVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPDR-LLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEV 2448
Cdd:cd12116 312 VPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGsRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEI 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 2449 EQVLAQLPGVEVAAVLALPGAN-----GVLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:cd12116 392 EAALAAHPGVAQAAVVVREDGGdrrlvAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
549-1041 |
1.81e-103 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 341.96 E-value: 1.81e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 549 PERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVV 628
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 629 AASGCDAVLTDAQGLAGF-APSVAIAVDELKLDGAGENgSGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAA 707
Cdd:cd12116 81 EDAEPALVLTDDALPDRLpAGLPVLLLALAAAAAAPAA-PRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 708 EALALSADDRVLHVAGLAVD-TTLEQILAAWSRGACVVARPDELLEPQRFLAFLSERAITVTDLAPAyaneLVRASVADD 786
Cdd:cd12116 160 ERLGLGPGDRLLAVTTYAFDiSLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPA----TWRMLLDAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 787 WRDLALRCLVVGGDVLPVALAQRWfelgLDRRCALINAYGPTEATISSHYHRVQaiDASRPVPLGQLLPGRIAAVLDAHG 866
Cdd:cd12116 236 WQGRAGLTALCGGEALPPDLAARL----LSRVGSLWNLYGPTETTIWSTAARVT--AAAGPIPIGRPLANTQVYVLDAAL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 867 RIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPlrLPSGES-LRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIE 945
Cdd:cd12116 310 RPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVP--DPFAGPgSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 946 LEEIEHCLGQLPQVRAAAAGVVGEGAAQRLVAWVECAGEDGFGQAdlnqtdsdqteseRWHRALCERLPAYMVPTQFVAL 1025
Cdd:cd12116 388 LGEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAGAAPDAA-------------ALRAHLRATLPAYMVPSAFVRL 454
|
490
....*....|....*.
gi 1246793773 1026 PRLPRNASGKIDRRAL 1041
Cdd:cd12116 455 DALPLTANGKLDRKAL 470
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
538-1041 |
2.03e-102 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 339.64 E-value: 2.03e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 538 VDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDT 617
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 618 EWPQARRAEVVAASGCDAVLTDAQGLAGFAPSVAIA-VDELKLDGAGENGSGENAAPNQLAYILYTSGSTGIPKGVEVGH 696
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVAlLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 697 AALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGAC-VVARPDELLEPQRFLAFLSERAITVTDLAPAYA 775
Cdd:cd17646 161 AGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARlVVARPGGHRDPAYLAALIREHGVTTCHFVPSML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 776 NELVRASVADDWRdlALRCLVVGGDVLPVALAQRWFELGldrRCALINAYGPTEATISSHYHRVQAIDASRPVPLGQLLP 855
Cdd:cd17646 241 RVFLAEPAAGSCA--SLRRVFCSGEALPPELAARFLALP---GAELHNLYGPTEAAIDVTHWPVRGPAETPSVPIGRPVP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 856 GRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLrlPSGESLRMYRSGDRVRLLDDGELQFLGRADF 935
Cdd:cd17646 316 NTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPD--PFGPGSRMYRTGDLARWRPDGALEFLGRSDD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 936 QVKLRGYRIELEEIEHCLGQLPQVRAAAAGVVGEGA-AQRLVAWVECAGedgfGQADLNQtdsdqtesERWHRALCERLP 1014
Cdd:cd17646 394 QVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAgAARLVGYVVPAA----GAAGPDT--------AALRAHLAERLP 461
|
490 500
....*....|....*....|....*..
gi 1246793773 1015 AYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd17646 462 EYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
588-964 |
9.53e-102 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 334.62 E-value: 9.53e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQ--GLAGFAPSVAIAVDELKLDGAGEN 665
Cdd:TIGR01733 28 VAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSAlaSRLAGLVLPVILLDPLELAALDDA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 666 GSGE----NAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGA 741
Cdd:TIGR01733 108 PAPPppdaPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 742 C-VVARPDELLEPQRFLAFL-SERAITVTDLAPAYANELVRAsvaDDWRDLALRCLVVGGDVLPVALAQRWFELGLDRRc 819
Cdd:TIGR01733 188 TlVVPPEDEERDDAALLAALiAEHPVTVLNLTPSLLALLAAA---LPPALASLRLVILGGEALTPALVDRWRARGPGAR- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 820 aLINAYGPTEATISSHYHRVQAIDASR--PVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASER 897
Cdd:TIGR01733 264 -LINLYGPTETTVWSTATLVDPDDAPResPVPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAE 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 898 RFAPLRLPSGESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA 964
Cdd:TIGR01733 343 RFVPDPFAGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
2051-2522 |
2.11e-100 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 333.86 E-value: 2.11e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLD 2130
Cdd:cd17646 13 DAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2131 DSGARIVIGWGAAPAWVPASvrwLDAESVLDVVSAYEE--PPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAG 2208
Cdd:cd17646 93 DAGPAVVLTTADLAARLPAG---GDVALLGDEALAAPPatPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLW 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2209 VLPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGG 2288
Cdd:cd17646 170 MQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSMLRVFLAEPAA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2289 TAVLPRECLVTGGEALTGALVQQVRALaPTLRIVNHYGPTETTVGILTCTVPEEWPvEQGVPVGHPLAGNEAWVLDRFGL 2368
Cdd:cd17646 250 GSCASLRRVFCSGEALPPELAARFLAL-PGAELHNLYGPTEAAIDVTHWPVRGPAE-TPSVPIGRPVPNTRLYVLDDALR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2369 PAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEV 2448
Cdd:cd17646 328 PVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2449 EQVLAQLPGVEVAAVLALPGANGVLQL-------GACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQA 2521
Cdd:cd17646 408 EAALAAHPAVTHAVVVARAAPAGAARLvgyvvpaAGAAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAA 487
|
.
gi 1246793773 2522 L 2522
Cdd:cd17646 488 L 488
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
3533-4011 |
5.77e-100 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 332.13 E-value: 5.77e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3533 PARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFIL 3612
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3613 EDSGVCLSVSQRALAVELP--GTALCLDDPFTRAQLDAvepgELP-EVPTEAPAYLIYTSGSTGTPKGVVVTHRNVERLF 3689
Cdd:cd17656 82 LDSGVRVVLTQRHLKSKLSfnKSTILLEDPSISQEDTS----NIDyINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3690 T-AATQTGRFSFDehDVWSlFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNqTPSAFyaLQ 3768
Cdd:cd17656 158 HfEREKTNINFSD--KVLQ-FATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVF-LPVAF--LK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3769 SQAMRRE----LALNVRAVVFGGEALEPSrlQPWRE--RYPQAELVNMYGITETTVhVSFHRLSDEDLQSPTSRIGSALP 3842
Cdd:cd17656 232 FIFSEREfinrFPTCVKHIITAGEQLVIT--NEFKEmlHEHNVHLHNHYGPSETHV-VTTYTINPEAEIPELPPIGKPIS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3843 DLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE---RGGQRFYRSGDLGRYRADGSLEYRGRGDDQV 3919
Cdd:cd17656 309 NTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPdpfDPNERMYRTGDLARYLPDGNIEFLGRADHQV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3920 KLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEG-AWLMAYAVAADgAEPDPQsLREALRALLPDYMLPRLIQLLPALP 3998
Cdd:cd17656 389 KIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGeKYLCAYFVMEQ-ELNISQ-LREYLAKQLPEYMIPSFFVPLDQLP 466
|
490
....*....|...
gi 1246793773 3999 LTANGKLDRKALP 4011
Cdd:cd17656 467 LTPNGKVDRKALP 479
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
2051-2522 |
1.42e-99 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 331.62 E-value: 1.42e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLD 2130
Cdd:cd17651 10 DAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2131 DSGARIVIGWGAAPAWVPASVRWLDAESVLDVVSAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVL 2210
Cdd:cd17651 90 DAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2211 PVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVD--CLKIVPSHLAGLLAAAGG 2288
Cdd:cd17651 170 RASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISrvFLPTVALRALAEHGRPLG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2289 TAVLPRECLVTGGEALT-GALVQQVRALAPTLRIVNHYGPTETTVgiLTCTV----PEEWPveQGVPVGHPLAGNEAWVL 2363
Cdd:cd17651 250 VRLAALRYLLTGGEQLVlTEDLREFCAGLPGLRLHNHYGPTETHV--VTALSlpgdPAAWP--APPPIGRPIDNTRVYVL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2364 DRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRV 2443
Cdd:cd17651 326 DAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRI 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2444 ELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQG------SLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKI 2517
Cdd:cd17651 406 ELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGdpeapvDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKL 485
|
....*
gi 1246793773 2518 DRQAL 2522
Cdd:cd17651 486 DRRAL 490
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
549-1042 |
3.15e-99 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 328.94 E-value: 3.15e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 549 PERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVV 628
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 629 AASGCDAVLTdaqglagfapsvaiavdelkldgagengsgenAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAE 708
Cdd:cd17649 81 EDSGAGLLLT--------------------------------HHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 709 ALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARPDELLEPQRFLAFLSER-AITVTDLAPAYANELVRASVADDW 787
Cdd:cd17649 129 RYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRElGVTVLDLPPAYLQQLAEEADRTGD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 788 RD-LALRCLVVGGDVLPVALAQRWFELGldrrCALINAYGPTEATISSHYHRVQAIDASRP--VPLGQLLPGRIAAVLDA 864
Cdd:cd17649 209 GRpPSLRLYIFGGEALSPELLRRWLKAP----VRLFNAYGPTEATVTPLVWKCEAGAARAGasMPIGRPLGGRSAYILDA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 865 HGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPlRLPSGESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRI 944
Cdd:cd17649 285 DLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVP-DPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRI 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 945 ELEEIEHCLGQLPQVRAAAAGVVGEGAAQRLVAWVEcAGEDGFGQADLnqtdsdqtesERWHRALCERLPAYMVPTQFVA 1024
Cdd:cd17649 364 ELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVV-LRAAAAQPELR----------AQLRTALRASLPDYMVPAHLVF 432
|
490
....*....|....*...
gi 1246793773 1025 LPRLPRNASGKIDRRALP 1042
Cdd:cd17649 433 LARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
2052-2522 |
7.31e-99 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 329.29 E-value: 7.31e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDD 2131
Cdd:cd17655 13 HTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVIGWGAapawVPASVRWLDAESVLDVVSAYEEPP---RVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAG 2208
Cdd:cd17655 93 SGADILLTQSH----LQPPIAFIGLIDLLDEDTIYHEESenlEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEW 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2209 VLPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGG 2288
Cdd:cd17655 169 ANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLKLLDAADDS 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2289 TAVLPREcLVTGGEALTGALVQQVRALAPT-LRIVNHYGPTETTVGILTCTVPEEWPVEQGVPVGHPLAGNEAWVLDRFG 2367
Cdd:cd17655 249 EGLSLKH-LIVGGEALSTELAKKIIELFGTnPTITNAYGPTETTVDASIYQYEPETDQQVSVPIGKPLGNTRIYILDQYG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2368 LPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGE 2447
Cdd:cd17655 328 RPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGE 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 2448 VEQVLAQLPGVEVAAVLALPGANGVLQLGACIQG----SLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:cd17655 408 IEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSekelPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
2050-2522 |
1.28e-98 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 326.97 E-value: 1.28e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2050 AQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVL 2129
Cdd:cd12115 13 PDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 DDSGARIVIgwgaapawvpasvrwldaesvldvvsayeepprvdVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYV--- 2206
Cdd:cd12115 93 EDAQARLVL-----------------------------------TDPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLqwa 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2207 AGVLPVLDLGedASLATLStVAADLGFTALFGALLSGRRVRLLPAELAFdaqalAAHLQAHPVDCLKIVPShlagllaaa 2286
Cdd:cd12115 138 AAAFSAEELA--GVLASTS-ICFDLSVFELFGPLATGGKVVLADNVLAL-----PDLPAAAEVTLINTVPS--------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2287 GGTAVLPRECLVTG-------GEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPEEwpVEQGVPVGHPLAGNE 2359
Cdd:cd12115 201 AAAELLRHDALPASvrvvnlaGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPG--ASGEVSIGRPLANTQ 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2360 AWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIR 2439
Cdd:cd12115 279 AYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2440 GYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI------QGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLG 2513
Cdd:cd12115 359 GFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIvaepgaAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTP 438
|
....*....
gi 1246793773 2514 NGKIDRQAL 2522
Cdd:cd12115 439 NGKIDRSAL 447
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1597-2625 |
4.36e-98 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 349.34 E-value: 4.36e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1597 AFPLTPLQRGVLLESLRGDGADPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVwEGLSVPHQIVLADAAAP-W 1675
Cdd:PRK10252 7 HLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFT-EDNGEVWQWVDPALTFPlP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1676 QTLDWSALDDAAQDAQlqRWLADDAAQGVDFAHA-PLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAG 1754
Cdd:PRK10252 86 EIIDLRTQPDPHAAAQ--ALMQADLQQDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1755 AQGATLRLPPAPGFQA----YLDWRERQDLARQRGWWRERLSGYAGTAALPAPVAAAHHPVQREeCERRLSAHDSERLRA 1830
Cdd:PRK10252 164 LRGEPTPASPFTPFADvveeYQRYRASEAWQRDAAFWAEQRRQLPPPASLSPAPLPGRSASADI-LRLKLEFTDGAFRQL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1831 FCRERGCTLSDLIAMVWGLANARYGNHDDVVLG---ATRSGRPPelAGVESMVgvfINTLPLRLRIDAGQPALDLLSALR 1907
Cdd:PRK10252 243 AAQASGVQRPDLALALVALWLGRLCGRMDYAAGfifMRRLGSAA--LTATGPV---LNVLPLRVHIAAQETLPELATRLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1908 SQSLEVAENEAVGLGEILADSGL--DADRLFASLLVVENFPAmapaQLPFA-----LRVRETRAANHYALTLRVSERECV 1980
Cdd:PRK10252 318 AQLKKMRRHQRYDAEQIVRDSGRaaGDEPLFGPVLNIKVFDY----QLDFPgvqaqTHTLATGPVNDLELALFPDEHGGL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1981 RLEALLDAARVDRAAVAAMLDLAVAGLLRLLQRPDCRVA--ELLGGDDAVQ--------APQPQRASSATAQSLLWQMPa 2050
Cdd:PRK10252 394 SIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGdvDILLPGEYAQlaqvnataVEIPETTLSALVAQQAAKTP- 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLD 2130
Cdd:PRK10252 473 DAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLE 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2131 DSGARIVIGWGA-APAWVPASVRWLDAESVLDVVSAYEepPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGV 2209
Cdd:PRK10252 553 DARPSLLITTADqLPRFADVPDLTSLCYNAPLAPQGAA--PLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWM 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2210 LPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPS----HLAGLLAA 2285
Cdd:PRK10252 631 QNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSmlaaFVASLTPE 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2286 AGGTAVLPRECLVTGGEALTGALVQQVRALAPTlRIVNHYGPTETTVGIltctvpEEWPVE---------QGVPVGHPLA 2356
Cdd:PRK10252 711 GARQSCASLRQVFCSGEALPADLCREWQQLTGA-PLHNLYGPTEAAVDV------SWYPAFgeelaavrgSSVPIGYPVW 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2357 GNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQV 2436
Cdd:PRK10252 784 NTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQL 863
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2437 KIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQ------------GSLEGVAEALAQRLPEYLCPSRWR 2504
Cdd:PRK10252 864 KIRGQRIELGEIDRAMQALPDVEQAVTHACVINQAAATGGDARQlvgylvsqsglpLDTSALQAQLRERLPPHMVPVVLL 943
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2505 AVESMPRLGNGKIDRQALAdlLQQDDADSSAEAIdETPVNEVLRELWQKLLGREHIGAHDNFFALGGDSILSLQLVARAR 2584
Cdd:PRK10252 944 QLDQLPLSANGKLDRKALP--LPELKAQVPGRAP-KTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLS 1020
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*..
gi 1246793773 2585 QA-GLALMPRQLYDHPTLAGLSAQVQASSP-----APATIKPATEAE 2625
Cdd:PRK10252 1021 RQfARQVTPGQVMVASTVAKLATLLDAEEDesrrlGFGTILPLREGD 1067
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
3533-4011 |
7.19e-98 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 325.12 E-value: 7.19e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3533 PARIAVSAEDGELDYATLDRRSSQLATLLIRQGAG-PGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFI 3611
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3612 LEDSGvclsvsqralavelpgtalclddpftrAQLDAVEPGELpevpteapAYLIYTSGSTGTPKGVVVTHRNVERLFTA 3691
Cdd:cd17648 81 LEDTG---------------------------ARVVITNSTDL--------AYAIYTSGTTGKPKGVLVEHGSVVNLRTS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3692 ATqtGRFSFDEHD--VWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAfyaLQS 3769
Cdd:cd17648 126 LS--ERYFGRDNGdeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSV---LQQ 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3770 QAMRRELALnvRAVVFGGEALEPSRLQPWRERYPqAELVNMYGITETTV--HVSFHRLSDEDLQSptsrIGSALPDLAVH 3847
Cdd:cd17648 201 YDLARLPHL--KRVDAAGEEFTAPVFEKLRSRFA-GLIINAYGPTETTVtnHKRFFPGDQRFDKS----LGRPVRNTKCY 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3848 VLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE----------RG-GQRFYRSGDLGRYRADGSLEYRGRGD 3916
Cdd:cd17648 274 VLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPnpfqteqeraRGrNARLYKTGDLVRWLPSGELEYLGRND 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3917 DQVKLRGYRIEPGEIAAKIASLPQVSDAAV------TVEGQGEGAWLMAYAVAADGAEPDpQSLREALRALLPDYMLPRL 3990
Cdd:cd17648 354 FQVKIRGQRIEPGEVEAALASYPGVRECAVvakedaSQAQSRIQKYLVGYYLPEPGHVPE-SDLLSFLRAKLPRYMVPAR 432
|
490 500
....*....|....*....|.
gi 1246793773 3991 IQLLPALPLTANGKLDRKALP 4011
Cdd:cd17648 433 LVRLEGIPVTINGKLDVRALP 453
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
541-1042 |
2.35e-97 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 325.07 E-value: 2.35e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 541 IARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWP 620
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 621 QARRAEVVAASGCDAVLT--DAQGLAGFAPSVAIAVDELKLDGAGENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHAA 698
Cdd:cd17651 81 AERLAFMLADAGPVLVLThpALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 699 LAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARPDEL-LEPQRFLAFLSERAITVTDLAPAYANE 777
Cdd:cd17651 161 LANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVrTDPPALAAWLDEQRISRVFLPTVALRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 778 LVRASVADDWRDLALRCLVVGGDVLPVALAQRWFELGLdRRCALINAYGPTEATI-SSHYHRVQAIDASRPVPLGQLLPG 856
Cdd:cd17651 241 LAEHGRPLGVRLAALRYLLTGGEQLVLTEDLREFCAGL-PGLRLHNHYGPTETHVvTALSLPGDPAAWPAPPPIGRPIDN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 857 RIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLrlPSGESLRMYRSGDRVRLLDDGELQFLGRADFQ 936
Cdd:cd17651 320 TRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPD--PFVPGARMYRTGDLARWLPDGELEFLGRADDQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 937 VKLRGYRIELEEIEHCLGQLPQVRAAAAGVVGEGAA-QRLVAWVECAgedgfgqadlnQTDSDQTESerWHRALCERLPA 1015
Cdd:cd17651 398 VKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGeKRLVAYVVGD-----------PEAPVDAAE--LRAALATHLPE 464
|
490 500
....*....|....*....|....*..
gi 1246793773 1016 YMVPTQFVALPRLPRNASGKIDRRALP 1042
Cdd:cd17651 465 YMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
2051-2522 |
2.49e-95 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 317.71 E-value: 2.49e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLD 2130
Cdd:cd17643 2 EAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2131 DSGARIVIGwgaapawvpasvrwldaesvldvvsayeepprvdvDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVL 2210
Cdd:cd17643 82 DSGPSLLLT-----------------------------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2211 PVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPS--HLAGLLAAAGG 2288
Cdd:cd17643 127 RWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSafYQLVEAADRDG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2289 TAVLPRECLVTGGEALTGALVQQ--VRALAPTLRIVNHYGPTETTV----GILTctvPEEWPVEQGVPVGHPLAGNEAWV 2362
Cdd:cd17643 207 RDPLALRYVIFGGEALEAAMLRPwaGRFGLDRPQLVNMYGITETTVhvtfRPLD---AADLPAAAASPIGRPLPGLRVYV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2363 LDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHP--LAPDRLlYRSGDLARLDGEGRIVYLGRGDHQVKIRG 2440
Cdd:cd17643 284 LDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPfgGPGSRM-YRTGDLARRLPDGELEYLGRADEQVKIRG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2441 YRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI--QGSLEGVAEAL----AQRLPEYLCPSRWRAVESMPRLGN 2514
Cdd:cd17643 363 FRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVvaDDGAAADIAELrallKELLPDYMVPARYVPLDALPLTVN 442
|
....*...
gi 1246793773 2515 GKIDRQAL 2522
Cdd:cd17643 443 GKLDRAAL 450
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
2051-2522 |
1.11e-94 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 315.35 E-value: 1.11e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLD 2130
Cdd:cd17652 2 DAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2131 DSGARIVIgwgaapawvpasvrwldaesvldvvsayeepprvdVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVL 2210
Cdd:cd17652 82 DARPALLL-----------------------------------TTPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2211 PVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPShlagLLAAAGGTA 2290
Cdd:cd17652 127 AAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPA----ALAALPPDD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2291 VLPRECLVTGGEALTGALVQQvraLAPTLRIVNHYGPTETTVGiltCTVPEEWPVEQGVPVGHPLAGNEAWVLDRFGLPA 2370
Cdd:cd17652 203 LPDLRTLVVAGEACPAELVDR---WAPGRRMINAYGPTETTVC---ATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2371 PVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPL-APDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVE 2449
Cdd:cd17652 277 PPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVE 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 2450 QVLAQLPGVEVAAVLALPGANGVLQLGACIQGS------LEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:cd17652 357 AALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPApgaaptAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
3525-4011 |
1.28e-94 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 315.26 E-value: 1.28e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAP 3604
Cdd:cd17645 4 FEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3605 AARRGFILEDSGVCLSVSQralavelpgtalclddpftraqldavePGELpevpteapAYLIYTSGSTGTPKGVVVTHRN 3684
Cdd:cd17645 84 GERIAYMLADSSAKILLTN---------------------------PDDL--------AYVIYTSGSTGLPKGVMIEHHN 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3685 VERLftAATQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTV-LNQTPSA 3763
Cdd:cd17645 129 LVNL--CEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITIsFLPTGAA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3764 --FYALQSQAMRrelalnvrAVVFGGEALEPSRLQPWRerypqaeLVNMYGITETTVHVSFHRLSDEDLQSPtsrIGSAL 3841
Cdd:cd17645 207 eqFMQLDNQSLR--------VLLTGGDKLKKIERKGYK-------LVNNYGPTENTVVATSFEIDKPYANIP---IGKPI 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3842 PDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFV---ERGGQRFYRSGDLGRYRADGSLEYRGRGDDQ 3918
Cdd:cd17645 269 DNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIvhpFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQ 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3919 VKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEG-AWLMAYAVAADgaEPDPQSLREALRALLPDYMLPRLIQLLPAL 3997
Cdd:cd17645 349 VKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGrKYLVAYVTAPE--EIPHEELREWLKNDLPDYMIPTYFVHLKAL 426
|
490
....*....|....
gi 1246793773 3998 PLTANGKLDRKALP 4011
Cdd:cd17645 427 PLTANGKVDRKALP 440
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
549-1041 |
3.45e-94 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 315.36 E-value: 3.45e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 549 PERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVV 628
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 629 AASGCDAVLTDAQGLAGFAPSVAIAVDELKLDGAGENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAE 708
Cdd:cd12114 81 ADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 709 ALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVV-ARPDELLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDW 787
Cdd:cd12114 161 RFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVlPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 788 RDLALRCLVVGGDVLPVALAQRWFELGLDrrCALINAYGPTEATISSHYHRVQAIDAS-RPVPLGQLLPGRIAAVLDAHG 866
Cdd:cd12114 241 LLPSLRLVLLSGDWIPLDLPARLRALAPD--ARLISLGGATEASIWSIYHPIDEVPPDwRSIPYGRPLANQRYRVLDPRG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 867 RIVPRGVCGELALGGIGLAEGYRGDAAASERRFapLRLPSGEslRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIEL 946
Cdd:cd12114 319 RDCPDWVPGELWIGGRGVALGYLGDPELTAARF--VTHPDGE--RLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIEL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 947 EEIEHCLGQLPQVRAAAAGVVGEGAAQRLVAWVECagedgfgqadlnQTDSDQTESERWHRALCERLPAYMVPTQFVALP 1026
Cdd:cd12114 395 GEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVP------------DNDGTPIAPDALRAFLAQTLPAYMIPSRVIALE 462
|
490
....*....|....*
gi 1246793773 1027 RLPRNASGKIDRRAL 1041
Cdd:cd12114 463 ALPLTANGKVDRAAL 477
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
549-1041 |
1.37e-92 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 309.56 E-value: 1.37e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 549 PERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVV 628
Cdd:cd05945 5 PDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 629 AASGCDAVLTDaqglagfapsvaiavdelkldgagengsgenaaPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAE 708
Cdd:cd05945 85 DAAKPALLIAD---------------------------------GDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 709 ALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARPDELLE-PQRFLAFLSERAITVTDLAPAYAnELVRASVADDW 787
Cdd:cd05945 132 DFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATAdPKQLFRFLAEHGITVWVSTPSFA-AMCLLSPTFTP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 788 RDLA-LRCLVVGGDVLPVALAQRWFELGLDRRcaLINAYGPTEATISSHYHRVQA--IDASRPVPLGQLLPGRIAAVLDA 864
Cdd:cd05945 211 ESLPsLRHFLFCGEVLPHKTARALQQRFPDAR--IYNTYGPTEATVAVTYIEVTPevLDGYDRLPIGYAKPGAKLVILDE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 865 HGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPlrlpsGESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRI 944
Cdd:cd05945 289 DGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFP-----DEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRI 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 945 ELEEIEHCLGQLPQVRAAAAGVVGEG-AAQRLVAWVEcaGEDGFGQADLNqtdsdqteseRWHRALCERLPAYMVPTQFV 1023
Cdd:cd05945 364 ELEEIEAALRQVPGVKEAVVVPKYKGeKVTELIAFVV--PKPGAEAGLTK----------AIKAELAERLPPYMIPRRFV 431
|
490
....*....|....*...
gi 1246793773 1024 ALPRLPRNASGKIDRRAL 1041
Cdd:cd05945 432 YLDELPLNANGKIDRKAL 449
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
2051-2522 |
6.97e-92 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 307.76 E-value: 6.97e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLD 2130
Cdd:cd17649 2 DAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2131 DSGARIVIGwgaapawvpasvrwldaesvldvvsayEEPprvdvdaDTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVL 2210
Cdd:cd17649 82 DSGAGLLLT---------------------------HHP-------RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2211 PVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTA 2290
Cdd:cd17649 128 ERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2291 ---VLPRECLVTGGEALTGALVQqvRALAPTLRIVNHYGPTETTVGILTCTVPEE----WPVeqgVPVGHPLAGNEAWVL 2363
Cdd:cd17649 208 dgrPPSLRLYIFGGEALSPELLR--RWLKAPVRLFNAYGPTEATVTPLVWKCEAGaaraGAS---MPIGRPLGGRSAYIL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2364 DRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPL-APDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYR 2442
Cdd:cd17649 283 DADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2443 VELGEVEQVLAQLPGVEVAAVLALPGANG-------VLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNG 2515
Cdd:cd17649 363 IELGEIEAALLEHPGVREAAVVALDGAGGkqlvayvVLRAAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNG 442
|
....*..
gi 1246793773 2516 KIDRQAL 2522
Cdd:cd17649 443 KLDRKAL 449
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
2050-2522 |
1.04e-91 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 307.25 E-value: 1.04e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2050 AQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVL 2129
Cdd:cd05945 5 PDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 DDSGARIVIgwgaapawvpasvrwldaesvldvvsayeepprvdVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGV 2209
Cdd:cd05945 85 DAAKPALLI-----------------------------------ADGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWM 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2210 LPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGT 2289
Cdd:cd05945 130 LSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2290 -AVLPRecLVT---GGEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPEEwPVEQG--VPVGHPLAGNEAWVL 2363
Cdd:cd05945 210 pESLPS--LRHflfCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIEVTPE-VLDGYdrLPIGYAKPGAKLVIL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2364 DRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPlapDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRV 2443
Cdd:cd05945 287 DEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE---GQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRI 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2444 ELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQGS-------LEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGK 2516
Cdd:cd05945 364 ELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKpgaeaglTKAIKAELAERLPPYMIPRRFVYLDELPLNANGK 443
|
....*.
gi 1246793773 2517 IDRQAL 2522
Cdd:cd05945 444 IDRKAL 449
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
2628-3043 |
3.30e-91 |
|
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380457 [Multi-domain] Cd Length: 428 Bit Score: 304.95 E-value: 3.30e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2628 FGLTPIQHWFFEQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARFQRDAaGQWQQTLGDWQADRFAHR- 2706
Cdd:cd19534 2 VPLTPIQRWFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRRED-GGWQQRIRGDVEELFRLEv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2707 -----EADAGQREDLLAQWQAGLS-FDGALLRVlALPDPQDGDTRVLFAAHHLLVDAVSWGIIVDDLQHAYAERRAGRSP 2780
Cdd:cd19534 81 vdlssLAQAAAIEALAAEAQSSLDlEEGPLLAA-ALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2781 ALAAEAcGFGAWQAALRQLSA-ATLDGWRSYWRAQAADAEAIaLPwQDSDNRYADTVHLHDRFERDWTERLLTQTARAYG 2859
Cdd:cd19534 160 PLPSKT-SFQTWAELLAEYAQsPALLEELAYWRELPAADYWG-LP-KDPEQTYGDARTVSFTLDEEETEALLQEANAAYR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2860 NEPQEVLLTALALALRDGGDAATLWVEMEGHGRDDLGAGLDLSRTVGWFTARYPLALHLPAGEDLGAALRSTKDRMRAVP 2939
Cdd:cd19534 237 TEINDLLLAALALAFQDWTGRAPPAIFLEGHGREEIDPGLDLSRTVGWFTSMYPVVLDLEASEDLGDTLKRVKEQLRRIP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2940 DRGLGFGVLRYLHGE----LAELPVPQVCFNYLGQLRAGERDGWALCEEPDGGGRAGGNRR--RHLLDVNAMLVDGELRL 3013
Cdd:cd19534 317 NKGIGYGILRYLTPEgtkrLAFHPQPEISFNYLGQFDQGERDDALFVSAVGGGGSDIGPDTprFALLDINAVVEGGQLVI 396
|
410 420 430
....*....|....*....|....*....|
gi 1246793773 3014 DWAWPQDAASREAMQALSRRYLAVLRELIA 3043
Cdd:cd19534 397 TVSYSRNMYHEETIQQLADSYKEALEALIE 426
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
549-1042 |
1.29e-90 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 303.41 E-value: 1.29e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 549 PERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVV 628
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 629 AASGCDAVLTDaqglagfapsvaiavdelkldgagengsgenaaPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAE 708
Cdd:cd17652 81 ADARPALLLTT---------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 709 ALALSADDRVLHVAGLAVDTTLEQILAAWSRGAC-VVARPDELLEPQRFLAFLSERAITVTDLAPAYANELVRASVaddw 787
Cdd:cd17652 128 AFDVGPGSRVLQFASPSFDASVWELLMALLAGATlVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPDDL---- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 788 rdLALRCLVVGGDVLPVALAQRWfelGLDRRcaLINAYGPTEATISSHYHRVQAidASRPVPLGQLLPGRIAAVLDAHGR 867
Cdd:cd17652 204 --PDLRTLVVAGEACPAELVDRW---APGRR--MINAYGPTETTVCATMAGPLP--GGGVPPIGRPVPGTRVYVLDARLR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 868 IVPRGVCGELALGGIGLAEGYRGDAAASERRFA--PLRLPSGeslRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIE 945
Cdd:cd17652 275 PVPPGVPGELYIAGAGLARGYLNRPGLTAERFVadPFGAPGS---RMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIE 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 946 LEEIEHCLGQLPQVRAAAAGVVGEGAA-QRLVAWVECAGEDGFGQADLNQtdsdqteserwhrALCERLPAYMVPTQFVA 1024
Cdd:cd17652 352 LGEVEAALTEHPGVAEAVVVVRDDRPGdKRLVAYVVPAPGAAPTAAELRA-------------HLAERLPGYMVPAAFVV 418
|
490
....*....|....*...
gi 1246793773 1025 LPRLPRNASGKIDRRALP 1042
Cdd:cd17652 419 LDALPLTPNGKLDRRALP 436
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
549-1041 |
1.86e-90 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 303.46 E-value: 1.86e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 549 PERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVV 628
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 629 AASGCDAVLTDaqglagfapsvaiavdelkldgagengsgenaaPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAE 708
Cdd:cd17643 81 ADSGPSLLLTD---------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 709 ALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARPDEL-LEPQRFLAFLSERAITVTDLAPAYANELVRASVADDW 787
Cdd:cd17643 128 WFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVaRSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 788 RDLALRCLVVGGDVLPVALAQRWFELGLDRRCALINAYGPTEATISSHYHRVQAIDASRP--VPLGQLLPGRIAAVLDAH 865
Cdd:cd17643 208 DPLALRYVIFGGEALEAAMLRPWAGRFGLDRPQLVNMYGITETTVHVTFRPLDAADLPAAaaSPIGRPLPGLRVYVLDAD 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 866 GRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRlPSGESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIE 945
Cdd:cd17643 288 GRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANP-FGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 946 LEEIEHCLGQLPQVRAAAAGV-VGEGAAQRLVAWVECAGEDGFGQADLnqtdsdqteserwHRALCERLPAYMVPTQFVA 1024
Cdd:cd17643 367 LGEIEAALATHPSVRDAAVIVrEDEPGDTRLVAYVVADDGAAADIAEL-------------RALLKELLPDYMVPARYVP 433
|
490
....*....|....*..
gi 1246793773 1025 LPRLPRNASGKIDRRAL 1041
Cdd:cd17643 434 LDALPLTVNGKLDRAAL 450
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
88-507 |
1.61e-89 |
|
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380461 [Multi-domain] Cd Length: 432 Bit Score: 299.95 E-value: 1.61e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 88 APLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQGEDSVAAGGGAAVESADLR-- 165
Cdd:cd19538 2 IPLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEATPKle 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 166 ------GRGQDEIDALVEgfrlRPFELQRQRPLRMQLLRLdgqgdGPVRHWLQVVVHHIACDGVSLGLLTQDLSRAYRVE 239
Cdd:cd19538 82 ikevdeEELESEINEAVR----YPFDLSEEPPFRATLFEL-----GENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 240 CGLAAEPAPPLPCQYGDYARWQRDTL-------DRLDASLRHHVEALSGAPHLHELPLDHERPAVLGQSGAKLRLAFPPG 312
Cdd:cd19538 153 CKGEAPELAPLPVQYADYALWQQELLgdesdpdSLIARQLAYWKKQLAGLPDEIELPTDYPRPAESSYEGGTLTFEIDSE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 313 LSERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDDPDFASLVAR 392
Cdd:cd19538 233 LHQQLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLER 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 393 CRDHQLAALEHQALPLERVIETLQVERSSRHAPLFQLMFALRHDADLALDLHGVQAHALTLPEDVAKHELTLEV-----L 467
Cdd:cd19538 313 VKETNLEAYEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPSLDLPGLEAKLELRTVGSAKFDLTFELreqynD 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1246793773 468 VGAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENP 507
Cdd:cd19538 393 GTPNGIEGFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
549-1044 |
1.33e-87 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 296.93 E-value: 1.33e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 549 PERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVV 628
Cdd:cd17655 11 PDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYIL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 629 AASGCDAVLTDAQGLAGFAPSVAIAVDElklDGAGENGSGENAAP----NQLAYILYTSGSTGIPKGVEVGHAALAAHID 704
Cdd:cd17655 91 EDSGADILLTQSHLQPPIAFIGLIDLLD---EDTIYHEESENLEPvsksDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 705 AAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGAC-VVARPDELLEPQRFLAFLSERAITVTDLAPAYANELVRAsv 783
Cdd:cd17655 168 WANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTlYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLKLLDAA-- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 784 aDDWRDLALRCLVVGGDVLPVALAQRWFELGLDRrCALINAYGPTEATISSHYHRVQAIDASRP-VPLGQLLPGRIAAVL 862
Cdd:cd17655 246 -DDSEGLSLKHLIVGGEALSTELAKKIIELFGTN-PTITNAYGPTETTVDASIYQYEPETDQQVsVPIGKPLGNTRIYIL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 863 DAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGEslRMYRSGDRVRLLDDGELQFLGRADFQVKLRGY 942
Cdd:cd17655 324 DQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGE--RMYRTGDLARWLPDGNIEFLGRIDHQVKIRGY 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 943 RIELEEIEHCLGQLPQVRAAAAGVV-GEGAAQRLVAWVecAGEDGFGQADLNQTdsdqteserwhraLCERLPAYMVPTQ 1021
Cdd:cd17655 402 RIELGEIEARLLQHPDIKEAVVIARkDEQGQNYLCAYI--VSEKELPVAQLREF-------------LARELPDYMIPSY 466
|
490 500
....*....|....*....|...
gi 1246793773 1022 FVALPRLPRNASGKIDRRALPAP 1044
Cdd:cd17655 467 FIKLDEIPLTPNGKVDRKALPEP 489
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
537-1041 |
8.14e-87 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 294.06 E-value: 8.14e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 537 VVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLD 616
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 617 TEWPQARRAEVVAASGCDAVLTDAqglagfapsvaiavdelkldgagengsgenaaPNQLAYILYTSGSTGIPKGVEVGH 696
Cdd:cd05918 81 PSHPLQRLQEILQDTGAKVVLTSS--------------------------------PSDAAYVIFTSGSTGKPKGVVIEH 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 697 AALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARPDELLePQRFLAFLSERAITVTDLAPAYAN 776
Cdd:cd05918 129 RALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDR-LNDLAGFINRLRVTWAFLTPSVAR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 777 ELVRASVADdwrdlaLRCLVVGGDVLPVALAQRWFElgldrRCALINAYGPTEATISSHYHRVqaIDASRPVPLGQLLPG 856
Cdd:cd05918 208 LLDPEDVPS------LRTLVLGGEALTQSDVDTWAD-----RVRLINAYGPAECTIAATVSPV--VPSTDPRNIGRPLGA 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 857 RiAAVLDA--HGRIVPRGVCGELALGGIGLAEGYRGDAAASERRF-----APLRLPSGESLRMYRSGDRVRLLDDGELQF 929
Cdd:cd05918 275 T-CWVVDPdnHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFiedpaWLKQEGSGRGRRLYRTGDLVRYNPDGSLEY 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 930 LGRADFQVKLRGYRIELEEIEHCLGQ-LPQVRAAAAGVV---GEGAAQRLVAWVECAGEDGFGQAD----LNQTDSDQTE 1001
Cdd:cd05918 354 VGRKDTQVKIRGQRVELGEIEHHLRQsLPGAKEVVVEVVkpkDGSSSPQLVAFVVLDGSSSGSGDGdslfLEPSDEFRAL 433
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1246793773 1002 SERWHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05918 434 VAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
2051-2522 |
1.59e-83 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 284.55 E-value: 1.59e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLD 2130
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2131 DSGARIVIGWGAAPAWVPASVRWLDAESVLDVVSAyeEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVL 2210
Cdd:cd12114 82 DAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPA--PPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDIN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2211 PVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTA 2290
Cdd:cd12114 160 RRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2291 VLPR--ECLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTC---TVPEEWPVeqgVPVGHPLAGNEAWVLDR 2365
Cdd:cd12114 240 ALLPslRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHpidEVPPDWRS---IPYGRPLANQRYRVLDP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2366 FGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPlaPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVEL 2445
Cdd:cd12114 317 RGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIEL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2446 GEVEQVLAQLPGVEVAAVLALPGANG------VLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDR 2519
Cdd:cd12114 395 GEIEAALQAHPGVARAVVVVLGDPGGkrlaafVVPDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDR 474
|
...
gi 1246793773 2520 QAL 2522
Cdd:cd12114 475 AAL 477
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
539-1041 |
6.96e-83 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 281.51 E-value: 6.96e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 539 DAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTE 618
Cdd:cd12115 3 DLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 619 WPQARRAEVVAASGCDAVLTDaqglagfapsvaiavdelkldgagengsgenaaPNQLAYILYTSGSTGIPKGVEVGHAA 698
Cdd:cd12115 83 YPPERLRFILEDAQARLVLTD---------------------------------PDDLAYVIYTSGSTGRPKGVAIEHRN 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 699 LAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVarpdeLLEPQRFLAFLSERA-ITVTDLAPAYANE 777
Cdd:cd12115 130 AAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVV-----LADNVLALPDLPAAAeVTLINTVPSAAAE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 778 LVRASVADDwrdlALRCLVVGGDVLPVALAQRWFELGLDRRcaLINAYGPTEATISSHYHRVQAiDASRPVPLGQLLPGR 857
Cdd:cd12115 205 LLRHDALPA----SVRVVNLAGEPLPRDLVQRLYARLQVER--VVNLYGPSEDTTYSTVAPVPP-GASGEVSIGRPLANT 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 858 IAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGEslRMYRSGDRVRLLDDGELQFLGRADFQV 937
Cdd:cd12115 278 QAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGA--RLYRTGDLVRWRPDGLLEFLGRADNQV 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 938 KLRGYRIELEEIEHCLGQLPQVRAAAAGVVGEGAAQR-LVAWVECAGEDGFGQADLNQTdsdqteserwhraLCERLPAY 1016
Cdd:cd12115 356 KVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERrLVAYIVAEPGAAGLVEDLRRH-------------LGTRLPAY 422
|
490 500
....*....|....*....|....*
gi 1246793773 1017 MVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd12115 423 MVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
539-1041 |
6.38e-82 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 278.04 E-value: 6.38e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 539 DAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTE 618
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 619 WPQARRAEVVAASGCDAVLTdaqglagfapsvaiavdelkldgagengsgeNAAPNQLAYILYTSGSTGIPKGVEVGHAA 698
Cdd:cd17653 81 LPSARIQAILRTSGATLLLT-------------------------------TDSPDDLAYIIFTSGSTGIPKGVMVPHRG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 699 LAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVarpdeLLEPQRFLAFLSeRAITVTDLAPAYANEL 778
Cdd:cd17653 130 VLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLV-----LADPSDPFAHVA-RTVDALMSTPSILSTL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 779 VRASVADdwrdlaLRCLVVGGDVLPVALAQRWFElgldRRCaLINAYGPTEATISSHYHRVQAIDasrPVPLGQLLPGRI 858
Cdd:cd17653 204 SPQDFPN------LKTIFLGGEAVPPSLLDRWSP----GRR-LYNAYGPTECTISSTMTELLPGQ---PVTIGKPIPNST 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 859 AAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGEslRMYRSGDRVRLLDDGELQFLGRADFQVK 938
Cdd:cd17653 270 CYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGS--RMYRTGDYGRWTEDGGLEFLGREDNQVK 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 939 LRGYRIELEEIEHCLGQL-PQVRAAAAGVVGegaaQRLVAWVECAGEDGfgqadlnqtdsDQTESErwhraLCERLPAYM 1017
Cdd:cd17653 348 VRGFRINLEEIEEVVLQSqPEVTQAAAIVVN----GRLVAFVTPETVDV-----------DGLRSE-----LAKHLPSYA 407
|
490 500
....*....|....*....|....
gi 1246793773 1018 VPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd17653 408 VPDRIIALDSFPLTANGKVDRKAL 431
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
88-507 |
1.24e-80 |
|
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380462 [Multi-domain] Cd Length: 427 Bit Score: 274.26 E-value: 1.24e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 88 APLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQGEDS------VAAGGGAAVES 161
Cdd:cd19539 2 IPLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGgvprqeILPPGPAPLEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 162 ADLRGRGQD---EIDALVEGFRLRPFELQRQRPLRMQLLRldgqgDGPVRHWLQVVVHHIACDGVSLGLLTQDLSRAYRV 238
Cdd:cd19539 82 RDLSDPDSDrerRLEELLRERESRGFDLDEEPPIRAVLGR-----FDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 239 ECGLAAEPAPPLPCQYGDYARWQRDTL--DRLDASLRHHVEALSGAPHLHeLPLDHERPAVLGQSGAKLRLAFPPGLSER 316
Cdd:cd19539 157 RRKGPAAPLPELRQQYKEYAAWQREALaaPRAAELLDFWRRRLRGAEPTA-LPTDRPRPAGFPYPGADLRFELDAELVAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 317 VAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDDPDFASLVARCRDH 396
Cdd:cd19539 236 LRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 397 QLAALEHQALPLERVIETLQVERSSRHAPLFQLMFALRHDADLALDLHG-VQAHALTLPEDVAKHELTLEVLVGAGGMSA 475
Cdd:cd19539 316 LVDAQRHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGELELAGgLSYTEGSDIPDGAKFDLNLTVTEEGTGLRG 395
|
410 420 430
....*....|....*....|....*....|..
gi 1246793773 476 VWEYNTALWNPATVARWAERYFVALAAMLENP 507
Cdd:cd19539 396 SLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
2052-2524 |
1.39e-80 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 274.19 E-value: 1.39e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDD 2131
Cdd:cd17653 13 AVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVIgwgaapawVPASvrwldaesvldvvsayeepprvdvdADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLP 2211
Cdd:cd17653 93 SGATLLL--------TTDS-------------------------PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2212 VLDLGEDASLATLSTVAADLGFTALFGALLSGrrvrllpAELAFDAQALAAHLQAHPVDCLKIVPShlagllaaagGTAV 2291
Cdd:cd17653 140 RLDVGPGSRVAQVLSIAFDACIGEIFSTLCNG-------GTLVLADPSDPFAHVARTVDALMSTPS----------ILST 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2292 LPR------ECLVTGGEALTGALVqqvRALAPTLRIVNHYGPTETTVgilTCTVPEEWPVEQgVPVGHPLAGNEAWVLDR 2365
Cdd:cd17653 203 LSPqdfpnlKTIFLGGEAVPPSLL---DRWSPGRRLYNAYGPTECTI---SSTMTELLPGQP-VTIGKPIPNSTCYILDA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2366 FGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVEL 2445
Cdd:cd17653 276 DLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINL 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2446 GEVEQVLAQL-PGVEVAAVLAlpgANGVLQLGACIQGS-LEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALA 2523
Cdd:cd17653 356 EEIEEVVLQSqPEVTQAAAIV---VNGRLVAFVTPETVdVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALR 432
|
.
gi 1246793773 2524 D 2524
Cdd:cd17653 433 E 433
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
537-1043 |
3.02e-80 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 273.99 E-value: 3.02e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 537 VVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLD 616
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 617 TEWPQARRAEVVAASGCDAVLTdaqglagfapsvaiavdelkldgagengsgenaapnqlAYILYTSGSTGIPKGVEVGH 696
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT--------------------------------------ALILYTSGTTGRPKGVMLTH 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 697 AALAAHIDAAAEALALSADDRVL------HVAGLAVdttleQILAAWSRGACVVARPDelLEPQRFLAFLSERAITVTDL 770
Cdd:COG0318 123 RNLLANAAAIAAALGLTPGDVVLvalplfHVFGLTV-----GLLAPLLAGATLVLLPR--FDPERVLELIERERVTVLFG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 771 APAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFE-LGldrrCALINAYGPTEATISSHYHRVQAIDAsRPVP 849
Cdd:COG0318 196 VPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEErFG----VRIVEGYGLTETSPVVTVNPEDPGER-RPGS 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 850 LGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPlrlpsgeslRMYRSGDRVRLLDDGELQF 929
Cdd:COG0318 271 VGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRD---------GWLRTGDLGRLDEDGYLYI 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 930 LGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQRLVAWVECAGEDGFGQADLnqtdsdqteserwHRA 1008
Cdd:COG0318 342 VGRKKDMIISGGENVYPAEVEEVLAAHPGVAeAAVVGVPDEKWGERVVAFVVLRPGAELDAEEL-------------RAF 408
|
490 500 510
....*....|....*....|....*....|....*
gi 1246793773 1009 LCERLPAYMVPTQFVALPRLPRNASGKIDRRALPA 1043
Cdd:COG0318 409 LRERLARYKVPRRVEFVDELPRTASGKIDRRALRE 443
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
3078-3481 |
3.24e-80 |
|
Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.
Pssm-ID: 395541 [Multi-domain] Cd Length: 454 Bit Score: 274.21 E-value: 3.24e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3078 QDVYPLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFAVQGLPSPRQ--LPHRQVS 3155
Cdd:pfam00668 2 QDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQviLEERPFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3156 LPLAE-QDWSGLEPAQARSRLSELQAQQceaGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLY 3234
Cdd:pfam00668 82 LEIIDiSDLSESEEEEAIEAFIQRDLQS---PFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3235 AALRESRTPQLPAAPPFRDYLHWLR----GQDEAAARAFWREQLTGLEP-AALPE-ATEPAEG-YASSTRRFDLAAASA- 3306
Cdd:pfam00668 159 QQLLKGEPLPLPPKTPYKDYAEWLQqylqSEDYQKDAAYWLEQLEGELPvLQLPKdYARPADRsFKGDRLSFTLDEDTEe 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3307 ----WAQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRPpeLAGVERMLGVFINSVPLRVTPAGEATPAPWLQAL 3382
Cdd:pfam00668 239 llrkLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRP--SPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3383 QQRNLDLRTHGYLPLAQIQR----AGAADAVSPFDVLLVFENLP------TESREERSGMRIEELDHRAhSNYPLMLTAI 3452
Cdd:pfam00668 317 QEDLLSAEPHQGYPFGDLVNdlrlPRDLSRHPLFDPMFSFQNYLgqdsqeEEFQLSELDLSVSSVIEEE-AKYDLSLTAS 395
|
410 420 430
....*....|....*....|....*....|....*.
gi 1246793773 3453 PDAGGLRIE-----AALDRSKLDGWL--VEQMLDDL 3481
Cdd:pfam00668 396 ERGGGLTIKidyntSLFDEETIERFAehFKELLEQA 431
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
2050-2533 |
5.95e-80 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 273.22 E-value: 5.95e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2050 AQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVL 2129
Cdd:COG0318 13 PDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 DDSGARIVIGwgaapawvpasvrwldaesvldvvsayeepprvdvdadtpAYLIYTSGSTGTPKGVVVSQGNLANYVAGV 2209
Cdd:COG0318 93 EDSGARALVT----------------------------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2210 LPVLDLGEDASLATLSTVAADLGFTA-LFGALLSGRRVRLLPAelaFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGG 2288
Cdd:COG0318 133 AAALGLTPGDVVLVALPLFHVFGLTVgLLAPLLAGATLVLLPR---FDPERVLELIERERVTVLFGVPTMLARLLRHPEF 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2289 TAV-LPR-ECLVTGGEALTGALVQQVRALAPTlRIVNHYGPTETTVgiLTCTVPEEWPVEQGVPVGHPLAGNEAWVLDRF 2366
Cdd:COG0318 210 ARYdLSSlRLVVSGGAPLPPELLERFEERFGV-RIVEGYGLTETSP--VVTVNPEDPGERRPGSVGRPLPGVEVRIVDED 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2367 GLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHplapdrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELG 2446
Cdd:COG0318 287 GRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDG-------WLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPA 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2447 EVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQ------GSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQ 2520
Cdd:COG0318 360 EVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVlrpgaeLDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRR 439
|
490
....*....|...
gi 1246793773 2521 ALADLLQQDDADS 2533
Cdd:COG0318 440 ALRERYAAGALEA 452
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
2051-2522 |
7.02e-80 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 273.54 E-value: 7.02e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLD 2130
Cdd:cd17644 15 DAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYILE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2131 DSGARIVIgwgaapawvpasvrwldaesvldvvsayeepprvdVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVL 2210
Cdd:cd17644 95 DAQISVLL-----------------------------------TQPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2211 PVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPS--HLAGLLAAAGG 2288
Cdd:cd17644 140 KEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAywHLLVLELLLST 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2289 TAVL--PRECLVtGGEALTGALVQQ-VRALAPTLRIVNHYGPTETTVGILTC--TVPEEWPVEQgVPVGHPLAGNEAWVL 2363
Cdd:cd17644 220 IDLPssLRLVIV-GGEAVQPELVRQwQKNVGNFIQLINVYGPTEATIAATVCrlTQLTERNITS-VPIGRPIANTQVYIL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2364 DRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLA--PDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGY 2441
Cdd:cd17644 298 DENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNssESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2442 RVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI------QGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNG 2515
Cdd:cd17644 378 RIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIvphyeeSPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNG 457
|
....*..
gi 1246793773 2516 KIDRQAL 2522
Cdd:cd17644 458 KIDRRAL 464
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
549-1042 |
1.10e-79 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 272.77 E-value: 1.10e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 549 PERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARraevv 628
Cdd:cd17644 14 PDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQER----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 629 aasgCDAVLTDAQglagfapsVAIAVDElkldgagengsgenaaPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAE 708
Cdd:cd17644 89 ----LTYILEDAQ--------ISVLLTQ----------------PENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 709 ALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARPDELL-EPQRFLAFLSERAITVTDLAPAYANELVRASVADDW 787
Cdd:cd17644 141 EYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRsSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 788 R-DLALRCLVVGGDVLPVALAQRWFELgLDRRCALINAYGPTEATISSHYHRVQAI--DASRPVPLGQLLPGRIAAVLDA 864
Cdd:cd17644 221 DlPSSLRLVIVGGEAVQPELVRQWQKN-VGNFIQLINVYGPTEATIAATVCRLTQLteRNITSVPIGRPIANTQVYILDE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 865 HGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRI 944
Cdd:cd17644 300 NLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 945 ELEEIEHCLGQLPQVRAAAAgVVGEGAA--QRLVAWVecagedgfgQADLNQTDSdqteSERWHRALCERLPAYMVPTQF 1022
Cdd:cd17644 380 ELGEIEAVLSQHNDVKTAVV-IVREDQPgnKRLVAYI---------VPHYEESPS----TVELRQFLKAKLPDYMIPSAF 445
|
490 500
....*....|....*....|
gi 1246793773 1023 VALPRLPRNASGKIDRRALP 1042
Cdd:cd17644 446 VVLEELPLTPNGKIDRRALP 465
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
2052-2522 |
1.79e-79 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 272.81 E-value: 1.79e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDD 2131
Cdd:cd17656 4 AVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVIgwgaAPAWVPASVRWLDAESVLDVVSAYEEPP---RVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAG 2208
Cdd:cd17656 84 SGVRVVL----TQRHLKSKLSFNKSTILLEDPSISQEDTsniDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2209 VLPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLkIVPSHLAGLLAAAGG 2288
Cdd:cd17656 160 EREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVV-FLPVAFLKFIFSERE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2289 TAVLPRECL---VTGGEAL--TGALVQQVRALAPTLRivNHYGPTETTVgILTCTVPEEWPVEQGVPVGHPLAGNEAWVL 2363
Cdd:cd17656 239 FINRFPTCVkhiITAGEQLviTNEFKEMLHEHNVHLH--NHYGPSETHV-VTTYTINPEAEIPELPPIGKPISNTWIYIL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2364 DRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRV 2443
Cdd:cd17656 316 DQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2444 ELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGA--CIQGSL--EGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDR 2519
Cdd:cd17656 396 ELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAyfVMEQELniSQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDR 475
|
...
gi 1246793773 2520 QAL 2522
Cdd:cd17656 476 KAL 478
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
2052-2528 |
1.79e-78 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 269.80 E-value: 1.79e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDD 2131
Cdd:cd05918 15 APAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHPLQRLQEILQD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVIgwgaapawvpasvrwldaesvldvVSayeepprvdvDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLP 2211
Cdd:cd05918 95 TGAKVVL------------------------TS----------SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2212 VLDLGEDASLATLSTVAADLGFTALFGALLSG----------RRVRLLPAELAFDaqalaahlqahpVDCLKIVPShlag 2281
Cdd:cd05918 141 ALGLTSESRVLQFASYTFDVSILEIFTTLAAGgclcipseedRLNDLAGFINRLR------------VTWAFLTPS---- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2282 llaaaggTAVL--PREC-----LVTGGEALTGALVQQvraLAPTLRIVNHYGPTETTVGiltCTVPEEWPVEQGVPVGHP 2354
Cdd:cd05918 205 -------VARLldPEDVpslrtLVLGGEALTQSDVDT---WADRVRLINAYGPAECTIA---ATVSPVVPSTDPRNIGRP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2355 LAGNeAWVLDRF--GLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHP-------LAPDRLLYRSGDLARLDGEGR 2425
Cdd:cd05918 272 LGAT-CWVVDPDnhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVRYNPDGS 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2426 IVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVE---VAAVLALPGANGVLQLGACIQGS-------------------- 2482
Cdd:cd05918 351 LEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAkevVVEVVKPKDGSSSPQLVAFVVLDgsssgsgdgdslflepsdef 430
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1246793773 2483 ---LEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLLQQ 2528
Cdd:cd05918 431 ralVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAES 479
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
3520-4010 |
2.29e-78 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 270.61 E-value: 2.29e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRV---GLCLPrgcDLLVALLAILKTGAAY 3596
Cdd:PRK04813 3 DIIETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIivfGHMSP---EMLATFLGAVKAGHAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3597 VPVDPHAPAARRGFILEdsgvclsVSQRAL--AVElpgtalclDDPFTRAQLDAVEPGELPEVPTEAPA----------- 3663
Cdd:PRK04813 80 IPVDVSSPAERIEMIIE-------VAKPSLiiATE--------ELPLEILGIPVITLDELKDIFATGNPydfdhavkgdd 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3664 --YLIYTSGSTGTPKGVVVTHRNVERlFTAaTQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQ 3741
Cdd:PRK04813 145 nyYIIFTSGTTGKPKGVQISHDNLVS-FTN-WMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTAN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3742 PDAFLDLLAEYGVTVLNQTPS-AFYALQSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHV 3820
Cdd:PRK04813 223 FKQLFETLPQLPINVWVSTPSfADMCLLDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATVAV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3821 SFHRLSDEDL-QSPTSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGGQRFYRSGD 3899
Cdd:PRK04813 303 TSIEITDEMLdQYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTFDGQPAYHTGD 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3900 LGrYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDA-AVTVEGQGEGAWLMAYAVAADGA-EPDPQ---SL 3974
Cdd:PRK04813 383 AG-YLEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAvVVPYNKDHKVQYLIAYVVPKEEDfEREFEltkAI 461
|
490 500 510
....*....|....*....|....*....|....*.
gi 1246793773 3975 REALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK04813 462 KKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
3662-4006 |
4.66e-78 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 263.38 E-value: 4.66e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3662 PAYLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEavcRQ 3741
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNL--LAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK---FD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3742 PDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELAL-NVRAVVFGGEALEPSRLQPWRERyPQAELVNMYGITETTVHV 3820
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLsSLRALVSGGAPLPPELLERFEEA-PGIKLVNGYGLTETGGTV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3821 SFHRLSDEDLQSPTsrIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFveRGGqrFYRSGDL 3900
Cdd:cd04433 156 ATGPPDDDARKPGS--VGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD--EDG--WYRTGDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3901 GRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSLREALR 3979
Cdd:cd04433 230 GRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVgVPDPEWGERVVAVVVLRPGADLDAEELRAHVR 309
|
330 340
....*....|....*....|....*..
gi 1246793773 3980 ALLPDYMLPRLIQLLPALPLTANGKLD 4006
Cdd:cd04433 310 ERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
3081-3471 |
4.38e-76 |
|
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380459 [Multi-domain] Cd Length: 419 Bit Score: 260.84 E-value: 4.38e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3081 YPLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFAVQGLPSPRQLPHRQVSLPLAE 3160
Cdd:cd19536 2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQAQVPVTE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3161 QDWSGLEpaQARSRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHW-LVWTRHHLIVDGWSSALLLDEVWRLYAALRE 3239
Cdd:cd19536 82 LDLTPLE--EQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERERFlLVISDHHSILDGWSLYLLVKEILAVYNQLLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3240 SRTPQLPAAPPFRDYLHWLRGQ-DEAAARAFWREQLTGLEPAALP--EATEPAEGYASSTRRFDLAAAS---AWAQSHGL 3313
Cdd:cd19536 160 YKPLSLPPAQPYRDFVAHERASiQQAASERYWREYLAGATLATLPalSEAVGGGPEQDSELLVSVPLPVrsrSLAKRSGI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3314 TASSLLQGALALVLQRYYGRDDFALGITIAGRPPELAGVERMLGVFINSVPLRVTPAGEATpAPWLQALQQRNLDLRTHG 3393
Cdd:cd19536 240 PLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTLSEETV-EDLLKRAQEQELESLSHE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3394 YLPLAQIQRagAADAVSPFDVLLVFENLP----TESREERSGMRIEELDHRAHSNYPLMLTAIPDAGGLRIEAALDRSKL 3469
Cdd:cd19536 319 QVPLADIQR--CSEGEPLFDSIVNFRHFDldfgLPEWGSDEGMRRGLLFSEFKSNYDVNLSVLPKQDRLELKLAYNSQVL 396
|
..
gi 1246793773 3470 DG 3471
Cdd:cd19536 397 DE 398
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1139-1559 |
1.09e-74 |
|
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380457 [Multi-domain] Cd Length: 428 Bit Score: 257.18 E-value: 1.09e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1139 EVGLSPIQRWFFDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAP-AIQA 1217
Cdd:cd19534 1 EVPLTPIQRWFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEELfRLEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1218 QDWRgAADLDSRVDAAFARMQEATPLA-GPLVALTHAH-CDDGERLLICAHHLIVDAVSWRLLLGELFDGLAALARGE-- 1293
Cdd:cd19534 81 VDLS-SLAQAAAIEALAAEAQSSLDLEeGPLLAAALFDgTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEpi 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1294 AWTPSargASYADYVEALREA--DDAQRFDAGFWRELAAQPMQALPQDRPVALADARqsnvgRIVQTLDAGLTADLLERA 1371
Cdd:cd19534 160 PLPSK---TSFQTWAELLAEYaqSPALLEELAYWRELPAADYWGLPKDPEQTYGDAR-----TVSFTLDEEETEALLQEA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1372 GEAYRCRTDEVLLIALARALATRTGRNRLWLDRERHGR-DVLDGRDWSSVLGWYTAVHPLPLDLGVADGPAQ-IGALKEQ 1449
Cdd:cd19534 232 NAAYRTEINDLLLAALALAFQDWTGRAPPAIFLEGHGReEIDPGLDLSRTVGWFTSMYPVVLDLEASEDLGDtLKRVKEQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1450 IRALARRGLDYMPL-----VASARIPALPAGQLLFNYHGVVDAG--AHPAFEVEPRTLASGNGADNPPGALVEINARVQA 1522
Cdd:cd19534 312 LRRIPNKGIGYGILryltpEGTKRLAFHPQPEISFNYLGQFDQGerDDALFVSAVGGGGSDIGPDTPRFALLDINAVVEG 391
|
410 420 430
....*....|....*....|....*....|....*..
gi 1246793773 1523 GRLGLVWNYAGEAYDAATIEAWSQAFAAELAALVAHC 1559
Cdd:cd19534 392 GQLVITVSYSRNMYHEETIQQLADSYKEALEALIEHC 428
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
3529-4007 |
1.17e-74 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 257.15 E-value: 1.17e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARR 3608
Cdd:cd17631 5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3609 GFILEDSgvclsvsqralavelpGTALCLDDpftraqldavepgelpevpteaPAYLIYTSGSTGTPKGVVVTHRNVerL 3688
Cdd:cd17631 85 AYILADS----------------GAKVLFDD----------------------LALLMYTSGTTGRPKGAMLTHRNL--L 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3689 FTAATQTGRFSFDEHDVW----SLFHSHAFD-FAVWELWgawlYGGRAVLVPEAvcrQPDAFLDLLAEYGVTVLNQTPSA 3763
Cdd:cd17631 125 WNAVNALAALDLGPDDVLlvvaPLFHIGGLGvFTLPTLL----RGGTVVILRKF---DPETVLDLIERHRVTSFFLVPTM 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3764 FYALQSQAMRRELAL-NVRAVVFGGEALEPSRLQPWRERYPqaELVNMYGITETTVHVSFhrLSDEDLQsptSRIGSA-- 3840
Cdd:cd17631 198 IQALLQHPRFATTDLsSLRAVIYGGAPMPERLLRALQARGV--KFVQGYGMTETSPGVTF--LSPEDHR---RKLGSAgr 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3841 -LPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFveRGGqrFYRSGDLGRYRADGSLEYRGRGDDQV 3919
Cdd:cd17631 271 pVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF--RDG--WFHTGDLGRLDEDGYLYIVDRKKDMI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3920 KLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEGAW---LMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPA 3996
Cdd:cd17631 347 ISGGENVYPAEVEDVLYEHPAVAEVAVI--GVPDEKWgeaVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFVDA 424
|
490
....*....|.
gi 1246793773 3997 LPLTANGKLDR 4007
Cdd:cd17631 425 LPRNATGKILK 435
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
3521-4010 |
2.77e-74 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 257.49 E-value: 2.77e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3521 LVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVD 3600
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3601 PHAPAARRGFILEDSGVclsvsqralavelpgTALCLDDPFTRAQLDAVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVV 3680
Cdd:cd05936 81 PLYTPRELEHILNDSGA---------------KALIVAVSFTDLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3681 THRNverLFTAATQTGRFSFDEHD-------VWSLFHSHAFDFAvweLWGAWLYGGRAVLVPEAVcrqPDAFLDLLAEYG 3753
Cdd:cd05936 146 THRN---LVANALQIKAWLEDLLEgddvvlaALPLFHVFGLTVA---LLLPLALGATIVLIPRFR---PIGVLKEIRKHR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3754 VTVLNQTPSAFYALQSQAMRRELAL-NVRAVVFGGEALEPSRLQPWRERYpQAELVNMYGITETTVHVSFHRLSDEdlQS 3832
Cdd:cd05936 217 VTIFPGVPTMYIALLNAPEFKKRDFsSLRLCISGGAPLPVEVAERFEELT-GVPIVEGYGLTETSPVVAVNPLDGP--RK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3833 PTSrIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFveRGGqrFYRSGDLGRYRADGSLEYR 3912
Cdd:cd05936 294 PGS-IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAF--VDG--WLRTGDIGYMDEDGYFFIV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3913 GRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLI 3991
Cdd:cd05936 369 DRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVgVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQV 448
|
490
....*....|....*....
gi 1246793773 3992 QLLPALPLTANGKLDRKAL 4010
Cdd:cd05936 449 EFRDELPKSAVGKILRREL 467
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
2052-2522 |
7.86e-74 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 255.47 E-value: 7.86e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDD 2131
Cdd:cd17650 3 AIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVIgwgaapawvpasvrwldaesvldvvsayeepprvdVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLP 2211
Cdd:cd17650 83 SGAKLLL-----------------------------------TQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2212 VLDL-GEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTA 2290
Cdd:cd17650 128 EYELdSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2291 VLPR--ECLVTGGEALTGA-LVQQVRALAPTLRIVNHYGPTETTVgilTCTVPEEWPVEQG----VPVGHPLAGNEAWVL 2363
Cdd:cd17650 208 LDLSamRLLIVGSDGCKAQdFKTLAARFGQGMRIINSYGVTEATI---DSTYYEEGRDPLGdsanVPIGRPLPNTAMYVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2364 DRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRV 2443
Cdd:cd17650 285 DERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRI 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2444 ELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQGS----LEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDR 2519
Cdd:cd17650 365 ELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAatlnTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDR 444
|
...
gi 1246793773 2520 QAL 2522
Cdd:cd17650 445 RAL 447
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
3080-3453 |
3.14e-73 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.
Pssm-ID: 380469 [Multi-domain] Cd Length: 422 Bit Score: 252.62 E-value: 3.14e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3080 VYPLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFAVQGLPSPRQLPHRQVSLPLA 3159
Cdd:cd19547 1 VYPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDLAPPWA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3160 EQDWSGLEPAQARSRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAALRE 3239
Cdd:cd19547 81 LLDWSGEDPDRRAELLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3240 SRTPQLPAAPPFRDYLHWLR---GQDEAAARaFWREQLTGLEPAALPEATEPAEGYASS-----TRRFDLAAASAwAQSH 3311
Cdd:cd19547 161 GREPQLSPCRPYRDYVRWIRartAQSEESER-FWREYLRDLTPSPFSTAPADREGEFDTvvhefPEQLTRLVNEA-ARGY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3312 GLTASSLLQGALALVLQRYYGRDDFALGITIAGRPPELAGVERMLGVFINSVPLRVTPAGEATPAPWLQALQQRNLDLRT 3391
Cdd:cd19547 239 GVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDLATTAA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 3392 HGYLPLAQIQRAGAADAVSP---FDVLLVFENLPTES-REERSGMRIEELDHRAHSNYPLMLTAIP 3453
Cdd:cd19547 319 HGHVPLAQIKSWASGERLSGgrvFDNLVAFENYPEDNlPGDDLSIQIIDLHAQEKTEYPIGLIVLP 384
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
549-1041 |
7.73e-73 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 252.39 E-value: 7.73e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 549 PERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVV 628
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 629 AASGCDAVLTDaqglagfapsvaiavdelkldgagengsgenaaPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDA-AA 707
Cdd:cd17650 81 EDSGAKLLLTQ---------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAwRR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 708 EALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARPDEL-LEPQRFLAFLSERAITVTDLAPAyaneLVRASVAD- 785
Cdd:cd17650 128 EYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVkLDPAALYDLILKSRITLMESTPA----LIRPVMAYv 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 786 DWRDL---ALRCLVVGGDVLPValaqRWFELGLDR---RCALINAYGPTEATISSHYHRVQA--IDASRPVPLGQLLPGR 857
Cdd:cd17650 204 YRNGLdlsAMRLLIVGSDGCKA----QDFKTLAARfgqGMRIINSYGVTEATIDSTYYEEGRdpLGDSANVPIGRPLPNT 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 858 IAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGEslRMYRSGDRVRLLDDGELQFLGRADFQV 937
Cdd:cd17650 280 AMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGE--RMYRTGDLARWRADGNVELLGRVDHQV 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 938 KLRGYRIELEEIEHCLGQLPQVRAAAAGVVGE-GAAQRLVAWVecagedgfgqadlnqTDSDQTESERWHRALCERLPAY 1016
Cdd:cd17650 358 KIRGFRIELGEIESQLARHPAIDEAVVAVREDkGGEARLCAYV---------------VAAATLNTAELRAFLAKELPSY 422
|
490 500
....*....|....*....|....*
gi 1246793773 1017 MVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd17650 423 MIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
2047-2522 |
4.28e-72 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 250.16 E-value: 4.28e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2047 QMPAQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQI 2126
Cdd:cd17645 9 ERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2127 AVLDDSGARIVIGwgaapawvpasvrwldaesvldvvsayeepprvdvDADTPAYLIYTSGSTGTPKGVVVSQGNLANYV 2206
Cdd:cd17645 89 YMLADSSAKILLT-----------------------------------NPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLC 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2207 AGVLPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVdCLKIVPSHLAGLLAAA 2286
Cdd:cd17645 134 EWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGI-TISFLPTGAAEQFMQL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2287 GGTAVlprECLVTGGEALTgalvqqvRALAPTLRIVNHYGPTETTVgilTCTVPEEWPVEQGVPVGHPLAGNEAWVLDRF 2366
Cdd:cd17645 213 DNQSL---RVLLTGGDKLK-------KIERKGYKLVNNYGPTENTV---VATSFEIDKPYANIPIGKPIDNTRVYILDEA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2367 GLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELG 2446
Cdd:cd17645 280 LQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPG 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2447 EVEQVLAQLPGVEVAAVLALPGANGVLQLGACI----QGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:cd17645 360 EIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVtapeEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
3520-4010 |
2.94e-70 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 248.87 E-value: 2.94e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEIARRYPARIAVSaEDGE---LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAY 3596
Cdd:COG0365 13 NCLDRHAEGRGDKVALIWEG-EDGEertLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3597 VPVD----PHAPAARrgfiLEDSGV----------------------------------CLSVSQRALAVELPGtALCLD 3638
Cdd:COG0365 92 SPVFpgfgAEALADR----IEDAEAkvlitadgglrggkvidlkekvdealeelpslehVIVVGRTGADVPMEG-DLDWD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3639 DpftraqLDAVEPGELPEVPTEA--PAYLIYTSGSTGTPKGVVVTHRNVerlFTAATQTGRFSFD--EHDV--------W 3706
Cdd:COG0365 167 E------LLAAASAEFEPEPTDAddPLFILYTSGTTGKPKGVVHTHGGY---LVHAATTAKYVLDlkPGDVfwctadigW 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3707 SLFHShafdfavWELWGAWLYGGRAVLVPEAVC-RQPDAFLDLLAEYGVTVLNQTPSAFYAL--QSQAMRRELAL-NVRA 3782
Cdd:COG0365 238 ATGHS-------YIVYGPLLNGATVVLYEGRPDfPDPGRLWELIEKYGVTVFFTAPTAIRALmkAGDEPLKKYDLsSLRL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3783 VVFGGEALEPSRLQPWRERYpQAELVNMYGITETTVHVSFHRLSDEdlQSPTSrIGSALPDLAVHVLDAAGQPVPLGVVG 3862
Cdd:COG0365 311 LGSAGEPLNPEVWEWWYEAV-GVPIVDGWGQTETGGIFISNLPGLP--VKPGS-MGKPVPGYDVAVVDEDGNPVPPGEEG 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3863 ELVVEGD--GVAQGYWQRPELTAERFVERGgQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQ 3940
Cdd:COG0365 387 ELVIKGPwpGMFRGYWNDPERYRETYFGRF-PGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPA 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 3941 VSDAAVT-VEGQGEGAWLMAYAVAADGAEPDP---QSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:COG0365 466 VAEAAVVgVPDEIRGQVVKAFVVLKPGVEPSDelaKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
88-510 |
8.76e-69 |
|
Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.
Pssm-ID: 395541 [Multi-domain] Cd Length: 454 Bit Score: 241.08 E-value: 8.76e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 88 APLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLD-RCIQGEDS-----VAAGGGAAVES 161
Cdd:pfam00668 5 YPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRtVFIRQENGepvqvILEERPFELEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 162 ADLRGRGQDE----IDALVEGFRLRPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSLGLLTQDLSRAYr 237
Cdd:pfam00668 85 IDISDLSESEeeeaIEAFIQRDLQSPFDLEKGPLFRAGLFRIAEN-----RHHLLLSMHHIIVDGVSLGILLRDLADLY- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 238 vECGLAAEPAPPLPCQ-YGDYARWQRDTL--DRLDASLRHHVEALSGAPHLHELPLDHERPAVLGQSGAKLRLAFPPGLS 314
Cdd:pfam00668 159 -QQLLKGEPLPLPPKTpYKDYAEWLQQYLqsEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 315 ERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDDPDFASLVARCR 394
Cdd:pfam00668 238 ELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 395 DHQLAALEHQALPLERVIETLQVERSSRHAPLFQLMFALRHDadlalDLHGVQAHALTL----------PEDVAKHELTL 464
Cdd:pfam00668 318 EDLLSAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNY-----LGQDSQEEEFQLseldlsvssvIEEEAKYDLSL 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1246793773 465 EVLVGAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENPHEP 510
Cdd:pfam00668 393 TASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQP 438
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
3080-3487 |
1.88e-68 |
|
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380467 [Multi-domain] Cd Length: 395 Bit Score: 237.97 E-value: 1.88e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3080 VYPLAPLQEGLLFHSLLNAEAdpYINQTTVALHGALDREAFAAAWQQALERHPILRSGFAVqgLPSPRQLphrQVSLPLA 3159
Cdd:cd19545 1 IYPCTPLQEGLMALTARQPGA--YVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQ--SDSGGLL---QVVVKES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3160 EQDWSGlepaqaRSRLSELQAQQCEAGFDLAAPpLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYaalre 3239
Cdd:cd19545 74 PISWTE------STSLDEYLEEDRAAPMGLGGP-LVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAY----- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3240 sRTPQLPAAPPFRDYLHWLRGQDEAAARAFWREQLTGLEPAALPEAtePAEGY-ASSTRRFDLAAASAWAQSHGLTASSL 3318
Cdd:cd19545 142 -QGEPVPQPPPFSRFVKYLRQLDDEAAAEFWRSYLAGLDPAVFPPL--PSSRYqPRPDATLEHSISLPSSASSGVTLATV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3319 LQGALALVLQRYYGRDDFALGITIAGRPPELAGVERMLGVFINSVPLRVTPAGEATPAPWLQALQQRNLDLRTHGYLPLA 3398
Cdd:cd19545 219 LRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3399 QIQRAGAADAVSP-FDVLLVFE-NLPTESREERSGMRIEEL-DHRAHSNYPLMLTAIPDAGGLRIEAALDRSKLDGWLVE 3475
Cdd:cd19545 299 NIRRLGPDARAACnFQTLLVVQpALPSSTSESLELGIEEESeDLEDFSSYGLTLECQLSGSGLRVRARYDSSVISEEQVE 378
|
410
....*....|..
gi 1246793773 3476 QMLDDLDFVLQQ 3487
Cdd:cd19545 379 RLLDQFEHVLQQ 390
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
2051-2522 |
2.97e-67 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 236.53 E-value: 2.97e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVG-VQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVL 2129
Cdd:cd17648 2 DRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 DDSGARIVIgwgaapawvpASVRWLdaesvldvvsayeepprvdvdadtpAYLIYTSGSTGTPKGVVVSQGNLANYVAGV 2209
Cdd:cd17648 82 EDTGARVVI----------TNSTDL-------------------------AYAIYTSGTTGKPKGVLVEHGSVVNLRTSL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2210 LPVLDLG--EDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPShlaglLAAAG 2287
Cdd:cd17648 127 SERYFGRdnGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPS-----VLQQY 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2288 GTAVLPR-ECLVTGGEALTGALVQQVRALAPTlRIVNHYGPTETTVGILTCTVPEEWPVEQGVpvGHPLAGNEAWVLDRF 2366
Cdd:cd17648 202 DLARLPHlKRVDAAGEEFTAPVFEKLRSRFAG-LIINAYGPTETTVTNHKRFFPGDQRFDKSL--GRPVRNTKCYVLNDA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2367 GLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPDR--------LLYRSGDLARLDGEGRIVYLGRGDHQVKI 2438
Cdd:cd17648 279 MKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnaRLYKTGDLVRWLPSGELEYLGRNDFQVKI 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2439 RGYRVELGEVEQVLAQLPGVEVAAVLALPGANG-------------VLQLGACIQGSLEgvaEALAQRLPEYLCPSRWRA 2505
Cdd:cd17648 359 RGQRIEPGEVEAALASYPGVRECAVVAKEDASQaqsriqkylvgyyLPEPGHVPESDLL---SFLRAKLPRYMVPARLVR 435
|
490
....*....|....*..
gi 1246793773 2506 VESMPRLGNGKIDRQAL 2522
Cdd:cd17648 436 LEGIPVTINGKLDVRAL 452
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
2052-2439 |
3.47e-67 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 234.90 E-value: 3.47e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGA-ASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLD 2130
Cdd:pfam00501 11 KTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2131 DSGARIVIGWGAAPA----------WVPASVRWLDAESVLDVVSAYEE--------PPRVDVDADTPAYLIYTSGSTGTP 2192
Cdd:pfam00501 91 DSGAKVLITDDALKLeellealgklEVVKLVLVLDRDPVLKEEPLPEEakpadvppPPPPPPDPDDLAYIIYTSGTTGKP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2193 KGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGF-----TALFGALLSGRRVRLLPAELAFDAQALAAHLQAH 2267
Cdd:pfam00501 171 KGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHdfglsLGLLGPLLAGATVVLPPGFPALDPAALLELIERY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2268 PVDCLKIVPSHLAG-LLAAAGGTAVLPR-ECLVTGGEALTGALVQQVRALAPTlRIVNHYGPTETTvGILTCTVPEEWPV 2345
Cdd:pfam00501 251 KVTVLYGVPTLLNMlLEAGAPKRALLSSlRLVLSGGAPLPPELARRFRELFGG-ALVNGYGLTETT-GVVTTPLPLDEDL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2346 EQGVPVGHPLAGNEAWVLD-RFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAhplapDRlLYRSGDLARLDGEG 2424
Cdd:pfam00501 329 RSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE-----DG-WYRTGDLGRRDEDG 402
|
410
....*....|....*
gi 1246793773 2425 RIVYLGRGDHQVKIR 2439
Cdd:pfam00501 403 YLEIVGRKKDQIKLG 417
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
3529-4012 |
6.79e-67 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 237.37 E-value: 6.79e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARR 3608
Cdd:TIGR03098 10 AARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3609 GFILEDSGVCLSVSQRALAVEL-PGTALCLD------------DPFTRAQLDAVEPGELPEVPTEAP---------AYLI 3666
Cdd:TIGR03098 90 AHILADCNVRLLVTSSERLDLLhPALPGCHDlrtliivgdpahASEGHPGEEPASWPKLLALGDADPphpvidsdmAAIL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3667 YTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVcrqPDAFL 3746
Cdd:TIGR03098 170 YTSGSTGRPKGVVLSHRNL--VAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHDYLL---PRDVL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3747 DLLAEYGVTVLNQTPSAFYALQSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITEttvhvSFHR-- 3824
Cdd:TIGR03098 245 KALEKHGITGLAAVPPLWAQLAQLDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLFLMYGLTE-----AFRSty 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3825 LSDEDLQSPTSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERF---------VERGGQRFY 3895
Cdd:TIGR03098 320 LPPEEVDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFrplppfpgeLHLPELAVW 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3896 rSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSL 3974
Cdd:TIGR03098 400 -SGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFgVPDPTLGQAIVLVVTPPGGEELDRAAL 478
|
490 500 510
....*....|....*....|....*....|....*...
gi 1246793773 3975 REALRALLPDYMLPRLIQLLPALPLTANGKLDRKALPK 4012
Cdd:TIGR03098 479 LAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
541-940 |
2.88e-66 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 232.20 E-value: 2.88e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 541 IARAADEFPERAALETAQG-RLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEW 619
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGrRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 620 PQARRAEVVAASGCDAVLTD----AQGLAGFAPSVAIAVDELKLDGAGENGSG----------------ENAAPNQLAYI 679
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDdalkLEELLEALGKLEVVKLVLVLDRDPVLKEEplpeeakpadvpppppPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 680 LYTSGSTGIPKGVEVGHA----ALAAHIDAAAEALALSADDRVLHVAGLAVDTTLE-QILAAWSRGACVV-ARPDELLEP 753
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRnlvaNVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSlGLLGPLLAGATVVlPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 754 QRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFELGldrRCALINAYGPTEATIS 833
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELF---GGALVNGYGLTETTGV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 834 SHYHRVQAIDASRPVPLGQLLPGRIAAVLD-AHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFaplrlpsgESLRM 912
Cdd:pfam00501 318 VTTPLPLDEDLRSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAF--------DEDGW 389
|
410 420
....*....|....*....|....*...
gi 1246793773 913 YRSGDRVRLLDDGELQFLGRADFQVKLR 940
Cdd:pfam00501 390 YRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
1594-1978 |
3.17e-65 |
|
Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.
Pssm-ID: 395541 [Multi-domain] Cd Length: 454 Bit Score: 230.68 E-value: 3.17e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1594 IEHAFPLTPLQRGVLLESLRGDGADPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGLSVPHQIVLADAAA 1673
Cdd:pfam00668 1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1674 PWQTLDWSALDDAAQDAQLQRWLADDAAQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTA 1753
Cdd:pfam00668 81 ELEIIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1754 GAQGATLRLPPAPGFQAYLDWRER----QDLARQRGWWRERLSGYAGTAALPAPVAAAhhPVQREECER---RLSAHDSE 1826
Cdd:pfam00668 161 LLKGEPLPLPPKTPYKDYAEWLQQylqsEDYQKDAAYWLEQLEGELPVLQLPKDYARP--ADRSFKGDRlsfTLDEDTEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1827 RLRAFCRERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPpeLAGVESMVGVFINTLPLRLRIDAGQPALDLLSAL 1906
Cdd:pfam00668 239 LLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRP--SPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1907 RSQSLEVAENEAVGLGEILADSGLDAD----RLFASLLVVENFP-------AMAPAQLPFALRVRETRAANhYALTLRVS 1975
Cdd:pfam00668 317 QEDLLSAEPHQGYPFGDLVNDLRLPRDlsrhPLFDPMFSFQNYLgqdsqeeEFQLSELDLSVSSVIEEEAK-YDLSLTAS 395
|
...
gi 1246793773 1976 ERE 1978
Cdd:pfam00668 396 ERG 398
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
3547-4011 |
3.66e-64 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 226.40 E-value: 3.66e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3547 YATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVCLSVSqral 3626
Cdd:cd05934 6 YAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3627 avelpgtalclddpftraqldavepgelpevpteAPAYLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEHDVW 3706
Cdd:cd05934 82 ----------------------------------DPASILYTSGTTGPPKGVVITHANL--TFAGYYSARRFGLGEDDVY 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3707 ----SLFHSHAfdfAVWELWGAWLYGGRAVLVPEAvcrQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALNVRA 3782
Cdd:cd05934 126 ltvlPLFHINA---QAVSVLAALSVGATLVLLPRF---SASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3783 VVFGGEALePSRLQPWRERYpQAELVNMYGITETTVHVsfhrLSDEDLQSPTSRIGSALPDLAVHVLDAAGQPVPLGVVG 3862
Cdd:cd05934 200 AAYGAPNP-PELHEEFEERF-GVRLLEGYGMTETIVGV----IGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3863 ELVV---EGDGVAQGYWQRPELTAERFveRGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLP 3939
Cdd:cd05934 274 ELVIrglRGWGFFKGYYNMPEATAEAM--RNG--WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHP 349
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 3940 QVSDAAV-TVEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKALP 4011
Cdd:cd05934 350 AVREAAVvAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
3529-4010 |
1.88e-62 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 224.68 E-value: 1.88e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARR 3608
Cdd:PRK06187 16 ARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3609 GFILEDSGVCLSVSQRALAVELPGTalclddpftRAQLDAV------EPGELPEVPTEAPAY------------------ 3664
Cdd:PRK06187 96 AYILNDAEDRVVLVDSEFVPLLAAI---------LPQLPTVrtviveGDGPAAPLAPEVGEYeellaaasdtfdfpdide 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3665 -----LIYTSGSTGTPKGVVVTHRNverLFT-AATQTGRFSFDEHDVwSL-----FHSHAfdfavwelWG----AWLYGG 3729
Cdd:PRK06187 167 ndaaaMLYTSGTTGHPKGVVLSHRN---LFLhSLAVCAWLKLSRDDV-YLvivpmFHVHA--------WGlpylALMAGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3730 RAVLVPEAvcrQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALN-VRAVVFGGEALEPSRLQPWRERYpQAELV 3808
Cdd:PRK06187 235 KQVIPRRF---DPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSsLRLVIYGGAALPPALLREFKEKF-GIDLV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3809 NMYGITETTVHVSFHRLSDEDLQSPTSRI--GSALPDLAVHVLDAAGQPVP--LGVVGELVVEGDGVAQGYWQRPELTAE 3884
Cdd:PRK06187 311 QGYGMTETSPVVSVLPPEDQLPGQWTKRRsaGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPEATAE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3885 RFveRGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEGAW---LMAYA 3961
Cdd:PRK06187 391 TI--DGG--WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVI--GVPDEKWgerPVAVV 464
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1246793773 3962 VAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK06187 465 VLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
549-1042 |
2.44e-62 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 222.28 E-value: 2.44e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 549 PERAALETAQGRLSYRELLTAADARAAALRRRLGAQARS-VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEV 627
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRPDDlVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 628 VAASGCDAVLTDaqglagfapsvaiavdelkldgagengsgenaaPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAA 707
Cdd:cd17648 81 LEDTGARVVITN---------------------------------STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 708 EA--LALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARPDE-LLEPQRFLAFLSERAITVTDLAPAYAN--ELVRAS 782
Cdd:cd17648 128 ERyfGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEmRFDPDRFYAYINREKVTYLSGTPSVLQqyDLARLP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 783 vaddwrdlALRCLVVGGDVLPvalAQRWFELGLDRRCALINAYGPTEATISSHYHR---VQAIDASrpvpLGQLLPGRIA 859
Cdd:cd17648 208 --------HLKRVDAAGEEFT---APVFEKLRSRFAGLIINAYGPTETTVTNHKRFfpgDQRFDKS----LGRPVRNTKC 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 860 AVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRF------APLRLPSGESLRMYRSGDRVRLLDDGELQFLGRA 933
Cdd:cd17648 273 YVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFlpnpfqTEQERARGRNARLYKTGDLVRWLPSGELEYLGRN 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 934 DFQVKLRGYRIELEEIEHCLGQLPQVRAAA------AGVVGEGAAQRLVAWVECAgEDGFGQADLnqtdsdqtesERWHR 1007
Cdd:cd17648 353 DFQVKIRGQRIEPGEVEAALASYPGVRECAvvakedASQAQSRIQKYLVGYYLPE-PGHVPESDL----------LSFLR 421
|
490 500 510
....*....|....*....|....*....|....*
gi 1246793773 1008 AlceRLPAYMVPTQFVALPRLPRNASGKIDRRALP 1042
Cdd:cd17648 422 A---KLPRYMVPARLVRLEGIPVTINGKLDVRALP 453
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
549-1042 |
1.01e-61 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 221.19 E-value: 1.01e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 549 PERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVV 628
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 629 AASGCDAVLTDAQ--GLAGFAPSVAIAVDELKLDGAGENGSGENAApNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAA 706
Cdd:cd17656 82 LDSGVRVVLTQRHlkSKLSFNKSTILLEDPSISQEDTSNIDYINNS-DDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 707 AEALALSADDRVLHVAGLAVDTTLEQILAAW-SRGACVVARPDELLEPQRFLAFLSERAITVTDLAPAYANELvrASVAD 785
Cdd:cd17656 161 REKTNINFSDKVLQFATCSFDVCYQEIFSTLlSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFI--FSERE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 786 DWRDLA--LRCLVVGGDVLPVAlaQRWFELGLDRRCALINAYGPTEATISSHYHRVQAIDASRPVPLGQLLPGRIAAVLD 863
Cdd:cd17656 239 FINRFPtcVKHIITAGEQLVIT--NEFKEMLHEHNVHLHNHYGPSETHVVTTYTINPEAEIPELPPIGKPISNTWIYILD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 864 AHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLrlPSGESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYR 943
Cdd:cd17656 317 QEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPD--PFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 944 IELEEIEHCLGQLPQVRAAAAGVVGEGAAQRLVawveCAgedgFGQADLNQTDSDQTESerwhraLCERLPAYMVPTQFV 1023
Cdd:cd17656 395 IELGEIEAQLLNHPGVSEAVVLDKADDKGEKYL----CA----YFVMEQELNISQLREY------LAKQLPEYMIPSFFV 460
|
490
....*....|....*....
gi 1246793773 1024 ALPRLPRNASGKIDRRALP 1042
Cdd:cd17656 461 PLDQLPLTPNGKVDRKALP 479
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
3080-3488 |
1.51e-60 |
|
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380464 [Multi-domain] Cd Length: 401 Bit Score: 215.25 E-value: 1.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3080 VYPLAPLQEGLLfHSLLNAEADpYINQTTVALHGALDREAFAAAWQQALERHPILRSGFAVQGLPSP-RQLPHRQVSLPL 3158
Cdd:cd19542 1 IYPCTPMQEGML-LSQLRSPGL-YFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTfLQVVLKSLDPPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3159 AE-QDWSGLEPAQARSrlsELQAQqceagfDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYaal 3237
Cdd:cd19542 79 EEvETDEDSLDALTRD---LLDDP------TLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAY--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3238 resRTPQLPAAPPFRDYLHWLRGQDEAAARAFWREQLTGLEPAALPEAT--EPAEGYASSTRRfDLAAASAWAQSHGLTA 3315
Cdd:cd19542 147 ---NGQLLPPAPPFSDYISYLQSQSQEESLQYWRKYLQGASPCAFPSLSpkRPAERSLSSTRR-SLAKLEAFCASLGVTL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3316 SSLLQGALALVLQRYYGRDDFALGITIAGRPPELAGVERMLGVFINSVPLRVTPAGEATPAPWLQALQQRNLDLRTHGYL 3395
Cdd:cd19542 223 ASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3396 PLAQIQRA-GAADAVSPFDVLLVFENLPTESREERSGMRIEELDH-RAHSNYPLMLTAIPDAGGLRIEAALDRSKLDGWL 3473
Cdd:cd19542 303 SLREIQRAlGLWPSGTLFNTLVSYQNFEASPESELSGSSVFELSAaEDPTEYPVAVEVEPSGDSLKVSLAYSTSVLSEEQ 382
|
410
....*....|....*
gi 1246793773 3474 VEQMLDDLDFVLQQV 3488
Cdd:cd19542 383 AEELLEQFDDILEAL 397
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
3520-4010 |
1.49e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 215.92 E-value: 1.49e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPV 3599
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3600 DPHAPAARRGFILEDSGVCL------------SVSQRALAVEL-----PGTALCLDDPFTRAQlDAVEPGEL----PEVP 3658
Cdd:PRK07656 86 NTRYTADEAAYILARGDAKAlfvlglflgvdySATTRLPALEHvviceTEEDDPHTEKMKTFT-DFLAAGDPaeraPEVD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3659 TEAPAYLIYTSGSTGTPKGVVVTHRNverLFTAATQTG-RFSFDEHD----VWSLFhsHAFDFAVweLWGAWLYGGrAVL 3733
Cdd:PRK07656 165 PDDVADILFTSGTTGRPKGAMLTHRQ---LLSNAADWAeYLGLTEGDrylaANPFF--HVFGYKA--GVNAPLMRG-ATI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3734 VPEAVCrQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELAL-NVRAVVFGGEALEPSRLQPWRERYPQAELVNMYG 3812
Cdd:PRK07656 237 LPLPVF-DPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLsSLRLAVTGAASMPVALLERFESELGVDIVLTGYG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3813 ITETTVHVSFHRLSDEDLQSPTSrIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgq 3892
Cdd:PRK07656 316 LSEASGVTTFNRLDDDRKTVAGT-IGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADG-- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3893 rFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDP 3971
Cdd:PRK07656 393 -WLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIgVPDERLGEVGKAYVVLKPGAELTE 471
|
490 500 510
....*....|....*....|....*....|....*....
gi 1246793773 3972 QSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK07656 472 EELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
3080-3461 |
1.93e-59 |
|
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380454 [Multi-domain] Cd Length: 427 Bit Score: 212.99 E-value: 1.93e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3080 VYPLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGF-AVQGlpSPRQLPHRQVSLPL 3158
Cdd:cd19531 1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFvEVDG--EPVQVILPPLPLPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3159 AEQDWSGLEPAQARSRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAALR 3238
Cdd:cd19531 79 PVVDLSGLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3239 ESRTPQLPAAPP-FRDYLHWLRG--QDEAAAR--AFWREQLTGLEPA-ALPeaTE---PAE-GYASSTRRFDLAAA---- 3304
Cdd:cd19531 159 AGRPSPLPPLPIqYADYAVWQREwlQGEVLERqlAYWREQLAGAPPVlELP--TDrprPAVqSFRGARVRFTLPAEltaa 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3305 -SAWAQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRP-PELagvERMLGVFINSVPLRVTPAGEATPAPWLQAL 3382
Cdd:cd19531 237 lRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNrAEL---EGLIGFFVNTLVLRTDLSGDPTFRELLARV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3383 QQRNLDLRTHGYLPLAQIqragaADAVSP---------FDVLLVFENLPtESREERSGMRIEELD-HRAHSNYPLMLTAI 3452
Cdd:cd19531 314 RETALEAYAHQDLPFEKL-----VEALQPerdlsrsplFQVMFVLQNAP-AAALELPGLTVEPLEvDSGTAKFDLTLSLT 387
|
....*....
gi 1246793773 3453 PDAGGLRIE 3461
Cdd:cd19531 388 ETDGGLRGS 396
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
3552-4010 |
2.30e-59 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 213.46 E-value: 2.30e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3552 RRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAA----YVPVDPHAPAARRGFILEDSGVCLSVSQRALA 3627
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3628 VELPGTALCLDDPFTRAQLDAVEPGELP----EVPTEAPAYLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEH 3703
Cdd:cd05922 81 DRLRDALPASPDPGTVLDADGIRAARASapahEVSHEDLALLLYTSGSTGSPKLVRLSHQNL--LANARSIAEYLGITAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3704 DVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCrqPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALNVRAV 3783
Cdd:cd05922 159 DRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVL--DDAFWEDLREHGATGLAGVPSTYAMLTRLGFDPAKLPSLRYL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3784 VFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSF---HRLsdedLQSPTSrIGSALPDLAVHVLDAAGQPVPLGV 3860
Cdd:cd05922 237 TQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYlppERI----LEKPGS-IGLAIPGGEFEILDDDGTPTPPGE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3861 VGELVVEGDGVAQGYWQRPeltAERFVERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQ 3940
Cdd:cd05922 312 PGEIVHRGPNVMKGYWNDP---PYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGL 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3941 VSDAAVTVEGQGEGAWLMAYAVAADGAEPDPqsLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:cd05922 389 IIEAAAVGLPDPLGEKLALFVTAPDKIDPKD--VLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
3525-4084 |
6.51e-59 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 226.48 E-value: 6.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPARIAV----SAEDG-----ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAA 3595
Cdd:TIGR03443 242 FADNAEKHPDRTCVvetpSFLDPssktrSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGAT 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3596 YVPVDPHAPAAR----------RGFI-LEDSGVcLSVSQR-------ALAVELPGTALCLDDPFTRAQLDAVEPG----- 3652
Cdd:TIGR03443 322 FSVIDPAYPPARqtiylsvakpRALIvIEKAGT-LDQLVRdyidkelELRTEIPALALQDDGSLVGGSLEGGETDvlapy 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3653 -ELPEVPT------EAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQtgRFSFDEHDVWSLFHSHAFD------FAVw 3719
Cdd:TIGR03443 401 qALKDTPTgvvvgpDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAK--RFGLSENDKFTMLSGIAHDpiqrdmFTP- 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3720 elwgawLYGGRAVLVPEAVCRQ-PDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALnvRAVVFGGEAL---EPSRL 3795
Cdd:TIGR03443 478 ------LFLGAQLLVPTADDIGtPGRLAEWMAKYGATVTHLTPAMGQLLSAQATTPIPSL--HHAFFVGDILtkrDCLRL 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3796 QPWRErypQAELVNMYGITETTVHVSFH----RLSDED-LQSPTSRI--GSALPD---LAVHVLDAAgQPVPLGVVGELV 3865
Cdd:TIGR03443 550 QTLAE---NVCIVNMYGTTETQRAVSYFeipsRSSDSTfLKNLKDVMpaGKGMKNvqlLVVNRNDRT-QTCGVGEVGEIY 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3866 VEGDGVAQGYWQRPELTAERFV-----------------ERGGQ--------RFYRSGDLGRYRADGSLEYRGRGDDQVK 3920
Cdd:TIGR03443 626 VRAGGLAEGYLGLPELNAEKFVnnwfvdpshwidldkenNKPERefwlgprdRLYRTGDLGRYLPDGNVECCGRADDQVK 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3921 LRGYRIEPGEIAAKIASLPQVSDaAVT----------------VEGQGEGAWLMAYAVAADGAEPDP------------Q 3972
Cdd:TIGR03443 706 IRGFRIELGEIDTHLSQHPLVRE-NVTlvrrdkdeeptlvsyiVPQDKSDELEEFKSEVDDEESSDPvvkglikyrkliK 784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3973 SLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKALPKPET--------QDRDEGVLESAS--ERRLAELWRQLlgge 4042
Cdd:TIGR03443 785 DIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTaqlaavakNRSASAADEEFTetEREIRDLWLEL---- 860
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1246793773 4043 LPGRGAH------FFARGGHSLLVVRLAEAIRAEFAIAVPLKSLFEQP 4084
Cdd:TIGR03443 861 LPNRPATispddsFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSP 908
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
1598-1946 |
1.34e-58 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.
Pssm-ID: 380469 [Multi-domain] Cd Length: 422 Bit Score: 210.25 E-value: 1.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1598 FPLTPLQRGVLLESLRGDGADPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGLSVPHQIVLADAAAPWQT 1677
Cdd:cd19547 2 YPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDLAPPWAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1678 LDWSALDDAAQDAQLQRWLADDAAQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQG 1757
Cdd:cd19547 82 LDWSGEDPDRRAELLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAHG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1758 ATLRLPPAPGFQAYLDW---RERQDLARQRgWWRERLSGYAGTAALPApvaaahhPVQREECERRLSAHDSERLRAF--- 1831
Cdd:cd19547 162 REPQLSPCRPYRDYVRWiraRTAQSEESER-FWREYLRDLTPSPFSTA-------PADREGEFDTVVHEFPEQLTRLvne 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1832 -CRERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPPELAGVESMVGVFINTLPLRLRIDAGQPALDLLSALRSQS 1910
Cdd:cd19547 234 aARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDL 313
|
330 340 350
....*....|....*....|....*....|....*....
gi 1246793773 1911 LEVAENEAVGLGEILADSG---LDADRLFASLLVVENFP 1946
Cdd:cd19547 314 ATTAAHGHVPLAQIKSWASgerLSGGRVFDNLVAFENYP 352
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
3535-4010 |
1.91e-58 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 210.61 E-value: 1.91e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3535 RIAVSAEDGELDYATLDRRSSQLATLLIRQGA-GPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILE 3613
Cdd:cd05941 2 RIAIVDDGDSITYADLVARAARLANRLLALGKdLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3614 DSGVCLSVsqralavelpgtalclddpftraqldavepgelpevpteAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAAT 3693
Cdd:cd05941 82 DSEPSLVL---------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRALV 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3694 QTGRFSFDEH--DVWSLFHSHAFDFAvweLWGAWLYGGRAVLVPEavcrqPDAFLDLLAEY--GVTVLNQTPsAFY---- 3765
Cdd:cd05941 123 DAWRWTEDDVllHVLPLHHVHGLVNA---LLCPLFAGASVEFLPK-----FDPKEVAISRLmpSITVFMGVP-TIYtrll 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3766 ------ALQSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAeLVNMYGITETTVHVSfHRLSDEdlQSPTSrIGS 3839
Cdd:cd05941 194 qyyeahFTDPQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHT-LLERYGMTEIGMALS-NPLDGE--RRPGT-VGM 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3840 ALPDLAVHVLD-AAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRG-DD 3917
Cdd:cd05941 269 PLPGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDG---WFKTGDLGVVDEDGYYWILGRSsVD 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3918 QVKLRGYRIEPGEIAAKIASLPQVSDAAVT---VEGQGEGAwlMAYAVAADGAEP-DPQSLREALRALLPDYMLPRLIQL 3993
Cdd:cd05941 346 IIKSGGYKVSALEIERVLLAHPGVSECAVIgvpDPDWGERV--VAVVVLRAGAAAlSLEELKEWAKQRLAPYKRPRRLIL 423
|
490
....*....|....*..
gi 1246793773 3994 LPALPLTANGKLDRKAL 4010
Cdd:cd05941 424 VDELPRNAMGKVNKKEL 440
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
1597-1946 |
2.51e-58 |
|
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380459 [Multi-domain] Cd Length: 419 Bit Score: 209.23 E-value: 2.51e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1597 AFPLTPLQRGVLLESLRGDGADPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGLSVPHQIVLADAAAPWQ 1676
Cdd:cd19536 1 MYPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQAQVPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1677 TLDWSALDDaaQDAQLQRWLADDAAQGVDFAHAPLARMSLIGRGG-GRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGA 1755
Cdd:cd19536 81 ELDLTPLEE--QLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDErERFLLVISDHHSILDGWSLYLLVKEILAVYNQLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1756 QGATLRLPPAPGFQAYLDWRER--QDLARQRgWWRERLSGYAGTAALPAPVAAAHHPVQREecERRLSAHDSERLRAFCR 1833
Cdd:cd19536 159 EYKPLSLPPAQPYRDFVAHERAsiQQAASER-YWREYLAGATLATLPALSEAVGGGPEQDS--ELLVSVPLPVRSRSLAK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1834 ERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPPELAGVESMVGVFINTLPLRLRIdAGQPALDLLSALRSQSLEV 1913
Cdd:cd19536 236 RSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTL-SEETVEDLLKRAQEQELES 314
|
330 340 350
....*....|....*....|....*....|...
gi 1246793773 1914 AENEAVGLGEILADSglDADRLFASLLVVENFP 1946
Cdd:cd19536 315 LSHEQVPLADIQRCS--EGEPLFDSIVNFRHFD 345
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
588-1042 |
1.42e-56 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 205.10 E-value: 1.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDaqglagfapsvaiavdelkldgagengs 667
Cdd:cd17645 51 VGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILLTN---------------------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 668 genaaPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARP 747
Cdd:cd17645 103 -----PDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 748 DEL-LEPQRFLAFLSERAITVTDLAPAYANELVRASvaddwrDLALRCLVVGGDVLPVALAQRWfelgldrrcALINAYG 826
Cdd:cd17645 178 SERrLDLDALNDYFNQEGITISFLPTGAAEQFMQLD------NQSLRVLLTGGDKLKKIERKGY---------KLVNNYG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 827 PTEATISSHYHRVQAIDASrpVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPS 906
Cdd:cd17645 243 PTENTVVATSFEIDKPYAN--IPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 907 GEslRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAAGVVGEGAAQR-LVAWVecaged 985
Cdd:cd17645 321 GE--RMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKyLVAYV------ 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 986 gfgqadlnqTDSDQTESERWHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRALP 1042
Cdd:cd17645 393 ---------TAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKALP 440
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
3529-4010 |
1.74e-56 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 206.84 E-value: 1.74e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARR 3608
Cdd:cd05959 14 NEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3609 GFILEDSGVCLSVSQRALA----------------VELPGTALCLDDPFTRAQLDAVEPGELPEVPTEA--PAYLIYTSG 3670
Cdd:cd05959 94 AYYLEDSRARVVVVSGELApvlaaaltksehtlvvLIVSGGAGPEAGALLLAELVAAEAEQLKPAATHAddPAFWLYSSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3671 STGTPKGVVVTHRN---VERLFtaATQTGRFSfdEHDVW----SLFHSHAFD----FAVWelwgawlYGGRAVLVPEAVc 3739
Cdd:cd05959 174 STGRPKGVVHLHADiywTAELY--ARNVLGIR--EDDVCfsaaKLFFAYGLGnsltFPLS-------VGATTVLMPERP- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3740 rQPDAFLDLLAEYGVTVLNQTPsAFYA--LQSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYpQAELVNMYGITEtT 3817
Cdd:cd05959 242 -TPAAVFKRIRRYRPTVFFGVP-TLYAamLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARF-GLDILDGIGSTE-M 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3818 VHVSfhrLSD--EDLQSPTSriGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVerGGqrFY 3895
Cdd:cd05959 318 LHIF---LSNrpGRVRYGTT--GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ--GE--WT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3896 RSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEGawLM---AYAVAADGAEP--- 3969
Cdd:cd05959 389 RTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDG--LTkpkAFVVLRPGYEDsea 466
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1246793773 3970 DPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:cd05959 467 LEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
3081-3488 |
2.11e-56 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380453 [Multi-domain] Cd Length: 427 Bit Score: 204.18 E-value: 2.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3081 YPLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFAvQGLPSPRQLPHRQVSLP-LA 3159
Cdd:cd19066 2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFC-EEAGRYEQVVLDKTVRFrIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3160 EQDWSGLepAQARSRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAALRE 3239
Cdd:cd19066 81 IIDLRNL--ADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3240 SRTPQLPAAPPFRDYLHWLRGQ--DEAAAR--AFWREQLTGL-EPAALPEATEPAEGYASSTRRFDLAAASAW------- 3307
Cdd:cd19066 159 QKPTLPPPVGSYADYAAWLEKQleSEAAQAdlAYWTSYLHGLpPPLPLPKAKRPSQVASYEVLTLEFFLRSEEtkrlrev 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3308 AQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRPPElaGVERMLGVFINSVPLRVTPAGEATPAPWLQALQQRNL 3387
Cdd:cd19066 239 ARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDE--AVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3388 DLRTHGYLPLAQIQRA-----GAADAVSpFDVLLVFENLPTESREERSGMRIEEL-DHRAHSNYPLMLTAIPDA-GGLRI 3460
Cdd:cd19066 317 EAIEHQRVPFIELVRHlgvvpEAPKHPL-FEPVFTFKNNQQQLGKTGGFIFTTPVyTSSEGTVFDLDLEASEDPdGDLLL 395
|
410 420
....*....|....*....|....*...
gi 1246793773 3461 EAALDRSKLDGWLVEQMLDDLDFVLQQV 3488
Cdd:cd19066 396 RLEYSRGVYDERTIDRFAERYMTALRQL 423
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
2178-2518 |
3.97e-56 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 200.20 E-value: 3.97e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2178 TPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGE-DASLATLStVAADLGFTALFGALLSGRRVRLLPAelaFD 2256
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEgDVFLSTLP-LFHIGGLFGLLGALLAGGTVVLLPK---FD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2257 AQALAAHLQAHPVDCLKIVPS-HLAGLLAAAGGTAVLPR-ECLVTGGEALTGALVQQVRAlAPTLRIVNHYGPTETTVGI 2334
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTlLARLLKAPESAGYDLSSlRALVSGGAPLPPELLERFEE-APGIKLVNGYGLTETGGTV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2335 LTCTVPEEWpvEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFvahplapDRLLYRS 2414
Cdd:cd04433 156 ATGPPDDDA--RKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD-------EDGWYRT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2415 GDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQ------GSLEGVAE 2488
Cdd:cd04433 227 GDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVlrpgadLDAEELRA 306
|
330 340 350
....*....|....*....|....*....|
gi 1246793773 2489 ALAQRLPEYLCPSRWRAVESMPRLGNGKID 2518
Cdd:cd04433 307 HVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
3080-3467 |
6.47e-56 |
|
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.
Pssm-ID: 380466 [Multi-domain] Cd Length: 413 Bit Score: 202.28 E-value: 6.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3080 VYPLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFAVQGLPSPRQLPHRQVSLPLA 3159
Cdd:cd19544 1 IYPLAPLQEGILFHHLLAEEGDPYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAILWEGLSEPVQVVWRQAELPVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3160 EqdwsgLEPAQARSRLSELQAqQCEAG---FDLAAPPLMRLALLR-RSADEHWLVWTRHHLIVDGWSSALLLDEVwrlyA 3235
Cdd:cd19544 81 E-----LTLDPGDDALAQLRA-RFDPRryrLDLRQAPLLRAHVAEdPANGRWLLLLLFHHLISDHTSLELLLEEI----Q 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3236 ALRESRTPQLPAAPPFRDYL-HWLRGQDEAAARAFWREQLTGLEpaalpEATEP-------AEGYASSTRRFDLAAASA- 3306
Cdd:cd19544 151 AILAGRAAALPPPVPYRNFVaQARLGASQAEHEAFFREMLGDVD-----EPTAPfglldvqGDGSDITEARLALDAELAq 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3307 ----WAQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRPPELAGVERMLGVFINSVPLRVTPAGEATPAPwLQAL 3382
Cdd:cd19544 226 rlraQARRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFINTLPLRVRLGGRSVREA-VRQT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3383 QQRNLDLRTHGYLPLAQIQRAGAADAVSP-FDVLLVF--ENLPTESREERSGMRIEELDHRAHSNYPLMLtAIPDAG-GL 3458
Cdd:cd19544 305 HARLAELLRHEHASLALAQRCSGVPAPTPlFSALLNYrhSAAAAAAAALAAWEGIELLGGEERTNYPLTL-SVDDLGdGF 383
|
....*....
gi 1246793773 3459 RIEAALDRS 3467
Cdd:cd19544 384 SLTAQVVAP 392
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
675-1037 |
2.07e-55 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 197.89 E-value: 2.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 675 QLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARPDEllEPQ 754
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF--DPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 755 RFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFELgldRRCALINAYGPTEATISS 834
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEA---PGIKLVNGYGLTETGGTV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 835 HYHRVqAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPlrlpsgeslRMYR 914
Cdd:cd04433 156 ATGPP-DDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDED---------GWYR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 915 SGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQRLVAWVECAGEDGFGQADLN 993
Cdd:cd04433 226 TGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAeAAVVGVPDPEWGERVVAVVVLRPGADLDAEELR 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1246793773 994 QtdsdqteserwhrALCERLPAYMVPTQFVALPRLPRNASGKID 1037
Cdd:cd04433 306 A-------------HVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
3550-4010 |
4.13e-54 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 197.65 E-value: 4.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3550 LDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDP-HAPAARRgFILEDSGVclsvsqRALAV 3628
Cdd:cd05971 12 LKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFAlFGPEALE-YRLSNSGA------SALVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3629 ELPgtalclDDPftraqldavepgelpevpteapAYLIYTSGSTGTPKGVVVTHR-------NVERLFTAATQTGRFSFD 3701
Cdd:cd05971 85 DGS------DDP----------------------ALIIYTSGTTGPPKGALHAHRvllghlpGVQFPFNLFPRDGDLYWT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3702 EHDvWslfhshAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELA-LNV 3780
Cdd:cd05971 137 PAD-W------AWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAqVKL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3781 RAVVFGGEALEPSRLQpWRERYPQAELVNMYGITETTVHVSfhrlSDEDLQSP-TSRIGSALPDLAVHVLDAAGQPVPLG 3859
Cdd:cd05971 210 RAIATGGESLGEELLG-WAREQFGVEVNEFYGQTECNLVIG----NCSALFPIkPGSMGKPIPGHRVAIVDDNGTPLPPG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3860 VVGELVVE-GDGVAQ-GYWQRPELTAERFVerGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIAS 3937
Cdd:cd05971 285 EVGEIAVElPDPVAFlGYWNNPSATEKKMA--GD--WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLK 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 3938 LPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQ---SLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:cd05971 361 HPAVLMAAVVgIPDPIRGEIVKAFVVLNPGETPSDAlarEIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRREL 437
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
89-507 |
1.67e-53 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380453 [Multi-domain] Cd Length: 427 Bit Score: 195.71 E-value: 1.67e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 89 PLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVL-DRCIQGEDSVA-----AGGGAAVESA 162
Cdd:cd19066 3 PLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLrTRFCEEAGRYEqvvldKTVRFRIEII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 163 DLR------GRGQDEIDALVEgfrlRPFELQRQRPLRMQLLRLDGQGDgpvrHWLqVVVHHIACDGVSLGLLTQDLSRAY 236
Cdd:cd19066 83 DLRnladpeARLLELIDQIQQ----TIYDLERGPLVRVALFRLADERD----VLV-VAIHHIIVDGGSFQILFEDISSVY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 237 RVECGLAAEPAPPLPcQYGDYARWQRDTLDR--LDASLRHHVEALSGAPHLHELPLDHERPAVLGQSGAKLRLAFPPGLS 314
Cdd:cd19066 154 DAAERQKPTLPPPVG-SYADYAAWLEKQLESeaAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEET 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 315 ERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDDPDFASLVARCR 394
Cdd:cd19066 233 KRLREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 395 DHQLAALEHQALPLERVIETLQVERSSRHAPLFQLMFALrHDADLALDLHGVQAHALTL--PEDVAKHELTLEVLVGA-G 471
Cdd:cd19066 313 EQSREAIEHQRVPFIELVRHLGVVPEAPKHPLFEPVFTF-KNNQQQLGKTGGFIFTTPVytSSEGTVFDLDLEASEDPdG 391
|
410 420 430
....*....|....*....|....*....|....*.
gi 1246793773 472 GMSAVWEYNTALWNPATVARWAERYFVALAAMLENP 507
Cdd:cd19066 392 DLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
3547-4010 |
2.23e-53 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 195.77 E-value: 2.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3547 YATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVclsvsQRAL 3626
Cdd:cd17654 19 YADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHV-----SYLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3627 AVELPGTALCLDDPFTRaQLDAVEPGELpevpteapAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQTgrFSFDEHDVW 3706
Cdd:cd17654 94 QNKELDNAPLSFTPEHR-HFNIRTDECL--------AYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSL--FNITSEDIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3707 SLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAE-YGVTVLNQTPSAFYALQSQAMRREL---ALNVRA 3782
Cdd:cd17654 163 FLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILFKrHRITVLQATPTLFRRFGSQSIKSTVlsaTSSLRV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3783 VVFGGEALePSR--LQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQSPtsrIGSALPDLAVHVLDAAGQPVPlgv 3860
Cdd:cd17654 243 LALGGEPF-PSLviLSSWRGKGNRTRIFNIYGITEVSCWALAYKVPEEDSPVQ---LGSPLLGTVIEVRDQNGSEGT--- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3861 vGELVVEGD---GVAQGYWQRPELTaerfverggqrFYRSGDLGRyRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIAS 3937
Cdd:cd17654 316 -GQVFLGGLnrvCILDDEVTVPKGT-----------MRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQVIES 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 3938 LPQVSDAAVTVEGQGEgawLMAYAVAADGAEPDPQSLREAL--RALLPDYMLprliqLLPALPLTANGKLDRKAL 4010
Cdd:cd17654 383 CLGVESCAVTLSDQQR---LIAFIVGESSSSRIHKELQLTLlsSHAIPDTFV-----QIDKLPLTSHGKVDKSEL 449
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
3535-4010 |
4.41e-52 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 191.91 E-value: 4.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3535 RIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILED 3614
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3615 SgvclsvsqRALAVELPGTALClddpftraqldavepgelpevpteapaYLIYTSGSTGTPKGVVVTHRNVeRLFTAATQ 3694
Cdd:cd05919 81 C--------EARLVVTSADDIA---------------------------YLLYSSGTTGPPKGVMHAHRDP-LLFADAMA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3695 TGRFSFDEHDV----------WSLFHShafdfavweLWGAWLYGGRAVLVPEAvcRQPDAFLDLLAEYGVTVLNQTPsAF 3764
Cdd:cd05919 125 REALGLTPGDRvfssakmffgYGLGNS---------LWFPLAVGASAVLNPGW--PTAERVLATLARFRPTVLYGVP-TF 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3765 YA--LQSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYpQAELVNMYGITETtVHVSFHRLSDEdlqsptSRIGSA-- 3840
Cdd:cd05919 193 YAnlLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHF-GGPILDGIGATEV-GHIFLSNRPGA------WRLGSTgr 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3841 -LPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFveRGGqrFYRSGDLGRYRADGSLEYRGRGDDQV 3919
Cdd:cd05919 265 pVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF--NGG--WYRTGDKFCRDADGWYTHAGRADDML 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3920 KLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPD---PQSLREALRALLPDYMLPRLIQLLP 3995
Cdd:cd05919 341 KVGGQWVSPVEVESLIIQHPAVAEAAVVaVPESTGLSRLTAFVVLKSPAAPQeslARDIHRHLLERLSAHKVPRRIAFVD 420
|
490
....*....|....*
gi 1246793773 3996 ALPLTANGKLDRKAL 4010
Cdd:cd05919 421 ELPRTATGKLQRFKL 435
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
1597-1974 |
1.04e-51 |
|
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380467 [Multi-domain] Cd Length: 395 Bit Score: 189.43 E-value: 1.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1597 AFPLTPLQRGVLLESLRGDGAdpYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGLSVPHQIVLADAAAPWQ 1676
Cdd:cd19545 1 IYPCTPLQEGLMALTARQPGA--YVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVKESPISWT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1677 tldwsalddaaQDAQLQRWLADDAAQGVDFaHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTagaQ 1756
Cdd:cd19545 79 -----------ESTSLDEYLEEDRAAPMGL-GGPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQ---G 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1757 GATLRLPPAPGFQAYLDwreRQDLARQRGWWRERLSGyAGTAALPAPVAAAHHPVQREECERRLSAhdserlrAFCRERG 1836
Cdd:cd19545 144 EPVPQPPPFSRFVKYLR---QLDDEAAAEFWRSYLAG-LDPAVFPPLPSSRYQPRPDATLEHSISL-------PSSASSG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1837 CTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPPELAGVESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAEN 1916
Cdd:cd19545 213 VTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPF 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 1917 EAVGLGEILADS-GLDADRLFASLLVVE-NFPAMAPAQLPFALRVRETRAANH--YALTLRV 1974
Cdd:cd19545 293 EHTGLQNIRRLGpDARAACNFQTLLVVQpALPSSTSESLELGIEEESEDLEDFssYGLTLEC 354
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
3529-4010 |
1.76e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 193.72 E-value: 1.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARR 3608
Cdd:PRK06178 43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3609 GFILEDSGVCLSVSQRALA--VE--LPGTAL----------------------CLDDP---------FTRAQLDAVEPGE 3653
Cdd:PRK06178 123 SYELNDAGAEVLLALDQLApvVEqvRAETSLrhvivtsladvlpaeptlplpdSLRAPrlaaagaidLLPALRACTAPVP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3654 LPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVerLFTAATQTG-RFSFDEHDVWSLFhshafdfaVWELWGA-----WLY 3727
Cdd:PRK06178 203 LPPPALDALAALNYTGGTTGMPKGCEHTQRDM--VYTAAAAYAvAVVGGEDSVFLSF--------LPEFWIAgenfgLLF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3728 ----GGRAVLVPEAvcrQPDAFLDLLAEYGVTVLNQTPSAFYAL--QSQAMRRELAL--NVRAVVFGgEALEPSRLQPWR 3799
Cdd:PRK06178 273 plfsGATLVLLARW---DAVAFMAAVERYRVTRTVMLVDNAVELmdHPRFAEYDLSSlrQVRVVSFV-KKLNPDYRQRWR 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3800 ERYPQAELVNMYGITETTVHVSFHR---LSDEDLQSPTSRIGSALPDLAVHVLD-AAGQPVPLGVVGELVVEGDGVAQGY 3875
Cdd:PRK06178 349 ALTGSVLAEAAWGMTETHTCDTFTAgfqDDDFDLLSQPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGY 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3876 WQRPELTAERFveRGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAV---TVEGQG 3952
Cdd:PRK06178 429 WNKPEATAEAL--RDG--WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVvgrPDPDKG 504
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 3953 EGAwlMAYAVAADGAEPDPQSLREALRALLPDYMLPRlIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK06178 505 QVP--VAFVQLKPGADLTAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKVRKQDL 559
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
88-431 |
2.52e-51 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380455 [Multi-domain] Cd Length: 421 Bit Score: 188.82 E-value: 2.52e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 88 APLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQgedsVAAGGGAAV-----ESA 162
Cdd:cd19532 2 EPMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFF----TDPEDGEPMqgvlaSSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 163 D----LRGRGQDEIDALVEGFRLRPFELQRQRPLRMQLLRLdgqgdGPVRHWLQVVVHHIACDGVSLGLLTQDLSRAYRv 238
Cdd:cd19532 78 LrlehVQISDEAEVEEEFERLKNHVYDLESGETMRIVLLSL-----SPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYN- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 239 ecglaAEPAPPLPCQYGDYARWQRDTLD--RLDASLRHHVEALSGAPHlhELPL-----DHERPAVL--GQSGAKLRLaf 309
Cdd:cd19532 152 -----GQPLLPPPLQYLDFAARQRQDYEsgALDEDLAYWKSEFSTLPE--PLPLlpfakVKSRPPLTryDTHTAERRL-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 310 PPGLSERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDDPDFASL 389
Cdd:cd19532 223 DAALAARIKEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADV 302
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1246793773 390 VARCRDHQLAALEHQALPLERVIETLQVERSSRHAPLFQLMF 431
Cdd:cd19532 303 LKETRDKAYAALAHSRVPFDVLLDELGVPRSATHSPLFQVFI 344
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
3526-4010 |
2.65e-51 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 190.62 E-value: 2.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3526 AEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAayVPVdpHA-P 3604
Cdd:cd05920 22 ARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA--VPV--LAlP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3605 AARRgfiLEDSGVCLSVSQRALAVelPGTALCLDDPFTRAQLDAvepgELPEvpteaPAYLIYTSGSTGTPKGVVVTHRN 3684
Cdd:cd05920 98 SHRR---SELSAFCAHAEAVAYIV--PDRHAGFDHRALARELAE----SIPE-----VALFLLSGGTTGTPKLIPRTHND 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3685 VERLFTAATQTGRfsFDEHDVW--SLFHSHAFDFAVWELWGAWLYGGRAVLVPEAvcrQPDAFLDLLAEYGVTVLNQTPS 3762
Cdd:cd05920 164 YAYNVRASAEVCG--LDQDTVYlaVLPAAHNFPLACPGVLGTLLAGGRVVLAPDP---SPDAAFPLIEREGVTVTALVPA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3763 -AFYALQSQAMRRELALNVRAVVFGGEALEPSRLQpwreRYPQA---ELVNMYGITETTvhVSFHRLSDEDLQSPTSRIG 3838
Cdd:cd05920 239 lVSLWLDAAASRRADLSSLRLLQVGGARLSPALAR----RVPPVlgcTLQQVFGMAEGL--LNYTRLDDPDEVIIHTQGR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3839 SALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQ 3918
Cdd:cd05920 313 PMSPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDG---FYRTGDLVRRTPDGYLVVEGRIKDQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3919 VKLRGYRIEPGEIAAKIASLPQVSDAA-VTVEGQGEGAWLMAYAVAADgAEPDPQSLREALRAL-LPDYMLPRLIQLLPA 3996
Cdd:cd05920 390 INRGGEKIAAEEVENLLLRHPAVHDAAvVAMPDELLGERSCAFVVLRD-PPPSAAQLRRFLRERgLAAYKLPDRIEFVDS 468
|
490
....*....|....
gi 1246793773 3997 LPLTANGKLDRKAL 4010
Cdd:cd05920 469 LPLTAVGKIDKKAL 482
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
3547-4010 |
7.52e-50 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 184.85 E-value: 7.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3547 YATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVclsvsqRAL 3626
Cdd:cd05972 3 FRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGA------KAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3627 AVELpgtalclddpftraqldavepgelpevptEAPAYLIYTSGSTGTPKGVVVTHRnverLFTAATQTGRFSFDEHD-- 3704
Cdd:cd05972 77 VTDA-----------------------------EDPALIYFTSGTTGLPKGVLHTHS----YPLGHIPTAAYWLGLRPdd 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3705 -VWSLfHSHAFDFAVW-ELWGAWLYGGrAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALNVRA 3782
Cdd:cd05972 124 iHWNI-ADPGWAKGAWsSFFGPWLLGA-TVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKFSHLRL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3783 VVFGGEALEPSRLQPWRERYpQAELVNMYGITETTVHVSFHRlsDEDLQsPTSrIGSALPDLAVHVLDAAGQPVPLGVVG 3862
Cdd:cd05972 202 VVSAGEPLNPEVIEWWRAAT-GLPIRDGYGQTETGLTVGNFP--DMPVK-PGS-MGRPTPGYDVAIIDDDGRELPPGEEG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3863 ELVVEGD--GVAQGYWQRPELTAERFveRGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQ 3940
Cdd:cd05972 277 DIAIKLPppGLFLGYVGDPEKTEASI--RGD--YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPA 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 3941 VSDAAVT-----VEGQgegaWLMAYAVAADGAEPDP---QSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:cd05972 353 VAEAAVVgspdpVRGE----VVKAFVVLTSGYEPSEelaEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
3541-4009 |
2.33e-49 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 186.68 E-value: 2.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3541 EDGELDYATLDRRSSQLATLLiRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPV-DPHAP--AARRGFILEDSG- 3616
Cdd:cd05931 21 REETLTYAELDRRARAIAARL-QAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLpPPTPGrhAERLAAILADAGp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3617 -VCLSVSQRALAVELPGTALCLDDPFTRAQLDAVE-----PGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVerLFT 3690
Cdd:cd05931 100 rVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPdtsaaDWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNL--LAN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3691 AATQTGRFSFDEHDV---W-SLFHshafDFAVWELWGA-WLYGGRAVLV-PEAVCRQPDAFLDLLAEYGVTVlNQTPSAF 3764
Cdd:cd05931 178 VRQIRRAYGLDPGDVvvsWlPLYH----DMGLIGGLLTpLYSGGPSVLMsPAAFLRRPLRWLRLISRYRATI-SAAPNFA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3765 YALQSQAMRRE----LAL-NVRAVVFGGEALEPSRLQPWRERY------PQAeLVNMYGITETTVHVSF---------HR 3824
Cdd:cd05931 253 YDLCVRRVRDEdlegLDLsSWRVALNGAEPVRPATLRRFAEAFapfgfrPEA-FRPSYGLAEATLFVSGgppgtgpvvLR 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3825 LSDEDLQSPTSRI-------------GSALPDLAVHVLDAAG-QPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERG 3890
Cdd:cd05931 332 VDRDALAGRAVAVaaddpaarelvscGRPLPDQEVRIVDPETgRELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALA 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3891 GQ---RFYRSGDLGrYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSD----AAVTVEGQGEGAWLMAYAVA 3963
Cdd:cd05931 412 ATdegGWLRTGDLG-FLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRpgcvAAFSVPDDGEERLVVVAEVE 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3964 ADGAEPDPQSLREALRALLPDY--MLPRLIQLLP--ALPLTANGKLDRKA 4009
Cdd:cd05931 491 RGADPADLAAIAAAIRAAVAREhgVAPADVVLVRpgSIPRTSSGKIQRRA 540
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
3083-3314 |
2.73e-49 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 176.77 E-value: 2.73e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3083 LAPLQEGLLFhslLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFaVQGLPSPRQLPHRQVSLPLAEQD 3162
Cdd:COG4908 1 LSPAQKRFLF---LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRF-VEEDGEPVQRIDPDADLPLEVVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3163 WSGLEPAQARSRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAALRESRT 3242
Cdd:COG4908 77 LSALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3243 PQLPAAP-PFRDYLHWLR----GQDEAAARAFWREQLTGLEPA-ALP-EATEPAEG-YASSTRRFDLAAA-----SAWAQ 3309
Cdd:COG4908 157 PPLPELPiQYADYAAWQRawlqSEALEKQLEYWRQQLAGAPPVlELPtDRPRPAVQtFRGATLSFTLPAEltealKALAK 236
|
....*
gi 1246793773 3310 SHGLT 3314
Cdd:COG4908 237 AHGAT 241
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
3525-4010 |
4.61e-49 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 185.35 E-value: 4.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAayVPVdpHAP 3604
Cdd:COG1021 31 LRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPV--FAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3605 AARRgfILEDSGVClSVSQ---------------RALAVEL------PGTALCLDDPFTRAQLDAV----EPGELPEVPT 3659
Cdd:COG1021 107 PAHR--RAEISHFA-EQSEavayiipdrhrgfdyRALARELqaevpsLRHVLVVGDAGEFTSLDALlaapADLSEPRPDP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3660 EAPAYLIYTSGSTGTPKGVVVTHRnvERLFTAATQTGRFSFDEHDVW--SLFHSHAFDFAVWELWGAWLYGGRAVLVPEA 3737
Cdd:COG1021 184 DDVAFFQLSGGTTGLPKLIPRTHD--DYLYSVRASAEICGLDADTVYlaALPAAHNFPLSSPGVLGVLYAGGTVVLAPDP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3738 vcrQPDAFLDLLAEYGVTVLNQTPSAFYA-LQSQAMRRELALNVRAVVFGGEALEPSRlqpwRERYPQA---ELVNMYGI 3813
Cdd:COG1021 262 ---SPDTAFPLIERERVTVTALVPPLALLwLDAAERSRYDLSSLRVLQVGGAKLSPEL----ARRVRPAlgcTLQQVFGM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3814 TETTVhvSFHRLSD-EDLQSPTsrIGSAL-PDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGg 3891
Cdd:COG1021 335 AEGLV--NYTRLDDpEEVILTT--QGRPIsPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDG- 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3892 qrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTV---EGQGEGAwlMAYAVaADGAE 3968
Cdd:COG1021 410 --FYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAmpdEYLGERS--CAFVV-PRGEP 484
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1246793773 3969 PDPQSLREALRAL-LPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:COG1021 485 LTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
3544-4013 |
7.93e-49 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 184.64 E-value: 7.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3544 ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGfiledsgVCLSVSQ 3623
Cdd:cd17647 20 SFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQN-------IYLGVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3624 -RALAVelpgtalclddpfTRAQLDAVEPGELPEvpteapayLIYTSGSTGTPKGVVVTHRNVERLFTAATQtgRFSFDE 3702
Cdd:cd17647 93 pRGLIV-------------IRAAGVVVGPDSNPT--------LSFTSGSEGIPKGVLGRHFSLAYYFPWMAK--RFNLSE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3703 HDVWSLFHSHAFDFAVWELWGAwLYGGRAVLVPEAV-CRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALNvR 3781
Cdd:cd17647 150 NDKFTMLSGIAHDPIQRDMFTP-LFLGAQLLVPTQDdIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQATTPFPKLH-H 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3782 AVvFGGEAL---EPSRLQPWRERYpqaELVNMYGITETTVHVSFH----RLSDED-LQSPTSRI--GSALPDLAVHVLDA 3851
Cdd:cd17647 228 AF-FVGDILtkrDCLRLQTLAENV---RIVNMYGTTETQRAVSYFevpsRSSDPTfLKNLKDVMpaGRGMLNVQLLVVNR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3852 --AGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVER--------GGQ-----------------RFYRSGDLGRYR 3904
Cdd:cd17647 304 ndRTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNwfvepdhwNYLdkdnnepwrqfwlgprdRLYRTGDLGRYL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3905 ADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTV-EGQGEGAWLMAYAVA----------ADGAEPDPQS 3973
Cdd:cd17647 384 PNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVrRDKDEEPTLVSYIVPrfdkpddesfAQEDVPKEVS 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 3974 -----------------LREALRALLPDYMLPRLIQLLPALPLTANGKLDRKALPKP 4013
Cdd:cd17647 464 tdpivkgligyrklikdIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
3536-4005 |
1.73e-48 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 182.80 E-value: 1.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3536 IAVSAEDG-ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILED 3614
Cdd:cd05911 1 AQIDADTGkELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3615 SG------------VCLSVSQRA--------LAVELPG-TALCLDDPFTRAQLDAVEPGELPEVPTEaPAYLIYTSGSTG 3673
Cdd:cd05911 81 SKpkviftdpdgleKVKEAAKELgpkdkiivLDDKPDGvLSIEDLLSPTLGEEDEDLPPPLKDGKDD-TAAILYSSGTTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3674 TPKGVVVTHRNverlFTAATQTGRFSFDEHDVWS--------LFHSHAFDFAVWELwgawLYGGRAVLVPEAvcrQPDAF 3745
Cdd:cd05911 160 LPKGVCLSHRN----LIANLSQVQTFLYGNDGSNdvilgflpLYHIYGLFTTLASL----LNGATVIIMPKF---DSELF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3746 LDLLAEYGVTVLNQTPSAFYALQSQAMRRELAL-NVRAVVFGG-----EALEpsRLQPwreRYPQAELVNMYGITETTVH 3819
Cdd:cd05911 229 LDLIEKYKITFLYLVPPIAAALAKSPLLDKYDLsSLRVILSGGaplskELQE--LLAK---RFPNATIKQGYGMTETGGI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3820 VSFHRLSDEDLQSptsrIGSALPDLAVHVLDAAG-QPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSG 3898
Cdd:cd05911 304 LTVNPDGDDKPGS----VGRLLPNVEAKIVDDDGkDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDG---WLHTG 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3899 DLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAV---TVEGQGEGAwlMAYAVAADGAEPDPQSLR 3975
Cdd:cd05911 377 DIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVigiPDEVSGELP--RAYVVRKPGEKLTEKEVK 454
|
490 500 510
....*....|....*....|....*....|...
gi 1246793773 3976 EALRALLPDYMlpRL---IQLLPALPLTANGKL 4005
Cdd:cd05911 455 DYVAKKVASYK--QLrggVVFVDEIPKSASGKI 485
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
3544-4010 |
2.45e-48 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 180.75 E-value: 2.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3544 ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVCLSVsq 3623
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3624 ralavelpgtalclddpfTRAQLDAVepgelpevpteapAYLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEH 3703
Cdd:cd05935 79 ------------------VGSELDDL-------------ALIPYTSGTTGLPKGCMHTHFSA--AANALQSAVWTGLTPS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3704 DVW----SLFHSHAFDFAVwelwGAWLYGGRAVLVPEAVCRqpDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALN 3779
Cdd:cd05935 126 DVIlaclPLFHVTGFVGSL----NTAVYVGGTYVLMARWDR--ETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3780 -VRAVVFGGEALEPSRLQPWRERYpQAELVNMYGITETT--VHVS-FHRLSDEDLQSPTSRIGSALPDLAvhvldaAGQP 3855
Cdd:cd05935 200 sLKVLTGGGAPMPPAVAEKLLKLT-GLRFVEGYGLTETMsqTHTNpPLRPKLQCLGIP*FGVDARVIDIE------TGRE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3856 VPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKI 3935
Cdd:cd05935 273 LPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKL 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 3936 ASLPQVSDAAV-TVEGQGEGAWLMAYAVAADG--AEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:cd05935 353 YKHPAI*EVCViSVPDERVGEEVKAFIVLRPEyrGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
90-327 |
2.48e-48 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 174.07 E-value: 2.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 90 LSLGQERLWFLEqfePGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLdRC----IQGE--DSVAAGGGAAVESAD 163
Cdd:COG4908 1 LSPAQKRFLFLE---PGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPAL-RTrfveEDGEpvQRIDPDADLPLEVVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 164 LRG----RGQDEIDALVEGFRLRPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSLGLLTQDLSRAYRVE 239
Cdd:COG4908 77 LSAlpepEREAELEELVAEEASRPFDLARGPLLRAALIRLGED-----EHVLLLTIHHIISDGWSLGILLRELAALYAAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 240 CGLAAEPAPPLPCQYGDYARWQRDTL--DRLDASLRHHVEALSGAPHLHELPLDHERPAVLGQSGAKLRLAFPPGLSERV 317
Cdd:COG4908 152 LEGEPPPLPELPIQYADYAAWQRAWLqsEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEAL 231
|
250
....*....|
gi 1246793773 318 AAYAQASRAT 327
Cdd:COG4908 232 KALAKAHGAT 241
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
3535-4010 |
5.63e-48 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 181.36 E-value: 5.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3535 RIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILED 3614
Cdd:cd05926 5 ALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3615 SGVCLSV--------SQRALAVELPGTA-LCLDDPFTRAQLDAVEPGELPEVPTEA----------PAYLIYTSGSTGTP 3675
Cdd:cd05926 85 LGSKLVLtpkgelgpASRAASKLGLAILeLALDVGVLIRAPSAESLSNLLADKKNAksegvplpddLALILHTSGTTGRP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3676 KGVVVTHRNVERLFTAATQTgrFSFDEHD----VWSLFHSHAFDFAVWelwgAWLYGGRAVLVPEAVcrQPDAFLDLLAE 3751
Cdd:cd05926 165 KGVPLTHRNLAASATNITNT--YKLTPDDrtlvVMPLFHVHGLVASLL----STLAAGGSVVLPPRF--SASTFWPDVRD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3752 YGVTVLNQTPSAFYALQSQAM---RRELALnVRAVVFGGEALEPSRLQPWRERYpQAELVNMYGITETTvhvsfHRLSDE 3828
Cdd:cd05926 237 YNATWYTAVPTIHQILLNRPEpnpESPPPK-LRFIRSCSASLPPAVLEALEATF-GAPVLEAYGMTEAA-----HQMTSN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3829 DLQSPTSRIGSA-LPDLA-VHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRAD 3906
Cdd:cd05926 310 PLPPGPRKPGSVgKPVGVeVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDG---WFRTGDLGYLDAD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3907 GSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDA---AVTVEGQGEGAWlmAYAVAADGAEPDPQSLREALRALLP 3983
Cdd:cd05926 387 GYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAvafGVPDEKYGEEVA--AAVVLREGASVTEEELRAFCRKHLA 464
|
490 500
....*....|....*....|....*..
gi 1246793773 3984 DYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:cd05926 465 AFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
2052-2523 |
6.89e-48 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 181.52 E-value: 6.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHpDARQIA-VLD 2130
Cdd:TIGR03098 16 ATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLL-KAEQVAhILA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2131 DSGARIVIGWGA-------APAWVP---------------------ASVRWLDAESVLDVVSAyeePPRVDVDadtPAYL 2182
Cdd:TIGR03098 95 DCNVRLLVTSSErldllhpALPGCHdlrtliivgdpahaseghpgeEPASWPKLLALGDADPP---HPVIDSD---MAAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2183 IYTSGSTGTPKGVVVSQGNLanyVAGVLPV---LDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELafdaqa 2259
Cdd:TIGR03098 169 LYTSGSTGRPKGVVLSHRNL---VAGAQSVatyLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHDYLL------ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2260 laahlqahPVDCLKIVPSHlagllAAAGGTAVLP------------------RECLVTGGeALTGALVQQVRALAPTLRI 2321
Cdd:TIGR03098 240 --------PRDVLKALEKH-----GITGLAAVPPlwaqlaqldwpesaapslRYLTNSGG-AMPRATLSRLRSFLPNARL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2322 VNHYGPTEttvGILTCTVPEEWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFV 2401
Cdd:TIGR03098 306 FLMYGLTE---AFRSTYLPPEEVDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2402 AHPLAPDRLLYR-----SGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALP----GANGV 2472
Cdd:TIGR03098 383 PLPPFPGELHLPelavwSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPdptlGQAIV 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 2473 LQLGACIQGSL--EGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALA 2523
Cdd:TIGR03098 463 LVVTPPGGEELdrAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALA 515
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
3530-4022 |
2.63e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 180.18 E-value: 2.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3530 RRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRG 3609
Cdd:PRK06188 23 KRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3610 FILEDSGVCLSVS------QRALAV--ELPGTA--LCLDD-PFTR---AQLDAVEPGEL--PEVPTEaPAYLIYTSGSTG 3673
Cdd:PRK06188 103 YVLEDAGISTLIVdpapfvERALALlaRVPSLKhvLTLGPvPDGVdllAAAAKFGPAPLvaAALPPD-IAGLAYTGGTTG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3674 TPKGVVVTHRNVERLftAATQTGRFSFDEHD----VWSLFHSHAFDFAVwelwgAWLYGGRAVLVPEAvcrQPDAFLDLL 3749
Cdd:PRK06188 182 KPKGVMGTHRSIATM--AQIQLAEWEWPADPrflmCTPLSHAGGAFFLP-----TLLRGGTVIVLAKF---DPAEVLRAI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3750 AEYGVTVLNQTPSAFYAL--QSQAMRRELAlNVRAVVFGGEALEPSRLQPWRERYPQAeLVNMYGITETTVHVSFHRLSD 3827
Cdd:PRK06188 252 EEQRITATFLVPTMIYALldHPDLRTRDLS-SLETVYYGASPMSPVRLAEAIERFGPI-FAQYYGQTEAPMVITYLRKRD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3828 EDLQSPtSRIGSA---LPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFveRGGqrFYRSGDLGRYR 3904
Cdd:PRK06188 330 HDPDDP-KRLTSCgrpTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF--RDG--WLHTGDVARED 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3905 ADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLP 3983
Cdd:PRK06188 405 EDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIgVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKERKG 484
|
490 500 510
....*....|....*....|....*....|....*....
gi 1246793773 3984 DYMLPRLIQLLPALPLTANGKLDRKALPKPETQDRDEGV 4022
Cdd:PRK06188 485 SVHAPKQVDFVDSLPLTALGKPDKKALRARYWEGRGRAV 523
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
2050-2522 |
5.44e-47 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 177.76 E-value: 5.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2050 AQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVL 2129
Cdd:cd05936 13 PDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 DDSGARIVIgwgaapawvpasvrwlDAESVLDVVSAYE-EPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNL---ANY 2205
Cdd:cd05936 93 NDSGAKALI----------------VAVSFTDLLAAGApLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLvanALQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2206 VAGVLPVLDLGEDASLATLSTVAAdLGFT-ALFGALLSGRRVRLLPaelAFDAQALAAHLQAHPVDCLKIVPSHLAGLLA 2284
Cdd:cd05936 157 IKAWLEDLLEGDDVVLAALPLFHV-FGLTvALLLPLALGATIVLIP---RFRPIGVLKEIRKHRVTIFPGVPTMYIALLN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2285 AAGGTAVLPRE--CLVTGGEALTGALVQQVRALAPTlRIVNHYGPTETtvGILTCTVPEEWPVEQGvPVGHPLAGNEAWV 2362
Cdd:cd05936 233 APEFKKRDFSSlrLCISGGAPLPVEVAERFEELTGV-PIVEGYGLTET--SPVVAVNPLDGPRKPG-SIGIPLPGTEVKI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2363 LDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVahplapDRLLyRSGDLARLDGEGRIVYLGRGDHQVKIRGYR 2442
Cdd:cd05936 309 VDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV------DGWL-RTGDIGYMDEDGYFFIVDRKKDMIIVGGFN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2443 VELGEVEQVLAQLPGVEVAAVLALPGANG--------VLQLGACIqgSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGN 2514
Cdd:cd05936 382 VYPREVEEVLYEHPAVAEAAVVGVPDPYSgeavkafvVLKEGASL--TEEEIIAFCREQLAGYKVPRQVEFRDELPKSAV 459
|
....*...
gi 1246793773 2515 GKIDRQAL 2522
Cdd:cd05936 460 GKILRREL 467
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
1598-1974 |
9.96e-47 |
|
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380464 [Multi-domain] Cd Length: 401 Bit Score: 174.80 E-value: 9.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1598 FPLTPLQRGVLLESLRGDGAdpYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGLSVP-HQIVLADAAAPWQ 1676
Cdd:cd19542 2 YPCTPMQEGMLLSQLRSPGL--YFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTfLQVVLKSLDPPIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1677 TLDwSALDDAAQdaqlqrwLADDAAQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYtagaQ 1756
Cdd:cd19542 80 EVE-TDEDSLDA-------LTRDLLDDPTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAY----N 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1757 GATLrlPPAPGFQAYLDWRERQDLARQRGWWRERLSGYAGTaalpapvaaaHHP--VQREECERRLSAHDS--ERLRAFC 1832
Cdd:cd19542 148 GQLL--PPAPPFSDYISYLQSQSQEESLQYWRKYLQGASPC----------AFPslSPKRPAERSLSSTRRslAKLEAFC 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1833 RERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPPELAGVESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLE 1912
Cdd:cd19542 216 ASLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLR 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 1913 VAENEAVGLGEILADSGLDADR-LFASLLVVENFPAmAPAQLPFALRVRETRA---ANHYALTLRV 1974
Cdd:cd19542 296 SLPHQHLSLREIQRALGLWPSGtLFNTLVSYQNFEA-SPESELSGSSVFELSAaedPTEYPVAVEV 360
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
3529-3947 |
2.16e-46 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 177.04 E-value: 2.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIA-VSAEDG-ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAA 3606
Cdd:cd05904 15 ASAHPSRPAlIDAATGrALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3607 RRGFILEDSGVCLSVSQRALAVELPGTAL---CLDDPFTRAQ-----LDAVEPGELP--EVPTEAPAYLIYTSGSTGTPK 3676
Cdd:cd05904 95 EIAKQVKDSGAKLAFTTAELAEKLASLALpvvLLDSAEFDSLsfsdlLFEADEAEPPvvVIKQDDVAALLYSSGTTGRSK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3677 GVVVTHRNverlFTAATQTGRFSFDEHD--------VWSLFHSHAFdfaVWELWGAWLYGGRAVLVPEAVCRqpdAFLDL 3748
Cdd:cd05904 175 GVMLTHRN----LIAMVAQFVAGEGSNSdsedvflcVLPMFHIYGL---SSFALGLLRLGATVVVMPRFDLE---ELLAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3749 LAEYGVTVLNQTPSAFYALQSQAMRRELAL-NVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHrLSD 3827
Cdd:cd05904 245 IERYKVTHLPVVPPIVLALVKSPIVDKYDLsSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTGVVAMC-FAP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3828 EDLQSPTSRIGSALPDLAVHVLD-AAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRAD 3906
Cdd:cd05904 324 EKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEG---WLHTGDLCYIDED 400
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1246793773 3907 GSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT 3947
Cdd:cd05904 401 GYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVI 441
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2078-2523 |
2.22e-46 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 175.71 E-value: 2.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2078 LDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAW----LPLDPQHPDARQIAVLDDSGARIVI-GWGAAPAWVPASVR 2152
Cdd:cd05922 10 LLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLglvfVPLNPTLKESVLRYLVADAGGRIVLaDAGAADRLRDALPA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2153 WLDAESVLDV---VSAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAA 2229
Cdd:cd05922 90 SPDPGTVLDAdgiRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2230 DLGFTALFGALLSGRRVRL-----LPAELAFDAQALAahlqahpVDCLKIVPSHLAGLLAAAGGTAVLPRECLVT-GGEA 2303
Cdd:cd05922 170 DYGLSVLNTHLLRGATLVLtndgvLDDAFWEDLREHG-------ATGLAGVPSTYAMLTRLGFDPAKLPSLRYLTqAGGR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2304 LTGALVQQVRALAPTLRIVNHYGPTETTVGIltCTVPEEWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGG 2383
Cdd:cd05922 243 LPQETIARLRELLPGAQVYVMYGQTEATRRM--TYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2384 NLSLGYWQRAeqtaerfvAHPLAPDR--LLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVA 2461
Cdd:cd05922 321 NVMKGYWNDP--------PYRRKEGRggGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 2462 AVLALPGANGVlQLGACIQGSLEG----VAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALA 2523
Cdd:cd05922 393 AAVGLPDPLGE-KLALFVTAPDKIdpkdVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
87-507 |
2.66e-46 |
|
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.
Pssm-ID: 380468 [Multi-domain] Cd Length: 440 Bit Score: 174.98 E-value: 2.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 87 PAPLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDrciqgedSVAAGGGAAVESADL-- 164
Cdd:cd19546 4 EVPATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILR-------TTFPGDGGDVHQRILda 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 165 -RGR--------GQDEIDALVEGFRLRPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSLGLLTQDLSRA 235
Cdd:cd19546 77 dAARpelpvvpaTEEELPALLADRAAHLFDLTRETPWRCTLFALSDT-----EHVLLLVVHRIAADDESLDVLVRDLAAA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 236 Y--RVEcGLAAEPAPpLPCQYGDYARWQRDTLDRLDA-------SLRHHVEALSGAPHLHELPLDHERPAVLGQSGAKLR 306
Cdd:cd19546 152 YgaRRE-GRAPERAP-LPLQFADYALWERELLAGEDDrdsligdQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 307 LAFPPGLSERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRV-RPELDSLVGLFVNTVVLRTQLHDDPD 385
Cdd:cd19546 230 LRLDAEVHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDeEGDLEGMVGPFARPLALRTDLSGDPT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 386 FASLVARCRDHQLAALEHQALPLERVIETLQVERSSRHAPLFQLMFALRHDADLALD---LHGVQAHALTLPEDVAKHEL 462
Cdd:cd19546 310 FRELLGRVREAVREARRHQDVPFERLAELLALPPSADRHPVFQVALDVRDDDNDPWDapeLPGLRTSPVPLGTEAMELDL 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 463 TLEVLV------GAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENP 507
Cdd:cd19546 390 SLALTErrnddgDPDGLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
2050-2523 |
3.59e-46 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 176.24 E-value: 3.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2050 AQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVL 2129
Cdd:PRK04813 16 PDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIEMII 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 DDSGARIVIGWGAAPAWVpASVRWLDAESVLDVVSAYEEPPRVD-VDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAG 2208
Cdd:PRK04813 96 EVAKPSLIIATEELPLEI-LGIPVITLDELKDIFATGNPYDFDHaVKGDDNYYIIFTSGTTGKPKGVQISHDNLVSFTNW 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2209 VLPVLDLGEDASL---ATLSTvaaDLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAA 2285
Cdd:PRK04813 175 MLEDFALPEGPQFlnqAPYSF---DLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVWVSTPSFADMCLLD 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2286 AGGTAV-LPRecLVT---GGEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPEEWpVEQG--VPVGHPLAGNE 2359
Cdd:PRK04813 252 PSFNEEhLPN--LTHflfCGEELPHKTAKKLLERFPSATIYNTYGPTEATVAVTSIEITDEM-LDQYkrLPIGYAKPDSP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2360 AWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPdrlLYRSGDLARLDgEGRIVYLGRGDHQVKIR 2439
Cdd:PRK04813 329 LLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTFDGQP---AYHTGDAGYLE-DGLLFYQGRIDFQIKLN 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2440 GYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI---QGSLEG-------VAEALAQRLPEYLCPSRWRAVESM 2509
Cdd:PRK04813 405 GYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVvpkEEDFERefeltkaIKKELKERLMEYMIPRKFIYRDSL 484
|
490
....*....|....
gi 1246793773 2510 PRLGNGKIDRQALA 2523
Cdd:PRK04813 485 PLTPNGKIDRKALI 498
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
3529-4010 |
1.63e-45 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 174.28 E-value: 1.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLI-RQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAAR 3607
Cdd:PRK06839 12 AYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3608 RGFILEDSG---VCLSVSQRALAVELPGTA-----LCLDDP---FTRAQLDAVEPGElpevptEAPAYLIYTSGSTGTPK 3676
Cdd:PRK06839 92 LIFQLKDSGttvLFVEKTFQNMALSMQKVSyvqrvISITSLkeiEDRKIDNFVEKNE------SASFIICYTSGTTGKPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3677 GVVVTHRNVerLFTAATQTGRFSFDEHDV----WSLFHSHAFD-FAvwelWGAWLYGGRaVLVPEAVcrQPDAFLDLLAE 3751
Cdd:PRK06839 166 GAVLTQENM--FWNALNNTFAIDLTMHDRsivlLPLFHIGGIGlFA----FPTLFAGGV-IIVPRKF--EPTKALSMIEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3752 YGVTVLNQTPSAFYALQSQAMRRELALN-VRAVVFGGEALEPSRLQPWRER-YPQAElvnMYGITETTVHVSFhrLSDED 3829
Cdd:PRK06839 237 HKVTVVMGVPTIHQALINCSKFETTNLQsVRWFYNGGAPCPEELMREFIDRgFLFGQ---GFGMTETSPTVFM--LSEED 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3830 LQSPTSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFveRGGqrFYRSGDLGRYRADGSL 3909
Cdd:PRK06839 312 ARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI--QDG--WLCTGDLARVDEDGFV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3910 EYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLP 3988
Cdd:PRK06839 388 YIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVgRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIP 467
|
490 500
....*....|....*....|..
gi 1246793773 3989 RLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK06839 468 KEIVFLKELPKNATGKIQKAQL 489
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
536-1041 |
2.24e-45 |
|
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273780 [Multi-domain] Cd Length: 502 Bit Score: 173.79 E-value: 2.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 536 NVVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALClpRGLDWYCL--LLGAWRAGLSVI 613
Cdd:TIGR01734 1 KLIEAIQAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVY--GHMEPHMLvaFLGSIKSGHAYI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 614 PLDTEWPQARRAEVVAASGCDAVLTdAQGLAGFAPSVAI----AVDELKLDGAgeNGSGENA-APNQLAYILYTSGSTGI 688
Cdd:TIGR01734 79 PVDTSIPSERIEMIIEAAGPELVIH-TAELSIDAVGTQIitlsALEQAETSGG--PVSFDHAvKGDDNYYIIYTSGSTGN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 689 PKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARP-DELLEPQRFLAFLSERAITV 767
Cdd:TIGR01734 156 PKGVQISHDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDkDITNNFKLLFEELPKTGLNV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 768 TDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQrwfELgLDR--RCALINAYGPTEAT--ISSHYHRVQAID 843
Cdd:TIGR01734 236 WVSTPSFVDMCLLDPNFNQENYPHLTHFLFCGEELPVKTAK---AL-LERfpKATIYNTYGPTEATvaVTSVKITQEILD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 844 ASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAplrlpSGESLRMYRSGDRVRLlD 923
Cdd:TIGR01734 312 QYPRLPIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFF-----SHEGQPAYRTGDAGTI-T 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 924 DGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA--GVVGEGAAQRLVAWVECAGEDgfgqadlnqTDSDQTE 1001
Cdd:TIGR01734 386 DGQLFYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVvpKYNKDHKVEYLIAAIVPETED---------FEKEFQL 456
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1246793773 1002 SERWHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:TIGR01734 457 TKAIKKELKKSLPAYMIPRKFIYRDQLPLTANGKIDRKAL 496
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
89-507 |
2.88e-45 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380472 [Multi-domain] Cd Length: 430 Bit Score: 171.73 E-value: 2.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 89 PLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQGED-----SVAAGGGAAVESAD 163
Cdd:cd20484 3 PLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDgvpfqKIEPSKPLSFQEED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 164 LRGRGQDEIDALVEGFRLRPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSLGLLTQDLSRAYR-VECGL 242
Cdd:cd20484 83 ISSLKESEIIAYLREKAKEPFVLENGPLMRVHLFSRSEQ-----EHFVLITIHHIIFDGSSSLTLIHSLLDAYQaLLQGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 243 AAEPAPPLPcQYGDYARWQRDTLDRLD--ASLRHHVEALSGA-PHLhELPLDHERPAVLGQSGAKLRLAFPPGLSERVAA 319
Cdd:cd20484 158 QPTLASSPA-SYYDFVAWEQDMLAGAEgeEHRAYWKQQLSGTlPIL-ELPADRPRSSAPSFEGQTYTRRLPSELSNQIKS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 320 YAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDDPDFASLVarcRDHQLA 399
Cdd:cd20484 236 FARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFI---RKLQLT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 400 ---ALEHQALPLERVIETLQVERSSRHAPLFQLMFA----LRHDadlalDLHGVQAH-----ALTLPEDVAK---HELTL 464
Cdd:cd20484 313 vldGLDHAAYPFPAMVRDLNIPRSQANSPVFQVAFFyqnfLQST-----SLQQFLAEyqdvlSIEFVEGIHQegeYELVL 387
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1246793773 465 EVLVGAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENP 507
Cdd:cd20484 388 EVYEQEDRFTLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
2052-2519 |
3.74e-45 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 171.25 E-value: 3.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDD 2131
Cdd:cd17631 11 RTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILAD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVIgwgaapawvpasvrwldaesvldvvsayeepprvdvdaDTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLP 2211
Cdd:cd17631 91 SGAKVLF--------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2212 VLDLGEDASL---ATLSTVAADLGFTalFGALLSGRRVRLLPaelAFDAQALAAHLQAHPVDCLKIVPS-HLAGLLAAAG 2287
Cdd:cd17631 133 ALDLGPDDVLlvvAPLFHIGGLGVFT--LPTLLRGGTVVILR---KFDPETVLDLIERHRVTSFFLVPTmIQALLQHPRF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2288 GTAVLPR-ECLVTGGEALTGALVQQVRALAPtlRIVNHYGPTETTVGIltCTVPEEWPVEQGVPVGHPLAGNEAWVLDRF 2366
Cdd:cd17631 208 ATTDLSSlRAVIYGGAPMPERLLRALQARGV--KFVQGYGMTETSPGV--TFLSPEDHRRKLGSAGRPVFFVEVRIVDPD 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2367 GLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHplapdrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELG 2446
Cdd:cd17631 284 GREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDG-------WFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2447 EVEQVLAQLPGVEVAAVLALPG--------ANGVLQLGAciQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKID 2518
Cdd:cd17631 357 EVEDVLYEHPAVAEVAVIGVPDekwgeavvAVVVPRPGA--ELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKIL 434
|
.
gi 1246793773 2519 R 2519
Cdd:cd17631 435 K 435
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
87-496 |
1.85e-44 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380471 [Multi-domain] Cd Length: 430 Bit Score: 169.36 E-value: 1.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 87 PAPLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQ-----GEDSVAAGGGAAVES 161
Cdd:cd20483 1 PRPMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFegddfGEQQVLDDPSFHLIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 162 ADLRGRGQDE--IDALVEGFRLRPFELQRQRPLRMQLLRLdgqgdgPVRHW-LQVVVHHIACD-GVSLGLLTQ--DLSRA 235
Cdd:cd20483 81 IDLSEAADPEaaLDQLVRNLRRQELDIEEGEVIRGWLVKL------PDEEFaLVLASHHIAWDrGSSKSIFEQftALYDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 236 YRVECGLAAEPAPPLpcQYGDYARWQRDTLDrlDASLRHHV----EALSGAPHLHE-LPLDH-ERPAVLGQSGAKLRLAF 309
Cdd:cd20483 155 LRAGRDLATVPPPPV--QYIDFTLWHNALLQ--SPLVQPLLdfwkEKLEGIPDASKlLPFAKaERPPVKDYERSTVEATL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 310 PPGLSERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDDPDFASL 389
Cdd:cd20483 231 DKELLARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 390 VARCRDHQLAALEHQALPLERVIETLQVERSSRHAPLFQLMFALRhdadlaldLHGVQAHALTLPEDVAKH--------- 460
Cdd:cd20483 311 LESTKTTCLEAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQ--------VHGKFPEYDTGDFKFTDYdhydiptac 382
|
410 420 430
....*....|....*....|....*....|....*..
gi 1246793773 461 ELTLEVL-VGAGGMSAVWEYNTALWNPATVARWAERY 496
Cdd:cd20483 383 DIALEAEeDPDGGLDLRLEFSTTLYDSADMERFLDNF 419
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
3547-4010 |
2.83e-43 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 166.14 E-value: 2.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3547 YATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPV----DPHAPAARrgfiLEDSGVCLSVS 3622
Cdd:cd05969 3 FAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLfsafGPEAIRDR----LENSEAKVLIT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3623 QRALAvelpgtalclddpftraqlDAVEPgelpevptEAPAYLIYTSGSTGTPKGVVVTHRNVerlfTAATQTGRFSFDE 3702
Cdd:cd05969 79 TEELY-------------------ERTDP--------EDPTLLHYTSGTTGTPKGVLHVHDAM----IFYYFTGKYVLDL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3703 HD---VWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVcrQPDAFLDLLAEYGVTVLNQTPSAFYALQSQ--AMRRELA 3777
Cdd:cd05969 128 HPddiYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRF--DAESWYGIIERVKVTVWYTAPTAIRMLMKEgdELARKYD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3778 LN-VRAVVFGGEALEPSRLQpWRERYPQAELVNMYGITETTVHVSFHRLSDEdlQSPTSrIGSALPDLAVHVLDAAGQPV 3856
Cdd:cd05969 206 LSsLRFIHSVGEPLNPEAIR-WGMEVFGVPIHDTWWQTETGSIMIANYPCMP--IKPGS-MGKPLPGVKAAVVDENGNEL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3857 PLGVVGELVVEGD--GVAQGYWQRPELTAERFVerGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAK 3934
Cdd:cd05969 282 PPGTKGILALKPGwpSMFRGIWNDEERYKNSFI--DG--WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESA 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3935 IASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDpQSLREAL----RALLPDYMLPRLIQLLPALPLTANGKLDRKA 4009
Cdd:cd05969 358 LMEHPAVAEAGVIgKPDPLRGEIIKAFISLKEGFEPS-DELKEEIinfvRQKLGAHVAPREIEFVDNLPKTRSGKIMRRV 436
|
.
gi 1246793773 4010 L 4010
Cdd:cd05969 437 L 437
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
1600-1839 |
4.69e-43 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 159.05 E-value: 4.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1600 LTPLQRGVLLEslrGDGADPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGlSVPHQIVLADAAAPWQTLD 1679
Cdd:COG4908 1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEED-GEPVQRIDPDADLPLEVVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1680 WSALDDAAQDAQLQRWLADDAAQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGAT 1759
Cdd:COG4908 77 LSALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1760 LRLPPAPG-FQAYLDW----RERQDLARQRGWWRERLSGYAGTAALPAPVAAAHHPVQR-EECERRLSAHDSERLRAFCR 1833
Cdd:COG4908 157 PPLPELPIqYADYAAWqrawLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRgATLSFTLPAELTEALKALAK 236
|
....*.
gi 1246793773 1834 ERGCTL 1839
Cdd:COG4908 237 AHGATV 242
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
3518-4010 |
6.10e-43 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 166.59 E-value: 6.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3518 TGNLVSRFAEIARRyPARIAVSAEDGE-LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAY 3596
Cdd:PRK07514 2 NNNLFDALRAAFAD-RDAPFIETPDGLrYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3597 VPVDPHAPAARRGFILEDSG----VCLSVSQRALA--VELPGTA--LCLDDPFT--RAQLDAVEPGELPEVPTEA--PAY 3664
Cdd:PRK07514 81 LPLNTAYTLAELDYFIGDAEpalvVCDPANFAWLSkiAAAAGAPhvETLDADGTgsLLEAAAAAPDDFETVPRGAddLAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3665 LIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEHDVW----SLFHSHAFDFAvweLWGAWLYGGRAVLVPEAvcr 3740
Cdd:PRK07514 161 ILYTSGTTGRSKGAMLSHGNL--LSNALTLVDYWRFTPDDVLihalPIFHTHGLFVA---TNVALLAGASMIFLPKF--- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3741 QPDAFLDLLAEygVTVLNQTPSaFYA--LQSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAELvNMYGITETTV 3818
Cdd:PRK07514 233 DPDAVLALMPR--ATVMMGVPT-FYTrlLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAIL-ERYGMTETNM 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3819 HVSfHRLSDEdlqsptsRI----GSALPDLAVHVLD-AAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqr 3893
Cdd:PRK07514 309 NTS-NPYDGE-------RRagtvGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADG--- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3894 FYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQ-----GEGAwlMAYAVAADGAE 3968
Cdd:PRK07514 378 FFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVI--GVphpdfGEGV--TAVVVPKPGAA 453
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1246793773 3969 PDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK07514 454 LDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
3082-3491 |
6.58e-43 |
|
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380462 [Multi-domain] Cd Length: 427 Bit Score: 164.47 E-value: 6.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3082 PLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFAVQGLPSPRQ--LPHRQVSLPLA 3159
Cdd:cd19539 3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQeiLPPGPAPLEVR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3160 EQDWSGLEPAQARSRLSELQAQQceaGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAALRE 3239
Cdd:cd19539 83 DLSDPDSDRERRLEELLRERESR---GFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3240 SRTPQLPAAP-PFRDYLHWLRGQDE----AAARAFWREQLTGLEPAALPEA-TEPAE-GYASSTRRFDL-----AAASAW 3307
Cdd:cd19539 160 GPAAPLPELRqQYKEYAAWQREALAapraAELLDFWRRRLRGAEPTALPTDrPRPAGfPYPGADLRFELdaelvAALREL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3308 AQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRPPELAgvERMLGVFINSVPLRVTPAGEATPAPWLQALQQRNL 3387
Cdd:cd19539 240 AKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRF--ESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3388 DLRTHGYLPLAQIQrAGAADAVSP-----FDVLLVFENLPTESREERSGMRIEEL-DHRAHSNYPLMLTAIPDAGGLRIE 3461
Cdd:cd19539 318 DAQRHQELPFQQLV-AELPVDRDAgrhplVQIVFQVTNAPAGELELAGGLSYTEGsDIPDGAKFDLNLTVTEEGTGLRGS 396
|
410 420 430
....*....|....*....|....*....|
gi 1246793773 3462 AALDRSKLDGWLVEQMLDDLDFVLQQVPAL 3491
Cdd:cd19539 397 LGYATSLFDEETIQGFLADYLQVLRQLLAN 426
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
3529-4005 |
9.40e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 166.65 E-value: 9.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLcLPRGCDLLVAL-LAILKTGAAYVPVDPHAPAAR 3607
Cdd:PRK08316 21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAA-LGHNSDAYALLwLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3608 RGFILEDSGVCLSVSQRALA--VELPGTALCLDDPFTRAQLDAVEPGE-----------------LPEVPTEAPAYLIYT 3668
Cdd:PRK08316 100 LAYILDHSGARAFLVDPALAptAEAALALLPVDTLILSLVLGGREAPGgwldfadwaeagsvaepDVELADDDLAQILYT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3669 SGSTGTPKGVVVTHRNVERLFTAATQTGRFSFDEHDVWS--LFHS---HAFdfavwelWGAWLY-GGRAVLVPEAvcrQP 3742
Cdd:PRK08316 180 SGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHAlpLYHCaqlDVF-------LGPYLYvGATNVILDAP---DP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3743 DAFLDLLAEYGVTVLNQTPSAFYALQSQAM--RRELAlNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITE----T 3816
Cdd:PRK08316 250 ELILRTIEAERITSFFAPPTVWISLLRHPDfdTRDLS-SLRKGYYGASIMPVEVLKELRERLPGLRFYNCYGQTEiaplA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3817 TVhvsfhrLSDEDLQsptSRIGSA-LPDLAVH--VLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFveRGGqr 3893
Cdd:PRK08316 329 TV------LGPEEHL---RRPGSAgRPVLNVEtrVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF--RGG-- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3894 FYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEGAWLMAYA---VAADGAEPD 3970
Cdd:PRK08316 396 WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVI--GLPDPKWIEAVTavvVPKAGATVT 473
|
490 500 510
....*....|....*....|....*....|....*
gi 1246793773 3971 PQSLREALRALLPDYMLPRLIQLLPALPLTANGKL 4005
Cdd:PRK08316 474 EDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
1645-1978 |
1.14e-42 |
|
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380454 [Multi-domain] Cd Length: 427 Bit Score: 163.68 E-value: 1.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1645 VRRQPMLRTAIVWEGlSVPHQIVLADAAAPWQTLDWSALDDAAQDAQLQRWLADDAAQGVDFAHAPLARMSLIGRGGGRY 1724
Cdd:cd19531 49 VARHEALRTTFVEVD-GEPVQVILPPLPLPLPVVDLSGLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1725 WLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGATLRLPPAPgFQaYLD-------WRERQDLARQRGWWRERLSG---- 1793
Cdd:cd19531 128 VLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRPSPLPPLP-IQ-YADyavwqreWLQGEVLERQLAYWREQLAGappv 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1794 --------------YAGtaalpapvaaahhpvqrEECERRLSAHDSERLRAFCRERGCTLSdliaMV----WGLANARYG 1855
Cdd:cd19531 206 lelptdrprpavqsFRG-----------------ARVRFTLPAELTAALRALARREGATLF----MTllaaFQVLLHRYS 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1856 NHDDVVLGATRSGRP-PELagvESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAENEAVGLGEILADsgLDADR 1934
Cdd:cd19531 265 GQDDIVVGTPVAGRNrAEL---EGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALEAYAHQDLPFEKLVEA--LQPER 339
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 1935 ------LFASLLVVENFPaMAPAQLPfALRVRETRAANHYA---LTLRVSERE 1978
Cdd:cd19531 340 dlsrspLFQVMFVLQNAP-AAALELP-GLTVEPLEVDSGTAkfdLTLSLTETD 390
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
89-507 |
1.14e-42 |
|
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380465 [Multi-domain] Cd Length: 423 Bit Score: 163.91 E-value: 1.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 89 PLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQGEDS------VAAGGGAAVESA 162
Cdd:cd19543 3 PLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLgeplqvVLKDRKLPWREL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 163 DLRGRGQDEIDALVEGF----RLRPFELQRQRPLRMQLLRLdgqgdGPVRHWLQVVVHHIACDGVSLGLLTQDLSRAYR- 237
Cdd:cd19543 83 DLSHLSEAEQEAELEALaeedRERGFDLARAPLMRLTLIRL-----GDDRYRLVWSFHHILLDGWSLPILLKELFAIYAa 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 238 VECGLAAEPAPPLPcqYGDYARW--QRDtldrLDASLRHHVEALSGAPHLHELPLDHERPAVLGQSGAKLRLAFPPGLSE 315
Cdd:cd19543 158 LGEGQPPSLPPVRP--YRDYIAWlqRQD----KEAAEAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 316 RVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRvRPELD---SLVGLFVNTVVLRTQLHDDPDFASLVAR 392
Cdd:cd19543 232 RLQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGR-PAELPgieTMVGLFINTLPVRVRLDPDQTVLELLKD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 393 CRDHQLAALEHQALPLERVietlQvERSSRHAPLFQLMFALRHDADLALDLHGVQAHALTLpEDVAKHE-----LTLEVL 467
Cdd:cd19543 311 LQAQQLELREHEYVPLYEI----Q-AWSEGKQALFDHLLVFENYPVDESLEEEQDEDGLRI-TDVSAEEqtnypLTVVAI 384
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1246793773 468 VGaGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENP 507
Cdd:cd19543 385 PG-EELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
3518-4010 |
6.21e-42 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 163.45 E-value: 6.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3518 TGNLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYV 3597
Cdd:cd05923 2 TVFEMLRRAASRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3598 PVDPHAPAARRGFILEDSGVCLSVSQRALAV--ELPGTALCL----DDPFTRAQLDAVEPGELPEVPTEAPAYLIYTSGS 3671
Cdd:cd05923 82 LINPRLKAAELAELIERGEMTAAVIAVDAQVmdAIFQSGVRVlalsDLVGLGEPESAGPLIEDPPREPEQPAFVFYTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3672 TGTPKGVVVTHRNVE-RLFTAATQTGrFSFDEHDV----WSLFHSHAFdFAVweLWGAWLYGGRAVLVPEAvcrQPDAFL 3746
Cdd:cd05923 162 TGLPKGAVIPQRAAEsRVLFMSTQAG-LRHGRHNVvlglMPLYHVIGF-FAV--LVAALALDGTYVVVEEF---DPADAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3747 DLLAEYGVTVLNQTPSAFYALQSQAMRRELAL-NVRAVVFGGEALEPSRLQPWrERYPQAELVNMYGITETTvhvsfhrl 3825
Cdd:cd05923 235 KLIEQERVTSLFATPTHLDALAAAAEFAGLKLsSLRHVTFAGATMPDAVLERV-NQHLPGEKVNIYGTTEAM-------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3826 sdEDLQSPTSRIGSAL-PDL-----AVHVLDAAGQPVPLGVVGELVV--EGDGVAQGYWQRPELTAERFVErggqRFYRS 3897
Cdd:cd05923 306 --NSLYMRDARTGTEMrPGFfsevrIVRIGGSPDEALANGEEGELIVaaAADAAFTGYLNQPEATAKKLQD----GWYRT 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3898 GDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAePDPQSLRE 3976
Cdd:cd05923 380 GDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIgVADERWGQSVTACVVPREGT-LSADELDQ 458
|
490 500 510
....*....|....*....|....*....|....*
gi 1246793773 3977 ALRAL-LPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:cd05923 459 FCRASeLADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
539-1043 |
6.81e-42 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 163.80 E-value: 6.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 539 DAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTE 618
Cdd:TIGR03098 4 HLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 619 WPQARRAEVVAASGCDAVLTDAQGLAGFAPSVA--------IAVDEL----------------KLDGAGENGSGENAAPN 674
Cdd:TIGR03098 84 LKAEQVAHILADCNVRLLVTSSERLDLLHPALPgchdlrtlIIVGDPahaseghpgeepaswpKLLALGDADPPHPVIDS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 675 QLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVarPDELLEPQ 754
Cdd:TIGR03098 164 DMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVV--LHDYLLPR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 755 RFLAFLSERAIT-VTDLAPAYAnELVRasvaDDWRDLA---LRCLVVGGDVLPVALAQRWFELGLDRRCALInaYGPTEA 830
Cdd:TIGR03098 242 DVLKALEKHGITgLAAVPPLWA-QLAQ----LDWPESAapsLRYLTNSGGAMPRATLSRLRSFLPNARLFLM--YGLTEA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 831 tISSHYHRVQAIDaSRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPL-RLPSGES 909
Cdd:TIGR03098 315 -FRSTYLPPEEVD-RRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLpPFPGELH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 910 LR--MYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQV-RAAAAGVVGEGAAQRLVAWVECAGEDG 986
Cdd:TIGR03098 393 LPelAVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVaEAVAFGVPDPTLGQAIVLVVTPPGGEE 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 987 FGQADLnqtdsdqteserwHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRALPA 1043
Cdd:TIGR03098 473 LDRAAL-------------LAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
2061-2540 |
5.75e-41 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 162.20 E-value: 5.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2061 SWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLdpqHPD--ARQIAV-LDDSGARIV 2137
Cdd:COG0365 39 TLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPV---FPGfgAEALADrIEDAEAKVL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2138 I----GW------------GAAPAWVPaSVR----------------WLDAESVLDVVSAYEEPprVDVDADTPAYLIYT 2185
Cdd:COG0365 116 ItadgGLrggkvidlkekvDEALEELP-SLEhvivvgrtgadvpmegDLDWDELLAAASAEFEP--EPTDADDPLFILYT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2186 SGSTGTPKGVVVSQGNLANYVAGVLP-VLDLGEDASLATlstvAADLGFT-----ALFGALLSGRRVRLLPAELAF-DAQ 2258
Cdd:COG0365 193 SGTTGKPKGVVHTHGGYLVHAATTAKyVLDLKPGDVFWC----TADIGWAtghsyIVYGPLLNGATVVLYEGRPDFpDPG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2259 ALAAHLQAHPVDCLKIVP-------SHLAGLLAAAGGTAVlprECLVTGGEALTGALVQQVRAlAPTLRIVNHYGPTETT 2331
Cdd:COG0365 269 RLWELIEKYGVTVFFTAPtairalmKAGDEPLKKYDLSSL---RLLGSAGEPLNPEVWEWWYE-AVGVPIVDGWGQTETG 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2332 VGILTCtvPEEWPVEQGVPvGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLS--LGYWQRAEQTAERFVAHPlaPDr 2409
Cdd:COG0365 345 GIFISN--LPGLPVKPGSM-GKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPWPGmfRGYWNDPERYRETYFGRF--PG- 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2410 lLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANG--------VLQLGAciQG 2481
Cdd:COG0365 419 -WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRgqvvkafvVLKPGV--EP 495
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 2482 SLEGVAE---ALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLLQQDDA-DSSA----EAIDE 2540
Cdd:COG0365 496 SDELAKElqaHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGRPLgDTSTledpEALDE 562
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
3525-4006 |
7.46e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 161.21 E-value: 7.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAP 3604
Cdd:PRK07798 9 FEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3605 AARRGFILEDSGVCLSVSQRALA-------VELPG--TALCLDDPFTRAQL-------DAVEPGElPEVPTEAPA----Y 3664
Cdd:PRK07798 89 EDELRYLLDDSDAVALVYEREFAprvaevlPRLPKlrTLVVVEDGSGNDLLpgavdyeDALAAGS-PERDFGERSpddlY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3665 LIYTSGSTGTPKGVVVTHRNVER-LFTAAT-QTGRFSFDEHDVWS---------------LFHSHAFdfavWELWGAWLY 3727
Cdd:PRK07798 168 LLYTGGTTGMPKGVMWRQEDIFRvLLGGRDfATGEPIEDEEELAKraaagpgmrrfpappLMHGAGQ----WAAFAALFS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3728 GGRAVLVPEAVCRqPDAFLDLLAEYGVTVLNQTPSAFYA--LQSQAMRRELAL-NVRAVVFGGEALEPSRLQPWRERYPQ 3804
Cdd:PRK07798 244 GQTVVLLPDVRFD-ADEVWRTIEREKVNVITIVGDAMARplLDALEARGPYDLsSLFAIASGGALFSPSVKEALLELLPN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3805 AELVNMYGITETTVHvSFHRLSDEDLQSPTSRIGsalPDLAVHVLDAAGQPVPLG--VVGELVVEGDgVAQGYWQRPELT 3882
Cdd:PRK07798 323 VVLTDSIGSSETGFG-GSGTVAKGAVHTGGPRFT---IGPRTVVLDEDGNPVEPGsgEIGWIARRGH-IPLGYYKDPEKT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3883 AERFVERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEGAWlmAYAV 3962
Cdd:PRK07798 398 AETFPTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVV--GVPDERW--GQEV 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1246793773 3963 AA-----DGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLD 4006
Cdd:PRK07798 474 VAvvqlrEGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
3535-4010 |
1.45e-40 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 158.03 E-value: 1.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3535 RIAVSAEDGELDYATLDRRSSQLATLLIRQGAG-PGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILE 3613
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIvPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3614 DSGvclsvsqralavelPGTALCLDdpftraQLDAVEPgelpevpteaPAYLIYTSGSTGTPKGVVVTHRNVERLF-TAA 3692
Cdd:cd05958 81 KAR--------------ITVALCAH------ALTASDD----------ICILAFTSGTTGAPKATMHFHRDPLASAdRYA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3693 TQTGRFSFDEHDVWS--LFHSHAFDFAVWELWGAwlyGGRAVLVPEAVcrqPDAFLDLLAEYGVTVLNQTPSAFYA-LQS 3769
Cdd:cd05958 131 VNVLRLREDDRFVGSppLAFTFGLGGVLLFPFGV---GASGVLLEEAT---PDLLLSAIARYKPTVLFTAPTAYRAmLAH 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3770 QAMRRELALNVRAVVFGGEALEPSRLQPWRERYpQAELVNMYGITEttvhvSFHRL--SDEDLQSPtSRIGSALPDLAVH 3847
Cdd:cd05958 205 PDAAGPDLSSLRKCVSAGEALPAALHRAWKEAT-GIPIIDGIGSTE-----MFHIFisARPGDARP-GATGKPVPGYEAK 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3848 VLDAAGQPVPLGVVGELVVEGDgvaQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIE 3927
Cdd:cd05958 278 VVDDEGNPVPDGTIGRLAVRGP---TGCRYLADKRQRTYVQGG---WNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3928 PGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQ---SLREALRALLPDYMLPRLIQLLPALPLTANG 4003
Cdd:cd05958 352 PPEVEDVLLQHPAVAECAVVgHPDESRGVVVKAFVVLRPGVIPGPVlarELQDHAKAHIAPYKYPRAIEFVTELPRTATG 431
|
....*..
gi 1246793773 4004 KLDRKAL 4010
Cdd:cd05958 432 KLQRFAL 438
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
3525-4007 |
1.64e-40 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 160.71 E-value: 1.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPAR--IAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPH 3602
Cdd:PRK12583 24 FDATVARFPDReaLVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3603 APAARRGFILEDSGV----CL----SVSQRALAVEL--------PGTALCLDDPFTR--AQLDAVEPGEL---PEVPTEA 3661
Cdd:PRK12583 104 YRASELEYALGQSGVrwviCAdafkTSDYHAMLQELlpglaegqPGALACERLPELRgvVSLAPAPPPGFlawHELQARG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3662 -------------------PAYLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEHDVW----SLFHSHAFDFAV 3718
Cdd:PRK12583 184 etvsrealaerqasldrddPINIQYTSGTTGFPKGATLSHHNI--LNNGYFVAESLGLTEHDRLcvpvPLYHCFGMVLAN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3719 WelwgAWLYGGRAVLVPeAVCRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALN-VRAVVFGGEALEPSRLQP 3797
Cdd:PRK12583 262 L----GCMTVGACLVYP-NEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSsLRTGIMAGAPCPIEVMRR 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3798 WRERYPQAELVNMYGITETTvHVSFHRLSDEDLQSPTSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQ 3877
Cdd:PRK12583 337 VMDEMHMAEVQIAYGMTETS-PVSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYWN 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3878 RPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAW 3956
Cdd:PRK12583 416 NPEATAESIDEDG---WMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFgVPDEKYGEE 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 3957 LMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDR 4007
Cdd:PRK12583 493 IVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
2051-2524 |
2.22e-40 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 157.45 E-value: 2.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVG-VQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVL 2129
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 DDSGARIVIgwgaapawvpasvrwldaesvldvvsayeepprvdvdadTPAYLIYTSGSTGTPKGVVVSQGNLANYVAG- 2208
Cdd:cd05941 81 TDSEPSLVL---------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRAl 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2209 -----------VLPVLDLGEDASLatlstvaadlgFTALFGALLSGRRVRLLPAelaFDAQALAAHLQAHPVDCLKIVP- 2276
Cdd:cd05941 122 vdawrwteddvLLHVLPLHHVHGL-----------VNALLCPLFAGASVEFLPK---FDPKEVAISRLMPSITVFMGVPt 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2277 -------SHLAGLLAAAGGTAVLPREC--LVTGGEALTGALVQQVRALApTLRIVNHYGPTETtvGILTcTVPEEWPVEQ 2347
Cdd:cd05941 188 iytrllqYYEAHFTDPQFARAAAAERLrlMVSGSAALPVPTLEEWEAIT-GHTLLERYGMTEI--GMAL-SNPLDGERRP 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2348 GVpVGHPLAGNEAWVLDRF-GLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAhplapDRLlYRSGDLARLDGEGRI 2426
Cdd:cd05941 264 GT-VGMPLPGVQARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTD-----DGW-FKTGDLGVVDEDGYY 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2427 VYLGRG-DHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGAN-G-------VLQLGACiQGSLEGVAEALAQRLPEY 2497
Cdd:cd05941 337 WILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDwGervvavvVLRAGAA-ALSLEELKEWAKQRLAPY 415
|
490 500
....*....|....*....|....*..
gi 1246793773 2498 LCPSRWRAVESMPRLGNGKIDRQALAD 2524
Cdd:cd05941 416 KRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
3529-4010 |
7.77e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 157.28 E-value: 7.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVS--AEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAA 3606
Cdd:PRK09088 5 ARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3607 RRGFILEDSGVCLSVSQRALAVelpGTALCLDDPFTRAQLDAVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNve 3686
Cdd:PRK09088 85 ELDALLQDAEPRLLLGDDAVAA---GRTDVEDLAAFIASADALEPADTPSIPPERVSLILFTSGTSGQPKGVMLSERN-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3687 rLFTAATQTGRFSFDEHDvwSLFHSHAFDFAVWELWGAW---LYGGRAVLVPEAVcrQPDAFLDLLAE--YGVTVLNQTP 3761
Cdd:PRK09088 160 -LQQTAHNFGVLGRVDAH--SSFLCDAPMFHIIGLITSVrpvLAVGGSILVSNGF--EPKRTLGRLGDpaLGITHYFCVP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3762 SAFYALQSQAMRRELALNVRAVVFGGEALEPSR-LQPWRERypQAELVNMYGITET-TVhvsFHRLSDEDLQSptSRIGS 3839
Cdd:PRK09088 235 QMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEdILGWLDD--GIPMVDGFGMSEAgTV---FGMSVDCDVIR--AKAGA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3840 A---LPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGD 3916
Cdd:PRK09088 308 AgipTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDG---WFRTGDIARRDADGFFWVVDRKK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3917 DQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEGAW---LMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQL 3993
Cdd:PRK09088 385 DMFISGGENVYPAEIEAVLADHPGIRECAVV--GMADAQWgevGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRL 462
|
490
....*....|....*..
gi 1246793773 3994 LPALPLTANGKLDRKAL 4010
Cdd:PRK09088 463 VDALPRTASGKLQKARL 479
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
3510-3946 |
9.28e-40 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 159.11 E-value: 9.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3510 TSRERYACTGNLVSRFAEIARRYPARIAVSAEDG----ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVA 3585
Cdd:COG1022 2 SEFSDVPPADTLPDLLRRRAARFPDRVALREKEDgiwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3586 LLAILKTGAAYVPVDPHAPAARRGFILEDSGV-CLSVS-----QRALAV--ELPG--TALCLDDPFTRAQLDAV------ 3649
Cdd:COG1022 82 DLAILAAGAVTVPIYPTSSAEEVAYILNDSGAkVLFVEdqeqlDKLLEVrdELPSlrHIVVLDPRGLRDDPRLLsldell 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3650 -------EPGELPEVPTEA----PAYLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEHDVWSLF--HSHAFDF 3716
Cdd:COG1022 162 algrevaDPAELEARRAAVkpddLATIIYTSGTTGRPKGVMLTHRNL--LSNARALLERLPLGPGDRTLSFlpLAHVFER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3717 aVWELwgAWLYGGRAVlvpeAVCRQPDAFLDLLAEYGVTVL--------------------------------------- 3757
Cdd:COG1022 240 -TVSY--YALAAGATV----AFAESPDTLAEDLREVKPTFMlavprvwekvyagiqakaeeagglkrklfrwalavgrry 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3758 ------NQTPSAFYALQSQ--------AMRRELALNVRAVVFGGEALEPsRLQpwreRYPQA---ELVNMYGITETTVHV 3820
Cdd:COG1022 313 ararlaGKSPSLLLRLKHAladklvfsKLREALGGRLRFAVSGGAALGP-ELA----RFFRAlgiPVLEGYGLTETSPVI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3821 SFHRLSDedlqsptSRIGSalpdlavhvldaAGQPVP-----LGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFY 3895
Cdd:COG1022 388 TVNRPGD-------NRIGT------------VGPPLPgvevkIAEDGEILVRGPNVMKGYYKNPEATAEAFDADG---WL 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 3896 RSGDLGRYRADGSLEYRGRGDDQVKLR-GYRIEPGEIAAKIASLPQVSDAAV 3946
Cdd:COG1022 446 HTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVV 497
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
282-1101 |
1.00e-39 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 163.70 E-value: 1.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 282 APHLHELPLDHERPAVLGQSGAKLRLAFPPglservAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRP 361
Cdd:TIGR03443 8 NPTLSVLPHDYLRPANNRLVEATYSLQLPS------AEVTAGGGSTPFIILLAAFAALVYRLTGDEDIVLGTSSNKSGRP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 362 eldslvglfvntVVLRTQLHDDPDFASLVARCRDHQLAALEHQALPLERVIETLQVE-RSSRHAPLFQLMFalrhdadla 440
Cdd:TIGR03443 82 ------------FVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAkKLERTPPLFRLAF--------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 441 LDLHGVQAhaltlpEDVAKHELT-LEVLVGAGGMSAVWE--YNTALWNPATVARWAERYFVALAAMLENPHEPALSWPwp 517
Cdd:TIGR03443 141 QDAPDNQQ------TTYSTGSTTdLTVFLTPSSPELELSiyYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKVS-- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 518 adeLALDDKRE--PAPRT-------VGNVVDAIARAADEFPER-------AALETAQGR--LSYRELLTAADARAAALRR 579
Cdd:TIGR03443 213 ---LITPSQKSllPDPTKdldwsgfRGAIHDIFADNAEKHPDRtcvvetpSFLDPSSKTrsFTYKQINEASNILAHYLLK 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 580 RLGAQARSVALCLPRGLDWYCLLLGAWRAG--LSVIplDTEWPQAR----------RAEVVAASgcdavltdaqglAG-F 646
Cdd:TIGR03443 290 TGIKRGDVVMIYAYRGVDLVVAVMGVLKAGatFSVI--DPAYPPARqtiylsvakpRALIVIEK------------AGtL 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 647 APSVAIAVD-ELKL-----------DGAGENGSGENAAPNQLAYIL--------------------YTSGSTGIPKGVEV 694
Cdd:TIGR03443 356 DQLVRDYIDkELELrteipalalqdDGSLVGGSLEGGETDVLAPYQalkdtptgvvvgpdsnptlsFTSGSEGIPKGVLG 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 695 GHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGA-CVVARPDELLEPQRFLAFLSERAITVTDLAPA 773
Cdd:TIGR03443 436 RHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAqLLVPTADDIGTPGRLAEWMAKYGATVTHLTPA 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 774 YANELVRASVAddwRDLALRCLVVGGDVLP-------VALAQrwfelgldrRCALINAYGPTEATISSHYHRVQAIDASR 846
Cdd:TIGR03443 516 MGQLLSAQATT---PIPSLHHAFFVGDILTkrdclrlQTLAE---------NVCIVNMYGTTETQRAVSYFEIPSRSSDS 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 847 P--------VPLG------QLLpgriaaVLDAHGRIVPRGV--CGELALGGIGLAEGYRGDAAASERRFA------PLRL 904
Cdd:TIGR03443 584 TflknlkdvMPAGkgmknvQLL------VVNRNDRTQTCGVgeVGEIYVRAGGLAEGYLGLPELNAEKFVnnwfvdPSHW 657
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 905 PS--------------GESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAAGVVGEG 970
Cdd:TIGR03443 658 IDldkennkperefwlGPRDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDK 737
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 971 AAQR-LVAWVecagEDGFGQADLNQ--TDSDQTESE-------RWHRALCE--------RLPAYMVPTQFVALPRLPRNA 1032
Cdd:TIGR03443 738 DEEPtLVSYI----VPQDKSDELEEfkSEVDDEESSdpvvkglIKYRKLIKdireylkkKLPSYAIPTVIVPLKKLPLNP 813
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1033 SGKIDRRALPAPPV--LAQAERTPPRTAEESALCE-------VWAEVL---QCEVGIHDSFFRLGGDSIRSLQVVARLRE 1100
Cdd:TIGR03443 814 NGKVDKPALPFPDTaqLAAVAKNRSASAADEEFTEtereirdLWLELLpnrPATISPDDSFFDLGGHSILATRMIFELRK 893
|
.
gi 1246793773 1101 R 1101
Cdd:TIGR03443 894 K 894
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
3529-4019 |
9.49e-39 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 154.96 E-value: 9.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAV-----SAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVdPHA 3603
Cdd:cd05970 27 AKEYPDKLALvwcddAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPA-THQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3604 PAAR-----------RGFILEDSGVCLSVSQRALA--VELPGTALCLDD------PFTRAQLDAVEPGELPEVPTEA--- 3661
Cdd:cd05970 106 LTAKdivyriesadiKMIVAIAEDNIPEEIEKAAPecPSKPKLVWVGDPvpegwiDFRKLIKNASPDFERPTANSYPcge 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3662 -PAYLIYTSGSTGTPKgvVVTHRNVERLFTAATQTGRFSFDEHDVWSLFHSHAFDFAVW-ELWGAWLyGGRAVLVPEAVC 3739
Cdd:cd05970 186 dILLVYFSSGTTGMPK--MVEHDFTYPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWgKIYGQWI-AGAAVFVYDYDK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3740 RQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALNVRAVVFGGEALEPSRLQPWRErYPQAELVNMYGITETTVH 3819
Cdd:cd05970 263 FDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKE-KTGIKLMEGFGQTETTLT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3820 V-SFHRLSDEdlqsPTSrIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGD-----GVAQGYWQRPELTAERFVERggqr 3893
Cdd:cd05970 342 IaTFPWMEPK----PGS-MGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTAEVWHDG---- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3894 FYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDpq 3972
Cdd:cd05970 413 YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTgVPDPIRGQVVKATIVLAKGYEPS-- 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 3973 slrEALRALLPD--------YMLPRLIQLLPALPLTANGKLDRKalpkpETQDRD 4019
Cdd:cd05970 491 ---EELKKELQDhvkkvtapYKYPRIVEFVDELPKTISGKIRRV-----EIRERD 537
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
537-1041 |
9.57e-39 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 153.49 E-value: 9.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 537 VVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLD 616
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 617 tewPQARRAEVvaasgcDAVLTDAQglagfaPSVAIAVDELKLDGAGENGSGENAA--PNQLAYILYTSGSTGIPKGVEV 694
Cdd:cd05936 81 ---PLYTPREL------EHILNDSG------AKALIVAVSFTDLLAAGAPLGERVAltPEDVAVLQYTSGTTGVPKGAML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 695 GHA--ALAAHIDAAAEALALSADDRVL------HVAGLAVdttleQILAAWSRGACVVARPDelLEPQRFLAFLSERAIT 766
Cdd:cd05936 146 THRnlVANALQIKAWLEDLLEGDDVVLaalplfHVFGLTV-----ALLLPLALGATIVLIPR--FRPIGVLKEIRKHRVT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 767 VTDLAPAYANELVRAsVADDWRDL-ALRCLVVGGDVLPVALAQRWFELgldRRCALINAYGPTEATISSHYHRVQaiDAS 845
Cdd:cd05936 219 IFPGVPTMYIALLNA-PEFKKRDFsSLRLCISGGAPLPVEVAERFEEL---TGVPIVEGYGLTETSPVVAVNPLD--GPR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 846 RPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLpsgeslrmyRSGDRVRLLDDG 925
Cdd:cd05936 293 KPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL---------RTGDIGYMDEDG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 926 ELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA-GVVGEGAAQRLVAWVECAGEDGFGQADLnqtdsdqteser 1004
Cdd:cd05936 364 YFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVvGVPDPYSGEAVKAFVVLKEGASLTEEEI------------ 431
|
490 500 510
....*....|....*....|....*....|....*...
gi 1246793773 1005 whRALC-ERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05936 432 --IAFCrEQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
3547-4005 |
1.04e-38 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 155.81 E-value: 1.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3547 YATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPV----DPHAPAAR------RGFILEDSG 3616
Cdd:cd17634 87 YRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIfggfAPEAVAGRiidsssRLLITADGG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3617 V-------CLSVSQRALAVELPG--TALCLD------------DPFTRAQLDAVEPGELPE-VPTEAPAYLIYTSGSTGT 3674
Cdd:cd17634 167 VragrsvpLKKNVDDALNPNVTSveHVIVLKrtgsdidwqegrDLWWRDLIAKASPEHQPEaMNAEDPLFILYTSGTTGK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3675 PKGVVVTHRNverLFTAATQTGRFSFDEH--DVWSLFHSHAfdfavWELWGAWL-YG----GRAVLVPEAVCRQPDA--F 3745
Cdd:cd17634 247 PKGVLHTTGG---YLVYAATTMKYVFDYGpgDIYWCTADVG-----WVTGHSYLlYGplacGATTLLYEGVPNWPTParM 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3746 LDLLAEYGVTVLNQTPSAFYALQ---SQAMRRELALNVRAVVFGGEALEPsrlQPWR--------ERYPqaeLVNMYGIT 3814
Cdd:cd17634 319 WQVVDKHGVNILYTAPTAIRALMaagDDAIEGTDRSSLRILGSVGEPINP---EAYEwywkkigkEKCP---VVDTWWQT 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3815 ETTVHVSFHRLSDEDLQSPTSRIgsALPDLAVHVLDAAGQPVPLGVVGELVVEGD--GVAQGYWQRPELTAERFVERGgQ 3892
Cdd:cd17634 393 ETGGFMITPLPGAIELKAGSATR--PVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHERFEQTYFSTF-K 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3893 RFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDP 3971
Cdd:cd17634 470 GMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVgIPHAIKGQAPYAYVVLNHGVEPSP 549
|
490 500 510
....*....|....*....|....*....|....*...
gi 1246793773 3972 qSLREALRALLPDYM----LPRLIQLLPALPLTANGKL 4005
Cdd:cd17634 550 -ELYAELRNWVRKEIgplaTPDVVHWVDSLPKTRSGKI 586
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
3545-4005 |
3.00e-38 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 150.99 E-value: 3.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3545 LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSgvclsvSQR 3624
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRA------KAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3625 ALavelpgtalclddpFTRAQLDAVEPGELPEvpteAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAatQTGRFSFDEHD 3704
Cdd:cd05903 76 VF--------------VVPERFRQFDPAAMPD----AVALLLFTSGTTGEPKGVMHSHNTLSASIRQ--YAERLGLGPGD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3705 VW----SLFHSHAFDFAVWElwgAWLYGGRAVLvpeavCR--QPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELAL 3778
Cdd:cd05903 136 VFlvasPMAHQTGFVYGFTL---PLLLGAPVVL-----QDiwDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3779 -NVRAVVFGGEALEPSRLQPWRERYpQAELVNMYGITETTVHVSFHRLSDEDLQSPTSriGSALPDLAVHVLDAAGQPVP 3857
Cdd:cd05903 208 sRLRTFVCGGATVPRSLARRAAELL-GAKVCSAYGSTECPGAVTSITPAPEDRRLYTD--GRPLPGVEIKVVDDTGATLA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3858 LGVVGELVVEGDGVAQGYWQRPELTAERFVErggqRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIAS 3937
Cdd:cd05903 285 PGVEGELLSRGPSVFLGYLDRPDLTADAAPE----GWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLG 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 3938 LPQVSDAAVTV---EGQGEGAwlMAYAVAADGAEPDPQSLREAL-RALLPDYMLPRLIQLLPALPLTANGKL 4005
Cdd:cd05903 361 HPGVIEAAVVAlpdERLGERA--CAVVVTKSGALLTFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
3501-4005 |
4.68e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 153.01 E-value: 4.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3501 PSQTRSAAWTsreryactgNLVSRFAEIArryPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGC 3580
Cdd:PRK07786 11 PYLARRQNWV---------NQLARHALMQ---PDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3581 DLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVCLSVSQRALA---------VELPGTALCLDDPFTRAQLD---- 3647
Cdd:PRK07786 79 EFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALApvatavrdiVPLLSTVVVAGGSSDDSVLGyedl 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3648 ---AVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVerlfTAATQTGRFSFD---EHDVW----SLFHSHAFDFA 3717
Cdd:PRK07786 159 laeAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANL----TGQAMTCLRTNGadiNSDVGfvgvPLFHIAGIGSM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3718 VWELwgawLYGGRAVLVPEAVCrQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALNVRAVVFGGEALEPSRLQP 3797
Cdd:PRK07786 235 LPGL----LLGAPTVIYPLGAF-DPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3798 WRERYPQAELVNMYGITETTvHVSFHRLSDEDLQSPTSrIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQ 3877
Cdd:PRK07786 310 MAATFPEAQILAAFGQTEMS-PVTCMLLGEDAIRKLGS-VGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3878 RPELTAERFveRGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEGAW- 3956
Cdd:PRK07786 388 NPEATAEAF--AGG--WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVI--GRADEKWg 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 3957 ---LMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKL 4005
Cdd:PRK07786 462 evpVAVAAVRNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
603-1041 |
9.78e-38 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 151.20 E-value: 9.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 603 LGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQGLAGFAPSVAIAVDELKLDGAGENGSGENAA--PNQLAYIL 680
Cdd:PRK04813 70 LGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLIIATEELPLEILGIPVITLDELKDIFATGNPYDFDHAvkGDDNYYII 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 681 YTSGSTGIPKGVEVGHaalaahidaaaealalsaddrvlhvaglavDTTLEqiLAAWsrgacvvARPD-ELLEPQRFLA- 758
Cdd:PRK04813 150 FTSGTTGKPKGVQISH------------------------------DNLVS--FTNW-------MLEDfALPEGPQFLNq 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 759 ----F-LSeraitVTDLAPAYA-----NELVRAsVADDWRDL--ALRCLVVG---------------------------- 798
Cdd:PRK04813 191 apysFdLS-----VMDLYPTLAsggtlVALPKD-MTANFKQLfeTLPQLPINvwvstpsfadmclldpsfneehlpnlth 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 799 ----GDVLPVALAQRWFELGLDRRcaLINAYGPTEAT--ISSHYHRVQAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRG 872
Cdd:PRK04813 265 flfcGEELPHKTAKKLLERFPSAT--IYNTYGPTEATvaVTSIEITDEMLDQYKRLPIGYAKPDSPLLIIDEEGTKLPDG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 873 VCGELALGGIGLAEGYRGDAAASERRFAPLrlpsgESLRMYRSGDRVRLlDDGELQFLGRADFQVKLRGYRIELEEIEHC 952
Cdd:PRK04813 343 EQGEIVISGPSVSKGYLNNPEKTAEAFFTF-----DGQPAYHTGDAGYL-EDGLLFYQGRIDFQIKLNGYRIELEEIEQN 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 953 LGQLPQVRAA-AAGVVGEGAAQRLVAWVECAGEDGFGQADLNQtdsdQTESErwhraLCERLPAYMVPTQFVALPRLPRN 1031
Cdd:PRK04813 417 LRQSSYVESAvVVPYNKDHKVQYLIAYVVPKEEDFEREFELTK----AIKKE-----LKERLMEYMIPRKFIYRDSLPLT 487
|
490
....*....|
gi 1246793773 1032 ASGKIDRRAL 1041
Cdd:PRK04813 488 PNGKIDRKAL 497
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
3545-4010 |
1.02e-37 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 150.05 E-value: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3545 LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVclsvsqR 3624
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA------K 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3625 ALAVELPgtalclDDPFTraqldavepgelpevpteapayLIYTSGSTGTPKGVVVTHRNVERLFTAATQtgRFSFDEHD 3704
Cdd:cd05907 80 ALFVEDP------DDLAT----------------------IIYTSGTTGRPKGVMLSHRNILSNALALAE--RLPATEGD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3705 VWSLF--HSHAFDFAVWELwgAWLYGGRAVLVPEAvcrqPDAFLDLLAEYGVTVLNQTP-------SAFYALQSQAMRRE 3775
Cdd:cd05907 130 RHLSFlpLAHVFERRAGLY--VPLLAGARIYFASS----AETLLDDLSEVRPTVFLAVPrvwekvyAAIKVKAVPGLKRK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3776 LAL-----NVRAVVFGGEALEPSRLqpwreRYPQAELVNM---YGITETTVHVSFHRLSDEDLQSptsrIGSALPDLAVH 3847
Cdd:cd05907 204 LFDlavggRLRFAASGGAPLPAELL-----HFFRALGIPVyegYGLTETSAVVTLNPPGDNRIGT----VGKPLPGVEVR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3848 VldaagqpvplGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKLR-GYRI 3926
Cdd:cd05907 275 I----------ADDGEILVRGPNVMLGYYKNPEATAEALDADG---WLHTGDLGEIDEDGFLHITGRKKDLIITSgGKNI 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3927 EPGEIAAKIASLPQVSDAAVTVEGQ---------------------GEGAWLMAYAVAADGAEPDPQSLREALRALLPDY 3985
Cdd:cd05907 342 SPEPIENALKASPLISQAVVIGDGRpflvalivpdpealeawaeehGIAYTDVAELAANPAVRAEIEAAVEAANARLSRY 421
|
490 500 510
....*....|....*....|....*....|..
gi 1246793773 3986 MLPRLIQLLPaLP-------LTANGKLDRKAL 4010
Cdd:cd05907 422 EQIKKFLLLP-EPftiengeLTPTLKLKRPVI 452
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
1598-1948 |
5.12e-37 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380453 [Multi-domain] Cd Length: 427 Bit Score: 147.17 E-value: 5.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1598 FPLTPLQRGVLLESLRGDGADPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTaIVWEGLSVPHQIVLADAAAP-WQ 1676
Cdd:cd19066 2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRT-RFCEEAGRYEQVVLDKTVRFrIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1677 TLDWSALDDaaQDAQLQRWLADDAAQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQ 1756
Cdd:cd19066 81 IIDLRNLAD--PEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1757 GATLRLPPAPGFQAYLDW----RERQDLARQRGWWRERLSGYAGTAALPAPVAAAHHP-VQREECERRLSAHDSERLRAF 1831
Cdd:cd19066 159 QKPTLPPPVGSYADYAAWlekqLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVAsYEVLTLEFFLRSEETKRLREV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1832 CRERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPPElaGVESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSL 1911
Cdd:cd19066 239 ARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDE--AVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSR 316
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1246793773 1912 EVAENEAVGLGEILADSG----LDADRLFASLLVVENFPAM 1948
Cdd:cd19066 317 EAIEHQRVPFIELVRHLGvvpeAPKHPLFEPVFTFKNNQQQ 357
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
3667-4007 |
5.56e-37 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 145.11 E-value: 5.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3667 YTSGSTGTPKGVVVTHRNVerlFTAATQTG-RFSFDEHDVW----SLFHshAFDFAVWELwGAWLYGGRAVLVPEAVcrQ 3741
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNI---VNNGYFIGeRLGLTEQDRLcipvPLFH--CFGSVLGVL-ACLTHGATMVFPSPSF--D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3742 PDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELAL-NVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVhV 3820
Cdd:cd05917 81 PLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLsSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETSP-V 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3821 SFHRLSDEDLQSPTSRIGSALPDLAVHVLDAAGQPVP-LGVVGELVVEGDGVAQGYWQRPELTAErfvERGGQRFYRSGD 3899
Cdd:cd05917 160 STQTRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEKTAE---AIDGDGWLHTGD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3900 LGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSLREAL 3978
Cdd:cd05917 237 LAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVgVPDERYGEEVCAWIRLKEGAELTEEDIKAYC 316
|
330 340
....*....|....*....|....*....
gi 1246793773 3979 RALLPDYMLPRLIQLLPALPLTANGKLDR 4007
Cdd:cd05917 317 KGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
3520-4010 |
5.85e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 148.88 E-value: 5.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPV 3599
Cdd:PRK06145 3 NLSASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3600 DPHAPAARRGFILEDSGV-CLSVSQRALAVELPGTALCLDDPFTRAQLDAVEPGELPEVPTEAPA-----YLIYTSGSTG 3673
Cdd:PRK06145 83 NYRLAADEVAYILGDAGAkLLLVDEEFDAIVALETPKIVIDAAAQADSRRLAQGGLEIPPQAAVAptdlvRLMYTSGTTD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3674 TPKGVVVTHRNVErlFTAATQTGRFSFDEHD----VWSLFHSHAFDFAvwelwgawlygGRAVLVPEAVCR-----QPDA 3744
Cdd:PRK06145 163 RPKGVMHSYGNLH--WKSIDHVIALGLTASErllvVGPLYHVGAFDLP-----------GIAVLWVGGTLRihrefDPEA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3745 FLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALN-VRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFH 3823
Cdd:PRK06145 230 VLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDsLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3824 RLSDEdlqspTSRIGS---ALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVerGGqrFYRSGDL 3900
Cdd:PRK06145 310 EAGRE-----IEKIGStgrALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFY--GD--WFRSGDV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3901 GRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEGAW---LMAYAVAADGAEPDPQSLREA 3977
Cdd:PRK06145 381 GYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVI--GVHDDRWgerITAVVVLNPGATLTLEALDRH 458
|
490 500 510
....*....|....*....|....*....|...
gi 1246793773 3978 LRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK06145 459 CRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
3507-4008 |
6.19e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 150.15 E-value: 6.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3507 AAWTSRERYACTGNLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVAL 3586
Cdd:PRK05605 20 APWTPHDLDYGDTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3587 LAILKTGAAYVPVDPHAPAARRGFILEDSGVCLSVS-----------------QRALAVELPG-------TALCLDDPF- 3641
Cdd:PRK05605 100 YAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVwdkvaptverlrrttplETIVSVNMIAampllqrLALRLPIPAl 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3642 --TRAQLDAVEPG-------------------ELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNverLFTAATQ-----T 3695
Cdd:PRK05605 180 rkARAALTGPAPGtvpwetlvdaaiggdgsdvSHPRPTPDDVALILYTSGTTGKPKGAQLTHRN---LFANAAQgkawvP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3696 GRFSFDE--HDVWSLFHSHAF----DFAVwelwgawLYGGRAVLVPEAvcrQPDAFLDLLAEYGVTVLNQTPSAFYALQS 3769
Cdd:PRK05605 257 GLGDGPErvLAALPMFHAYGLtlclTLAV-------SIGGELVLLPAP---DIDLILDAMKKHPPTWLPGVPPLYEKIAE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3770 QAMRRELALN-VRAVVFGGEALEPSRLQPWrERYPQAELVNMYGITETTVHVSFHRLSDEdlQSPTSrIGSALPDLAVHV 3848
Cdd:PRK05605 327 AAEERGVDLSgVRNAFSGAMALPVSTVELW-EKLTGGLLVEGYGLTETSPIIVGNPMSDD--RRPGY-VGVPFPDTEVRI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3849 LDA--AGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVErggqRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRI 3926
Cdd:PRK05605 403 VDPedPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLD----GWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3927 EPGEIAAKIASLPQVSDAAVTVEGQGEGAW-LMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKL 4005
Cdd:PRK05605 479 YPAEVEEVLREHPGVEDAAVVGLPREDGSEeVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKV 558
|
...
gi 1246793773 4006 DRK 4008
Cdd:PRK05605 559 RRR 561
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
648-1041 |
7.24e-37 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 147.59 E-value: 7.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 648 PSVAIAVDELklDGAGENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVD 727
Cdd:cd05922 93 PGTVLDADGI--RAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 728 TTLEQILAAWSRGACVVARPDELLePQRFLAFLSERAITVTDLAPAYANELVRAsvadDWRDLA---LRCLVVGGDVLPV 804
Cdd:cd05922 171 YGLSVLNTHLLRGATLVLTNDGVL-DDAFWEDLREHGATGLAGVPSTYAMLTRL----GFDPAKlpsLRYLTQAGGRLPQ 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 805 ALAQRWFELGLDRRCALInaYGPTEATISSHY---HRVqaidASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGG 881
Cdd:cd05922 246 ETIARLRELLPGAQVYVM--YGQTEATRRMTYlppERI----LEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRG 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 882 IGLAEGYRGDaaaserrfAPLRLPSGESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRA 961
Cdd:cd05922 320 PNVMKGYWND--------PPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIE 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 962 AAAGVVGEGAAQRLVAWVEcagedgfgqADLNQTDSDQTeserwhRALCERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05922 392 AAAVGLPDPLGEKLALFVT---------APDKIDPKDVL------RSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
3529-4010 |
1.10e-36 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 148.16 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDG----ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGA---------- 3594
Cdd:cd12119 6 ARLHGDREIVSRTHEgevhRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAvlhtinprlf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3595 ----AYV--------------------PVDPHAPAARRGFILEDSgvclsvsqRALAVELPGTALCLDDpftraQLDAVE 3650
Cdd:cd12119 86 peqiAYIinhaedrvvfvdrdflplleAIAPRLPTVEHVVVMTDD--------AAMPEPAGVGVLAYEE-----LLAAES 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3651 P-GELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQTGRFSFDEHDVW----SLFHSHAfdfavwelWG-- 3723
Cdd:cd12119 153 PeYDWPDFDENTAAAICYTSGTTGNPKGVVYSHRSLVLHAMAALLTDGLGLSESDVVlpvvPMFHVNA--------WGlp 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3724 --AWLYGGRAVLVPEAVcrQPDAFLDLLAEYGVTVLNQTPSAFYALQS--QAMRRELaLNVRAVVFGGEALEPSRLQPWR 3799
Cdd:cd12119 225 yaAAMVGAKLVLPGPYL--DPASLAELIEREGVTFAAGVPTVWQGLLDhlEANGRDL-SSLRRVVIGGSAVPRSLIEAFE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3800 ERYpqAELVNMYGITETTVHVSFHRLSDEDLQSP-------TSRIGSALPDLAVHVLDAAGQPVPL--GVVGELVVEGDG 3870
Cdd:cd12119 302 ERG--VRVIHAWGMTETSPLGTVARPPSEHSNLSedeqlalRAKQGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPW 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3871 VAQGYWQRPELTAERFveRGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveG 3950
Cdd:cd12119 380 VTKSYYKNDEESEALT--EDG--WLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVI--G 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 3951 QGEGAWL---MAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:cd12119 454 VPHPKWGerpLAVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
586-1041 |
1.12e-36 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 146.85 E-value: 1.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 586 RSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQglagfapsvaiaVDELKLDGAGEN 665
Cdd:cd17654 42 RAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNKE------------LDNAPLSFTPEH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 666 GSGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVA 745
Cdd:cd17654 110 RHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 746 RPDEL-LEPQRFLAFLSER-AITVTDLAPAYANELVRASVADDW--RDLALRCLVVGGDVLPVALAQR-WFELGLdrRCA 820
Cdd:cd17654 190 VPTSVkVLPSKLADILFKRhRITVLQATPTLFRRFGSQSIKSTVlsATSSLRVLALGGEPFPSLVILSsWRGKGN--RTR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 821 LINAYGPTEATISSHYHRVQAIDAsrPVPLGQLLPGRIAAVLDAHGrivpRGVCGELALGGIGLAeGYRGDaaaserrfa 900
Cdd:cd17654 268 IFNIYGITEVSCWALAYKVPEEDS--PVQLGSPLLGTVIEVRDQNG----SEGTGQVFLGGLNRV-CILDD--------- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 901 PLRLPSGEslrMYRSGDRVRlLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagvvgegaaqrlVAWve 980
Cdd:cd17654 332 EVTVPKGT---MRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCA------------VTL-- 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 981 cagedgFGQADLNQTDSDQTESERWHRAL-CERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd17654 394 ------SDQQRLIAFIVGESSSSRIHKELqLTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
1142-1373 |
2.13e-36 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 139.79 E-value: 2.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1142 LSPIQRWFFDSAPAQPDrYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPaIQAQDWR 1221
Cdd:COG4908 1 LSPAQKRFLFLEPGSNA-YNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLP-LEVVDLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1222 GAADlDSRVDAAFARMQE--ATPL---AGPLVALTHAHCDDGE-RLLICAHHLIVDAVSWRLLLGELFDGLAALARGEAW 1295
Cdd:COG4908 79 ALPE-PEREAELEELVAEeaSRPFdlaRGPLLRAALIRLGEDEhVLLLTIHHIISDGWSLGILLRELAALYAALLEGEPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1296 TPSARGASYADYVEALREADDAQRFDA--GFWRELAAQ--PMQALPQDRPValADARQSNVGRIVQTLDAGLTADLLERA 1371
Cdd:COG4908 158 PLPELPIQYADYAAWQRAWLQSEALEKqlEYWRQQLAGapPVLELPTDRPR--PAVQTFRGATLSFTLPAELTEALKALA 235
|
..
gi 1246793773 1372 GE 1373
Cdd:COG4908 236 KA 237
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
1599-1940 |
4.94e-36 |
|
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.
Pssm-ID: 380466 [Multi-domain] Cd Length: 413 Bit Score: 143.73 E-value: 4.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1599 PLTPLQRGVLLESLRGDGADPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGLSVPHQIVLADAAAPWQTL 1678
Cdd:cd19544 3 PLAPLQEGILFHHLLAEEGDPYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAILWEGLSEPVQVVWRQAELPVEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1679 DWSALDDAAqdAQLQRwLADDAAQGVDFAHAPLARMSLI-GRGGGRYWLVWSIHHLIVDGWSTPLLVGEmLQRYTAGaQG 1757
Cdd:cd19544 83 TLDPGDDAL--AQLRA-RFDPRRYRLDLRQAPLLRAHVAeDPANGRWLLLLLFHHLISDHTSLELLLEE-IQAILAG-RA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1758 ATLrLPPAP--GFQAYLdwRERQDLARQRGWWRERLSGYAGTAALPAPVAAAHHPVQREECERRLSAHDSERLRAFCRER 1835
Cdd:cd19544 158 AAL-PPPVPyrNFVAQA--RLGASQAEHEAFFREMLGDVDEPTAPFGLLDVQGDGSDITEARLALDAELAQRLRAQARRL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1836 GCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPPELAGVESMVGVFINTLPLRLRIDaGQPALDLLSALRSQSLEVAE 1915
Cdd:cd19544 235 GVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFINTLPLRVRLG-GRSVREAVRQTHARLAELLR 313
|
330 340
....*....|....*....|....*.
gi 1246793773 1916 NEAVGLGEILADSGLDADR-LFASLL 1940
Cdd:cd19544 314 HEHASLALAQRCSGVPAPTpLFSALL 339
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
3529-4025 |
6.59e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 146.64 E-value: 6.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQ-GAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAAR 3607
Cdd:PRK08314 20 ARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3608 RGFILEDSG----VCLS-------------------VSQRA--------------LAVELPGTALclDDPFTRAQLDAVE 3650
Cdd:PRK08314 100 LAHYVTDSGarvaIVGSelapkvapavgnlrlrhviVAQYSdylpaepeiavpawLRAEPPLQAL--APGGVVAWKEALA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3651 PGELPEVPTEAP---AYLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEHDVW----SLFHSHAFdfaVWELWG 3723
Cdd:PRK08314 178 AGLAPPPHTAGPddlAVLPYTSGTTGVPKGCMHTHRTV--MANAVGSVLWSNSTPESVVlavlPLFHVTGM---VHSMNA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3724 AWLYGGRAVLVPeavcR-QPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALNVRAVVFGGEALEPS----RLQpw 3798
Cdd:PRK08314 253 PIYAGATVVLMP----RwDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMPEavaeRLK-- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3799 rERYpQAELVNMYGITETTVHVSFHRLSDEDLQSptsrIGSALPDLAVHVLDAA-GQPVPLGVVGELVVEGDGVAQGYWQ 3877
Cdd:PRK08314 327 -ELT-GLDYVEGYGLTETMAQTHSNPPDRPKLQC----LGIPTFGVDARVIDPEtLEELPPGEVGEIVVHGPQVFKGYWN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3878 RPELTAERFVERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDA---AVTVEGQGEG 3954
Cdd:PRK08314 401 RPEATAEAFIEIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEAcviATPDPRRGET 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 3955 AwlMAYAVAADGAE--PDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKALpkpetQDRDEGVLES 4025
Cdd:PRK08314 481 V--KAVVVLRPEARgkTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL-----QEQEKARAAK 546
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
1138-1577 |
8.90e-36 |
|
Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.
Pssm-ID: 395541 [Multi-domain] Cd Length: 454 Bit Score: 144.01 E-value: 8.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1138 GEVGLSPIQ--RWFFDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQV---AAPGPA 1212
Cdd:pfam00668 3 DEYPLSPAQkrMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVileERPFEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1213 PAIQAQDWrGAADLDSRVDAaFARMQEATPL---AGPLV-ALTHAHCDDGERLLICAHHLIVDAVSWRLLLGELFDGLAA 1288
Cdd:pfam00668 83 EIIDISDL-SESEEEEAIEA-FIQRDLQSPFdleKGPLFrAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1289 LARGEAwTPSARGASYADYVEALREADDAQRF--DAGFWRELAAQ--PMQALPQDRPvALADaRQSNVGRIVQTLDAGlT 1364
Cdd:pfam00668 161 LLKGEP-LPLPPKTPYKDYAEWLQQYLQSEDYqkDAAYWLEQLEGelPVLQLPKDYA-RPAD-RSFKGDRLSFTLDED-T 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1365 ADLLERAGEAYRCRTDEVLLIALARALATRTGRNRLWLDRERHGRdvlDGRDWSSVLGWYTAVHPLPLDL-GVADGPAQI 1443
Cdd:pfam00668 237 EELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGR---PSPDIERMVGMFVNTLPLRIDPkGGKTFSELI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1444 GALKEQIR-ALARRGLDYMPLVASARIPALPAGQLLF-------NYHGvvdagahPAFEVEPRTLASGN------GADNP 1509
Cdd:pfam00668 314 KRVQEDLLsAEPHQGYPFGDLVNDLRLPRDLSRHPLFdpmfsfqNYLG-------QDSQEEEFQLSELDlsvssvIEEEA 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 1510 PGALvEINARVQAGRLGLVWNYAGEAYDAATIEAWSQAFAAELAALVAHCLQPGSGALTASDLPQARL 1577
Cdd:pfam00668 387 KYDL-SLTASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKL 453
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
3520-4020 |
1.76e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 145.68 E-value: 1.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQ-GAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVP 3598
Cdd:PRK05677 25 NIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3599 VDPHAPAARRGFILEDSG----VCLSVSQRALAVELPGTALC---------LDDPFTRAQLDA--------VEPGELPE- 3656
Cdd:PRK05677 105 TNPLYTAREMEHQFNDSGakalVCLANMAHLAEKVLPKTGVKhvivtevadMLPPLKRLLINAvvkhvkkmVPAYHLPQa 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3657 --------------VPTEAP-----AYLIYTSGSTGTPKGVVVTHRNV--ERLFTAATQTGRFSFDEHDVWS---LFHSH 3712
Cdd:PRK05677 185 vkfndalakgagqpVTEANPqaddvAVLQYTGGTTGVAKGAMLTHRNLvaNMLQCRALMGSNLNEGCEILIAplpLYHIY 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3713 AFDFAVWELwgaWLYGGRAVLVPEAvcRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRREL---ALNVRAVvfGGEA 3789
Cdd:PRK05677 265 AFTFHCMAM---MLIGNHNILISNP--RDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLdfsALKLTLS--GGMA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3790 LEPSRLQPWRErYPQAELVNMYGITETTVHVSFHRLsdEDLQSPTsrIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGD 3869
Cdd:PRK05677 338 LQLATAERWKE-VTGCAICEGYGMTETSPVVSVNPS--QAIQVGT--IGIPVPSTLCKVIDDDGNELPLGEVGELCVKGP 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3870 GVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSD-AAVTV 3948
Cdd:PRK05677 413 QVMKGYWQRPEATDEILDSDG---WLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQcAAIGV 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 3949 EGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKALpkpetqdRDE 4020
Cdd:PRK05677 490 PDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL-------RDE 554
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
3113-3397 |
2.93e-35 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380472 [Multi-domain] Cd Length: 430 Bit Score: 142.07 E-value: 2.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3113 GALDREAFAAAWQQALERHPILRSGF-AVQGLPSprQLPHRQVSLPLAEQDWSGLEPAQArsrLSELQAQQCEAgFDLAA 3191
Cdd:cd20484 34 SKLDVEKFKQACQFVLEQHPILKSVIeEEDGVPF--QKIEPSKPLSFQEEDISSLKESEI---IAYLREKAKEP-FVLEN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3192 PPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAALRESRTP-QLPAAPPFRDYLHW----LRGQDEAAA 3266
Cdd:cd20484 108 GPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPtLASSPASYYDFVAWeqdmLAGAEGEEH 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3267 RAFWREQLTG----LE-PAALPEATEPAEGYASSTRRFDLAAAS---AWAQSHGLTASSLLQGALALVLQRYYGRDDFAL 3338
Cdd:cd20484 188 RAYWKQQLSGtlpiLElPADRPRSSAPSFEGQTYTRRLPSELSNqikSFARSQSINLSTVFLGIFKLLLHRYTGQEDIIV 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 3339 GITIAGRPPElaGVERMLGVFINSVPLRVTPAGEATPAPWLQALQQRNLDLRTHGYLPL 3397
Cdd:cd20484 268 GMPTMGRPEE--RFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLDHAAYPF 324
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
2061-2517 |
2.93e-35 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 143.51 E-value: 2.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2061 SWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIG- 2139
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2140 -------WGAAPAW--------VPASVRW-LDAESVLDVVSAYEE---PPRVDVDADTPAYLIYTSGSTGTPKGVVVSQG 2200
Cdd:cd05911 90 pdglekvKEAAKELgpkdkiivLDDKPDGvLSIEDLLSPTLGEEDedlPPPLKDGKDDTAAILYSSGTTGLPKGVCLSHR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2201 NL-ANY--VAGVLPVLDLGEDASLATLSTVAAdLGFTALFGALLSGRRVRLLPaelAFDAQALAAHLQAHPVDCLKIVPS 2277
Cdd:cd05911 170 NLiANLsqVQTFLYGNDGSNDVILGFLPLYHI-YGLFTTLASLLNGATVIIMP---KFDSELFLDLIEKYKITFLYLVPP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2278 HLAGLLAAAGGTA-VLP--REcLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVgilTCTVPEEWPVEQGvPVGHP 2354
Cdd:cd05911 246 IAAALAKSPLLDKyDLSslRV-ILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGG---ILTVNPDGDDKPG-SVGRL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2355 LAGNEAWVLDRFG-LPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFvahplAPDRLLyRSGDLARLDGEGRIVYLGRGD 2433
Cdd:cd05911 321 LPNVEAKIVDDDGkDSLGPNEPGEICVRGPQVMKGYYNNPEATKETF-----DEDGWL-HTGDIGYFDEDGYLYIVDRKK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2434 HQVKIRGYRVELGEVEQVLAQLPGVEVAAVLA--------LPGANGVLQLGACIqgSLEGVAEALAQRLPEYlcpSRWRA 2505
Cdd:cd05911 395 ELIKYKGFQVAPAELEAVLLEHPGVADAAVIGipdevsgeLPRAYVVRKPGEKL--TEKEVKDYVAKKVASY---KQLRG 469
|
490
....*....|....*.
gi 1246793773 2506 ----VESMPRLGNGKI 2517
Cdd:cd05911 470 gvvfVDEIPKSASGKI 485
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
2061-2608 |
4.31e-35 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 148.67 E-value: 4.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2061 SWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGW 2140
Cdd:TIGR03443 270 SFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIVI 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2141 GAAPAWVPASVRWLDAE-------------------------SVLDVVSAYE----EPPRVDVDADTPAYLIYTSGSTGT 2191
Cdd:TIGR03443 350 EKAGTLDQLVRDYIDKElelrteipalalqddgslvggslegGETDVLAPYQalkdTPTGVVVGPDSNPTLSFTSGSEGI 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2192 PKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADL----GFTALFgallsgrrvrlLPAELafdaqalaahlqah 2267
Cdd:TIGR03443 430 PKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPiqrdMFTPLF-----------LGAQL-------------- 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2268 pvdclkIVPSHLAGLLAAAGGTAVLPRECLVTG-----GEALTGALVQQV---------------------RALAPTLRI 2321
Cdd:TIGR03443 485 ------LVPTADDIGTPGRLAEWMAKYGATVTHltpamGQLLSAQATTPIpslhhaffvgdiltkrdclrlQTLAENVCI 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2322 VNHYGPTETTVGILTCTVPeewPVEQG----------VPVGHPLAGNEAWVLDRFGLPAPVGVA--GELYLGGGNLSLGY 2389
Cdd:TIGR03443 559 VNMYGTTETQRAVSYFEIP---SRSSDstflknlkdvMPAGKGMKNVQLLVVNRNDRTQTCGVGevGEIYVRAGGLAEGY 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2390 WQRAEQTAERFVA----------------------HPLAP-DRLlYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELG 2446
Cdd:TIGR03443 636 LGLPELNAEKFVNnwfvdpshwidldkennkpereFWLGPrDRL-YRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELG 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2447 EVEQVLAQLPGVE----------------VAAVLALPGANGVLQLGACIQGSLEG----------------VAEALAQRL 2494
Cdd:TIGR03443 715 EIDTHLSQHPLVRenvtlvrrdkdeeptlVSYIVPQDKSDELEEFKSEVDDEESSdpvvkglikyrklikdIREYLKKKL 794
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2495 PEYLCPSRWRAVESMPRLGNGKIDRQAL-----ADL-LQQDDADSSAEAIDETPVNEVLRELWQKLLGRE--HIGAHDNF 2566
Cdd:TIGR03443 795 PSYAIPTVIVPLKKLPLNPNGKVDKPALpfpdtAQLaAVAKNRSASAADEEFTETEREIRDLWLELLPNRpaTISPDDSF 874
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1246793773 2567 FALGGDSILSLQLVARARQAGLALMPRQL-YDHPTLAGLSAQV 2608
Cdd:TIGR03443 875 FDLGGHSILATRMIFELRKKLNVELPLGLiFKSPTIKGFAKEV 917
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
551-1041 |
5.70e-35 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 141.45 E-value: 5.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 551 RAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAA 630
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 631 SGCDAVLTDAqglagfapsvaiavdelkldgagengsgenaapNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEAL 710
Cdd:cd05919 81 CEARLVVTSA---------------------------------DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 711 AL-SADDRVLHVAGLAVDTTL-EQILAAWSRGACVVARPdELLEPQRFLAFLSERAITVTDLAPA-YANELVRASVADDw 787
Cdd:cd05919 128 LGlTPGDRVFSSAKMFFGYGLgNSLWFPLAVGASAVLNP-GWPTAERVLATLARFRPTVLYGVPTfYANLLDSCAGSPD- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 788 RDLALRCLVVGGDVLPVALAQRWFELGLdrrCALINAYGPTEatiSSHYHRVQAIDASRPVPLGQLLPGRIAAVLDAHGR 867
Cdd:cd05919 206 ALRSLRLCVSAGEALPRGLGERWMEHFG---GPILDGIGATE---VGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEGH 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 868 IVPRGVCGELALGGIGLAEGYRGDAAASERRFAplrlpsGEslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELE 947
Cdd:cd05919 280 TIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN------GG---WYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 948 EIEHCLGQLPQV-RAAAAGVVGEGAAQRLVAWVECAGEdgfgqadlnqTDSDQTESERWHRALCERLPAYMVPTQFVALP 1026
Cdd:cd05919 351 EVESLIIQHPAVaEAAVVAVPESTGLSRLTAFVVLKSP----------AAPQESLARDIHRHLLERLSAHKVPRRIAFVD 420
|
490
....*....|....*
gi 1246793773 1027 RLPRNASGKIDRRAL 1041
Cdd:cd05919 421 ELPRTATGKLQRFKL 435
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
3545-4013 |
6.19e-35 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 142.92 E-value: 6.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3545 LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVCLSVSQ- 3623
Cdd:PRK12406 12 RSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3624 ---RALAVELPGT--------------------ALCLDDPFT---RAQLDAVEPGELPevPTEAPAYLIYTSGSTGTPKG 3677
Cdd:PRK12406 92 dllHGLASALPAGvtvlsvptppeiaaayrispALLTPPAGAidwEGWLAQQEPYDGP--PVPQPQSMIYTSGTTGHPKG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3678 VVVTHRNVERLFTAATQTGRFSFDEHDVWS-----LFHSHAFDFAVwelwGAWLYGGRAVLVPEAvcrQPDAFLDLLAEY 3752
Cdd:PRK12406 170 VRRAAPTPEQAAAAEQMRALIYGLKPGIRAlltgpLYHSAPNAYGL----RAGRLGGVLVLQPRF---DPEELLQLIERH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3753 GVTVLNQTPSAFYALQS--QAMRRELALN-VRAVVFGGEALEPSRLQPWRERYPQAeLVNMYGITETTVhVSFHRlSDED 3829
Cdd:PRK12406 243 RITHMHMVPTMFIRLLKlpEEVRAKYDVSsLRHVIHAAAPCPADVKRAMIEWWGPV-IYEYYGSTESGA-VTFAT-SEDA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3830 LQSPTSrIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQ-GYWQRPELTAErfVERGGqrFYRSGDLGRYRADGS 3908
Cdd:PRK12406 320 LSHPGT-VGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAE--IDRGG--FITSGDVGYLDADGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3909 LEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGE-GAWLMAYAVAADGAEPDPQSLREALRALLPDYML 3987
Cdd:PRK12406 395 LFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEfGEALMAVVEPQPGATLDEADIRAQLKARLAGYKV 474
|
490 500
....*....|....*....|....*.
gi 1246793773 3988 PRLIQLLPALPLTANGKLDRKALPKP 4013
Cdd:PRK12406 475 PKHIEIMAELPREDSGKIFKRRLRDP 500
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
3507-4010 |
8.99e-35 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 144.17 E-value: 8.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3507 AAWTSRERYACTGNLVSRFAEIARRYPArIAVSAEDGE---LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLL 3583
Cdd:cd05968 52 AAWFVGGRMNIVEQLLDKWLADTRTRPA-LRWEGEDGTsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3584 VALLAILKTGAAYVPV--------------DPHAPA-------ARRGFILE-----------DSGVCLSVSQRALAVELP 3631
Cdd:cd05968 131 PAFLAVARIGGIVVPIfsgfgkeaaatrlqDAEAKAlitadgfTRRGREVNlkeeadkacaqCPTVEKVVVVRHLGNDFT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3632 GTalcLDDPFTRAQLDAVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVErlfTAATQTGRFSFD--EHDVWSLF 3709
Cdd:cd05968 211 PA---KGRDLSYDEEKETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFP---LKAAQDMYFQFDlkPGDLLTWF 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3710 HSHAFDFAVWELWGAWLYGGRAVL---VPEAvcRQPDAFLDLLAEYGVTVLNQTPS---AFYALQSQAMRRELALNVRav 3783
Cdd:cd05968 285 TDLGWMMGPWLIFGGLILGATMVLydgAPDH--PKADRLWRMVEDHEITHLGLSPTlirALKPRGDAPVNAHDLSSLR-- 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3784 VFGGEAlEPSRLQPWR--------ERYPqaeLVNMYGITEttvhVSFHRLSDEDLQ--SPTSrIGSALPDLAVHVLDAAG 3853
Cdd:cd05968 361 VLGSTG-EPWNPEPWNwlfetvgkGRNP---IINYSGGTE----ISGGILGNVLIKpiKPSS-FNGPVPGMKADVLDESG 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3854 QPVPlGVVGELVVEGD--GVAQGYWQRPeltaERFVERGGQRF---YRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEP 3928
Cdd:cd05968 432 KPAR-PEVGELVLLAPwpGMTRGFWRDE----DRYLETYWSRFdnvWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGP 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3929 GEIAAKIASLPQVSD-AAVTVEGQGEGAWLMAYAVAADGAEPDPqSLREALRALLPDYM----LPRLIQLLPALPLTANG 4003
Cdd:cd05968 507 AEIESVLNAHPAVLEsAAIGVPHPVKGEAIVCFVVLKPGVTPTE-ALAEELMERVADELgkplSPERILFVKDLPKTRNA 585
|
....*..
gi 1246793773 4004 KLDRKAL 4010
Cdd:cd05968 586 KVMRRVI 592
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
3532-4004 |
9.19e-35 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 142.05 E-value: 9.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3532 YPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFI 3611
Cdd:cd12118 17 YPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3612 LEDSGVclsvsqRALAVelpgtalclDDPFTRAQLDAV-EPGELPEVPTEA--PAYLIYTSGSTGTPKGVVVTHRNVerl 3688
Cdd:cd12118 97 LRHSEA------KVLFV---------DREFEYEDLLAEgDPDFEWIPPADEwdPIALNYTSGTTGRPKGVVYHHRGA--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3689 FTAATQTG-RFSFDEHDV--WSL--FHSHAFDFAvwelWGAWLYGGRAVLVPEAvcrQPDAFLDLLAEYGVTVLNQTPSA 3763
Cdd:cd12118 159 YLNALANIlEWEMKQHPVylWTLpmFHCNGWCFP----WTVAAVGGTNVCLRKV---DAKAIYDLIEKHKVTHFCGAPTV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3764 FYALQSQAMRRELALNVRAVVFGGEALEPSRLqpwrerypqaeLVNM----------YGITETTVHVSF-------HRLS 3826
Cdd:cd12118 232 LNMLANAPPSDARPLPHRVHVMTAGAPPPAAV-----------LAKMeelgfdvthvYGLTETYGPATVcawkpewDELP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3827 DEDLQSPTSRIGSALPDL-AVHVLDAAG-QPVPL-GV-VGELVVEGDGVAQGYWQRPELTAERFveRGGqrFYRSGDLGR 3902
Cdd:cd12118 301 TEERARLKARQGVRYVGLeEVDVLDPETmKPVPRdGKtIGEIVFRGNIVMKGYLKNPEATAEAF--RGG--WFHSGDLAV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3903 YRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTV---EGQGEGawLMAYAVAADGAEPDPQSLREALR 3979
Cdd:cd12118 377 IHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVArpdEKWGEV--PCAFVELKEGAKVTEEEIIAFCR 454
|
490 500
....*....|....*....|....*
gi 1246793773 3980 ALLPDYMLPRLIQLLPaLPLTANGK 4004
Cdd:cd12118 455 EHLAGFMVPKTVVFGE-LPKTSTGK 478
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
3545-4012 |
9.42e-35 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 140.73 E-value: 9.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3545 LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPV-DPHAPAArrgfiledsgvclsVSQ 3623
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLfTAFGPKA--------------IEH 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3624 RalaVELPGTALCLDDPFTRAQLDavepgelpevptEAPAYLIYTSGSTGTPKGVVVTHRNVerlfTAATQTGRFSFDEH 3703
Cdd:cd05973 67 R---LRTSGARLVVTDAANRHKLD------------SDPFVMMFTSGTTGLPKGVPVPLRAL----AAFGAYLRDAVDLR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3704 DvwslfhshafDFAVWEL----WGAWLYggRAVLVPEAVCR---------QPDAFLDLLAEYGVTVLNQTPSAFYALQSQ 3770
Cdd:cd05973 128 P----------EDSFWNAadpgWAYGLY--YAITGPLALGHptilleggfSVESTWRVIERLGVTNLAGSPTAYRLLMAA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3771 AMRRELALNV--RAVVFGGEALEPSRLQpWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQSPTSriGSALPDLAVHV 3848
Cdd:cd05973 196 GAEVPARPKGrlRRVSSAGEPLTPEVIR-WFDAALGVPIHDHYGQTELGMVLANHHALEHPVHAGSA--GRAMPGWRVAV 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3849 LDAAGQPVPLGVVGELVVEGDGVA----QGYWQRPELTAErfverggQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGY 3924
Cdd:cd05973 273 LDDDGDELGPGEPGRLAIDIANSPlmwfRGYQLPDTPAID-------GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGY 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3925 RIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQ---SLREALRALLPDYMLPRLIQLLPALPLT 4000
Cdd:cd05973 346 RIGPFDVESALIEHPAVAEAAVIgVPDPERTEVVKAFVVLRGGHEGTPAladELQLHVKKRLSAHAYPRTIHFVDELPKT 425
|
490
....*....|..
gi 1246793773 4001 ANGKLDRKALPK 4012
Cdd:cd05973 426 PSGKIQRFLLRR 437
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
2051-2524 |
1.87e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 141.58 E-value: 1.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHpDARQIA-VL 2129
Cdd:PRK07656 20 DKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRY-TADEAAyIL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 DDSGARIVIGWGA-APAWVPASVRWLDAESVldVVSAYEEPPRVD---------------------VDADTPAYLIYTSG 2187
Cdd:PRK07656 99 ARGDAKALFVLGLfLGVDYSATTRLPALEHV--VICETEEDDPHTekmktftdflaagdpaerapeVDPDDVADILFTSG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2188 STGTPKGVVVSQGNLANYVAGVLPVLDLGE-DASLATLSTVAAdLGFTA-LFGALLSGRRVrlLPaELAFDaqalaahlq 2265
Cdd:PRK07656 177 TTGRPKGAMLTHRQLLSNAADWAEYLGLTEgDRYLAANPFFHV-FGYKAgVNAPLMRGATI--LP-LPVFD--------- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2266 ahPVDCLKIVPSHLAgllaaaggtAVLP-----------------------REClVTGGEALTGALVQQVRALAPTLRIV 2322
Cdd:PRK07656 244 --PDEVFRLIETERI---------TVLPgpptmynsllqhpdrsaedlsslRLA-VTGAASMPVALLERFESELGVDIVL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2323 NHYGPTETTvGILTCTVPEEWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAErfva 2402
Cdd:PRK07656 312 TGYGLSEAS-GVTTFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAA---- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2403 hPLAPDRLLYrSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGAN-G-------VLQ 2474
Cdd:PRK07656 387 -AIDADGWLH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERlGevgkayvVLK 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2475 LGACIqgSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALAD 2524
Cdd:PRK07656 465 PGAEL--TEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
537-1371 |
2.15e-34 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 147.24 E-value: 2.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 537 VVDAIARAADEFPERAAL-----ETAQGR-LSYRELLTAADARAAALRRRLGAQARSVaLCLPRGLDWYCLLLGAWRAGL 610
Cdd:PRK05691 11 LVQALQRRAAQTPDRLALrfladDPGEGVvLSYRDLDLRARTIAAALQARASFGDRAV-LLFPSGPDYVAAFFGCLYAGV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 611 SVIPL-----DTEWPQARRAEVVAASGCDAVLTDA----------QGLAGFAPSVaIAVDELKLDGAgENGSGENAAPNQ 675
Cdd:PRK05691 90 IAVPAyppesARRHHQERLLSIIADAEPRLLLTVAdlrdsllqmeELAAANAPEL-LCVDTLDPALA-EAWQEPALQPDD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 676 LAYILYTSGSTGIPKGVEVGHAALAAhidaaaealalsadDRVLHVAGLAVDTTLEQILAAW------------------ 737
Cdd:PRK05691 168 IAFLQYTSGSTALPKGVQVSHGNLVA--------------NEQLIRHGFGIDLNPDDVIVSWlplyhdmgliggllqpif 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 738 SRGACVVARPDELLE-PQRFLAFLSERAITVTDlAPAYANELVRASVADD---------WRDLALRCLVVGGDVLPvALA 807
Cdd:PRK05691 234 SGVPCVLMSPAYFLErPLRWLEAISEYGGTISG-GPDFAYRLCSERVSESalerldlsrWRVAYSGSEPIRQDSLE-RFA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 808 QRWFELGLDRRcALINAYGPTEAT-----------ISSHYHRVQAIDASRPVP-LGQLL-------PGRIAAVLD-AHGR 867
Cdd:PRK05691 312 EKFAACGFDPD-SFFASYGLAEATlfvsggrrgqgIPALELDAEALARNRAEPgTGSVLmscgrsqPGHAVLIVDpQSLE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 868 IVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLrlpsgESLRMYRSGDrVRLLDDGELQFLGRADFQVKLRGYRIELE 947
Cdd:PRK05691 391 VLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEH-----DGRTWLRTGD-LGFLRDGELFVTGRLKDMLIVRGHNLYPQ 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 948 EIEHCLGQlpQVRAAAAGVVGEGAaqrlvawVECAGEDGFGQA-----DLNQTDSDQTESERWHRALCErlpAYMVPTQF 1022
Cdd:PRK05691 465 DIEKTVER--EVEVVRKGRVAAFA-------VNHQGEEGIGIAaeisrSVQKILPPQALIKSIRQAVAE---ACQEAPSV 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1023 VALPR---LPRNASGKIDRRA---------LPAPPVLAQAERTPPRTAEESA------LCEVWAEVLQCE-VGIHDSFFR 1083
Cdd:PRK05691 533 VLLLNpgaLPKTSSGKLQRSAcrlrladgsLDSYALFPALQAVEAAQTAASGdelqarIAAIWCEQLKVEqVAADDHFFL 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1084 LGGDSIRSLQVVARLRER-GYAVTPKLMYQYQS----AAELAPQLIALQAAPAEAAPLVGEVGL--SPIQR--WFFDSAP 1154
Cdd:PRK05691 613 LGGNSIAATQVVARLRDElGIDLNLRQLFEAPTlaafSAAVARQLAGGGAAQAAIARLPRGQALpqSLAQNrlWLLWQLD 692
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1155 AQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPaIQAQDWRGAADLDSRVDAAF 1234
Cdd:PRK05691 693 PQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEFA-LQRIDLSDLPEAEREARAAQ 771
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1235 ARMQEA-TPL---AGPLVALTHAHCDDGE-RLLICAHHLIVDAVSWRLLLGELFDGLAALARGEAWTPSARGASYADYVE 1309
Cdd:PRK05691 772 IREEEArQPFdleKGPLLRVTLVRLDDEEhQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGA 851
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 1310 ALRE---ADDAQRfDAGFWR-ELA-AQPMQALPQDRPvaLADARQSNVGRIVQTLDAGLTADLLERA 1371
Cdd:PRK05691 852 WQRQwlaQGEAAR-QLAYWKaQLGdEQPVLELATDHP--RSARQAHSAARYSLRVDASLSEALRGLA 915
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
3521-4085 |
2.63e-34 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 146.85 E-value: 2.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3521 LVSRFAEIARRYPARIAVS--AEDGE----LDYATLDRRSSQLATLLIRQgAGPGQRVGLCLPRGCDLLVALLAILKTGA 3594
Cdd:PRK05691 11 LVQALQRRAAQTPDRLALRflADDPGegvvLSYRDLDLRARTIAAALQAR-ASFGDRAVLLFPSGPDYVAAFFGCLYAGV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3595 AYVPVDPHAPA--------------ARRGFILEDSGVCLSVSQ-RALAVELPGTALCLDdpftraQLDAV--EPGELPEV 3657
Cdd:PRK05691 90 IAVPAYPPESArrhhqerllsiiadAEPRLLLTVADLRDSLLQmEELAAANAPELLCVD------TLDPAlaEAWQEPAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3658 PTEAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQTGRFSFDEHDV---W-SLFHSHAFdfaVWELWGAWLYGGRAVL 3733
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPDDVivsWlPLYHDMGL---IGGLLQPIFSGVPCVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3734 V-PEAVCRQPDAFLDLLAEYGVTVlNQTPSAFYALQSQ-----AMRRELALNVRAVVFGGEALEPSRLQPWRERY----- 3802
Cdd:PRK05691 241 MsPAYFLERPLRWLEAISEYGGTI-SGGPDFAYRLCSErvsesALERLDLSRWRVAYSGSEPIRQDSLERFAEKFaacgf 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3803 -PQAELVNmYGITETTVHVS---------FHRLSDEDLQ---------SPTSRIGSALPDLAVHVLDAA-GQPVPLGVVG 3862
Cdd:PRK05691 320 dPDSFFAS-YGLAEATLFVSggrrgqgipALELDAEALArnraepgtgSVLMSCGRSQPGHAVLIVDPQsLEVLGDNRVG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3863 ELVVEGDGVAQGYWQRPELTAERFVERGGQRFYRSGDLGrYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVS 3942
Cdd:PRK05691 399 EIWASGPSIAHGYWRNPEASAKTFVEHDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3943 D----AAVTVEGQGEGAWLMAYAVAADGAEP-DPQSLREALRALLPD--YMLPRLIQLLP--ALPLTANGKLDRKA---- 4009
Cdd:PRK05691 478 RkgrvAAFAVNHQGEEGIGIAAEISRSVQKIlPPQALIKSIRQAVAEacQEAPSVVLLLNpgALPKTSSGKLQRSAcrlr 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 4010 -----------LPKPETQDRDEG-VLESASERRLAELWRQLLGGELPGRGAHFFARGGHSLLVVRLAEAIRAEFAIAVPL 4077
Cdd:PRK05691 558 ladgsldsyalFPALQAVEAAQTaASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDELGIDLNL 637
|
....*...
gi 1246793773 4078 KSLFEQPR 4085
Cdd:PRK05691 638 RQLFEAPT 645
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
3528-4012 |
3.25e-34 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 141.27 E-value: 3.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3528 IARRYPARIAVS-AEDGE---LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHA 3603
Cdd:cd05906 19 AAERGPTKGITYiDADGSeefQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3604 ----PAARRGFI-----LEDSGVCLSVSQRALAVELPGTALCLDDPFTRAQLDAVEPGELPEVPT---EAPAYLIYTSGS 3671
Cdd:cd05906 99 tydePNARLRKLrhiwqLLGSPVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADHDLPQsrpDDLALLMLTSGS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3672 TGTPKGVVVTHRNVERLFTAATQTGRFSFDE--------HDVWSLFHSHAFDFavwelwgawLYGGRAVLVP-EAVCRQP 3742
Cdd:cd05906 179 TGFPKAVPLTHRNILARSAGKIQHNGLTPQDvflnwvplDHVGGLVELHLRAV---------YLGCQQVHVPtEEILADP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3743 DAFLDLLAEYGVTVlNQTPSAFYALQSQAMRRE-----LALNVRAVVFGGEALEPS---RLQPWRERY--PQAELVNMYG 3812
Cdd:cd05906 250 LRWLDLIDRYRVTI-TWAPNFAFALLNDLLEEIedgtwDLSSLRYLVNAGEAVVAKtirRLLRLLEPYglPPDAIRPAFG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3813 ITETTVHVSFHRLSDEDLQSPTSR---IGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVER 3889
Cdd:cd05906 329 MTETCSGVIYSRSFPTYDHSQALEfvsLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTED 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3890 GgqrFYRSGDLGrYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQV---SDAAVTVEGQGEGAWLMA--YAVAA 3964
Cdd:cd05906 409 G---WFRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVepsFTAAFAVRDPGAETEELAifFVPEY 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 3965 DGAEPDPQSLREALRALL------PDYMLPrliqlLP--ALPLTANGKLDRKALPK 4012
Cdd:cd05906 485 DLQDALSETLRAIRSVVSrevgvsPAYLIP-----LPkeEIPKTSLGKIQRSKLKA 535
|
|
| NRPS-para261 |
TIGR01720 |
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately ... |
2923-3070 |
5.64e-34 |
|
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately downstream from a condensation domain (pfam00668), and is followed primarily by the end of the molecule or another condensation domain (in a few cases it is followed by pfam00501, an AMP-binding module). The converse is not true, pfam00668 domains are not always followed by this domain. This implicates this domain in possible post-condensation modification events. This model is 171 amino acids long and contains three very highly conserved regions. At the N-terminus is a nearly invariant lysine (position 11) followed by xxxRxxPxxGxGYG in which the proline and the first glycine are invariant. This is followed approximately 22 residues later by the motif FNYLG. Near the C-terminus of the domain is the sequence TxSD where the serine and aspartate are nearly invariant.
Pssm-ID: 273774 [Multi-domain] Cd Length: 153 Bit Score: 129.70 E-value: 5.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2923 DLGAALRSTKDRMRAVPDRGLGFGVLRYLHGE---LAELPVPQVCFNYLGQLRAGERDG-WALCEEPDGGGRAGGNRRRH 2998
Cdd:TIGR01720 1 ELGRLIKAVKEQLRRIPNKGVGYGVLRYLTEPeekLAASPQPEISFNYLGQFDADSNDElFQPSSYSPGEAISPESPRPY 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 2999 LLDVNAMLVDGELRLDWAWPQDAASREAMQALSRRYLAVLRELIACVQTAEPRP-TLADLPLAGLDNAPLDAL 3070
Cdd:TIGR01720 81 ALEINAMIEDGELTLTWSYPTQLFSEDTIEQLADRFKEALEALIAHCAGKEGGGlTPSDFSLKDLTQDELDEL 153
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
3520-4010 |
7.18e-34 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 140.42 E-value: 7.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEIARRYPARIAVSAEDG----------ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAI 3589
Cdd:PRK09274 7 NIARHLPRAAQERPDQLAVAVPGGrgadgklaydELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3590 LKTGAAYVPVDP-----------------------HAPAARRGFILEDSGV--CLSVSQRALaveLPGTALcldDPFTRA 3644
Cdd:PRK09274 87 FKAGAVPVLVDPgmgiknlkqclaeaqpdafigipKAHLARRLFGWGKPSVrrLVTVGGRLL---WGGTTL---ATLLRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3645 QldAVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQTGRFSFDEHDVWSlfhshafdFAVWELWGA 3724
Cdd:PRK09274 161 G--AAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPT--------FPLFALFGP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3725 WLyGGRAVlVPEAVCRQP-----DAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELAL-NVRAVVFGGEALEPSRLQPW 3798
Cdd:PRK09274 231 AL-GMTSV-IPDMDPTRPatvdpAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLpSLRRVISAGAPVPIAVIERF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3799 RERYPQ-AELVNMYGITE----TTVHvsfhrlSDEDLQSPTSR--------IGSALPDLAVHVLD---------AAGQPV 3856
Cdd:PRK09274 309 RAMLPPdAEILTPYGATEalpiSSIE------SREILFATRAAtdngagicVGRPVDGVEVRIIAisdapipewDDALRL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3857 PLGVVGELVVEGDGVAQGYWQRPELTAERFVERGGQRFY-RSGDLGRYRADGSLEYRGRGDDQVKLRGYRI--EPGEiaA 3933
Cdd:PRK09274 383 ATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDGQGDVWhRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLytIPCE--R 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3934 KIASLPQVSDAA-VTVEGQGEGAWLMAYAVaADGAEPDPQSLREALRALLPDYMLPRLIQLL---PALPLTA--NGKLDR 4007
Cdd:PRK09274 461 IFNTHPGVKRSAlVGVGVPGAQRPVLCVEL-EPGVACSKSALYQELRALAAAHPHTAGIERFlihPSFPVDIrhNAKIFR 539
|
...
gi 1246793773 4008 KAL 4010
Cdd:PRK09274 540 EKL 542
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
3520-4010 |
7.47e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 139.79 E-value: 7.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVgLCLPRGCD-LLVALLAILKTGAAYVP 3598
Cdd:PRK07470 8 NLAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRI-LVHSRNCNqMFESMFAAFRLGAVWVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3599 VDPHAPAARRGFILEDSGVCLSVSQ-------RALAVELPGTALCLDDPFTRAQLD--------AVEPGELPEVPTEAPA 3663
Cdd:PRK07470 87 TNFRQTPDEVAYLAEASGARAMICHadfpehaAAVRAASPDLTHVVAIGGARAGLDyealvarhLGARVANAAVDHDDPC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3664 YLIYTSGSTGTPKGVVVTH--------RNVERLFTAATqtgrfsfdEHDVwSLF---HSHafdfavwelwGAWLY----- 3727
Cdd:PRK07470 167 WFFFTSGTTGRPKAAVLTHgqmafvitNHLADLMPGTT--------EQDA-SLVvapLSH----------GAGIHqlcqv 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3728 --GGRAVLVPeAVCRQPDAFLDLLAEYGVTVLNQTPSAFYAL-QSQAMRRELALNVRAVVFGGEALepsrlqpWRERYPQ 3804
Cdd:PRK07470 228 arGAATVLLP-SERFDPAEVWALVERHRVTNLFTVPTILKMLvEHPAVDRYDHSSLRYVIYAGAPM-------YRADQKR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3805 A------ELVNMYGITETTVHVS-----FHRLSDEdlqsPTSRIGS---ALPDLAVHVLDAAGQPVPLGVVGELVVEGDG 3870
Cdd:PRK07470 300 AlaklgkVLVQYFGLGEVTGNITvlppaLHDAEDG----PDARIGTcgfERTGMEVQIQDDEGRELPPGETGEICVIGPA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3871 VAQGYWQRPELTAERFveRGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveG 3950
Cdd:PRK07470 376 VFAGYYNNPEANAKAF--RDG--WFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVL--G 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 3951 QGEGAW---LMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK07470 450 VPDPVWgevGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
89-507 |
8.01e-34 |
|
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380456 [Multi-domain] Cd Length: 419 Bit Score: 137.50 E-value: 8.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 89 PLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQGEDsvaagGG----------AA 158
Cdd:cd19533 3 PLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEE-----GEpyqwidpytpVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 159 VESADLRGRGQDEIDALV---EGFRlRPFELQRqRPL-RMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSLGLLTQ---D 231
Cdd:cd19533 78 IRHIDLSGDPDPEGAAQQwmqEDLR-KPLPLDN-DPLfRHALFTLGDN-----RHFWYQRVHHIVMDGFSFALFGQrvaE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 232 LSRAYRVECGLAAEPAPPL------PCQYGDYARWQRDTLdrldaslrHHVEALSGAPHLHELpldheRPAVLGQSGAKL 305
Cdd:cd19533 151 IYTALLKGRPAPPAPFGSFldlveeEQAYRQSERFERDRA--------FWTEQFEDLPEPVSL-----ARRAPGRSLAFL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 306 R--LAFPPGLSERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDD 383
Cdd:cd19533 218 RrtAELPPELTRTLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 384 PDFASLVARCRDHQLAALEHQALPLERVIETLQVERSSRH--APLFQLMfalRHDADLALDLHGVQAHAL-TLPEDvakh 460
Cdd:cd19533 298 QTFAELVAQVSRELRSLLRHQRYRYEDLRRDLGLTGELHPlfGPTVNYM---PFDYGLDFGGVVGLTHNLsSGPTN---- 370
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1246793773 461 ELTLEVL--VGAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENP 507
Cdd:cd19533 371 DLSIFVYdrDDESGLRIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
3529-4010 |
9.71e-34 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 138.56 E-value: 9.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARR 3608
Cdd:PRK03640 12 AFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3609 GFILEDSGV-CLSVSQRALAVELPGTALCLDDpftRAQLDAVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNveR 3687
Cdd:PRK03640 92 LWQLDDAEVkCLITDDDFEAKLIPGISVKFAE---LMNGPKEEAEIQEEFDLDEVATIMYTSGTTGKPKGVIQTYGN--H 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3688 LFTAATQTGRFSFDEHDVW----SLFHSHAFDFAVWELwgawLYGGRAVLVPEAvcrQPDAFLDLLAEYGVTVLNQTPSA 3763
Cdd:PRK03640 167 WWSAVGSALNLGLTEDDCWlaavPIFHISGLSILMRSV----IYGMRVVLVEKF---DAEKINKLLQTGGVTIISVVSTM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3764 FYALQSQAMRRELALNVRAVVFGGEALEPSRLQPWRERypQAELVNMYGITETTVHVSfhRLSDEDLQsptSRIGSA--- 3840
Cdd:PRK03640 240 LQRLLERLGEGTYPSSFRCMLLGGGPAPKPLLEQCKEK--GIPVYQSYGMTETASQIV--TLSPEDAL---TKLGSAgkp 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3841 LPDLAVHVLDaAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFveRGGqrFYRSGDLGRYRADGSLEYRGRGDDQVK 3920
Cdd:PRK03640 313 LFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF--QDG--WFKTGDIGYLDEEGFLYVLDRRSDLII 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3921 LRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEGAWLM---AYAVAadGAEPDPQSLREALRALLPDYMLPRLIQLLPAL 3997
Cdd:PRK03640 388 SGGENIYPAEIEEVLLSHPGVAEAGVV--GVPDDKWGQvpvAFVVK--SGEVTEEELRHFCEEKLAKYKVPKRFYFVEEL 463
|
490
....*....|...
gi 1246793773 3998 PLTANGKLDRKAL 4010
Cdd:PRK03640 464 PRNASGKLLRHEL 476
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
3665-4007 |
1.02e-33 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 135.09 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3665 LIYTSGSTGTPKGVVVTHRNverLFTAATQT-GRFSFDEHDVW----SLFHSHAFD--FAVWELwgawlyGGRAVLVPEA 3737
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGN---LIAANLQLiHAMGLTEADVYlnmlPLFHIAGLNlaLATFHA------GGANVVMEKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3738 vcrQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALNVRAVVFGGEAlePSRLQPWRERYPqAELVNMYGITETT 3817
Cdd:cd17637 76 ---DPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVLGLDA--PETIQRFEETTG-ATFWSLYGQTETS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3818 VHVSFHRLSDEdlqsPTSrIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFveRGGqrFYRS 3897
Cdd:cd17637 150 GLVTLSPYRER----PGS-AGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF--RNG--WHHT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3898 GDLGRYRADGSLEYRGRG--DDQVKLRGYRIEPGEIAAKIASLPQVsdAAVTVEGQ-----GEGawLMAYAVAADGAEPD 3970
Cdd:cd17637 221 GDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAI--AEVCVIGVpdpkwGEG--IKAVCVLKPGATLT 296
|
330 340 350
....*....|....*....|....*....|....*..
gi 1246793773 3971 PQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDR 4007
Cdd:cd17637 297 ADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
3474-4012 |
1.42e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 139.29 E-value: 1.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3474 VEQMLDDLDFVLQQVPALQRFDALPLLPSQTRSAAWTSRERYACTGNLVsRFAeiARRYPARIAVSAEDGELDYATLDRR 3553
Cdd:PRK07788 7 VSGYLTRGSAEAHYLRVMIRSGAVDLERPDNGLRLAADIRRYGPFAGLV-AHA--ARRAPDRAALIDERGTLTYAELDEQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3554 SSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDP--HAP-----AARRG---------------FI 3611
Cdd:PRK07788 84 SNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTgfSGPqlaevAAREGvkalvyddeftdllsAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3612 LEDSGVCLSVSQRALAVELPG-TALCLDDpftraQLDAVEPGELPEVPTEApAYLIYTSGSTGTPKGVVvtHRNVERLFT 3690
Cdd:PRK07788 164 PPDLGRLRAWGGNPDDDEPSGsTDETLDD-----LIAGSSTAPLPKPPKPG-GIVILTSGTTGTPKGAP--RPEPSPLAP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3691 AATQTGRFSFDEHDVWSLFHS--HAFDFAVWELwgAWLYGGRAVLV----PEAVcrqpdafLDLLAEYGVTVLNQTP--- 3761
Cdd:PRK07788 236 LAGLLSRVPFRAGETTLLPAPmfHATGWAHLTL--AMALGSTVVLRrrfdPEAT-------LEDIAKHKATALVVVPvml 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3762 SAFYALQSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAeLVNMYGITEttvhVSFHRLSD-EDLQSPTSRIGSA 3840
Cdd:PRK07788 307 SRILDLGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPV-LYNLYGSTE----VAFATIATpEDLAEAPGTVGRP 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3841 LPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYwqrpelTAERFVER-GGqrFYRSGDLGRYRADGSLEYRGRGDDQV 3919
Cdd:PRK07788 382 PKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY------TDGRDKQIiDG--LLSSGDVGYFDEDGLLFVDGRDDDMI 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3920 KLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALP 3998
Cdd:PRK07788 454 VSGGENVFPAEVEDLLAGHPDVVEAAVIgVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELP 533
|
570
....*....|....
gi 1246793773 3999 LTANGKLDRKALPK 4012
Cdd:PRK07788 534 RNPTGKVLKRELRE 547
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
588-1041 |
1.71e-33 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 136.70 E-value: 1.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQglagfapsvaiavdelkldgagengs 667
Cdd:cd05972 28 VAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDAE-------------------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 668 genaapnQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLA-VDTTLEQILAAWSRGACVVAR 746
Cdd:cd05972 82 -------DPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNIADPGwAKGAWSSFFGPWLLGATVFVY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 747 PDELLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRdLALRCLVVGGDVLPVALAQRWFE-LGLDRRcaliNAY 825
Cdd:cd05972 155 EGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKF-SHLRLVVSAGEPLNPEVIEWWRAaTGLPIR----DGY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 826 GPTEATISSHYHRVQAIdasRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELA--LGGIGLAEGYRGDAAASERRFaplr 903
Cdd:cd05972 230 GQTETGLTVGNFPDMPV---KPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAikLPPPGLFLGYVGDPEKTEASI---- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 904 lpSGEslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQV-RAAAAGVVGEGAAQRLVAWVECA 982
Cdd:cd05972 303 --RGD---YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVaEAAVVGSPDPVRGEVVKAFVVLT 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 983 geDGFGQadlnqTDSDQTESERWHRalcERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05972 378 --SGYEP-----SEELAEELQGHVK---KVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
536-1041 |
5.16e-33 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 137.11 E-value: 5.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 536 NVVDAIARAADE-FPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIP 614
Cdd:cd05959 4 NAATLVDLNLNEgRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 615 LDTEWP--------QARRAEVVAASG-CDAVLTDAQGLAGFAPSVAIAVD---------ELKLDGAGENGSGENAA--PN 674
Cdd:cd05959 84 VNTLLTpddyayylEDSRARVVVVSGeLAPVLAAALTKSEHTLVVLIVSGgagpeagalLLAELVAAEAEQLKPAAthAD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 675 QLAYILYTSGSTGIPKG-VEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTL-EQILAAWSRGACVVARPdELLE 752
Cdd:cd05959 164 DPAFWLYSSGSTGRPKGvVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLgNSLTFPLSVGATTVLMP-ERPT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 753 PQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFEL-GLDrrcaLINAYGPTEAT 831
Cdd:cd05959 243 PAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARfGLD----ILDGIGSTEML 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 832 issHYHRVQAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFaplrlpSGEslr 911
Cdd:cd05959 319 ---HIFLSNRPGRVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF------QGE--- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 912 MYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVGEGAAQRLVAWVECagedgfgqAD 991
Cdd:cd05959 387 WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAA--VVGVEDEDGLTKPKAF--------VV 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 992 LNQTDSDQTESERWHRALC-ERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05959 457 LRPGYEDSEALEEELKEFVkDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2062-2522 |
7.25e-33 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 134.73 E-value: 7.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2062 WTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIgwg 2141
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2142 aapawvpasvrwldaesvldvvsayeepprvdVDadtPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGE-DAS 2220
Cdd:cd05934 81 --------------------------------VD---PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEdDVY 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2221 LATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPREClvtG 2300
Cdd:cd05934 126 LTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRAA---Y 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2301 GEALTGALVQQVRAlAPTLRIVNHYGPTETTVGILTctvpeewPVEQGVPVGH---PLAGNEAWVLDRFGLPAPVGVAGE 2377
Cdd:cd05934 203 GAPNPPELHEEFEE-RFGVRLLEGYGMTETIVGVIG-------PRDEPRRPGSigrPAPGYEVRIVDDDGQELPAGEPGE 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2378 LYL---GGGNLSLGYWQRAEQTAERFvAHplapdrLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQ 2454
Cdd:cd05934 275 LVIrglRGWGFFKGYYNMPEATAEAM-RN------GWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILR 347
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 2455 LPGVEVAAVLALPGANGVLQLGACIQ----GSL--EGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:cd05934 348 HPAVREAAVVAVPDEVGEDEVKAVVVlrpgETLdpEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQL 421
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
3520-4003 |
7.80e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 137.18 E-value: 7.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPV 3599
Cdd:PRK06164 11 TLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3600 DPHAPAARRGFILEDSGVCLSV------------------------SQRALAVELPGTALCLDDPFTRAQLDAVEPGE-- 3653
Cdd:PRK06164 91 NTRYRSHEVAHILGRGRARWLVvwpgfkgidfaailaavppdalppLRAIAVVDDAADATPAPAPGARVQLFALPDPApp 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3654 ----LPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQTGRFSFDEHDVWSLFHSHAFDFAVweLWGAwLYGG 3729
Cdd:PRK06164 171 aaagERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFST--LLGA-LAGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3730 rAVLVPEAVCRQPDAfLDLLAEYGVTVLNQTPSAFYALQSQA-MRRELAlnvRAVVFGGEALEPSrlqpWRERYPQAE-- 3806
Cdd:PRK06164 248 -APLVCEPVFDAART-ARALRRHRVTHTFGNDEMLRRILDTAgERADFP---SARLFGFASFAPA----LGELAALARar 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3807 ---LVNMYGITETTVHVSFHRLSDEDLQSPTSRIGSALPDLAVHVLDAA-GQPVPLGVVGELVVEGDGVAQGYWQRPELT 3882
Cdd:PRK06164 319 gvpLTGLYGSSEVQALVALQPATDPVSVRIEGGGRPASPEARVRARDPQdGALLPDGESGEIEIRAPSLMRGYLDNPDAT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3883 AERFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDA---AVTVEGQGEGAwlmA 3959
Cdd:PRK06164 399 ARALTDDG---YFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAqvvGATRDGKTVPV---A 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1246793773 3960 YAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANG 4003
Cdd:PRK06164 473 FVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESA 516
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
2054-2522 |
1.02e-32 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 136.34 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2054 AVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSG 2133
Cdd:cd05959 22 AFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2134 ARIVIGWGA-APAWVPASVRWLDAESVLDVVSAYEEPPRVDV-----------------DADTPAYLIYTSGSTGTPKGV 2195
Cdd:cd05959 102 ARVVVVSGElAPVLAAALTKSEHTLVVLIVSGGAGPEAGALLlaelvaaeaeqlkpaatHADDPAFWLYSSGSTGRPKGV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2196 VVSQGNLanYVAGVL---PVLDLGEDASLatLStvAADLGFT-----ALFGALLSGRRVRLLPAELAFDAQALAAHLQAH 2267
Cdd:cd05959 182 VHLHADI--YWTAELyarNVLGIREDDVC--FS--AAKLFFAyglgnSLTFPLSVGATTVLMPERPTPAAVFKRIRRYRP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2268 PVdcLKIVPSHLAGLLAAAGGTAVLP---REClVTGGEALTGALVQQVRALApTLRIVNHYGPTETtVGILTCTVPEEwp 2344
Cdd:cd05959 256 TV--FFGVPTLYAAMLAAPNLPSRDLsslRLC-VSAGEALPAEVGERWKARF-GLDILDGIGSTEM-LHIFLSNRPGR-- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2345 VEQGVpVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHplapdrlLYRSGDLARLDGEG 2424
Cdd:cd05959 329 VRYGT-TGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQGE-------WTRTGDKYVRDDDG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2425 RIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI--------QGSL-EGVAEALAQRLP 2495
Cdd:cd05959 401 FYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVvlrpgyedSEALeEELKEFVKDRLA 480
|
490 500
....*....|....*....|....*..
gi 1246793773 2496 EYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:cd05959 481 PYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
543-1038 |
1.51e-32 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 134.27 E-value: 1.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 543 RAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQA 622
Cdd:cd17631 3 RRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 623 RRAEVVAASGCDAVLTDaqglagfapsvaiavdelkldgagengsgenaapnqLAYILYTSGSTGIPKGVEVGHAALAAH 702
Cdd:cd17631 83 EVAYILADSGAKVLFDD------------------------------------LALLMYTSGTTGRPKGAMLTHRNLLWN 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 703 IDAAAEALALSADDRVLHVAGL----AVDTTLEQILAawsRGACVVARPDelLEPQRFLAFLSERAITVTDLAPAYANEL 778
Cdd:cd17631 127 AVNALAALDLGPDDVLLVVAPLfhigGLGVFTLPTLL---RGGTVVILRK--FDPETVLDLIERHRVTSFFLVPTMIQAL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 779 VRASVADDWRDLALRCLVVGGDVLPVALAQRWfelgLDRRCALINAYGPTEAT-----ISSHYHRVQAIDASRPVPLGQl 853
Cdd:cd17631 202 LQHPRFATTDLSSLRAVIYGGAPMPERLLRAL----QARGVKFVQGYGMTETSpgvtfLSPEDHRRKLGSAGRPVFFVE- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 854 lpgriAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAplrlpSGeslrMYRSGDRVRLLDDGELQFLGRA 933
Cdd:cd17631 277 -----VRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFR-----DG----WFHTGDLGRLDEDGYLYIVDRK 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 934 DFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVGEGAAQrlvaWVECagedgfGQAdLNQTDSDQTESERWHRALC-ER 1012
Cdd:cd17631 343 KDMIISGGENVYPAEVEDVLYEHPAVAEVA--VIGVPDEK----WGEA------VVA-VVVPRPGAELDEDELIAHCrER 409
|
490 500
....*....|....*....|....*.
gi 1246793773 1013 LPAYMVPTQFVALPRLPRNASGKIDR 1038
Cdd:cd17631 410 LARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
3537-4014 |
2.25e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 134.35 E-value: 2.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3537 AVSAEDGELDYATLDRRSSQLATLLirqgaGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSG 3616
Cdd:PRK07787 18 AVRIGGRVLSRSDLAGAATAVAERV-----AGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3617 VclsvsqRALAVELPGTALCLddPFTRAQLDAVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQTG 3696
Cdd:PRK07787 93 A------QAWLGPAPDDPAGL--PHVPVRLHARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3697 RFSFDEHDVWSL--FHSHAFdfaVWELWGAWLYGGRAVLV----PEAVCRQPDAFLDLLaeYGV-TV---LNQTPSAFYA 3766
Cdd:PRK07787 165 QWTADDVLVHGLplFHVHGL---VLGVLGPLRIGNRFVHTgrptPEAYAQALSEGGTLY--FGVpTVwsrIAADPEAARA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3767 LQSqamrrelalnVRAVVFGGEALePSrlqPWRERYPQA---ELVNMYGITETTVHVSFHrlSDEDLQSPTsrIGSALPD 3843
Cdd:PRK07787 240 LRG----------ARLLVSGSAAL-PV---PVFDRLAALtghRPVERYGMTETLITLSTR--ADGERRPGW--VGLPLAG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3844 LAVHVLDAAGQPVPLGV--VGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGR-GDDQVK 3920
Cdd:PRK07787 302 VETRLVDEDGGPVPHDGetVGELQVRGPTLFDGYLNRPDATAAAFTADG---WFRTGDVAVVDPDGMHRIVGReSTDLIK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3921 LRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGE-GAWLMAYAVAADgaEPDPQSLREALRALLPDYMLPRLIQLLPALPL 3999
Cdd:PRK07787 379 SGGYRIGAGEIETALLGHPGVREAAVVGVPDDDlGQRIVAYVVGAD--DVAADELIDFVAQQLSVHKRPREVRFVDALPR 456
|
490
....*....|....*
gi 1246793773 4000 TANGKLDRKALPKPE 4014
Cdd:PRK07787 457 NAMGKVLKKQLLSEG 471
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
3108-3427 |
2.48e-32 |
|
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380463 [Multi-domain] Cd Length: 433 Bit Score: 133.32 E-value: 2.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3108 TVALHGALDREAFAAAWQQALERHPILRSGF-AVQGLPSPRQLPHRQVSLPLAEQDwsgLEPAQARSRLSELqaqqCEAG 3186
Cdd:cd19540 29 ALRLTGALDVDALRAALADVVARHESLRTVFpEDDGGPYQVVLPAAEARPDLTVVD---VTEDELAARLAEA----ARRG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3187 FDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAALRESRTPQLPAAPP-FRDYLHWLR------ 3259
Cdd:cd19540 102 FDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGRAPDWAPLPVqYADYALWQRellgde 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3260 -GQDEAAAR--AFWREQLTGLePAALPEATE---PAE-GYASSTRRFDL-----AAASAWAQSHGLTASSLLQGALALVL 3327
Cdd:cd19540 182 dDPDSLAARqlAYWRETLAGL-PEELELPTDrprPAVaSYRGGTVEFTIdaelhARLAALAREHGATLFMVLHAALAVLL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3328 QRYYGRDDFALGITIAGRP-PELagvERMLGVFINSVPLRVTPAGEATPAPWLQALQQRNLDLRTHGYLPLAQIQragaa 3406
Cdd:cd19540 261 SRLGAGDDIPIGTPVAGRGdEAL---DDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLAAFAHQDVPFERLV----- 332
|
330 340 350
....*....|....*....|....*....|
gi 1246793773 3407 DAVSP---------FDVLLVFENLPTESRE 3427
Cdd:cd19540 333 EALNPprstarhplFQVMLAFQNTAAATLE 362
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
2062-2524 |
3.29e-32 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 132.85 E-value: 3.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2062 WTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHpDARQIAV-LDDSGARIVIgw 2140
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLL-GPKDIEYrLEAAGAKAIV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2141 gaapawvpasvrwldaesvldvvsayeepprvdVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDAS 2220
Cdd:cd05972 78 ---------------------------------TDAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2221 LATLSTVAADLG-FTALFGALLSGRRVrLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPR-ECLV 2298
Cdd:cd05972 125 HWNIADPGWAKGaWSSFFGPWLLGATV-FVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKFSHlRLVV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2299 TGGEALTGALVQQVRA-LAPTLRivNHYGPTETTvgiLTCTVPEEWPVEQGvPVGHPLAGNEAWVLDRFGLPAPVGVAGE 2377
Cdd:cd05972 204 SAGEPLNPEVIEWWRAaTGLPIR--DGYGQTETG---LTVGNFPDMPVKPG-SMGRPTPGYDVAIIDDDGRELPPGEEGD 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2378 L--YLGGGNLSLGYWQRAEQTAERFVAHplapdrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQL 2455
Cdd:cd05972 278 IaiKLPPPGLFLGYVGDPEKTEASIRGD-------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEH 350
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 2456 PGVEVAAVLALPG--------ANGVLQLGACIQGSL-EGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALAD 2524
Cdd:cd05972 351 PAVAEAAVVGSPDpvrgevvkAFVVLTSGYEPSEELaEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
2049-2522 |
3.70e-32 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 133.37 E-value: 3.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2049 PAQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAV 2128
Cdd:cd17654 4 PALIIDQTTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2129 LDDSGarivigwgaapawvpasVRWLDAESVLDVVSAYEEPPRVDVDADTP---AYLIYTSGSTGTPKGVVVSQGNLANY 2205
Cdd:cd17654 84 MKKCH-----------------VSYLLQNKELDNAPLSFTPEHRHFNIRTDeclAYVIHTSGTTGTPKIVAVPHKCILPN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2206 VAGVLPVLDLGEDASLATLSTVAADLGFTALFGALLSG-------RRVRLLPAELAfdaqalAAHLQAHPVDCLKIVPSH 2278
Cdd:cd17654 147 IQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGatllivpTSVKVLPSKLA------DILFKRHRITVLQATPTL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2279 LAGLLAAAGGTAVLPR----ECLVTGGEAL-TGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPEEwpvEQGVPVGH 2353
Cdd:cd17654 221 FRRFGSQSIKSTVLSAtsslRVLALGGEPFpSLVILSSWRGKGNRTRIFNIYGITEVSCWALAYKVPEE---DSPVQLGS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2354 PLAGNEAWVLDRFGLPapvgVAGELYLGGgnLSLGYWQRAEQTAerfvahplaPDRLLYRSGDLARLDgEGRIVYLGRGD 2433
Cdd:cd17654 298 PLLGTVIEVRDQNGSE----GTGQVFLGG--LNRVCILDDEVTV---------PKGTMRATGDFVTVK-DGELFFLGRKD 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2434 HQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGAngvlQLGACIQGslEGVAEALAQRL-----PEYLCPSRWRAVES 2508
Cdd:cd17654 362 SQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQ----RLIAFIVG--ESSSSRIHKELqltllSSHAIPDTFVQIDK 435
|
490
....*....|....
gi 1246793773 2509 MPRLGNGKIDRQAL 2522
Cdd:cd17654 436 LPLTSHGKVDKSEL 449
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
3525-4012 |
6.56e-32 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 134.49 E-value: 6.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPARIAVSAEDG-ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHA 3603
Cdd:PRK06087 29 WQQTARAMPDKIAVVDNHGaSYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3604 PAARRGFILEDSG----VCLSVSQR--------ALAVELP--GTALCLD------DPFTRAQ-LDAVEP-GELPEVPTEA 3661
Cdd:PRK06087 109 REAELVWVLNKCQakmfFAPTLFKQtrpvdlilPLQNQLPqlQQIVGVDklapatSSLSLSQiIADYEPlTTAITTHGDE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3662 PAYLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEHDVW----SLFHSHAFDFAVWelwGAWLYGGRAVLVPEA 3737
Cdd:PRK06087 189 LAAVLFTSGTEGLPKGVMLTHNNI--LASERAYCARLNLTWQDVFmmpaPLGHATGFLHGVT---APFLIGARSVLLDIF 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3738 vcrQPDAFLDLLAEYGVT-VLNQTPSAF---YALQSQAMRRElalNVRAVVFGGEALePSRLQpwRERYPQA-ELVNMYG 3812
Cdd:PRK06087 264 ---TPDACLALLEQQRCTcMLGATPFIYdllNLLEKQPADLS---ALRFFLCGGTTI-PKKVA--RECQQRGiKLLSVYG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3813 ITETTVHVsFHRLSDedlqsPTSRI----GSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE 3888
Cdd:PRK06087 335 STESSPHA-VVNLDD-----PLSRFmhtdGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3889 RGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTV---EGQGEGawLMAYAV-AA 3964
Cdd:PRK06087 409 EG---WYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAmpdERLGER--SCAYVVlKA 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1246793773 3965 DGAEPDPQSLREAL-RALLPDYMLPRLIQLLPALPLTANGKLDRKALPK 4012
Cdd:PRK06087 484 PHHSLTLEEVVAFFsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
3527-4020 |
8.66e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 134.39 E-value: 8.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3527 EIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAA 3606
Cdd:PRK06710 32 QMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTER 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3607 RRGFILEDSG----VCLS-------------------VSQRALAVELPGTALClddPFTRAQ----------------LD 3647
Cdd:PRK06710 112 ELEYQLHDSGakviLCLDlvfprvtnvqsatkiehviVTRIADFLPFPKNLLY---PFVQKKqsnlvvkvsesetihlWN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3648 AVEPG-----ELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVerlfTAATQTG---RFSFDEHD-----VWSLFHSHAF 3714
Cdd:PRK06710 189 SVEKEvntgvEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNL----VSNTLMGvqwLYNCKEGEevvlgVLPFFHVYGM 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3715 DfAVWELwgAWLYGGRAVLVPEAVCRQpdaFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALN-VRAVVFGGEALePS 3793
Cdd:PRK06710 265 T-AVMNL--SIMQGYKMVLIPKFDMKM---VFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISsIRACISGSAPL-PV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3794 RLQPWRERYPQAELVNMYGITETT--VHVSFhrLSDEdlQSPTSrIGSALPDLAVHVLD-AAGQPVPLGVVGELVVEGDG 3870
Cdd:PRK06710 338 EVQEKFETVTGGKLVEGYGLTESSpvTHSNF--LWEK--RVPGS-IGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQ 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3871 VAQGYWQRPELTAErfVERGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VE 3949
Cdd:PRK06710 413 IMKGYWNKPEETAA--VLQDG--WLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIgVP 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 3950 GQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKALPKPETQDRDE 4020
Cdd:PRK06710 489 DPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEKRKNED 559
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
3554-4057 |
8.78e-32 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 135.93 E-value: 8.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3554 SSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVCLSVSQRALAVEL-PG 3632
Cdd:PRK06060 40 AARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRFqPS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3633 TALCLDDPFTRAQldAVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVvtHRNVERL-FTAATQTGRFSFDEHDVWSLFHS 3711
Cdd:PRK06060 120 RVAEAAELMSEAA--RVAPGGYEPMGGDALAYATYTSGTTGPPKAAI--HRHADPLtFVDAMCRKALRLTPEDTGLCSAR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3712 HAFDFAVW-ELWGAWLYGGRAVLVPEAVCRQPDAFLDllAEYGVTVLNQTPSaFYALQSQAMRRELALNVRAVVFGGEAL 3790
Cdd:PRK06060 196 MYFAYGLGnSVWFPLATGGSAVINSAPVTPEAAAILS--ARFGPSVLYGVPN-FFARVIDSCSPDSFRSLRCVVSAGEAL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3791 EPSRLQPWRERYPQAELVNmyGITETTVHVSFHRLSDEDLQSPTsrIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDG 3870
Cdd:PRK06060 273 ELGLAERLMEFFGGIPILD--GIGSTEVGQTFVSNRVDEWRLGT--LGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPA 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3871 VAQGYWQRPeltaERFVERGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEG 3950
Cdd:PRK06060 349 IAKGYWNRP----DSPVANEG--WLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVR 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3951 QGEGA-WLMAYAVAADGAEPDPQSLREALRALLPD---YMLPRLIQLLPALPLTANGKLDRKALpKPETQDRDEGVLESA 4026
Cdd:PRK06060 423 ESTGAsTLQAFLVATSGATIDGSVMRDLHRGLLNRlsaFKVPHRFAVVDRLPRTPNGKLVRGAL-RKQSPTKPIWELSLT 501
|
490 500 510
....*....|....*....|....*....|..
gi 1246793773 4027 SERRLAElwrqllgGELPGRGA-HFFARGGHS 4057
Cdd:PRK06060 502 EPGSGVR-------AQRDDLSAsNMTIAGGND 526
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
534-1041 |
8.87e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 133.49 E-value: 8.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 534 VGNVVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVI 613
Cdd:PRK07656 4 WMTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 614 PLDTEWPQARRAEVVAASGCDAVLtdaqGLAGFAPSVAIAVDEL-------------------------KLDGAGENGSG 668
Cdd:PRK07656 84 PLNTRYTADEAAYILARGDAKALF----VLGLFLGVDYSATTRLpalehvviceteeddphtekmktftDFLAAGDPAER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 669 ENA-APNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVDttleqILAAWSRGA 741
Cdd:PRK07656 160 APEvDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLaanpffHVFGYKAG-----VNAPLMRGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 742 CVVARPdeLLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDwRDLA-LRCLVVGGDVLPVALAQRwF--ELGLDRr 818
Cdd:PRK07656 235 TILPLP--VFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSA-EDLSsLRLAVTGAASMPVALLER-FesELGVDI- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 819 caLINAYGPTEA----TISShyhrvqaIDASR---PVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGD 891
Cdd:PRK07656 310 --VLTGYGLSEAsgvtTFNR-------LDDDRktvAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 892 AAASErrfaplrlpsgESLRM---YRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQV-RAAAAGVV 967
Cdd:PRK07656 381 PEATA-----------AAIDAdgwLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVaEAAVIGVP 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 968 GEGAAQRLVAWVECAGEDGFGQADLNQtdsdqteserWHRalcERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK07656 450 DERLGEVGKAYVVLKPGAELTEEELIA----------YCR---EHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
3499-4011 |
9.38e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 133.58 E-value: 9.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3499 LLPSQTRSAAWTSRERYACTGNLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPR 3578
Cdd:PRK13383 15 LNPPSPRAVLRLLREASRGGTNPYTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3579 GCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVCLSVSQRALAVELPGT--ALCLDDPFTraqLDAVEPGELPE 3656
Cdd:PRK13383 95 GRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGAddAVAVIDPAT---AGAEESGGRPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3657 VPTEAPAYLIyTSGSTGTPKGV------------VVTHRNVERLFTAAtqtgRFSFdehdVWSLFHSHAFDFAVW--ELW 3722
Cdd:PRK13383 172 VAAPGRIVLL-TSGTTGKPKGVprapqlrsavgvWVTILDRTRLRTGS----RISV----AMPMFHGLGLGMLMLtiALG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3723 GAWL----YGGRAVLVPEAVCRQpDAFldllaeygvTVLNQTPSAFYALQSQAMRRELALNVRAVVFGGEALEPSRLQPW 3798
Cdd:PRK13383 243 GTVLthrhFDAEAALAQASLHRA-DAF---------TAVPVVLARILELPPRVRARNPLPQLRVVMSSGDRLDPTLGQRF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3799 RERYPQAeLVNMYGITETTVHVsfhRLSDEDLQSPTSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGdgvaqgywqr 3878
Cdd:PRK13383 313 MDTYGDI-LYNGYGSTEVGIGA---LATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGG---------- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3879 pELTAERFVERGGQR----FYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGE 3953
Cdd:PRK13383 379 -ELAGTRYTDGGGKAvvdgMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIgVPDERF 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 3954 GAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKALP 4011
Cdd:PRK13383 458 GHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELP 515
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
2630-3043 |
9.99e-32 |
|
Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.
Pssm-ID: 395541 [Multi-domain] Cd Length: 454 Bit Score: 132.07 E-value: 9.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2630 LTPIQH--WFFEQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARFQRDAAGQWQQTLGD-----WQADR 2702
Cdd:pfam00668 7 LSPAQKrmWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEerpfeLEIID 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2703 FAHREADAGQR-EDLLAQWQAGLSFD---GALLRVlALPDPQDGDTRVLFAAHHLLVDAVSWGIIVDDLQHAYAERRAGR 2778
Cdd:pfam00668 87 ISDLSESEEEEaIEAFIQRDLQSPFDlekGPLFRA-GLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLLKGE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2779 SPALAAEAC--GFGAWQAALRQlSAATLDGwRSYWR-AQAADAEAIALPwqdsdNRYADTVhlHDRFERD--------WT 2847
Cdd:pfam00668 166 PLPLPPKTPykDYAEWLQQYLQ-SEDYQKD-AAYWLeQLEGELPVLQLP-----KDYARPA--DRSFKGDrlsftldeDT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2848 ERLLTQTARAYGNEPQEVLLTalalalrdggdAATLW-----------VEMEGHGRDdlgaGLDLSRTVGWFTARYPLAL 2916
Cdd:pfam00668 237 EELLRKLAKAHGTTLNDVLLA-----------AYGLLlsrytgqddivVGTPGSGRP----SPDIERMVGMFVNTLPLRI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2917 HLPAGEDLGAALRSTKDRMR-AVPDRGLGFGVLRY---LHGELAELPVPQVCF---NYLGQLRagERDGWALCEEPDGGG 2989
Cdd:pfam00668 302 DPKGGKTFSELIKRVQEDLLsAEPHQGYPFGDLVNdlrLPRDLSRHPLFDPMFsfqNYLGQDS--QEEEFQLSELDLSVS 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 2990 RAGGNRRRHLLDVNAMLVDGELRLDWAWPQDAASREAMQALSRRYLAVLRELIA 3043
Cdd:pfam00668 380 SVIEEEAKYDLSLTASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIA 433
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
3521-4010 |
1.19e-31 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 133.61 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3521 LVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVD 3600
Cdd:PRK07059 25 LADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3601 P-HAP----------AARRGFILEDSGVCL-----SVSQRALAVELPGTALCLDDPF----TRAQLDAVEPGELP----- 3655
Cdd:PRK07059 105 PlYTPrelehqlkdsGAEAIVVLENFATTVqqvlaKTAVKHVVVASMGDLLGFKGHIvnfvVRRVKKMVPAWSLPghvrf 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3656 ------------EVPTEAP---AYLIYTSGSTGTPKGVVVTHRNV-----------ERLFTAATQTGRFSFdehdVWSLF 3709
Cdd:PRK07059 185 ndalaegarqtfKPVKLGPddvAFLQYTGGTTGVSKGATLLHRNIvanvlqmeawlQPAFEKKPRPDQLNF----VCALP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3710 HSHAFDFAVWELWGAWLyGGRAVLVPEAvcRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELAL-NVRAVVFGGE 3788
Cdd:PRK07059 261 LYHIFALTVCGLLGMRT-GGRNILIPNP--RDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFsKLIVANGGGM 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3789 ALEPSRLQPWRERyPQAELVNMYGITETTVHVSFHRLSDEDLqspTSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVEG 3868
Cdd:PRK07059 338 AVQRPVAERWLEM-TGCPITEGYGLSETSPVATCNPVDATEF---SGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3869 DGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSD-AAVT 3947
Cdd:PRK07059 414 PQVMAGYWNRPDETAKVMTADG---FFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEvAAVG 490
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 3948 VEGQGEGAWLMAYAVAADGAEPDpQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK07059 491 VPDEHSGEAVKLFVVKKDPALTE-EDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
588-1041 |
2.44e-31 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 132.93 E-value: 2.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWpqarRAEVVA----ASGCDAVLTDAQGLAG-----FAPSVAIAVDELK 658
Cdd:COG0365 67 VAIYLPNIPEAVIAMLACARIGAVHSPVFPGF----GAEALAdrieDAEAKVLITADGGLRGgkvidLKEKVDEALEELP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 659 -------LDGAGENGSGENA-------------------APNQLAYILYTSGSTGIPKGvevghaalaahidaaaealal 712
Cdd:COG0365 143 slehvivVGRTGADVPMEGDldwdellaaasaefepeptDADDPLFILYTSGTTGKPKG--------------------- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 713 saddrVLHVAG---LAVDTTLEQIL-------------------------AAWSRGACVV---ARPDeLLEPQRFLAFLS 761
Cdd:COG0365 202 -----VVHTHGgylVHAATTAKYVLdlkpgdvfwctadigwatghsyivyGPLLNGATVVlyeGRPD-FPDPGRLWELIE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 762 ERAITVTDLAPAYANELVRAsvADDWR---DL-ALRCLVVGGDVLPVALAQRWFE-LGldrrCALINAYGPTEAT--ISS 834
Cdd:COG0365 276 KYGVTVFFTAPTAIRALMKA--GDEPLkkyDLsSLRLLGSAGEPLNPEVWEWWYEaVG----VPIVDGWGQTETGgiFIS 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 835 HYhrvqAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGG--IGLAEGYRGDAAASERRFaplrlpSGESLRM 912
Cdd:COG0365 350 NL----PGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRETY------FGRFPGW 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 913 YRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQRLVAWVECAgeDGFgqad 991
Cdd:COG0365 420 YRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAeAAVVGVPDEIRGQVVKAFVVLK--PGV---- 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1246793773 992 lnqTDSDQTESERwHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:COG0365 494 ---EPSDELAKEL-QAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
3529-4010 |
2.76e-31 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 132.32 E-value: 2.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIA--VSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAA 3606
Cdd:PRK05852 26 ATRLPEAPAlvVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3607 R----------RGFILEDSGVC----LSVSQRALAVELPGTALCLDDPFTRAQLDAVEPGELPEVPT---EAPAYLIYTS 3669
Cdd:PRK05852 106 EqrvrsqaagaRVVLIDADGPHdraePTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTPATSTPEglrPDDAMIMFTG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3670 GSTGTPKGVVVTHRNVE---RLFTAATQTGrfsfdEHD----VWSLFHSHAFDFAVWelwgAWLYGGRAVLVPEAVCRQP 3742
Cdd:PRK05852 186 GTTGLPKMVPWTHANIAssvRAIITGYRLS-----PRDatvaVMPLYHGHGLIAALL----ATLASGGAVLLPARGRFSA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3743 DAFLDLLAEYGVTVLNQTPSAFYAL----QSQAMRRELAlNVRAVVFGGEALEPSRLQPWRERYpQAELVNMYGITETTV 3818
Cdd:PRK05852 257 HTFWDDIKAVGATWYTAVPTIHQILleraATEPSGRKPA-ALRFIRSCSAPLTAETAQALQTEF-AAPVVCAFGMTEATH 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3819 HVSFHRLSDEDL-QSPTSRIGSALPDLA--VHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVErggqRFY 3895
Cdd:PRK05852 335 QVTTTQIEGIGQtENPVVSTGLVGRSTGaqIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTD----GWL 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3896 RSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAV-TVEGQGEGAWLMAYAVAADGAEPDPQSL 3974
Cdd:PRK05852 411 RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVfGVPDQLYGEAVAAVIVPRESAPPTAEEL 490
|
490 500 510
....*....|....*....|....*....|....*.
gi 1246793773 3975 REALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK05852 491 VQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
3661-4010 |
4.88e-31 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 127.06 E-value: 4.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3661 APAYLIYTSGSTGTPKGVVVTHRNverLFTAATQTG-RFSFDEHDVW--SLFHSHAFDFAVweLWgAWLYGGRAVLVPEa 3737
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAAN---LLASAAGLHsRLGFGGGDSWllSLPLYHVGGLAI--LV-RSLLAGAELVLLE- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3738 vcrQPDAFLDLLAEYGVTVLNQTPSAF-YALQSQAMRRELAlNVRAVVFGGEALEPSRLQPWRERypQAELVNMYGITET 3816
Cdd:cd17630 74 ---RNQALAEDLAPPGVTHVSLVPTQLqRLLDSGQGPAALK-SLRAVLLGGAPIPPELLERAADR--GIPLYTTYGMTET 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3817 TVHVSFHRLSDEDLQSptsrIGSALPDLAVHVLDAagqpvplgvvGELVVEGDGVAQGYWqRPELTAERFvergGQRFYR 3896
Cdd:cd17630 148 ASQVATKRPDGFGRGG----VGVLLPGRELRIVED----------GEIWVGGASLAMGYL-RGQLVPEFN----EDGWFT 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3897 SGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEGAWLMAYAVAADGAEP-DPQSLR 3975
Cdd:cd17630 209 TKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVV--GVPDEELGQRPVAVIVGRGPaDPAELR 286
|
330 340 350
....*....|....*....|....*....|....*
gi 1246793773 3976 EALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:cd17630 287 AWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
2061-2522 |
5.08e-31 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 129.50 E-value: 5.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2061 SWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIgw 2140
Cdd:cd05919 10 SVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVV-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2141 gaapawvpasvrwldaesvldvvsayeepprvdVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYV-AGVLPVLDLGEDA 2219
Cdd:cd05919 88 ---------------------------------TSADDIAYLLYSSGTTGPPKGVMHAHRDPLLFAdAMAREALGLTPGD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2220 SLATLSTV--AADLGfTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVdcLKIVPSHLAGLLAAAGGTAVLPRE-- 2295
Cdd:cd05919 135 RVFSSAKMffGYGLG-NSLWFPLAVGASAVLNPGWPTAERVLATLARFRPTV--LYGVPTFYANLLDSCAGSPDALRSlr 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2296 CLVTGGEALTGALVQQVRAlAPTLRIVNHYGPTETtVGILTCTVPEEWPVEQgvpVGHPLAGNEAWVLDRFGLPAPVGVA 2375
Cdd:cd05919 212 LCVSAGEALPRGLGERWME-HFGGPILDGIGATEV-GHIFLSNRPGAWRLGS---TGRPVPGYEIRLVDEEGHTIPPGEE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2376 GELYLGGGNLSLGYWQRAEQTAERFVAHplapdrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQL 2455
Cdd:cd05919 287 GDLLVRGPSAAVGYWNNPEKSRATFNGG-------WYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQH 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 2456 PGVEVAAVLALPGANG--------VLQLGACIQGSL-EGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:cd05919 360 PAVAEAAVVAVPESTGlsrltafvVLKSPAAPQESLaRDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
3520-4012 |
5.53e-31 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 132.44 E-value: 5.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEIARR-YPARIAVSAEDGELD---YATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAA 3595
Cdd:cd05967 54 NALDRHVEAGRGdQIALIYDSPVTGTERtytYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAI 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3596 YVPV----DPHAPAARrgfiLEDSGVCLSVSQRA-------------------LAVELPGTALCLDDPFTRAQLDAVE-- 3650
Cdd:cd05967 134 HSVVfggfAAKELASR----IDDAKPKLIVTASCgiepgkvvpykplldkaleLSGHKPHHVLVLNRPQVPADLTKPGrd 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3651 ---------PGELPEVPTEA--PAYLIYTSGSTGTPKGVVvthRNVERLFTAATQTGRFSFDEH---------DV-WSLF 3709
Cdd:cd05967 210 ldwsellakAEPVDCVPVAAtdPLYILYTSGTTGKPKGVV---RDNGGHAVALNWSMRNIYGIKpgdvwwaasDVgWVVG 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3710 HShafdFAVWE--LWGAW--LYGGRAVLVPEavcrqPDAFLDLLAEYGVTVLNQTPSAFYALQSQ-----AMRRELALNV 3780
Cdd:cd05967 287 HS----YIVYGplLHGATtvLYEGKPVGTPD-----PGAFWRVIEKYQVNALFTAPTAIRAIRKEdpdgkYIKKYDLSSL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3781 RAVVFGGEALEPSRLQpWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQSPTSRIGSALPDLAVHVLDAAGQPVPLGV 3860
Cdd:cd05967 358 RTLFLAGERLDPPTLE-WAENTLGVPVIDHWWQTETGWPITANPVGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3861 VGELVVEGD---GVAQGYWQRPEltaeRFVERGGQRF---YRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAK 3934
Cdd:cd05967 437 LGNIVIKLPlppGCLLTLWKNDE----RFKKLYLSKFpgyYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEES 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3935 IASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLP----RLIQLLPALPLTANGKLDRKA 4009
Cdd:cd05967 513 VLSHPAVAECAVVgVRDELKGQVPLGLVVLKEGVKITAEELEKELVALVREQIGPvaafRLVIFVKRLPKTRSGKILRRT 592
|
...
gi 1246793773 4010 LPK 4012
Cdd:cd05967 593 LRK 595
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
3507-4010 |
9.83e-31 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 134.28 E-value: 9.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3507 AAWTSRERYACTgnLVSRFAEIARRYPARIAVSAEDG-ELDYATLDRRSSQLATLLiRQGAGPGQRVGLCLPRGCDLLVA 3585
Cdd:PRK08633 605 DSWKSRKEALPP--LAEAWIDTAKRNWSRLAVADSTGgELSYGKALTGALALARLL-KRELKDEENVGILLPPSVAGALA 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3586 LLAILKTGAayVPVDPHAPAARRGFI--LEDSGVCLSVSQRA-----------LAVELPGTALCLDDPFTRAQ------- 3645
Cdd:PRK08633 682 NLALLLAGK--VPVNLNYTASEAALKsaIEQAQIKTVITSRKfleklknkgfdLELPENVKVIYLEDLKAKISkvdklta 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3646 --------LDAVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQTgrFSFDEHDV----WSLFHSha 3713
Cdd:PRK08633 760 llaarllpARLLKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDV--FNLRNDDVilssLPFFHS-- 835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3714 FDFAVwELWGAWLYGGRAVLVPEavcrqP-DAFL--DLLAEYGVTVLNQTPSAFYA-LQSQAMRRELALNVRAVVFGGEA 3789
Cdd:PRK08633 836 FGLTV-TLWLPLLEGIKVVYHPD-----PtDALGiaKLVAKHRATILLGTPTFLRLyLRNKKLHPLMFASLRLVVAGAEK 909
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3790 LEPSRLQPWRERYpQAELVNMYGITETTVHVSFH---RLSDEDLQSPTSRIGS---ALPDLAVHVLDA-AGQPVPLGVVG 3862
Cdd:PRK08633 910 LKPEVADAFEEKF-GIRILEGYGATETSPVASVNlpdVLAADFKRQTGSKEGSvgmPLPGVAVRIVDPeTFEELPPGEDG 988
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3863 ELVVEGDGVAQGYWQRPELTAERFVERGGQRFYRSGDLGRYRADGSLEYRGR-------GDDQVKLRgyRIEPgEIAAKI 3935
Cdd:PRK08633 989 LILIGGPQVMKGYLGDPEKTAEVIKDIDGIGWYVTGDKGHLDEDGFLTITDRysrfakiGGEMVPLG--AVEE-ELAKAL 1065
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 3936 -ASLPQVSDAAVTVEGQGEgawlmAYAVAADGAEPDPQSLREALRAL-LPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK08633 1066 gGEEVVFAVTAVPDEKKGE-----KLVVLHTCGAEDVEELKRAIKESgLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
3541-4007 |
2.35e-30 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 128.33 E-value: 2.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3541 EDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVcls 3620
Cdd:cd05914 4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3621 vsqralavelpgTALCLDDPftraqldavepgelpevptEAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQTGRFSF 3700
Cdd:cd05914 81 ------------KAIFVSDE-------------------DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGK 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3701 DEHDVWSLFHSHAFDFaVWELWGAWLYGGRAVLVPeavcRQPDAFLDLLAEYGVTV------------------LNQTPS 3762
Cdd:cd05914 130 GDKILSILPLHHIYPL-TFTLLLPLLNGAHVVFLD----KIPSAKIIALAFAQVTPtlgvpvplviekifkmdiIPKLTL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3763 A--------------FYALQSQAMRRELALNVRAVVFGGEALEPSRLQPWRE-RYPQAElvnMYGITETTVHVSFHRLSD 3827
Cdd:cd05914 205 KkfkfklakkinnrkIRKLAFKKVHEAFGGNIKEFVIGGAKINPDVEEFLRTiGFPYTI---GYGMTETAPIISYSPPNR 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3828 EDLQSptsrIGSALPDLAVHVLDaagqPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADG 3907
Cdd:cd05914 282 IRLGS----AGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDG---WFHTGDLGKIDAEG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3908 SLEYRGRGDDQVKL-RGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEGAWLMAYAVAADGAEPDPQSLREALR------- 3979
Cdd:cd05914 351 YLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLVALAYIDPDFLDVKALKQRNIIDAIKwevrdkv 430
|
490 500 510
....*....|....*....|....*....|
gi 1246793773 3980 -ALLPDYMLPRLIQLLPA-LPLTANGKLDR 4007
Cdd:cd05914 431 nQKVPNYKKISKVKIVKEeFEKTPKGKIKR 460
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
3529-4032 |
2.82e-30 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 129.49 E-value: 2.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARR 3608
Cdd:PRK06155 31 AERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3609 GFILEDSGVCLSVSQRALAVELPgTALCLDDPFTR--------AQLDAVEPGELPEVPTEAPA-----------YLIYTS 3669
Cdd:PRK06155 111 EHILRNSGARLLVVEAALLAALE-AADPGDLPLPAvwlldapaSVSVPAGWSTAPLPPLDAPApaaavqpgdtaAILYTS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3670 GSTGTPKGVVVTHrnvERLFTAATQTGR-FSFDEHDVW----SLFHSHAFDfavwELWGAWLYGGRAVLVPEAvcrQPDA 3744
Cdd:PRK06155 190 GTTGPSKGVCCPH---AQFYWWGRNSAEdLEIGADDVLyttlPLFHTNALN----AFFQALLAGATYVLEPRF---SASG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3745 FLDLLAEYGVTVLNQTPSAFYALQSQAMR-RELALNVRAVVFGGEAlePSRLQPWRERYPQAeLVNMYGITETTVHVSFH 3823
Cdd:PRK06155 260 FWPAVRRHGATVTYLLGAMVSILLSQPAReSDRAHRVRVALGPGVP--AALHAAFRERFGVD-LLDGYGSTETNFVIAVT 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3824 RLSdedlQSPTSrIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGD---GVAQGYWQRPELTaerfVERGGQRFYRSGDL 3900
Cdd:PRK06155 337 HGS----QRPGS-MGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPEKT----VEAWRNLWFHTGDR 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3901 GRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAV-TVEGQGEGAWLMAYAVAADGAEPDPQSLREALR 3979
Cdd:PRK06155 408 VVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVfPVPSELGEDEVMAAVVLRDGTALEPVALVRHCE 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 3980 ALLPDYMLPRLIQLLPALPLTANGKLDRKALpkpetqdRDEGVLESASERRLA 4032
Cdd:PRK06155 488 PRLAYFAVPRYVEFVAALPKTENGKVQKFVL-------REQGVTADTWDREAA 533
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
3081-3403 |
2.97e-30 |
|
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380456 [Multi-domain] Cd Length: 419 Bit Score: 127.10 E-value: 2.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3081 YPLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGF-AVQGLPSPRQLPHRQVSLPLA 3159
Cdd:cd19533 2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFtEEEGEPYQWIDPYTPVPIRHI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3160 eqDWSGLE-PAQARSRLSELQAQQceaGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAALR 3238
Cdd:cd19533 82 --DLSGDPdPEGAAQQWMQEDLRK---PLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3239 ESRTPQLPAAPPFRDYL----------HWLRGqdeaaaRAFWREQLTGL-EPAALpeaTEPAEGYASSTRRFDL------ 3301
Cdd:cd19533 157 KGRPAPPAPFGSFLDLVeeeqayrqseRFERD------RAFWTEQFEDLpEPVSL---ARRAPGRSLAFLRRTAelppel 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3302 -AAASAWAQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRppeLAGVER-MLGVFINSVPLRVTPAGEATPAPWL 3379
Cdd:cd19533 228 tRTLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGR---LGAAARqTPGMVANTLPLRLTVDPQQTFAELV 304
|
330 340
....*....|....*....|....
gi 1246793773 3380 QALQQRNLDLRTHGYLPLAQIQRA 3403
Cdd:cd19533 305 AQVSRELRSLLRHQRYRYEDLRRD 328
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
1142-1559 |
3.18e-30 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380453 [Multi-domain] Cd Length: 427 Bit Score: 127.14 E-value: 3.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1142 LSPIQRWFFDSAPAQPDR--YHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPAIQAQD 1219
Cdd:cd19066 4 LSPMQRGMWFLKKLATDPsaFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVRFRIEIID 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1220 WRGAADLDSRVDAAFARMQEaTPL---AGPLVALT-HAHCDDGERLLICAHHLIVDAVSWRLLLGELFDGLAALARGEAW 1295
Cdd:cd19066 84 LRNLADPEARLLELIDQIQQ-TIYdleRGPLVRVAlFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQKPT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1296 TPSARGaSYADYVEAL---READDAQRfDAGFWRELAAQ--PMQALPQD-RPVALADARQsnvGRIVQTLDAGLTADLLE 1369
Cdd:cd19066 163 LPPPVG-SYADYAAWLekqLESEAAQA-DLAYWTSYLHGlpPPLPLPKAkRPSQVASYEV---LTLEFFLRSEETKRLRE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1370 RAGEAYRCRTDeVLLIALARALATRTGRNRLWLDRERHGR---DVLDgrdwssVLGWYTAVHPLPLDLGV-ADGPAQIGA 1445
Cdd:cd19066 238 VARESGTTPTQ-LLLAAFALALKRLTASIDVVIGLTFLNRpdeAVED------TIGLFLNLLPLRIDTSPdATFPELLKR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1446 LKEQIRALARRGLDYMPLV--ASARIPALPAGQL---LFNYH------GVVDAGAHPAFEVEPRTlasgngadnPPGALV 1514
Cdd:cd19066 311 TKEQSREAIEHQRVPFIELvrHLGVVPEAPKHPLfepVFTFKnnqqqlGKTGGFIFTTPVYTSSE---------GTVFDL 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1246793773 1515 EINARVQA-GRLGLVWNYAGEAYDAATIEAWSQAFAAELAALVAHC 1559
Cdd:cd19066 382 DLEASEDPdGDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
3665-4005 |
3.50e-30 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 124.54 E-value: 3.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3665 LIYTSGSTGTPKGVVVTHRNVERLFTAATQTGRFSFDEHD--VWSLFHShafdFAVWELWGAWLYGGrAVLVPEAVCrQP 3742
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYliINPFFHT----FGYKAGIVACLLTG-ATVVPVAVF-DV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3743 DAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELAL-NVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVhVS 3821
Cdd:cd17638 79 DAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLsSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGV-AT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3822 FHRLSDeDLQSPTSRIGSALPDLAVHVLDAagqpvplgvvGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLG 3901
Cdd:cd17638 158 MCRPGD-DAETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADG---WLHTGDVG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3902 RYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSLREALRA 3980
Cdd:cd17638 224 ELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIgVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRE 303
|
330 340
....*....|....*....|....*
gi 1246793773 3981 LLPDYMLPRLIQLLPALPLTANGKL 4005
Cdd:cd17638 304 RLANYKVPRFVRFLDELPRNASGKV 328
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
3543-4010 |
4.45e-30 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 127.83 E-value: 4.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3543 GELDYATLDRRSSQLATLLiRQGAGPGQRVGLCLPRGCDLLVALLAILKTGaaYVPVDPHAPAARRGFI--LEDSGVCLS 3620
Cdd:cd05909 6 TSLTYRKLLTGAIALARKL-AKMTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTAGLRELRacIKLAGIKTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3621 VSQRAL----------AVELPGTALCLDDpfTRAQL---DAVEPG------------ELPEVPTEA--PAYLIYTSGSTG 3673
Cdd:cd05909 83 LTSKQFieklklhhlfDVEYDARIVYLED--LRAKIskaDKCKAFlagkfppkwllrIFGVAPVQPddPAVILFTSGSEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3674 TPKGVVVTHRNVerLFTAATQTGRFSFDEHDVW----SLFHShaFDFAVwELWGAWLYGGRAVLVPEAVcrQPDAFLDLL 3749
Cdd:cd05909 161 LPKGVVLSHKNL--LANVEQITAIFDPNPEDVVfgalPFFHS--FGLTG-CLWLPLLSGIKVVFHPNPL--DYKKIPELI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3750 AEYGVTVLNQTPSAFYALQSQAMRRELAlNVRAVVFGGEALEPSRLQPWRERYpQAELVNMYGITETTVHVSFHRlsded 3829
Cdd:cd05909 234 YDKKATILLGTPTFLRGYARAAHPEDFS-SLRLVVAGAEKLKDTLRQEFQEKF-GIRILEGYGTTECSPVISVNT----- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3830 LQSPtSRIGSA---LPDLAVHVLDAAG-QPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVErggqRFYRSGDLGRYRA 3905
Cdd:cd05909 307 PQSP-NKEGTVgrpLPGMEVKIVSVEThEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGD----GWYDTGDIGKIDG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3906 DGSLEYRGRGDDQVKLRG-----YRIEpgEIAAKIasLP-QVSDAAVTV--EGQGEgawlmAYAVAADGAEPDPQSLREA 3977
Cdd:cd05909 382 EGFLTITGRLSRFAKIAGemvslEAIE--DILSEI--LPeDNEVAVVSVpdGRKGE-----KIVLLTTTTDTDPSSLNDI 452
|
490 500 510
....*....|....*....|....*....|....
gi 1246793773 3978 LRAL-LPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:cd05909 453 LKNAgISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
3529-4010 |
1.30e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 127.07 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLI--RQGAGPgQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPhapaA 3606
Cdd:PRK13388 11 DRAGDDTIAVRYGDRTWTWREVLAEAAARAAALIalADPDRP-LHVGVLLGNTPEMLFWLAAAALGGYVLVGLNT----T 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3607 RRGFILE------DSGVCLSVSQ-RAL--AVELPGTALCLDDPFTRAQLDAVEPGELP--EVPTEAPAYLIYTSGSTGTP 3675
Cdd:PRK13388 86 RRGAALAadirraDCQLLVTDAEhRPLldGLDLPGVRVLDVDTPAYAELVAAAGALTPhrEVDAMDPFMLIFTSGTTGAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3676 KGVVVTHRNVerLFTAATQTGRFSFDEHDV----WSLFHSHafdfAVWELWGAWLYGGRAVLVPEAVcrQPDAFLDLLAE 3751
Cdd:PRK13388 166 KAVRCSHGRL--AFAGRALTERFGLTRDDVcyvsMPLFHSN----AVMAGWAPAVASGAAVALPAKF--SASGFLDDVRR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3752 YGVTVLNQTPSAFYALQSQAMRRELALNVRAVVFGGEAlEPSRLQPWRERYpQAELVNMYGITETTVHVSfhrlsdEDLQ 3831
Cdd:PRK13388 238 YGATYFNYVGKPLAYILATPERPDDADNPLRVAFGNEA-SPRDIAEFSRRF-GCQVEDGYGSSEGAVIVV------REPG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3832 SPTSRIGSALPDLAVH-----------VLDAAGQPV-PLGVVGELV-VEGDGVAQGYWQRPELTAERFveRGGqrFYRSG 3898
Cdd:PRK13388 310 TPPGSIGRGAPGVAIYnpetltecavaRFDAHGALLnADEAIGELVnTAGAGFFEGYYNNPEATAERM--RHG--MYWSG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3899 DLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAV-TVEGQGEGAWLMAYAVAADGAEPDPQSLREA 3977
Cdd:PRK13388 386 DLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVyAVPDERVGDQVMAALVLRDGATFDPDAFAAF 465
|
490 500 510
....*....|....*....|....*....|....*
gi 1246793773 3978 LRAL--LPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK13388 466 LAAQpdLGTKAWPRYVRIAADLPSTATNKVLKREL 500
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
673-1044 |
1.34e-29 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 126.86 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 673 PNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGA-CVVARPDELL 751
Cdd:cd17647 108 PDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAqLLVPTQDDIG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 752 EPQRFLAFLSERAITVTDLAPAYAnELVRASVADDWRDLaLRCLVVGgDVLPVALAQRWfeLGLDRRCALINAYGPTEAT 831
Cdd:cd17647 188 TPGRLAEWMAKYGATVTHLTPAMG-QLLTAQATTPFPKL-HHAFFVG-DILTKRDCLRL--QTLAENVRIVNMYGTTETQ 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 832 ISSHYHRVQA--------------IDASRPVPLGQLLpgriaaVLDAHGR--IVPRGVCGELALGGIGLAEGYRGDAAAS 895
Cdd:cd17647 263 RAVSYFEVPSrssdptflknlkdvMPAGRGMLNVQLL------VVNRNDRtqICGIGEVGEIYVRAGGLAEGYRGLPELN 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 896 ERRF-------------------APLRLPS-GESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQ 955
Cdd:cd17647 337 KEKFvnnwfvepdhwnyldkdnnEPWRQFWlGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQ 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 956 LPQVRAAAAGVVGEGAAQR-LVAWVECAGE--DGFGQADLNQTDSDQTES-----ERWHRA-------LCERLPAYMVPT 1020
Cdd:cd17647 417 HPLVRENITLVRRDKDEEPtLVSYIVPRFDkpDDESFAQEDVPKEVSTDPivkglIGYRKLikdirefLKKRLASYAIPS 496
|
410 420
....*....|....*....|....
gi 1246793773 1021 QFVALPRLPRNASGKIDRRALPAP 1044
Cdd:cd17647 497 LIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
3115-3385 |
2.17e-29 |
|
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380458 [Multi-domain] Cd Length: 423 Bit Score: 124.52 E-value: 2.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3115 LDREAFAAAWQQALERHPILRSGFavqgLPSPRQLPHRQVSLP-LAEQDWSGLEPAQARSRLSELQAQ---QCeagFDLA 3190
Cdd:cd19535 37 LDPDRLERAWNKLIARHPMLRAVF----LDDGTQQILPEVPWYgITVHDLRGLSEEEAEAALEELRERlshRV---LDVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3191 APPL--MRLALLRRSAdehwlvwTRHH-----LIVDGWSSALLLDEVWRLYAALREsrtpQLPAAPP-FRDYLHWLRGQD 3262
Cdd:cd19535 110 RGPLfdIRLSLLPEGR-------TRLHlsidlLVADALSLQILLRELAALYEDPGE----PLPPLELsFRDYLLAEQALR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3263 EAA---ARAFWREQLTGLEPA-ALPEATEPAE-GYASSTRRFDLAAASAW------AQSHGLTASSLLQGALALVLQRYY 3331
Cdd:cd19535 179 ETAyerARAYWQERLPTLPPApQLPLAKDPEEiKEPRFTRREHRLSAEQWqrlkerARQHGVTPSMVLLTAYAEVLARWS 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 3332 GRDDFALGITIAGRPPELAGVERMLGVFINSVPLRVTPAGEATPAPWLQALQQR 3385
Cdd:cd19535 259 GQPRFLLNLTLFNRLPLHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQ 312
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
3533-4010 |
2.46e-29 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 126.26 E-value: 2.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3533 PARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYV--------------- 3597
Cdd:PRK10946 37 SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVAPVnalfshqrselnaya 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3598 -PVDP--------HAPAARRGFILEDSGVCLSVSQRALavelpgtalcLDDPFTRAQLDAVEPGELPEVPTEAP----AY 3664
Cdd:PRK10946 117 sQIEPalliadrqHALFSDDDFLNTLVAEHSSLRVVLL----------LNDDGEHSLDDAINHPAEDFTATPSPadevAF 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3665 LIYTSGSTGTPKGVVVTHRNVERLFTAATQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLV--PEAVCRQP 3742
Cdd:PRK10946 187 FQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAHNYPMSSPGALGVFLAGGTVVLApdPSATLCFP 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3743 dafldLLAEYGVTVLNQTPSAFyALQSQAM-----RRELA-LNVRAVvfGGEALEPSRLQpwreRYPQ---AELVNMYGI 3813
Cdd:PRK10946 267 -----LIEKHQVNVTALVPPAV-SLWLQAIaeggsRAQLAsLKLLQV--GGARLSETLAR----RIPAelgCQLQQVFGM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3814 TETTVhvSFHRLSDEDLQSPTSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqr 3893
Cdd:PRK10946 335 AEGLV--NYTRLDDSDERIFTTQGRPMSPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANG--- 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3894 FYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAA-VTVEGQGEGAWLMAYAVAADGAEpdPQ 3972
Cdd:PRK10946 410 FYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAAlVSMEDELMGEKSCAFLVVKEPLK--AV 487
|
490 500 510
....*....|....*....|....*....|....*....
gi 1246793773 3973 SLREALRAL-LPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK10946 488 QLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
3082-3396 |
3.25e-29 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380471 [Multi-domain] Cd Length: 430 Bit Score: 123.91 E-value: 3.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3082 PLAPLQEGLLF-HSLLnaeADPYINQTTVALH--GALDREAFAAAWQQALERHPILRSGFaVQGLPSPRQLPHRQVSLPL 3158
Cdd:cd20483 3 PMSTFQRRLWFlHNFL---EDKTFLNLLLVCHikGKPDVNLLQKALSELVRRHEVLRTAY-FEGDDFGEQQVLDDPSFHL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3159 AEQDWSglEPAQARSRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAALR 3238
Cdd:cd20483 79 IVIDLS--EAADPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3239 ESRTPQLPAAPP--FRDYLHW----LRGQDEAAARAFWREQLTGLEPAA--LPEATE---PAEGYASSTRRFDLAAASA- 3306
Cdd:cd20483 157 AGRDLATVPPPPvqYIDFTLWhnalLQSPLVQPLLDFWKEKLEGIPDASklLPFAKAerpPVKDYERSTVEATLDKELLa 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3307 ----WAQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRP-PElagVERMLGVFINSVPLRVTPAGEATPAPWLQA 3381
Cdd:cd20483 237 rmkrICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPhPD---FDDLVGFFVNMLPIRCRMDCDMSFDDLLES 313
|
330
....*....|....*
gi 1246793773 3382 LQQRNLDLRTHGYLP 3396
Cdd:cd20483 314 TKTTCLEAYEHSAVP 328
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
672-1041 |
4.03e-29 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 124.08 E-value: 4.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 672 APNQLAYILYTSGSTGIPKGVEVGHAALA-AHIDAAAEALALSADDRVLH-------VAGLavdttLEQILAAWSRGACV 743
Cdd:cd05971 86 GSDDPALIIYTSGTTGPPKGALHAHRVLLgHLPGVQFPFNLFPRDGDLYWtpadwawIGGL-----LDVLLPSLYFGVPV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 744 VARPDELLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQrWF--ELGLDrrcal 821
Cdd:cd05971 161 LAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLG-WAreQFGVE----- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 822 IN-AYGPTEAT--ISSHyhrvQAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELAL---GGIGLAeGYRGDAAAS 895
Cdd:cd05971 235 VNeFYGQTECNlvIGNC----SALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVelpDPVAFL-GYWNNPSAT 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 896 ERRFAplrlpsGESLRmyrSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQR 974
Cdd:cd05971 310 EKKMA------GDWLL---TGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLmAAVVGIPDPIRGEI 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 975 LVAWVEcagedgfgqadLNQTDSDQTESERWHRALCE-RLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05971 381 VKAFVV-----------LNPGETPSDALAREIQELVKtRLAAHEYPREIEFVNELPRTATGKIRRREL 437
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
588-1042 |
4.60e-29 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 123.56 E-value: 4.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDaqglagfapsvaiavdelkldgagengs 667
Cdd:cd05934 31 VALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD---------------------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 668 genaapnqLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVdttleQILAAWSRGA 741
Cdd:cd05934 83 --------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLtvlplfHINAQAV-----SVLAALSVGA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 742 CVVARPDelLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRClvVGGDVLPVALAQRWFElgldrR--C 819
Cdd:cd05934 150 TLVLLPR--FSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRA--AYGAPNPPELHEEFEE-----RfgV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 820 ALINAYGPTEATISShyhrVQAIDASRPVP-LGQLLPGRIAAVLDAHGRIVPRGVCGEL---ALGGIGLAEGYRGDAAAS 895
Cdd:cd05934 221 RLLEGYGMTETIVGV----IGPRDEPRRPGsIGRPAPGYEVRIVDDDGQELPAGEPGELvirGLRGWGFFKGYYNMPEAT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 896 ERRFAPLrlpsgeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA-GVVGEGAAQR 974
Cdd:cd05934 297 AEAMRNG---------WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVvAVPDEVGEDE 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 975 LVAWVECagEDGfgqadlnQTDsDQTESERWHRalcERLPAYMVPTQFVALPRLPRNASGKIDRRALP 1042
Cdd:cd05934 368 VKAVVVL--RPG-------ETL-DPEELFAFCE---GQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
2050-2527 |
4.63e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 125.88 E-value: 4.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2050 AQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVL 2129
Cdd:PRK05605 46 GDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 DDSGARIVIGWG-AAP----------------------------------------------AWVPASVRW---LDAESV 2159
Cdd:PRK05605 126 EDHGARVAIVWDkVAPtverlrrttpletivsvnmiaampllqrlalrlpipalrkaraaltGPAPGTVPWetlVDAAIG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2160 LDVVSAyeEPPRVDvdADTPAYLIYTSGSTGTPKGVVVSQGNL-ANYVAGVLPVLDLGEDAS--LATLSTVAA-DLGFTA 2235
Cdd:PRK05605 206 GDGSDV--SHPRPT--PDDVALILYTSGTTGKPKGAQLTHRNLfANAAQGKAWVPGLGDGPErvLAALPMFHAyGLTLCL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2236 LFGALLSGRRVrLLPaelAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAV--------------LPREcLVTGG 2301
Cdd:PRK05605 282 TLAVSIGGELV-LLP---APDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVdlsgvrnafsgamaLPVS-TVELW 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2302 EALTGALvqqvralaptlrIVNHYGPTETTvgiltctvpeewPVEQGVP---------VGHPLAGNEAWVLDR--FGLPA 2370
Cdd:PRK05605 357 EKLTGGL------------LVEGYGLTETS------------PIIVGNPmsddrrpgyVGVPFPDTEVRIVDPedPDETM 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2371 PVGVAGELYLGGGNLSLGYWQRAEQTAERFvahplAPDrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQ 2450
Cdd:PRK05605 413 PDGEEGELLVRGPQVFKGYWNRPEETAKSF-----LDG--WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEE 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2451 VLAQLPGVEVAAVLALPGANG--------VLQLGACIQGslEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:PRK05605 486 VLREHPGVEDAAVVGLPREDGseevvaavVLEPGAALDP--EGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREV 563
|
....*
gi 1246793773 2523 ADLLQ 2527
Cdd:PRK05605 564 REELL 568
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
3545-4010 |
6.71e-29 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 123.06 E-value: 6.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3545 LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPvdphapaarrgfiledSGVCLSVSQR 3624
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP----------------ATTLLTPDDL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3625 ALAVELPGTALCLDDPFTRAqldavepgelpevptEAPAYLIYTSGSTGTPKGVVVTHR-----NVERLFTAATQTGrfs 3699
Cdd:cd05974 65 RDRVDRGGAVYAAVDENTHA---------------DDPMLLYFTSGTTSKPKLVEHTHRsypvgHLSTMYWIGLKPG--- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3700 fdehDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRReLALN 3779
Cdd:cd05974 127 ----DVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLAS-FDVK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3780 VRAVVFGGEALEPSRLQPWRERYPQAeLVNMYGITETTVHVSfhrlsdedlQSP-----TSRIGSALPDLAVHVLDAAGQ 3854
Cdd:cd05974 202 LREVVGAGEPLNPEVIEQVRRAWGLT-IRDGYGQTETTALVG---------NSPgqpvkAGSMGRPLPGYRVALLDPDGA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3855 PVPLGVVGelVVEGD----GVAQGYWQRPELTAErfVERGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGE 3930
Cdd:cd05974 272 PATEGEVA--LDLGDtrpvGLMKGYAGDPDKTAH--AMRGG--YYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3931 IAAKIASLPQVSDAAVTVEGQGEG-AWLMAYAVAADGAEPDPQ---SLREALRALLPDYMLPRLIQLLpALPLTANGKLD 4006
Cdd:cd05974 346 LESVLIEHPAVAEAAVVPSPDPVRlSVPKAFIVLRAGYEPSPEtalEIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIR 424
|
....
gi 1246793773 4007 RKAL 4010
Cdd:cd05974 425 RVEL 428
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
2373-2812 |
7.47e-29 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 128.75 E-value: 7.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2373 GVAGELYLGGGNLSLGYWQRAEQTAERFVAHPlapDRLLYRSGDLARLDgEGRIVYLGRGDHQVKIRGYRVELGEVEQVL 2452
Cdd:PRK05691 395 NRVGEIWASGPSIAHGYWRNPEASAKTFVEHD---GRTWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIEKTV 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2453 AQlpGVEVA-----AVLALP--GANGV---LQLGACIQGSLEgvAEALAQRLPEYLCPSRWRAVE--------SMPRLGN 2514
Cdd:PRK05691 471 ER--EVEVVrkgrvAAFAVNhqGEEGIgiaAEISRSVQKILP--PQALIKSIRQAVAEACQEAPSvvlllnpgALPKTSS 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2515 GKIDRQALADLLQQDDADSSA---------EAIDETPVNEV---LRELWQKLLGREHIGAHDNFFALGGDSILSLQLVAR 2582
Cdd:PRK05691 547 GKLQRSACRLRLADGSLDSYAlfpalqaveAAQTAASGDELqarIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVAR 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2583 ARQA-GLALMPRQLYDHPTLAGLSAQV----QASSPAPATIkPATEAEQSFGLTPIQH--WFFEQALDQPAHWNMSLYLK 2655
Cdd:PRK05691 627 LRDElGIDLNLRQLFEAPTLAAFSAAVarqlAGGGAAQAAI-ARLPRGQALPQSLAQNrlWLLWQLDPQSAAYNIPGGLH 705
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2656 LPGALDTAAFAAALADVAAAHPMLRARF--------QR-DAAGQWQQTLGDWQADRFAHREADAGQ-REDllaqwQAGLS 2725
Cdd:PRK05691 706 LRGELDEAALRASFQRLVERHESLRTRFyerdgvalQRiDAQGEFALQRIDLSDLPEAEREARAAQiREE-----EARQP 780
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2726 FD---GALLRVlALPDPQDGDTRVLFAAHHLLVDAVSWGIIVDDLQHAYAERRAGRSPALAAEACGFGAWQAALRQ-LSA 2801
Cdd:PRK05691 781 FDlekGPLLRV-TLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGAWQRQwLAQ 859
|
490
....*....|.
gi 1246793773 2802 ATLDGWRSYWR 2812
Cdd:PRK05691 860 GEAARQLAYWK 870
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
2050-2524 |
9.93e-29 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 123.96 E-value: 9.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2050 AQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRT--FAqLAAMAAVWHRGAAwLPLDPQHPDARQIA 2127
Cdd:cd05926 3 APALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGleFV-VAFLAAARAGAVV-APLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2128 VLDDSGARIVIGW--GAAPAWVPAS-VRWLDAESVLDVVSAYEEP----------------PRVDVDADTPAYLIYTSGS 2188
Cdd:cd05926 81 YLADLGSKLVLTPkgELGPASRAASkLGLAILELALDVGVLIRAPsaeslsnlladkknakSEGVPLPDDLALILHTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2189 TGTPKGVVVSQGNLANYVAGVLPVLDLGE-DASLAT--LSTVAADLGftALFGALLSGRRVrLLPAelAFDAQALAAHLQ 2265
Cdd:cd05926 161 TGRPKGVPLTHRNLAASATNITNTYKLTPdDRTLVVmpLFHVHGLVA--SLLSTLAAGGSV-VLPP--RFSASTFWPDVR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2266 AHPVDCLKIVPS--HLAGLLAAAGGTAVLP-----RECLVTGGEALTGALVQQVRalAPTLRIvnhYGPTETTVGIlTCT 2338
Cdd:cd05926 236 DYNATWYTAVPTihQILLNRPEPNPESPPPklrfiRSCSASLPPAVLEALEATFG--APVLEA---YGMTEAAHQM-TSN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2339 vpeewPVEQGVP----VGHPlAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVahplaPDRLLyRS 2414
Cdd:cd05926 310 -----PLPPGPRkpgsVGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAF-----KDGWF-RT 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2415 GDLARLDGEGRIVYLGRgdhqVK---IRGyrvelGE------VEQVLAQLPGVEVAAVLALP--------GANGVLQLGA 2477
Cdd:cd05926 378 GDLGYLDADGYLFLTGR----IKeliNRG-----GEkispleVDGVLLSHPAVLEAVAFGVPdekygeevAAAVVLREGA 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1246793773 2478 CIqgSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALAD 2524
Cdd:cd05926 449 SV--TEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
3513-4020 |
1.06e-28 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 124.78 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3513 ERYActgNLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQ-GAGPGQRVGLCLPrgcDLL---VALLA 3588
Cdd:PRK08974 20 DRYQ---SLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMP---NLLqypIALFG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3589 ILKTGAAYVPVDP--------H------APA------------------ARRGFILEDSGVCLSVSQRALA--------- 3627
Cdd:PRK08974 94 ILRAGMIVVNVNPlytpreleHqlndsgAKAivivsnfahtlekvvfktPVKHVILTRMGDQLSTAKGTLVnfvvkyikr 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3628 ----VELPGtALCLDDPFTRA-QLDAVEPgelpEVPTEAPAYLIYTSGSTGTPKGVVVTHRN-VERLFTAATQTGRFSFD 3701
Cdd:PRK08974 174 lvpkYHLPD-AISFRSALHKGrRMQYVKP----ELVPEDLAFLQYTGGTTGVAKGAMLTHRNmLANLEQAKAAYGPLLHP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3702 EHD--VWSLFHSHAFDFAVWELWGAWLyGGRAVLVPEAvcRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELAL- 3778
Cdd:PRK08974 249 GKElvVTALPLYHIFALTVNCLLFIEL-GGQNLLITNP--RDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFs 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3779 NVRAVVFGGEALEPSRLQPWrERYPQAELVNMYGITETTVHVSFHRLsdeDLQSPTSRIGSALPDLAVHVLDAAGQPVPL 3858
Cdd:PRK08974 326 SLKLSVGGGMAVQQAVAERW-VKLTGQYLLEGYGLTECSPLVSVNPY---DLDYYSGSIGLPVPSTEIKLVDDDGNEVPP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3859 GVVGELVVEGDGVAQGYWQRPELTAErfVERGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASL 3938
Cdd:PRK08974 402 GEPGELWVKGPQVMLGYWQRPEATDE--VIKDG--WLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLH 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3939 PQVSD-AAVTVEGQGEGAWLMAYAVAADgAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKALpkpetqd 4017
Cdd:PRK08974 478 PKVLEvAAVGVPSEVSGEAVKIFVVKKD-PSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL------- 549
|
...
gi 1246793773 4018 RDE 4020
Cdd:PRK08974 550 RDE 552
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
2052-2522 |
1.07e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 124.14 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLP----LDPQhpdarQIA 2127
Cdd:PRK06187 22 KEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPinirLKPE-----EIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2128 -VLDDSGARIV-----------------------IGWGAAPAwVPASVRWLDAESVLDvvSAYEEPPRVDVDADTPAYLI 2183
Cdd:PRK06187 97 yILNDAEDRVVlvdsefvpllaailpqlptvrtvIVEGDGPA-APLAPEVGEYEELLA--AASDTFDFPDIDENDAAAML 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2184 YTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLG-EDASLatlstVAADL----GFTALFGALLSGRRVrLLPAElaFDAQ 2258
Cdd:PRK06187 174 YTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSrDDVYL-----VIVPMfhvhAWGLPYLALMAGAKQ-VIPRR--FDPE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2259 ALAAHLQAHPVDCLKIVPS--HLAGLLAAAGGTAVLPRECLVTGGEALTGALVQQVRALApTLRIVNHYGPTETTvGILT 2336
Cdd:PRK06187 246 NLLDLIETERVTFFFAVPTiwQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKF-GIDLVQGYGMTETS-PVVS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2337 CTVPEEWPVEQG---VPVGHPLAGNEAWVLDRFG--LPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHplapdrlL 2411
Cdd:PRK06187 324 VLPPEDQLPGQWtkrRSAGRPLPGVEARIVDDDGdeLPPDGGEVGEIIVRGPWLMQGYWNRPEATAETIDGG-------W 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2412 YRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALP--------GANGVLQLGACIqgSL 2483
Cdd:PRK06187 397 LHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPdekwgerpVAVVVLKPGATL--DA 474
|
490 500 510
....*....|....*....|....*....|....*....
gi 1246793773 2484 EGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:PRK06187 475 KELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
539-1041 |
1.15e-28 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 123.59 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 539 DAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGlsVIPLdTE 618
Cdd:cd05920 19 DLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLG--AVPV-LA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 619 WPQARRAEVVAasgcdavltdaqgLAGFAPSVAIAV-DELKLDGAGENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHA 697
Cdd:cd05920 96 LPSHRRSELSA-------------FCAHAEAVAYIVpDRHAGFDHRALARELAESIPEVALFLLSGGTTGTPKLIPRTHN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 698 ALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQ--ILAAWSRGACVVARPDEllEPQRFLAFLSERAITVTDLAPAYA 775
Cdd:cd05920 163 DYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLACpgVLGTLLAGGRVVLAPDP--SPDAAFPLIEREGVTVTALVPALV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 776 NELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFE-LGldrrCALINAYGPTEATISshYHRVQAIDA------SRPV 848
Cdd:cd05920 241 SLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPvLG----CTLQQVFGMAEGLLN--YTRLDDPDEviihtqGRPM 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 849 -PLGQLLpgriaaVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPlrlpSGeslrMYRSGDRVRLLDDGEL 927
Cdd:cd05920 315 sPDDEIR------VVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTP----DG----FYRTGDLVRRTPDGYL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 928 QFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA-GVVGEGAAQRLVAWVECAGEdgfgqadlnqtdsdQTESERWH 1006
Cdd:cd05920 381 VVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVvAMPDELLGERSCAFVVLRDP--------------PPSAAQLR 446
|
490 500 510
....*....|....*....|....*....|....*.
gi 1246793773 1007 RALCER-LPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05920 447 RFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
3547-4010 |
1.77e-28 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 121.30 E-value: 1.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3547 YATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVclsvsqral 3626
Cdd:cd05912 4 FAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDV--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3627 avelpgtalclddpftraQLDAVepgelpevpteapAYLIYTSGSTGTPKGVVVTHRNveRLFTAATQTGRFSFDEHDVW 3706
Cdd:cd05912 75 ------------------KLDDI-------------ATIMYTSGTTGKPKGVQQTFGN--HWWSAIGSALNLGLTEDDNW 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3707 ----SLFHSHAFDFAVWELwgawLYGGRAVLVPEAvcrQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELAlNVRA 3782
Cdd:cd05912 122 lcalPLFHISGLSILMRSV----IYGMTVYLVDKF---DAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPN-NLRC 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3783 VVFGGEALEPSRLQPWRER-YPqaeLVNMYGITETTVHVSfhRLSDEDLQSPTSRIGSALPDLAVHVLDAAGQPvplGVV 3861
Cdd:cd05912 194 ILLGGGPAPKPLLEQCKEKgIP---VYQSYGMTETCSQIV--TLSPEDALNKIGSAGKPLFPVELKIEDDGQPP---YEV 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3862 GELVVEGDGVAQGYWQRPELTAERFveRGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQV 3941
Cdd:cd05912 266 GEILLKGPNVTKGYLNRPDATEESF--ENG--WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAI 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 3942 SDAAVTveGQGEGAWLM---AYAVAAdgAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:cd05912 342 KEAGVV--GIPDDKWGQvpvAFVVSE--RPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
2062-2522 |
1.96e-28 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 121.77 E-value: 1.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2062 WTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQH-PDARQIAvLDDSGARIVIGW 2140
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFgPEALEYR-LSNSGASALVTD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2141 GAapawvpasvrwldaesvldvvsayeepprvdvdaDTPAYLIYTSGSTGTPKGVVVSQgnlaNYVAGVLPVLDLGEDas 2220
Cdd:cd05971 86 GS----------------------------------DDPALIIYTSGTTGPPKGALHAH----RVLLGHLPGVQFPFN-- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2221 latLSTVAADLGFT--------ALFGALLS---------GRRVRLLPAELAFDAQALAAHLQA-HPVDCLKIVPSHLAGL 2282
Cdd:cd05971 126 ---LFPRDGDLYWTpadwawigGLLDVLLPslyfgvpvlAHRMTKFDPKAALDLMSRYGVTTAfLPPTALKMMRQQGEQL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2283 LAaaggtAVLPRECLVTGGEALTGALVQQVRAlAPTLRIVNHYGPTETTVGILTCTVpeEWPVEQGvPVGHPLAGNEAWV 2362
Cdd:cd05971 203 KH-----AQVKLRAIATGGESLGEELLGWARE-QFGVEVNEFYGQTECNLVIGNCSA--LFPIKPG-SMGKPIPGHRVAI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2363 LDRFGLPAPVGVAGE--LYLGGGNLSLGYWQRAEQTAERFVAHPLapdrllyRSGDLARLDGEGRIVYLGRGDHQVKIRG 2440
Cdd:cd05971 274 VDDNGTPLPPGEVGEiaVELPDPVAFLGYWNNPSATEKKMAGDWL-------LTGDLGRKDSDGYFWYVGRDDDVITSSG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2441 YRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI---QGslEGVAEALAQRLPEYLC--------PSRWRAVESM 2509
Cdd:cd05971 347 YRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVvlnPG--ETPSDALAREIQELVKtrlaaheyPREIEFVNEL 424
|
490
....*....|...
gi 1246793773 2510 PRLGNGKIDRQAL 2522
Cdd:cd05971 425 PRTATGKIRRREL 437
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
3661-4006 |
2.05e-28 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 119.33 E-value: 2.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3661 APAYLIYTSGSTGTPKGVVVTHRNverLFTAATQTGRF-SFDEHDVW----SLFHSHAFDFAVwelwGAWLYGGRAVLVP 3735
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQA---LLAQALVLAVLqAIDEGTVFlnsgPLFHIGTLMFTL----ATFHAGGTNVFVR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3736 EAVcrqPDAFLDLLAEYGVTvlnqtpSAFYALQSQAMRREL-------ALNVRAVVF--GGEALEPSRLQPWReRYPQAe 3806
Cdd:cd17636 74 RVD---AEEVLELIEAERCT------HAFLLPPTIDQIVELnadglydLSSLRSSPAapEWNDMATVDTSPWG-RKPGG- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3807 lvnmYGITETTVHVSFHRLSDEDLqsptSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERF 3886
Cdd:cd17636 143 ----YGQTEVMGLATFAALGGGAI----GGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3887 veRGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEGAW---LMAYAVA 3963
Cdd:cd17636 215 --RGG--WHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVI--GVPDPRWaqsVKAIVVL 288
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1246793773 3964 ADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLD 4006
Cdd:cd17636 289 KPGASVTEAELIEHCRARIASYKKPKSVEFADALPRTAGGADD 331
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
3660-4007 |
3.15e-28 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 118.90 E-value: 3.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3660 EAPAYLIYTSGSTGTPKGVVVTHRnverLFTAAT---QTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPE 3736
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANK----TFFAVPdilQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3737 AVcrQPDAFLDLLAEYGVTVLNQTPSAFYALQSqaMRRELALNV---RAVVFGGEALEPSRLQPWrERYPQAELVNMYGI 3813
Cdd:cd17635 77 NT--TYKSLFKILTTNAVTTTCLVPTLLSKLVS--ELKSANATVpslRLIGYGGSRAIAADVRFI-EATGLTNTAQVYGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3814 TETT--VHVSFHRLSDEdlqspTSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVErgg 3891
Cdd:cd17635 152 SETGtaLCLPTDDDSIE-----INAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLID--- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3892 qRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGE-GAWLMAYAVA-ADGAEP 3969
Cdd:cd17635 224 -GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEfGELVGLAVVAsAELDEN 302
|
330 340 350
....*....|....*....|....*....|....*...
gi 1246793773 3970 DPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDR 4007
Cdd:cd17635 303 AIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
1599-1977 |
3.44e-28 |
|
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380456 [Multi-domain] Cd Length: 419 Bit Score: 120.94 E-value: 3.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1599 PLTPLQRGVLL-ESLRGDGaDPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGLsVPHQIVLADAAAPWQT 1677
Cdd:cd19533 3 PLTSAQRGVWFaEQLDPEG-SIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEG-EPYQWIDPYTPVPIRH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1678 LDWSAldDAAQDAQLQRWLADDAAQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQG 1757
Cdd:cd19533 81 IDLSG--DPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1758 ATLRLPPAPGF----QAYLDWRERQDLARQRGWWRERLSGyagtaALPAPVAAAHHPVQREECERR---LSAHDSERLRA 1830
Cdd:cd19533 159 RPAPPAPFGSFldlvEEEQAYRQSERFERDRAFWTEQFED-----LPEPVSLARRAPGRSLAFLRRtaeLPPELTRTLLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1831 FCRERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRppelAGVES--MVGVFINTLPLRLRIDAGQPALDLLSALRS 1908
Cdd:cd19533 234 AAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGR----LGAAArqTPGMVANTLPLRLTVDPQQTFAELVAQVSR 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 1909 QSLEVAENEAVGLGEILADSGL--DADRLFASLLVVENFpamaPAQLPFALrvRETRAANHYA-----LTLRVSER 1977
Cdd:cd19533 310 ELRSLLRHQRYRYEDLRRDLGLtgELHPLFGPTVNYMPF----DYGLDFGG--VVGLTHNLSSgptndLSIFVYDR 379
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
3535-4005 |
3.99e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 121.93 E-value: 3.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3535 RIAVSAEDGE-LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILE 3613
Cdd:PRK08276 1 PAVIMAPSGEvVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3614 DSGVC-LSVSQRALAVELPGTALCLDDPFTRAQLDAVEPGELP------EVPTEAPA------YLIYTSGSTGTPKGVV- 3679
Cdd:PRK08276 81 DSGAKvLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRSyeealaAQPDTPIAdetagaDMLYSSGTTGRPKGIKr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3680 -VTHRNVER---LFTAATQTGRFSFDEHDVWS---LFHSHAFDFAVWELWGawlyGGRAVLVPEAvcrQPDAFLDLLAEY 3752
Cdd:PRK08276 161 pLPGLDPDEapgMMLALLGFGMYGGPDSVYLSpapLYHTAPLRFGMSALAL----GGTVVVMEKF---DAEEALALIERY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3753 GVTVLNQTPSAFyalqsqamRRELAL--NVRA--------VVFGGEALEP----SRLQPW-----RERYPQAElvnMYGI 3813
Cdd:PRK08276 234 RVTHSQLVPTMF--------VRMLKLpeEVRArydvsslrVAIHAAAPCPvevkRAMIDWwgpiiHEYYASSE---GGGV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3814 TETTvhvsfhrlSDEDLQSPTSrIGSALpDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqr 3893
Cdd:PRK08276 303 TVIT--------SEDWLAHPGS-VGKAV-LGEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHG--- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3894 FYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDP- 3971
Cdd:PRK08276 370 WVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFgVPDEEMGERVKAVVQPADGADAGDa 449
|
490 500 510
....*....|....*....|....*....|....*.
gi 1246793773 3972 --QSLREALRALLPDYMLPRLIQLLPALPLTANGKL 4005
Cdd:PRK08276 450 laAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
3082-3422 |
4.83e-28 |
|
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380461 [Multi-domain] Cd Length: 432 Bit Score: 120.45 E-value: 4.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3082 PLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGF-AVQGLPSPRQLPHRQVSLPLAE 3160
Cdd:cd19538 3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFpEEDGVPYQLILEEDEATPKLEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3161 QDWSglepaqaRSRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAALRES 3240
Cdd:cd19538 83 KEVD-------EEELESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3241 RTPQLPAAP-PFRDYLHWLR-------GQDEAAAR--AFWREQLTGLePAALPEATE---PAE-GYASSTRRFDLAAA-- 3304
Cdd:cd19538 156 EAPELAPLPvQYADYALWQQellgdesDPDSLIARqlAYWKKQLAGL-PDEIELPTDyprPAEsSYEGGTLTFEIDSElh 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3305 ---SAWAQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRppELAGVERMLGVFINSVPLRVTPAGEATPAPWLQA 3381
Cdd:cd19538 235 qqlLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGR--NDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLER 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3382 LQQRNLDLRTHGYLPLAQIqragaADAVSP---------FDVLLVFENLP 3422
Cdd:cd19538 313 VKETNLEAYEHQDIPFERL-----VEALNPtrsrsrhplFQIMLALQNTP 357
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
2179-2526 |
5.06e-28 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 118.20 E-value: 5.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2179 PAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLG-EDASLATL--STVAadlGFTALFGALLSGRRVRLLPAELAF 2255
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGgGDSWLLSLplYHVG---GLAILVRSLLAGAELVLLERNQAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2256 daqalAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPR-ECLVTGGEALTGALVQqvRALAPTLRIVNHYGPTETTVGI 2334
Cdd:cd17630 79 -----AEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSlRAVLLGGAPIPPELLE--RAADRGIPLYTTYGMTETASQV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2335 LTCTVPEEwpvEQGVpVGHPLAGNEAWVLDRfglpapvgvaGELYLGGGNLSLGYWqraeqtaeRFVAHPLAPDRLLYRS 2414
Cdd:cd17630 152 ATKRPDGF---GRGG-VGVLLPGRELRIVED----------GEIWVGGASLAMGYL--------RGQLVPEFNEDGWFTT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2415 GDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALP----GANGVLQLGACIQGSLEGVAEAL 2490
Cdd:cd17630 210 KDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPdeelGQRPVAVIVGRGPADPAELRAWL 289
|
330 340 350
....*....|....*....|....*....|....*.
gi 1246793773 2491 AQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLL 2526
Cdd:cd17630 290 KDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
2063-2522 |
7.40e-28 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 120.32 E-value: 7.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2063 TYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPL----DPQHPDARqiavLDDSGARIVI 2138
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLftafGPKAIEHR----LRTSGARLVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2139 gwgaapawvpasvrwLDAESvldvvsayeeppRVDVDADtPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGED 2218
Cdd:cd05973 78 ---------------TDAAN------------RHKLDSD-PFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2219 ASLATlstvAADLG-----FTALFGALLSGRRVRLLpaELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLP 2293
Cdd:cd05973 130 DSFWN----AADPGwayglYYAITGPLALGHPTILL--EGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2294 RECL---VTGGEALTGALVQQVRALAPTLrIVNHYGPTEttVGILTCTV-PEEWPVEQGvPVGHPLAGNEAWVLDRFGLP 2369
Cdd:cd05973 204 KGRLrrvSSAGEPLTPEVIRWFDAALGVP-IHDHYGQTE--LGMVLANHhALEHPVHAG-SAGRAMPGWRVAVLDDDGDE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2370 APVGVAGELYLGGGNLSL----GYWQRAEQtaerfvahplAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVEL 2445
Cdd:cd05973 280 LGPGEPGRLAIDIANSPLmwfrGYQLPDTP----------AIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2446 GEVEQVLAQLPGVEVAAVLALPGA--NGVLQLGACIQGSLEG---VAEALA----QRLPEYLCPSRWRAVESMPRLGNGK 2516
Cdd:cd05973 350 FDVESALIEHPAVAEAAVIGVPDPerTEVVKAFVVLRGGHEGtpaLADELQlhvkKRLSAHAYPRTIHFVDELPKTPSGK 429
|
....*.
gi 1246793773 2517 IDRQAL 2522
Cdd:cd05973 430 IQRFLL 435
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
88-507 |
7.91e-28 |
|
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380459 [Multi-domain] Cd Length: 419 Bit Score: 119.86 E-value: 7.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 88 APLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQGEDS------VAAGGGAAVES 161
Cdd:cd19536 2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLgqpvqvVHRQAQVPVTE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 162 ADLRG--RGQDEIDALVEGFRLRPFELQRQRPLRMQLLRLDGQGdgpvrHWLQVV-VHHIACDGVSLGLLTQDLSRAYRv 238
Cdd:cd19536 82 LDLTPleEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERE-----RFLLVIsDHHSILDGWSLYLLVKEILAVYN- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 239 ecGLAA----EPAPPLPcqYGDYARWQRDTLDRlDASLRHHVEALSGAPHLhelPLDHERPAVLGQSGAKLRLAFPPGLS 314
Cdd:cd19536 156 --QLLEykplSLPPAQP--YRDFVAHERASIQQ-AASERYWREYLAGATLA---TLPALSEAVGGGPEQDSELLVSVPLP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 315 ERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRP--ELDSLVGLFVNTVVLRTQLHDDPdFASLVAR 392
Cdd:cd19536 228 VRSRSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEEttGAERLLGLFLNTLPLRVTLSEET-VEDLLKR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 393 CRDHQLAALEHQALPLErvietlQVERSSRHAPLFQLMFALRH-DADLALDLHG---VQAHALTLPEDVAKHELTLEVLV 468
Cdd:cd19536 307 AQEQELESLSHEQVPLA------DIQRCSEGEPLFDSIVNFRHfDLDFGLPEWGsdeGMRRGLLFSEFKSNYDVNLSVLP 380
|
410 420 430
....*....|....*....|....*....|....*....
gi 1246793773 469 GAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENP 507
Cdd:cd19536 381 KQDRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
3523-4013 |
1.84e-27 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 120.63 E-value: 1.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3523 SRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPH 3602
Cdd:PRK13382 47 SGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3603 APAARRGFILEDSGV--------CLSVSQRALAvELPGTALCLD-----DPFTRAQLDAVEPGELPEVPTEAPAYLIYTS 3669
Cdd:PRK13382 127 FAGPALAEVVTREGVdtviydeeFSATVDRALA-DCPQATRIVAwtdedHDLTVEVLIAAHAGQRPEPTGRKGRVILLTS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3670 GSTGTPKGVvvTHRNVERLFTAATQTGRFSFDEHD----VWSLFHShafdfavwelWGAWLYGGRAVLVPEAVCRQ---P 3742
Cdd:PRK13382 206 GTTGTPKGA--RRSGPGGIGTLKAILDRTPWRAEEptviVAPMFHA----------WGFSQLVLAASLACTIVTRRrfdP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3743 DAFLDLLAEYGVTVLNQTPSAF---YALQSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAeLVNMYGITETTVH 3819
Cdd:PRK13382 274 EATLDLIDRHRATGLAVVPVMFdriMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDV-IYNNYNATEAGMI 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3820 VSfhrLSDEDLQSPTSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYwqrPELTAERFVERggqrFYRSGD 3899
Cdd:PRK13382 353 AT---ATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY---TSGSTKDFHDG----FMASGD 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3900 LGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSLREAL 3978
Cdd:PRK13382 423 VGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIgVDDEQYGQRLAAFVVLKPGASATPETLKQHV 502
|
490 500 510
....*....|....*....|....*....|....*
gi 1246793773 3979 RALLPDYMLPRLIQLLPALPLTANGKLDRKALPKP 4013
Cdd:PRK13382 503 RDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
3552-4010 |
1.93e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 120.56 E-value: 1.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3552 RRSSQLATLLIRQGAGpgqRVGLCLPRGCDLLVALLAILKTGAAYVPVDP--HAPAARRGFILEDSGVCLSVS-QRALAV 3628
Cdd:PRK07867 40 ARAAALRARLDPTRPP---HVGVLLDNTPEFSLLLGAAALSGIVPVGLNPtrRGAALARDIAHADCQLVLTESaHAELLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3629 ELPGTALCLD-DPFTRAQLDAVEPGELPEVPTEAPA---YLIYTSGSTGTPKGVVVTHRNVErlFTAATQTGRFSFDEHD 3704
Cdd:PRK07867 117 GLDPGVRVINvDSPAWADELAAHRDAEPPFRVADPDdlfMLIFTSGTSGDPKAVRCTHRKVA--SAGVMLAQRFGLGPDD 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3705 V----WSLFHSHafdfAVWELWGAWLYGGRAVlvpeAVCRQPDA--FLDLLAEYGVTVLNQTPSAFYALQSQAMRRELAL 3778
Cdd:PRK07867 195 VcyvsMPLFHSN----AVMAGWAVALAAGASI----ALRRKFSAsgFLPDVRRYGATYANYVGKPLSYVLATPERPDDAD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3779 NVRAVVFGGEAlEPSRLQPWRERYpQAELVNMYGITETTvhVSFHRLSDedlqSPTSRIGSALPDLAvhVLDAA-GQPVP 3857
Cdd:PRK07867 267 NPLRIVYGNEG-APGDIARFARRF-GCVVVDGFGSTEGG--VAITRTPD----TPPGALGPLPPGVA--IVDPDtGTECP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3858 LGV------------VGELV-VEGDGVAQGYWQRPELTAERFveRGGQrfYRSGDLGRYRADGSLEYRGRGDDQVKLRGY 3924
Cdd:PRK07867 337 PAEdadgrllnadeaIGELVnTAGPGGFEGYYNDPEADAERM--RGGV--YWSGDLAYRDADGYAYFAGRLGDWMRVDGE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3925 RIEPGEIAAKIASLPQVSDAAV-TVEGQGEGAWLMAYAVAADGAEPDPQSLREALRAL--LPDYMLPRLIQLLPALPLTA 4001
Cdd:PRK07867 413 NLGTAPIERILLRYPDATEVAVyAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLAAQpdLGPKQWPSYVRVCAELPRTA 492
|
....*....
gi 1246793773 4002 NGKLDRKAL 4010
Cdd:PRK07867 493 TFKVLKRQL 501
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
3547-3935 |
2.47e-27 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 119.00 E-value: 2.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3547 YATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGvclsvsqral 3626
Cdd:cd17640 8 YKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSE---------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3627 avelpGTALCLDDpftraqldavEPGELpevpteapAYLIYTSGSTGTPKGVVVTHRNverlftaatqtgrFSFDEHDVW 3706
Cdd:cd17640 78 -----SVALVVEN----------DSDDL--------ATIIYTSGTTGNPKGVMLTHAN-------------LLHQIRSLS 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3707 SLFHSHAFD--FAVWELWGAW---------LYGGravlvpEAVCRQPDAFLDLLAEYGVTVLNQTPSAFYAL-------- 3767
Cdd:cd17640 122 DIVPPQPGDrfLSILPIWHSYersaeyfifACGC------SQAYTSIRTLKDDLKRVKPHYIVSVPRLWESLysgiqkqv 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3768 -QSQAMRRELAL------NVRAVVFGGEALEPSRlqpwrERYPQA---ELVNMYGITETTVHVSFHRLSDEDLQSptsrI 3837
Cdd:cd17640 196 sKSSPIKQFLFLfflsggIFKFGISGGGALPPHV-----DTFFEAigiEVLNGYGLTETSPVVSARRLKCNVRGS----V 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3838 GSALPDLAVHVLDA-AGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGD 3916
Cdd:cd17640 267 GRPLPGTEIKIVDPeGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDG---WFNTGDLGWLTCGGELVLTGRAK 343
|
410 420
....*....|....*....|
gi 1246793773 3917 DQVKLR-GYRIEPGEIAAKI 3935
Cdd:cd17640 344 DTIVLSnGENVEPQPIEEAL 363
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
3525-4010 |
3.71e-27 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 119.98 E-value: 3.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQ-GAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHA 3603
Cdd:PRK08751 31 FATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3604 PAARRGFILEDSGV---------CLSVsQRALA------VELPGTALCLDdpFTRAQL---------------------- 3646
Cdd:PRK08751 111 TPRELKHQLIDSGAsvlvvidnfGTTV-QQVIAdtpvkqVITTGLGDMLG--FPKAALvnfvvkyvkklvpeyringair 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3647 --DAVEPGELPEVPT-----EAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQ----TGRFSFDEHDVWS---LFHsh 3712
Cdd:PRK08751 188 frEALALGRKHSMPTlqiepDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQwlagTGKLEEGCEVVITalpLYH-- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3713 afdfaVWELWGAWL----YGGRAVLVPEAvcRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALN-VRAVVFGG 3787
Cdd:PRK08751 266 -----IFALTANGLvfmkIGGCNHLISNP--RDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSsLKMTLGGG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3788 EALEPSRLQPWReRYPQAELVNMYGITETTVHVSFHRLsdeDLQSPTSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVE 3867
Cdd:PRK08751 339 MAVQRSVAERWK-QVTGLTLVEAYGLTETSPAACINPL---TLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIK 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3868 GDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSD-AAV 3946
Cdd:PRK08751 415 GPQVMKGYWKRPEETAKVMDADG---WLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEvAAV 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 3947 TVEGQGEGAWLMAYAVAADGAePDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK08751 492 GVPDEKSGEIVKVVIVKKDPA-LTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
1599-1949 |
4.20e-27 |
|
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380462 [Multi-domain] Cd Length: 427 Bit Score: 117.87 E-value: 4.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1599 PLTPLQRGVLLESLRGDGADPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGLSVPHQIVLADAAAPWQTL 1678
Cdd:cd19539 3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGPAPLEVR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1679 DWSAlDDAAQDAQLQRWLADDAAQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGA 1758
Cdd:cd19539 83 DLSD-PDSDRERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1759 TLRLPPAPG-FQAYLDWRERQD----LARQRGWWRERLSGYAGTAALPAPVAAAHHPVQREECERRLSAHDSERLRAFCR 1833
Cdd:cd19539 162 AAPLPELRQqYKEYAAWQREALaaprAAELLDFWRRRLRGAEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELAK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1834 ERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPPELAgvESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEV 1913
Cdd:cd19539 242 RARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRF--ESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDA 319
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1246793773 1914 AENEAVGLGEILADSGLDADR----LFASLLVVENFPAMA 1949
Cdd:cd19539 320 QRHQELPFQQLVAELPVDRDAgrhpLVQIVFQVTNAPAGE 359
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
3527-4010 |
5.89e-27 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 118.63 E-value: 5.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3527 EIARRYPARIAVSAEDG-----ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDP 3601
Cdd:PRK08008 15 DLADVYGHKTALIFESSggvvrRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3602 HAPAARRGFILEDSGVCLSVSQ-------RALAVE--LPGTALCLDDP----------FTraQLDAVEPGELPEVP---T 3659
Cdd:PRK08008 95 RLLREESAWILQNSQASLLVTSaqfypmyRQIQQEdaTPLRHICLTRValpaddgvssFT--QLKAQQPATLCYAPplsT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3660 EAPAYLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEHDVW----SLFHShafDFAVWELWGAWLYGGRAVLVP 3735
Cdd:PRK08008 173 DDTAEILFTSGTTSRPKGVVITHYNL--RFAGYYSAWQCALRDDDVYltvmPAFHI---DCQCTAAMAAFSAGATFVLLE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3736 EAVCRqpdAFLDLLAEYGVTVLNQTPSAFYALQSQ-AMRRELALNVRAVVFgGEALEPSRLQPWRERYpQAELVNMYGIT 3814
Cdd:PRK08008 248 KYSAR---AFWGQVCKYRATITECIPMMIRTLMVQpPSANDRQHCLREVMF-YLNLSDQEKDAFEERF-GVRLLTSYGMT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3815 ETTVHVSFHRLSDEDlQSPTsrIGSALPDLAVHVLDAAGQPVPLGVVGELVVE---GDGVAQGYWQRPELTAERFVERGg 3891
Cdd:PRK08008 323 ETIVGIIGDRPGDKR-RWPS--IGRPGFCYEAEIRDDHNRPLPAGEIGEICIKgvpGKTIFKEYYLDPKATAKVLEADG- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3892 qrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPD 3970
Cdd:PRK08008 399 --WLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVgIKDSIRDEAIKAFVVLNEGETLS 476
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1246793773 3971 PQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK08008 477 EEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
3555-4015 |
6.10e-27 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 118.72 E-value: 6.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3555 SQLATLLIRQGAG--PGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVCLSVSQRALAVELPG 3632
Cdd:cd05928 51 SRKAANVLSGACGlqRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3633 TALclDDPFTRAQL---DAVEPGELP---------------EVPTEAPAYLIYTSGSTGTPKGVVVTHRNverLFTAATQ 3694
Cdd:cd05928 131 VAS--ECPSLKTKLlvsEKSRDGWLNfkellneastehhcvETGSQEPMAIYFTSGTTGSPKMAEHSHSS---LGLGLKV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3695 TGRFSFD--EHDV-WSLFHSHAFDFAVWELWGAWLYGGrAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQA 3771
Cdd:cd05928 206 NGRYWLDltASDImWNTSDTGWIKSAWSSLFEPWIQGA-CVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQD 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3772 MRRELALNVRAVVFGGEALEPSRLQPWRERyPQAELVNMYGITETTVHVSfhrlSDEDLQSPTSRIGSALPDLAVHVLDA 3851
Cdd:cd05928 285 LSSYKFPSLQHCVTGGEPLNPEVLEKWKAQ-TGLDIYEGYGQTETGLICA----NFKGMKIKPGSMGKASPPYDVQIIDD 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3852 AGQPVPLGVVGELVVEGD-----GVAQGYWQRPELTAErfVERGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRI 3926
Cdd:cd05928 360 NGNVLPPGTEGDIGIRVKpirpfGLFSGYVDNPEKTAA--TIRGD--FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRI 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3927 EPGEIAAKIASLPQVSDAAV-TVEGQGEGAWLMAYAV-AADGAEPDPQSL----REALRALLPDYMLPRLIQLLPALPLT 4000
Cdd:cd05928 436 GPFEVESALIEHPAVVESAVvSSPDPIRGEVVKAFVVlAPQFLSHDPEQLtkelQQHVKSVTAPYKYPRKVEFVQELPKT 515
|
490
....*....|....*
gi 1246793773 4001 ANGKLDRKALPKPET 4015
Cdd:cd05928 516 VTGKIQRNELRDKEW 530
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
3525-4004 |
8.59e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 118.76 E-value: 8.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPARIAVSAEDGEL--DYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPH 3602
Cdd:PRK08315 22 LDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3603 APAARRGFILEDSGVCLSVSQRA------------LAVEL----PGTALCLDDPFTR--------------------AQL 3646
Cdd:PRK08315 102 YRLSELEYALNQSGCKALIAADGfkdsdyvamlyeLAPELatcePGQLQSARLPELRrviflgdekhpgmlnfdellALG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3647 DAVEPGELPEV-----PTEApaylI---YTSGSTGTPKGVVVTHRNV--ERLFTAATQtgRFSfdEHD-----VwSLFH- 3710
Cdd:PRK08315 182 RAVDDAELAARqatldPDDP----IniqYTSGTTGFPKGATLTHRNIlnNGYFIGEAM--KLT--EEDrlcipV-PLYHc 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3711 -----------SH---------AFDfavwelwgawlyggrAVLVPEAV----CRqpdafldllAEYGVtvlnqtPSAFYA 3766
Cdd:PRK08315 253 fgmvlgnlacvTHgatmvypgeGFD---------------PLATLAAVeeerCT---------ALYGV------PTMFIA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3767 LQSQAMRRELALN-VRAVVFGG-----EALEpsRLQpwrerypqaELVNM------YGITETTvHVSFHRLSDEDLQSPT 3834
Cdd:PRK08315 303 ELDHPDFARFDLSsLRTGIMAGspcpiEVMK--RVI---------DKMHMsevtiaYGMTETS-PVSTQTRTDDPLEKRV 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3835 SRIGSALPDLAVHVLDAA-GQPVPLGVVGELVVEGDGVAQGYWQRPELTAERfVERGGqrFYRSGDLGRYRADGSLEYRG 3913
Cdd:PRK08315 371 TTVGRALPHLEVKIVDPEtGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEA-IDADG--WMHTGDLAVMDEEGYVNIVG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3914 RGDDQVkLR-GYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLI 3991
Cdd:PRK08315 448 RIKDMI-IRgGENIYPREIEEFLYTHPKIQDVQVVgVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYI 526
|
570
....*....|...
gi 1246793773 3992 QLLPALPLTANGK 4004
Cdd:PRK08315 527 RFVDEFPMTVTGK 539
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
2061-2522 |
8.80e-27 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 116.81 E-value: 8.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2061 SWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIgw 2140
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2141 gaapawvpasvrwldAESVLDvvsayeepprvDVdadtpAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDL-GEDA 2219
Cdd:cd05935 79 ---------------VGSELD-----------DL-----ALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLtPSDV 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2220 SLATLST--VAadlGFTALFGALLSGRRVRLLPA----ELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLp 2293
Cdd:cd05935 128 ILACLPLfhVT---GFVGSLNTAVYVGGTYVLMArwdrETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKV- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2294 recLVTGGEALTGALVQQVRALApTLRIVNHYGPTETTVGilTCTVPEEWPVEQGVpvGHPLAGNEAWVLD-RFGLPAPV 2372
Cdd:cd05935 204 ---LTGGGAPMPPAVAEKLLKLT-GLRFVEGYGLTETMSQ--THTNPPLRPKLQCL--GIP*FGVDARVIDiETGRELPP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2373 GVAGELYLGGGNLSLGYWQRAEQTAERFVAhplAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVL 2452
Cdd:cd05935 276 NEVGEIVVRGPQIFKGYWNRPEETEESFIE---IKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKL 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 2453 AQLPGVEVAAVLALPG--------ANGVLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:cd05935 353 YKHPAI*EVCVISVPDervgeevkAFIVLRPEYRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
3547-4010 |
8.90e-27 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 118.84 E-value: 8.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3547 YATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPV----DPHAPAARrgfiLEDSGVCLSVS 3622
Cdd:PRK04319 76 YKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLfeafMEEAVRDR----LEDSEAKVLIT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3623 QRAL-----AVELPG--TALCLDDP---------FTRAQLDAVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVe 3686
Cdd:PRK04319 152 TPALlerkpADDLPSlkHVLLVGEDveegpgtldFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAM- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3687 rlfTAATQTGRFSFDEH--DV--------WSLFHSHAfdfavweLWGAWLYGgrAVLVPEAVCRQPDAFLDLLAEYGVTV 3756
Cdd:PRK04319 231 ---LQHYQTGKYVLDLHedDVywctadpgWVTGTSYG-------IFAPWLNG--ATNVIDGGRFSPERWYRILEDYKVTV 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3757 LNQTPSAFYALqsqaMRR--ELA-----------------LNVRAVVFGGEALEpsrlQPWRERYPQaelvnmygiTETT 3817
Cdd:PRK04319 299 WYTAPTAIRML----MGAgdDLVkkydlsslrhilsvgepLNPEVVRWGMKVFG----LPIHDNWWM---------TETG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3818 VHV-----SFhrlsdeDLQsPTSrIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGD--GVAQGYWQRPELTAERFVerG 3890
Cdd:PRK04319 362 GIMianypAM------DIK-PGS-MGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGwpSMMRGIWNNPEKYESYFA--G 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3891 GqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGE---GAWLMAYAVAADGA 3967
Cdd:PRK04319 432 D--WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVI--GKPDpvrGEIIKAFVALRPGY 507
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1246793773 3968 EPDpQSLREALRAL----LPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK04319 508 EPS-EELKEEIRGFvkkgLGAHAAPREIEFKDKLPKTRSGKIMRRVL 553
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
2063-2517 |
1.17e-26 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 116.71 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2063 TYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIgwga 2142
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2143 apawVPASVRWLDaesvldvvsaYEEPPrvdvdaDTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLA 2222
Cdd:cd05903 79 ----VPERFRQFD----------PAAMP------DAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2223 TLSTVAADLGFT-ALFGALLSGRRVRLLpaelafdaqalaahLQAHPVDCLKIVPSHLA-------------GLLAAAGG 2288
Cdd:cd05903 139 VASPMAHQTGFVyGFTLPLLLGAPVVLQ--------------DIWDPDKALALMREHGVtfmmgatpfltdlLNAVEEAG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2289 TAVLPRECLVTGGEALTGALVQQVRALAPTLrIVNHYGPTETTvGILTCTVPEEwPVEQGVPVGHPLAGNEAWVLDRFGL 2368
Cdd:cd05903 205 EPLSRLRTFVCGGATVPRSLARRAAELLGAK-VCSAYGSTECP-GAVTSITPAP-EDRRLYTDGRPLPGVEIKVVDDTGA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2369 PAPVGVAGELYLGGGNLSLGYWQRAEQTAErfvahplAPDRLLYRSGDLARLDGEGRIVYLGRgDHQVKIR-GYRVELGE 2447
Cdd:cd05903 282 TLAPGVEGELLSRGPSVFLGYLDRPDLTAD-------AAPEGWFRTGDLARLDEDGYLRITGR-SKDIIIRgGENIPVLE 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 2448 VEQVLAQLPGVEVAAVLALPG--------ANGVLQLGACIqgSLEGVAEAL-AQRLPEYLCPSRWRAVESMPRLGNGKI 2517
Cdd:cd05903 354 VEDLLLGHPGVIEAAVVALPDerlgeracAVVVTKSGALL--TFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
3520-4010 |
1.65e-26 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 118.00 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQ-GAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVP 3598
Cdd:PRK12492 25 SVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3599 VDPHAPAARRGFILEDSG----VCLSVSQRALAVELPGTALcldDPFTRAQLDAVEPGE--------LPEVPTEAPAY-- 3664
Cdd:PRK12492 105 TNPLYTAREMRHQFKDSGaralVYLNMFGKLVQEVLPDTGI---EYLIEAKMGDLLPAAkgwlvntvVDKVKKMVPAYhl 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3665 ------------------------------LIYTSGSTGTPKGVVVTHRN-VERLFTAATQTGRFSFDEHDVWS------ 3707
Cdd:PRK12492 182 pqavpfkqalrqgrglslkpvpvglddiavLQYTGGTTGLAKGAMLTHGNlVANMLQVRACLSQLGPDGQPLMKegqevm 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3708 -----LFHSHAFDFAVWELWgawLYGGRAVLVPEAvcRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELAL-NVR 3781
Cdd:PRK12492 262 iaplpLYHIYAFTANCMCMM---VSGNHNVLITNP--RDIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKDLDFsALK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3782 AVVFGGEALEPSRLQPWrERYPQAELVNMYGITETTVHVSFHRLSDedlQSPTSRIGSALPDLAVHVLDAAGQPVPLGVV 3861
Cdd:PRK12492 337 LTNSGGTALVKATAERW-EQLTGCTIVEGYGLTETSPVASTNPYGE---LARLGTVGIPVPGTALKVIDDDGNELPLGER 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3862 GELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQV 3941
Cdd:PRK12492 413 GELCIKGPQVMKGYWQQPEATAEALDAEG---WFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKV 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3942 SD-AAVTVEGQGEGAWLMAYAVAADGAePDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK12492 490 ANcAAIGVPDERSGEAVKLFVVARDPG-LSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
3497-4008 |
2.23e-26 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 118.05 E-value: 2.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3497 LPLLPSQTRSAAWTSR-ERYACTGnLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLC 3575
Cdd:PRK08279 15 LPDLPGILRGLKRTALiTPDSKRS-LGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3576 LPRGCDLLVALLAILKTGAAYVPVDPHApaarRGFILEDsgvCLSVSQ-RALAVE--------------LPGTALCLDDP 3640
Cdd:PRK08279 94 MENRPEYLAAWLGLAKLGAVVALLNTQQ----RGAVLAH---SLNLVDaKHLIVGeelveafeearadlARPPRLWVAGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3641 FTRAQLDAVE-------------PGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVER------LFTAATQTGRFsfd 3701
Cdd:PRK08279 167 DTLDDPEGYEdlaaaaagapttnPASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKamggfgGLLRLTPDDVL--- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3702 eHDVWSLFHSHAFDFAvwelWGAWLYGGRAVlvpeAVCRQPDA--FLDLLAEYGVTV-----------LNQTPSAfyalq 3768
Cdd:PRK08279 244 -YCCLPLYHNTGGTVA----WSSVLAAGATL----ALRRKFSAsrFWDDVRRYRATAfqyigelcrylLNQPPKP----- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3769 sqamrRELALNVRAVVfgGEALEPSRLQPWRERYPQAELVNMYGITETTVHvsfhrLSDEDlqsptSRIGSA--LPDLAV 3846
Cdd:PRK08279 310 -----TDRDHRLRLMI--GNGLRPDIWDEFQQRFGIPRILEFYAASEGNVG-----FINVF-----NFDGTVgrVPLWLA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3847 H--------------VLDAAG--QPVPLGVVGELVVEGDGVAQ--GYWQrPELTAE---RFVERGGQRFYRSGDLGRYRA 3905
Cdd:PRK08279 373 HpyaivkydvdtgepVRDADGrcIKVKPGEVGLLIGRITDRGPfdGYTD-PEASEKkilRDVFKKGDAWFNTGDLMRDDG 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3906 DGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAV-TVEGQG-EGAWLMAYAVAADGAEPDPQSLREALRALLP 3983
Cdd:PRK08279 452 FGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVyGVEVPGtDGRAGMAAIVLADGAEFDLAALAAHLYERLP 531
|
570 580
....*....|....*....|....*
gi 1246793773 3984 DYMLPRLIQLLPALPLTANGKLdRK 4008
Cdd:PRK08279 532 AYAVPLFVRLVPELETTGTFKY-RK 555
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
675-1041 |
3.87e-26 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 112.42 E-value: 3.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 675 QLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVdtTLEQILAAWsrgacvvarpd 748
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLlslplyHVGGLAI--LVRSLLAGA----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 749 ELLEPQRFLAFLSERA---ITVTDLAPAYANELVRASVADDWRDlALRCLVVGGDVLPVALAQRwfelGLDRRCALINAY 825
Cdd:cd17630 68 ELVLLERNQALAEDLAppgVTHVSLVPTQLQRLLDSGQGPAALK-SLRAVLLGGAPIPPELLER----AADRGIPLYTTY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 826 GPTE--ATISshyhrVQAIDASRPVPLGQLLPGRiaavldaHGRIVPRgvcGELALGGIGLAEGYRgdaaasERRFAPLR 903
Cdd:cd17630 143 GMTEtaSQVA-----TKRPDGFGRGGVGVLLPGR-------ELRIVED---GEIWVGGASLAMGYL------RGQLVPEF 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 904 LPSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVGEGAA---QRLVAWVE 980
Cdd:cd17630 202 NEDG----WFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAF--VVGVPDEelgQRPVAVIV 275
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 981 CAGEdgfgqadlnqtdsdqTESERWHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd17630 276 GRGP---------------ADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
588-1043 |
4.68e-26 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 114.91 E-value: 4.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 588 VALCLPRGLDWYCLLLGAWRAGLSVIPLdtewpqarraevVAASGCDAVLtdaQGLAGFAPSVAIAVDELKldgagengs 667
Cdd:cd05969 28 VFVLSPRSPELYFSMLGIGKIGAVICPL------------FSAFGPEAIR---DRLENSEAKVLITTEELY--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 668 gENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLA-VDTTLEQILAAWSRGACVVAR 746
Cdd:cd05969 84 -ERTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYWCTADPGwVTGTVYGIWAPWLNGVTNVVY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 747 PDElLEPQRFLAFLSERAITVTDLAPAYANELVRASV--ADDWRDLALRCLVVGGDVL-PVALaqRWFELGLDRRcaLIN 823
Cdd:cd05969 163 EGR-FDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDelARKYDLSSLRFIHSVGEPLnPEAI--RWGMEVFGVP--IHD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 824 AYGPTE-ATISSHYHRVQAIdasRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELAL--GGIGLAEGYRGDAAASERRFa 900
Cdd:cd05969 238 TWWQTEtGSIMIANYPCMPI---KPGSMGKPLPGVKAAVVDENGNELPPGTKGILALkpGWPSMFRGIWNDEERYKNSF- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 901 plrlPSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVraAAAGVVGEG---AAQRLVA 977
Cdd:cd05969 314 ----IDG----WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAV--AEAGVIGKPdplRGEIIKA 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 978 WVecAGEDGFgqadlNQTDSDQTESERWHRalcERLPAYMVPTQFVALPRLPRNASGKIDRRALPA 1043
Cdd:cd05969 384 FI--SLKEGF-----EPSDELKEEIINFVR---QKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKA 439
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
3082-3457 |
5.18e-26 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380455 [Multi-domain] Cd Length: 421 Bit Score: 114.09 E-value: 5.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3082 PLAPLQEGLLF-HSLLNaeaDP--YINQTTVALHGALDREAFAAAWQQALERHPILRSGF--------AVQG-LPSPR-Q 3148
Cdd:cd19532 3 PMSFGQSRFWFlQQYLE---DPttFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFftdpedgePMQGvLASSPlR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3149 LPHRQVSlplaeqdwsglEPAQARSRLSELQAQQceagFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLD 3228
Cdd:cd19532 80 LEHVQIS-----------DEAEVEEEFERLKNHV----YDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3229 EVWRLYaalreSRTPQLPAAPPFRDYLHWLRGQDE----AAARAFWREQLTGLePAALP-------EATEPAEGYASSTR 3297
Cdd:cd19532 145 DLERAY-----NGQPLLPPPLQYLDFAARQRQDYEsgalDEDLAYWKSEFSTL-PEPLPllpfakvKSRPPLTRYDTHTA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3298 RFDLAAASA-----WAQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRPPElaGVERMLGVFINSVPLRVTPAGE 3372
Cdd:cd19532 219 ERRLDAALAarikeASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDE--DFMETIGFFLNLLPLRFRRDPS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3373 ATPApwlQALQQ-RNldlrthgylplaQIQRAGAADAVsPFDVLL----------------VFENLPTESREERS--GMR 3433
Cdd:cd19532 297 QTFA---DVLKEtRD------------KAYAALAHSRV-PFDVLLdelgvprsathsplfqVFINYRQGVAESRPfgDCE 360
|
410 420
....*....|....*....|....*
gi 1246793773 3434 IEELD-HRAHSNYPLMLTAIPDAGG 3457
Cdd:cd19532 361 LEGEEfEDARTPYDLSLDIIDNPDG 385
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
3544-4009 |
1.11e-25 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 115.99 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3544 ELDYATLDRRSSQLATLLiRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPV-DPHAP--AARRGFILEDS--GVC 3618
Cdd:PRK12476 68 ELTWTQLGVRLRAVGARL-QQVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAepTVV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3619 LSVSQRALAVE-----LPG----TALCLDD-------PFTRAQLDavepgelpevpTEAPAYLIYTSGSTGTPKGVVVTH 3682
Cdd:PRK12476 147 LTTTAAAEAVEgflrnLPRlrrpRVIAIDAipdsageSFVPVELD-----------TDDVSHLQYTSGSTRPPVGVEITH 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3683 RNV-ERLFTAATQTGRFSFDEHDV-W-SLFHshafDFAVWELWGAWLYGGRAVLV-PEAVCRQPDAFLDLLAEYGVT--V 3756
Cdd:PRK12476 216 RAVgTNLVQMILSIDLLDRNTHGVsWlPLYH----DMGLSMIGFPAVYGGHSTLMsPTAFVRRPQRWIKALSEGSRTgrV 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3757 LNQTPSAFYALQSQ----AMRRELALNVRAVVFGGEALEPSRLQPWRERY-----PQAELVNMYGITETTVHVS------ 3821
Cdd:PRK12476 292 VTAAPNFAYEWAAQrglpAEGDDIDLSNVVLIIGSEPVSIDAVTTFNKAFapyglPRTAFKPSYGIAEATLFVAtiapda 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3822 ------FHRlsDEDLQSPTSRIGSALPDLAVHVL--------------DAAGQPVPLGVVGELVVEGDGVAQGYWQRPEL 3881
Cdd:PRK12476 372 epsvvyLDR--EQLGAGRAVRVAADAPNAVAHVScgqvarsqwavivdPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEE 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3882 TAERFVERGGQR---------------FYRSGDLGRYRaDGSLEYRGRGDDQVKLRGYRIEPGEIAAKIA-SLPQVSD-- 3943
Cdd:PRK12476 450 TERTFGAKLQSRlaegshadgaaddgtWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIEATVAeASPMVRRgy 528
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 3944 -AAVTVEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPD-YMLP-RLIQLLPA--LPLTANGKLDRKA 4009
Cdd:PRK12476 529 vTAFTVPAEDNERLVIVAERAAGTSRADPAPAIDAIRAAVSRrHGLAvADVRLVPAgaIPRTTSGKLARRA 599
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
3664-4006 |
2.45e-25 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 110.93 E-value: 2.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3664 YLIYTSGSTGTPKGVVVTHRNVERLFTAATQTGRFSFDEHDVWS----------------LFHShafdfAVWELWGAWLY 3727
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQEDIFRMLMGGADFGTGEFTPSEDAHkaaaaaagtvmfpappLMHG-----TGSWTAFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3728 GGRAVLVPEAVCRqPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALNV---RAVVFGGEALEPSRLQPWRERYPQ 3804
Cdd:cd05924 82 GGQTVVLPDDRFD-PEEVWRTIEKHKVTSMTIVGDAMARPLIDALRDAGPYDLsslFAISSGGALLSPEVKQGLLELVPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3805 AELVNMYGITETTVHVSFHrlSDEDLQSPTSRIGSAlPDLAVhvLDAAGQPVPLGVVGELVVEGDG-VAQGYWQRPELTA 3883
Cdd:cd05924 161 ITLVDAFGSSETGFTGSGH--SAGSGPETGPFTRAN-PDTVV--LDDDGRVVPPGSGGVGWIARRGhIPLGYYGDEAKTA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3884 ERFVERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEGAW---LMAY 3960
Cdd:cd05924 236 ETFPEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVV--GRPDERWgqeVVAV 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1246793773 3961 AVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLD 4006
Cdd:cd05924 314 VQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
2050-2522 |
4.52e-25 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 112.60 E-value: 4.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2050 AQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQ-HPDARQIAV 2128
Cdd:cd05923 17 ACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRlKAAELAELI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2129 LDDSGARIVIGWGA--APAWVPASVRWLdAESVLD------VVSAYEEPPRVDVDAdtPAYLIYTSGSTGTPKGVVVSQG 2200
Cdd:cd05923 97 ERGEMTAAVIAVDAqvMDAIFQSGVRVL-ALSDLVglgepeSAGPLIEDPPREPEQ--PAFVFYTSGTTGLPKGAVIPQR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2201 NLANYVAGVLPVLDL--GEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAElaFDAQALAAHLQAHPVDCLKIVPSH 2278
Cdd:cd05923 174 AAESRVLFMSTQAGLrhGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEE--FDPADALKLIEQERVTSLFATPTH 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2279 --LAGLLAAAGGTAVLPRECLVTGGEALTGALVQQVRALAPTlRIVNHYGPTEttvgILTCTVPEEWPVEQGVPVGHPLA 2356
Cdd:cd05923 252 ldALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPG-EKVNIYGTTE----AMNSLYMRDARTGTEMRPGFFSE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2357 GNEAWVLDRFGLPAPVGVAGELY--LGGGNLSLGYWQRAEQTAERFVahplapDRLlYRSGDLARLDGEGRIVYLGRGDH 2434
Cdd:cd05923 327 VRIVRIGGSPDEALANGEEGELIvaAAADAAFTGYLNQPEATAKKLQ------DGW-YRTGDVGYVDPSGDVRILGRVDD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2435 QVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQGSLEGVAE------ALAQRLPEYLCPSRWRAVES 2508
Cdd:cd05923 400 MIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSAdeldqfCRASELADFKRPRRYFFLDE 479
|
490
....*....|....
gi 1246793773 2509 MPRLGNGKIDRQAL 2522
Cdd:cd05923 480 LPKNAMNKVLRRQL 493
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
3661-4007 |
6.97e-25 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 108.65 E-value: 6.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3661 APAYLIYTSGSTGTPKGVVVTHRNVERLFTAatQTGRFSFDEHDVW----SLFHSHAfdfavweLWGAW--LYGGRAVLV 3734
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVC--NEDLFNISGEDAIlapgPLSHSLF-------LYGAIsaLYLGGTFIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3735 PEAVcrQPDAFLDLLAEYGVTVLNQTPSAfyaLQSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGIT 3814
Cdd:cd17633 72 QRKF--NPKSWIRKINQYNATVIYLVPTM---LQALARTLEPESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3815 ETTvHVSFhrLSDEDLQSPTSrIGSALPDLAVHVLDAAGqpvplGVVGELVVEGDGVAQGYwqrpelTAERFVERGGqrF 3894
Cdd:cd17633 147 ELS-FITY--NFNQESRPPNS-VGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGY------VRGGFSNPDG--W 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3895 YRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVaadGAEPDPQS 3973
Cdd:cd17633 210 MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVgIPDARFGEIAVALYS---GDKLTYKQ 286
|
330 340 350
....*....|....*....|....*....|....
gi 1246793773 3974 LREALRALLPDYMLPRLIQLLPALPLTANGKLDR 4007
Cdd:cd17633 287 LKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
3533-4012 |
7.09e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 111.79 E-value: 7.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3533 PARIAVSAEDGELDYATLDRRSSQLATLLiRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFIL 3612
Cdd:PRK07638 15 PNKIAIKENDRVLTYKDWFESVCKVANWL-NEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3613 EDSGVCLSVSQRALAVELPG--TALCLDD---PFTRAQLDAVEPGELPEvptEAPAYLIYTSGSTGTPKGVVVTHRNVER 3687
Cdd:PRK07638 94 AISNADMIVTERYKLNDLPDeeGRVIEIDewkRMIEKYLPTYAPIENVQ---NAPFYMGFTSGSTGKPKAFLRAQQSWLH 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3688 LFTAATQTGRFSFDEHDV--WSLFHSHafdFavweLWGA--WLY-GGRAVLVPEAVcrqPDAFLDLLAEYGVTVLNQTPS 3762
Cdd:PRK07638 171 SFDCNVHDFHMKREDSVLiaGTLVHSL---F----LYGAisTLYvGQTVHLMRKFI---PNQVLDKLETENISVMYTVPT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3763 AFYALQSQAMRRElalNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVhVSFhrLSDEDLQSPTSRIGSALP 3842
Cdd:PRK07638 241 MLESLYKENRVIE---NKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSF-VTA--LVDEESERRPNSVGRPFH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3843 DLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGY----WQRPELTAERFVErggqrfyrSGDLGRYRADGSLEYRGRGDDQ 3918
Cdd:PRK07638 315 NVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYiiggVLARELNADGWMT--------VRDVGYEDEEGFIYIVGREKNM 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3919 VKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEGAWlMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALP 3998
Cdd:PRK07638 387 ILFGGINIFPEEIESVLHEHPAVDEIVVI--GVPDSYW-GEKPVAIIKGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIP 463
|
490
....*....|....
gi 1246793773 3999 LTANGKLDRKALPK 4012
Cdd:PRK07638 464 YTNSGKIARMEAKS 477
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
3542-4004 |
7.24e-25 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 111.29 E-value: 7.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3542 DGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAayvpvdphaPAArrgfiledsgvCLSV 3621
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGA---------VAA-----------LINY 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3622 SQRALAVelpgtALCLDdpFTRAQLDAVEPgelpevpteapAYLIYTSGSTGTPKGVVVTHRNVER-LFTAATQTGRFSF 3700
Cdd:cd05940 61 NLRGESL-----AHCLN--VSSAKHLVVDA-----------ALYIYTSGTTGLPKAAIISHRRAWRgGAFFAGSGGALPS 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3701 DE-HDVWSLFHSHAFDFAvwelWGAWLYGGRAVLVPEAVcrQPDAFLDLLAEYGVTVLNQTPSAF-YALQSQAMRRELAL 3778
Cdd:cd05940 123 DVlYTCLPLYHSTALIVG----WSACLASGATLVIRKKF--SASNFWDDIRKYQATIFQYIGELCrYLLNQPPKPTERKH 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3779 NVRAVVfgGEALEPSRLQPWRERYPQAELVNMYGITETTvhVSFHRLSDEDlqSPTSRIGSALPDLA----VHVLDAAGQ 3854
Cdd:cd05940 197 KVRMIF--GNGLRPDIWEEFKERFGVPRIAEFYAATEGN--SGFINFFGKP--GAIGRNPSLLRKVAplalVKYDLESGE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3855 P----------VPLGVVGELVVEGDGVA--QGYWQRPELTAE--RFVERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVK 3920
Cdd:cd05940 271 PirdaegrcikVPRGEPGLLISRINPLEpfDGYTDPAATEKKilRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFR 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3921 LRGYRIEPGEIAAKIASLPQVSDA---AVTVEGQgEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPAL 3997
Cdd:cd05940 351 WKGENVSTTEVAAVLGAFPGVEEAnvyGVQVPGT-DGRAGMAAIVLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEM 429
|
....*..
gi 1246793773 3998 PLTANGK 4004
Cdd:cd05940 430 EITGTFK 436
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
3529-4010 |
8.18e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 112.09 E-value: 8.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAV-SAEDGE-LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAA 3606
Cdd:PRK13391 7 AQTTPDKPAViMASTGEvVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3607 RRGFILEDSGVCLSVSQ-------RALAVELPGTALCL--DDPFTRAQLDAVEP--GELPEVPTEAP---AYLIYTSGST 3672
Cdd:PRK13391 87 EAAYIVDDSGARALITSaakldvaRALLKQCPGVRHRLvlDGDGELEGFVGYAEavAGLPATPIADEslgTDMLYSSGTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3673 GTPKGV--------VVTHRNVERLFTAAtqtgrFSFDEHDVW----SLFHShAFDFAVwelwGAWLYGGRAVLVPEAVcr 3740
Cdd:PRK13391 167 GRPKGIkrplpeqpPDTPLPLTAFLQRL-----WGFRSDMVYlspaPLYHS-APQRAV----MLVIRLGGTVIVMEHF-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3741 QPDAFLDLLAEYGVTVLNQTPSAFYALQS--QAMRRELALNVRAVVFGGEALEPSRLQ--------PWRERYpqaelvnm 3810
Cdd:PRK13391 235 DAEQYLALIEEYGVTHTQLVPTMFSRMLKlpEEVRDKYDLSSLEVAIHAAAPCPPQVKeqmidwwgPIIHEY-------- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3811 YGITEtTVHVSFHRlSDEDLQSPTSrIGSALPDLaVHVLDAAGQPVPLGVVGELVVEGdGVAQGYWQRPELTAERFVERG 3890
Cdd:PRK13391 307 YAATE-GLGFTACD-SEEWLAHPGT-VGRAMFGD-LHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEARHPDG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3891 GqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAV-TVEGQGEGAWLMAYAVAADGAEP 3969
Cdd:PRK13391 382 T--WSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVfGVPNEDLGEEVKAVVQPVDGVDP 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1246793773 3970 DP---QSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK13391 460 GPalaAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
3520-4021 |
8.78e-25 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 113.04 E-value: 8.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEiarRYPARIAV--SAEDGE----LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTG 3593
Cdd:cd05966 57 NCLDRHLK---ERGDKVAIiwEGDEPDqsrtITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3594 AAYVPV----DPHAPAARrgfiLEDSGVCL-----SVSQRALAVEL-----------PGTALCL-------DDPFTRAQ- 3645
Cdd:cd05966 134 AVHSVVfagfSAESLADR----INDAQCKLvitadGGYRGGKVIPLkeivdealekcPSVEKVLvvkrtggEVPMTEGRd 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3646 --LDAVEPGELPEVPTEA-----PAYLIYTSGSTGTPKGVVvtHRNVERLFTAATqTGRFSFDEH--DV--------WSL 3708
Cdd:cd05966 210 lwWHDLMAKQSPECEPEWmdsedPLFILYTSGSTGKPKGVV--HTTGGYLLYAAT-TFKYVFDYHpdDIywctadigWIT 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3709 FHSHAfdfavwelwgawLYG----GRAVLVPEAVCRQPDA--FLDLLAEYGVTVLNQTPSAFYALQSQA----MRRELA- 3777
Cdd:cd05966 287 GHSYI------------VYGplanGATTVMFEGTPTYPDPgrYWDIVEKHKVTIFYTAPTAIRALMKFGdewvKKHDLSs 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3778 LNVRAVVfgGEALEPSrlqPWR--------ERYPqaeLVNMYGITETTVHVSfhrlsdedlqSP-----TSRIGSA---L 3841
Cdd:cd05966 355 LRVLGSV--GEPINPE---AWMwyyevigkERCP---IVDTWWQTETGGIMI----------TPlpgatPLKPGSAtrpF 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3842 PDLAVHVLDAAGQPVPLGVVGELVVEGD--GVAQGYWQRPEltaeRFVERGGQRF---YRSGDLGRYRADGSLEYRGRGD 3916
Cdd:cd05966 417 FGIEPAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDHE----RYEDTYFSKFpgyYFTGDGARRDEDGYYWITGRVD 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3917 DQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-----VEGQGegawLMAYAVAADGAEPDP---QSLREALRALLPDYMLP 3988
Cdd:cd05966 493 DVINVSGHRLGTAEVESALVAHPAVAEAAVVgrphdIKGEA----IYAFVTLKDGEEPSDelrKELRKHVRKEIGPIATP 568
|
570 580 590
....*....|....*....|....*....|...
gi 1246793773 3989 RLIQLLPALPLTANGKLDRKALPKPETQDRDEG 4021
Cdd:cd05966 569 DKIQFVPGLPKTRSGKIMRRILRKIAAGEEELG 601
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
3520-4028 |
8.78e-25 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 113.11 E-value: 8.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEIARRYPARIAVSAEDGE---LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAY 3596
Cdd:TIGR02188 61 NCVDRHLEARPDKVAIIWEGDEPGEvrkITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIH 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3597 VPV----DPHAPAARrgfiLEDSGVCLSVS-----QRALAVELPGT---AL---------CL--------DDPFTRAQ-- 3645
Cdd:TIGR02188 141 SVVfggfSAEALADR----INDAGAKLVITadeglRGGKVIPLKAIvdeALekcpvsvehVLvvrrtgnpVVPWVEGRdv 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3646 -LDAVEPGELPEVPTEA-----PAYLIYTSGSTGTPKGVVvtHRNVERLFTAATqTGRFSFDEH---------DV-WSLF 3709
Cdd:TIGR02188 217 wWHDLMAKASAYCEPEPmdsedPLFILYTSGSTGKPKGVL--HTTGGYLLYAAM-TMKYVFDIKdgdifwctaDVgWITG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3710 HSHAfdfavwelwgawLYG----GRAVLVPEAVCRQPDA--FLDLLAEYGVTVLNQTPSAFYALQSQA----MRRELA-L 3778
Cdd:TIGR02188 294 HSYI------------VYGplanGATTVMFEGVPTYPDPgrFWEIIEKHKVTIFYTAPTAIRALMRLGdewvKKHDLSsL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3779 NVRAVVfgGEALEPSrlqPWR--------ERYPqaeLVNMYGITETTVHVSFHRLSDEDLQSptsriGSA---LPDLAVH 3847
Cdd:TIGR02188 362 RLLGSV--GEPINPE---AWMwyykvvgkERCP---IVDTWWQTETGGIMITPLPGATPTKP-----GSAtlpFFGIEPA 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3848 VLDAAGQPVP-LGVVGELVVEGD--GVAQGYWQRPeltaERFVERGGQRF---YRSGDLGRYRADGSLEYRGRGDDQVKL 3921
Cdd:TIGR02188 429 VVDEEGNPVEgPGEGGYLVIKQPwpGMLRTIYGDH----ERFVDTYFSPFpgyYFTGDGARRDKDGYIWITGRVDDVINV 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3922 RGYRIEPGEIAAKIASLPQVSDAAV-----TVEGQGegawLMAYAVAADGAEPDP---QSLREALRALLPDYMLPRLIQL 3993
Cdd:TIGR02188 505 SGHRLGTAEIESALVSHPAVAEAAVvgipdDIKGQA----IYAFVTLKDGYEPDDelrKELRKHVRKEIGPIAKPDKIRF 580
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1246793773 3994 LPALPLTANGKLDRKALPK------PETQD----RDEGVLESASE 4028
Cdd:TIGR02188 581 VPGLPKTRSGKIMRRLLRKiaageaEILGDtstlEDPSVVEELIE 625
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
2062-2522 |
8.92e-25 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 111.05 E-value: 8.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2062 WTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGwg 2141
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2142 aapawvpasvrwldAESVLDvvsayeepprvDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDasl 2221
Cdd:cd05969 79 --------------TEELYE-----------RTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPD--- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2222 aTLSTVAADLG-----FTALFGALLSGrrVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPREC 2296
Cdd:cd05969 131 -DIYWCTADPGwvtgtVYGIWAPWLNG--VTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKYDLS 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2297 ----LVTGGEALTGALVQ-QVRALAptLRIVNHYGPTETTvGILTCTVPEEwPVEQGvPVGHPLAGNEAWVLDRFGLPAP 2371
Cdd:cd05969 208 slrfIHSVGEPLNPEAIRwGMEVFG--VPIHDTWWQTETG-SIMIANYPCM-PIKPG-SMGKPLPGVKAAVVDENGNELP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2372 VGVAGELYLGGGNLSL--GYWQRAEQTAERFVAHplapdrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVE 2449
Cdd:cd05969 283 PGTKGILALKPGWPSMfrGIWNDEERYKNSFIDG-------WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2450 QVLAQLPGVEVAAVLALPGangvLQLGACIQG--SL-EGV--AEALA--------QRLPEYLCPSRWRAVESMPRLGNGK 2516
Cdd:cd05969 356 SALMEHPAVAEAGVIGKPD----PLRGEIIKAfiSLkEGFepSDELKeeiinfvrQKLGAHVAPREIEFVDNLPKTRSGK 431
|
....*.
gi 1246793773 2517 IDRQAL 2522
Cdd:cd05969 432 IMRRVL 437
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
3544-4010 |
1.34e-24 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 110.63 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3544 ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPhapaarrgfiledsgvclSVSQ 3623
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDP------------------GMGR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3624 RALAVelpgtalCLDDpftraqldaVEPGELPEVP-TEAPAYLIYTSGSTGTPKGVVVTHRNverlFTAATQTGRFSFD- 3701
Cdd:cd05910 64 KNLKQ-------CLQE---------AEPDAFIGIPkADEPAAILFTSGSTGTPKGVVYRHGT----FAAQIDALRQLYGi 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3702 ---EHDVWSlfhshafdFAVWELWGAWLygGRAVLVPEAVCRQ-----PDAFLDLLAEYGVTVLNQTPSAFYALQSQAMR 3773
Cdd:cd05910 124 rpgEVDLAT--------FPLFALFGPAL--GLTSVIPDMDPTRparadPQKLVGAIRQYGVSIVFGSPALLERVARYCAQ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3774 RELAL-NVRAVVFGGEALEPSRLQPWRER-YPQAELVNMYGITETTVHVSfhrLSDEDL----QSPTSR-----IGSALP 3842
Cdd:cd05910 194 HGITLpSLRRVLSAGAPVPIALAARLRKMlSDEAEILTPYGATEALPVSS---IGSRELlattTAATSGgagtcVGRPIP 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3843 DLAVHVLDAAGQP---------VPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGGQRF-YRSGDLGRYRADGSLEYR 3912
Cdd:cd05910 271 GVRVRIIEIDDEPiaewddtleLPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNSEGFwHRMGDLGYLDDEGRLWFC 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3913 GRGDDQVKLRGYRI--EPGEIAAKIAslPQVSDAAVTVEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRL 3990
Cdd:cd05910 351 GRKAHRVITTGGTLytEPVERVFNTH--PGVRRSALVGVGKPGCQLPVLCVEPLPGTITPRARLEQELRALAKDYPHTQR 428
|
490 500
....*....|....*....|....*
gi 1246793773 3991 IQLL---PALPLTA--NGKLDRKAL 4010
Cdd:cd05910 429 IGRFlihPSFPVDIrhNAKIFREKL 453
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
2050-2522 |
1.36e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 111.62 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2050 AQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVL 2129
Cdd:PRK06188 26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 DDSGARIVI--------GWGAAPAWVPASVRWL------DAESVLDVVSAYEEPPRVDVDADT-PAYLIYTSGSTGTPKG 2194
Cdd:PRK06188 106 EDAGISTLIvdpapfveRALALLARVPSLKHVLtlgpvpDGVDLLAAAAKFGPAPLVAAALPPdIAGLAYTGGTTGKPKG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2195 VVVSQGNLANYVAGVLPVLDLGEDASL---ATLSTVAAdlgftALF-GALLSGRRVRLLPAelaFDAQALAAHLQAHPVD 2270
Cdd:PRK06188 186 VMGTHRSIATMAQIQLAEWEWPADPRFlmcTPLSHAGG-----AFFlPTLLRGGTVIVLAK---FDPAEVLRAIEEQRIT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2271 CLKIVPS-------HLAGLlaaaggTAVLPR-ECLVTGGEALTGA-LVQQVRALAPTLriVNHYGPTETTVGILTCTVPE 2341
Cdd:PRK06188 258 ATFLVPTmiyalldHPDLR------TRDLSSlETVYYGASPMSPVrLAEAIERFGPIF--AQYYGQTEAPMVITYLRKRD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2342 EWPVEQGV--PVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLapdrllyRSGDLAR 2419
Cdd:PRK06188 330 HDPDDPKRltSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDGWL-------HTGDVAR 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2420 LDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPG--------ANGVLQLGAciQGSLEGVAEALA 2491
Cdd:PRK06188 403 EDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDekwgeavtAVVVLRPGA--AVDAAELQAHVK 480
|
490 500 510
....*....|....*....|....*....|.
gi 1246793773 2492 QRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:PRK06188 481 ERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
588-1041 |
1.40e-24 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 111.25 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQGLAGF---APSVAIAVDELKLDGAG- 663
Cdd:cd05926 42 VAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPKGELGPAsraASKLGLAILELALDVGVl 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 664 -----------------ENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------H 720
Cdd:cd05926 122 irapsaeslsnlladkkNAKSEGVPLPDDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLvvmplfH 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 721 VAGLAVdtTLEQILAAwsrGACVVArpdellePQRFLA--FLSE---------------RAITVTDLAPAYANEL----- 778
Cdd:cd05926 202 VHGLVA--SLLSTLAA---GGSVVL-------PPRFSAstFWPDvrdynatwytavptiHQILLNRPEPNPESPPpklrf 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 779 VRASVADdwrdlalrclvvggdvLPVALAQRwFELGLdrRCALINAYGPTEATisshyHRVqaidASRPVPLGQLLPGRI 858
Cdd:cd05926 270 IRSCSAS----------------LPPAVLEA-LEATF--GAPVLEAYGMTEAA-----HQM----TSNPLPPGPRKPGSV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 859 -------AAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFaplrlpsgESLRMYRSGDRVRLLDDGELQFLG 931
Cdd:cd05926 322 gkpvgveVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAA--------FKDGWFRTGDLGYLDADGYLFLTG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 932 RADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA-GVVGEGAAQRLVAWVECAGEDGFGQADLnqtdsdqteserwhRALC 1010
Cdd:cd05926 394 RIKELINRGGEKISPLEVDGVLLSHPAVLEAVAfGVPDEKYGEEVAAAVVLREGASVTEEEL--------------RAFC 459
|
490 500 510
....*....|....*....|....*....|..
gi 1246793773 1011 -ERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05926 460 rKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
681-1041 |
1.48e-24 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 110.26 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 681 YTSGSTGIPKGVEVGHAALAAHIDA-AAEALALSADDRVLHVAGLAVDTTLEQILA-AWSRGACVVARPDELlePQRFLA 758
Cdd:cd05958 104 FTSGTTGAPKATMHFHRDPLASADRyAVNVLRLREDDRFVGSPPLAFTFGLGGVLLfPFGVGASGVLLEEAT--PDLLLS 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 759 FLSERAITVTDLAP-AYANELvrASVADDWRDLA-LRCLVVGGDVLPVALAQRWFE-LGLDrrcaLINAYGPTEATissH 835
Cdd:cd05958 182 AIARYKPTVLFTAPtAYRAML--AHPDAAGPDLSsLRKCVSAGEALPAALHRAWKEaTGIP----IIDGIGSTEMF---H 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 836 YHRVQAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGiglAEGYRGDAAASERRFAplrlpSGESLrmyRS 915
Cdd:cd05958 253 IFISARPGDARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRG---PTGCRYLADKRQRTYV-----QGGWN---IT 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 916 GDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVraAAAGVVGEGAAQRLV---AWVECAGEDGFGQADL 992
Cdd:cd05958 322 GDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAV--AECAVVGHPDESRGVvvkAFVVLRPGVIPGPVLA 399
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1246793773 993 NQTDSDQTeserwhralcERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05958 400 RELQDHAK----------AHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
2049-2525 |
1.72e-24 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 111.12 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2049 PAQAVAVE-EGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDpqhpDARQIA 2127
Cdd:PRK07514 15 DRDAPFIEtPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLN----TAYTLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2128 VLD----DSGARIVIGWGAAPAWVPA--------SVRWLDAE---SVLDVvsAYEEPPR---VDVDADTPAYLIYTSGST 2189
Cdd:PRK07514 91 ELDyfigDAEPALVVCDPANFAWLSKiaaaagapHVETLDADgtgSLLEA--AAAAPDDfetVPRGADDLAAILYTSGTT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2190 GTPKGVVVSQGNLA-NYVA-----GVLPvldlgEDASLATLSTVAADLGFTALFGALLSGRRVRLLPaelAFDAQALAah 2263
Cdd:PRK07514 169 GRSKGAMLSHGNLLsNALTlvdywRFTP-----DDVLIHALPIFHTHGLFVATNVALLAGASMIFLP---KFDPDAVL-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2264 lqahpvdclkivpshlagllaaaggtAVLPRECLVTG----------GEALTGALVQQVRAL----APTL---------- 2319
Cdd:PRK07514 239 --------------------------ALMPRATVMMGvptfytrllqEPRLTREAAAHMRLFisgsAPLLaethrefqer 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2320 ---RIVNHYGPTETtvGILTCTvpeewPVE---QGVPVGHPLAGNEAWVLDR-FGLPAPVGVAGELYLGGGNLSLGYWQR 2392
Cdd:PRK07514 293 tghAILERYGMTET--NMNTSN-----PYDgerRAGTVGFPLPGVSLRVTDPeTGAELPPGEIGMIEVKGPNVFKGYWRM 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2393 AEQTAERFvahplAPDRlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALP----- 2467
Cdd:PRK07514 366 PEKTAEEF-----RADG-FFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPhpdfg 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 2468 -GANGVLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKID----RQALADL 2525
Cdd:PRK07514 440 eGVTAVVVPKPGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQknllREQYADL 502
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
550-1041 |
2.37e-24 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 109.69 E-value: 2.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 550 ERAALETAQGRLSYRELLTAADARAAA-LRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRaevv 628
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRlLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAEL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 629 aasgcDAVLTDAQglagfapsVAIAVDelkldgagengsgenaapnqLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAE 708
Cdd:cd05941 77 -----EYVITDSE--------PSLVLD--------------------PALILYTSGTTGRPKGVVLTHANLAANVRALVD 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 709 ALALSADDRVL------HVAGL--AVDTTLeqilaaWSRGACVVARPDellEPQRFLAFLSERAITVTDLAPAYANEL-- 778
Cdd:cd05941 124 AWRWTEDDVLLhvlplhHVHGLvnALLCPL------FAGASVEFLPKF---DPKEVAISRLMPSITVFMGVPTIYTRLlq 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 779 -VRASVADDWRDLA-----LRCLVVGGDVLPVALAQRWFELGLDRrcaLINAYGPTEA--TISSHYHrvqaiDASRPVPL 850
Cdd:cd05941 195 yYEAHFTDPQFARAaaaerLRLMVSGSAALPVPTLEEWEAITGHT---LLERYGMTEIgmALSNPLD-----GERRPGTV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 851 GQLLPG---RIAAvlDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLpsgeslrmYRSGDRVRLLDDGEL 927
Cdd:cd05941 267 GMPLPGvqaRIVD--EETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW--------FKTGDLGVVDEDGYY 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 928 QFLGR-ADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVGEGAA---QRLVAWVecAGEDGFGQADLNqtdsdqtESE 1003
Cdd:cd05941 337 WILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECA--VIGVPDPdwgERVVAVV--VLRAGAAALSLE-------ELK 405
|
490 500 510
....*....|....*....|....*....|....*...
gi 1246793773 1004 RWHRalcERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05941 406 EWAK---QRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
2049-2526 |
2.45e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 110.28 E-value: 2.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2049 PAQAVAVE-EGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIA 2127
Cdd:PRK09088 9 PQRLAAVDlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2128 VLDDSGARIVIGwGAAPAwvPASVRWLDAESVLDVVSAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNL----A 2203
Cdd:PRK09088 89 LLQDAEPRLLLG-DDAVA--AGRTDVEDLAAFIASADALEPADTPSIPPERVSLILFTSGTSGQPKGVMLSERNLqqtaH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2204 NY------------------------VAGVLPVLDLG----------EDASLATLSTVAadLGFTALFGALLSGRRVRLL 2249
Cdd:PRK09088 166 NFgvlgrvdahssflcdapmfhiiglITSVRPVLAVGgsilvsngfePKRTLGRLGDPA--LGITHYFCVPQMAQAFRAQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2250 PAelaFDAQALAAHlqahpvdclkivpshlagllaaaggTAvlprecLVTGGEAltgALVQQVRA-LAPTLRIVNHYGPT 2328
Cdd:PRK09088 244 PG---FDAAALRHL-------------------------TA------LFTGGAP---HAAEDILGwLDDGIPMVDGFGMS 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2329 E--TTVGIltctvpeewPVEQGV------PVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERF 2400
Cdd:PRK09088 287 EagTVFGM---------SVDCDVirakagAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2401 VAHPlapdrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALP----GANGVLQLg 2476
Cdd:PRK09088 358 TGDG------WFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMAdaqwGEVGYLAI- 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 2477 ACIQGS---LEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLL 2526
Cdd:PRK09088 431 VPADGApldLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDAL 483
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
2050-2525 |
2.74e-24 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 110.75 E-value: 2.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2050 AQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVL 2129
Cdd:PRK05852 32 APALVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 DDSGARIVIGWGAAPA-WVPASVR-WLDAESVLDVVSAYEEPPRVDVDA---------------DTPAYLIYTSGSTGTP 2192
Cdd:PRK05852 112 QAAGARVVLIDADGPHdRAEPTTRwWPLTVNVGGDSGPSGGTLSVHLDAateptpatstpeglrPDDAMIMFTGGTTGLP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2193 KGVVVSQGNLANYVAGVLPVLDLG-EDASLATLSTVAADLGFTALFGALLSGRRVrLLPAELAFDAQALAAHLQAHPVDC 2271
Cdd:PRK05852 192 KMVPWTHANIASSVRAIITGYRLSpRDATVAVMPLYHGHGLIAALLATLASGGAV-LLPARGRFSAHTFWDDIKAVGATW 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2272 LKIVPS------HLAGLLAAAGGTAVLP--REClvtgGEALTGALVQ--QVRALAPtlrIVNHYGPTETTVGILTCTVP- 2340
Cdd:PRK05852 271 YTAVPTihqillERAATEPSGRKPAALRfiRSC----SAPLTAETAQalQTEFAAP---VVCAFGMTEATHQVTTTQIEg 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2341 ---EEWPVEQGVPVGHPlAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLapdrllyRSGDL 2417
Cdd:PRK05852 344 igqTENPVVSTGLVGRS-TGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWL-------RTGDL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2418 ARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI--QGSLEGVAEALAQ--- 2492
Cdd:PRK05852 416 GSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIvpRESAPPTAEELVQfcr 495
|
490 500 510
....*....|....*....|....*....|....
gi 1246793773 2493 -RLPEYLCPSRWRAVESMPRLGNGKIDRQALADL 2525
Cdd:PRK05852 496 eRLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQ 529
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
2061-2522 |
4.29e-24 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 109.91 E-value: 4.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2061 SWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGW 2140
Cdd:cd17647 20 SFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLIVI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2141 GAApawvpasvrwldaesvlDVVsayeepprvdVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDAS 2220
Cdd:cd17647 100 RAA-----------------GVV----------VGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2221 LATLSTVAADL----GFTALF-GA--LLSGRRVRLLPAELAfdaqalaAHLQAHPVDCLKIVPSHLAGLLAAAGGTAV-L 2292
Cdd:cd17647 153 FTMLSGIAHDPiqrdMFTPLFlGAqlLVPTQDDIGTPGRLA-------EWMAKYGATVTHLTPAMGQLLTAQATTPFPkL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2293 PRECLVtgGEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPEEWP-------VEQGVPVGHPLAGNEAWVLDR 2365
Cdd:cd17647 226 HHAFFV--GDILTKRDCLRLQTLAENVRIVNMYGTTETQRAVSYFEVPSRSSdptflknLKDVMPAGRGMLNVQLLVVNR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2366 FGLPAPVGVA--GELYLGGGNLSLGYWQRAEQTAERFV----AHP------------------LAPDRLLYRSGDLARLD 2421
Cdd:cd17647 304 NDRTQICGIGevGEIYVRAGGLAEGYRGLPELNKEKFVnnwfVEPdhwnyldkdnnepwrqfwLGPRDRLYRTGDLGRYL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2422 GEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI-------------------QGS 2482
Cdd:cd17647 384 PNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIvprfdkpddesfaqedvpkEVS 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 2483 LEGVA--------------EALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:cd17647 464 TDPIVkgligyrklikdirEFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
2047-2536 |
4.60e-24 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 110.22 E-value: 4.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2047 QMPAQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPR----TFAQLAAMAAvwhrGAAWLPLDPQHPD 2122
Cdd:PRK06087 35 AMPDKIAVVDNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGwcefTIIYLACLKV----GAVSVPLLPSWRE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2123 ARQIAVLDDSGARIVIgwgaAPAWVpASVRWLD--------------------------AESVLDVVSAYE---EPPrvD 2173
Cdd:PRK06087 111 AELVWVLNKCQAKMFF----APTLF-KQTRPVDlilplqnqlpqlqqivgvdklapatsSLSLSQIIADYEpltTAI--T 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2174 VDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFT-ALFGALLSGRRVRLL--- 2249
Cdd:PRK06087 184 THGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLhGVTAPFLIGARSVLLdif 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2250 -PAELA--FDAQALAAHLQAHP--VDCLKIVPSHLagllaaaggTAVLPRECLVTGGEALTGALVQQvrALAPTLRIVNH 2324
Cdd:PRK06087 264 tPDACLalLEQQRCTCMLGATPfiYDLLNLLEKQP---------ADLSALRFFLCGGTTIPKKVARE--CQQRGIKLLSV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2325 YGPTETTVGILtctVPEEWPVEQ-GVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAErfvah 2403
Cdd:PRK06087 333 YGSTESSPHAV---VNLDDPLSRfMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTAR----- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2404 PLAPDRLLYrSGDLARLDGEGRIVYLGRgDHQVKIR-GYRVELGEVEQVLAQLPGVEVAAVLALPG--------ANGVLQ 2474
Cdd:PRK06087 405 ALDEEGWYY-SGDLCRMDEAGYIKITGR-KKDIIVRgGENISSREVEDILLQHPKIHDACVVAMPDerlgerscAYVVLK 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 2475 lGACIQGSLEGVAEALA-QRLPEYLCPSRWRAVESMPRLGNGKIDRQALA-DLLQQDDADSSAE 2536
Cdd:PRK06087 483 -APHHSLTLEEVVAFFSrKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRkDIMRRLTQDVCEE 545
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
2063-2467 |
5.86e-24 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 109.25 E-value: 5.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2063 TYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDP-QHPD--ARQIavlDDSGARIVIg 2139
Cdd:cd05904 34 TYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPlSTPAeiAKQV---KDSGAKLAF- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2140 wgAAPAWVPaSVRWLDAESVL----DVVSAYE----------EPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNL--- 2202
Cdd:cd05904 110 --TTAELAE-KLASLALPVVLldsaEFDSLSFsdllfeadeaEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLiam 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2203 -ANYVAGVLPVLDlGEDASLATL--STVaadLGFTALFGALLS-GRRVRLLPaelAFDAQALAAHLQAHPVDCLKIVP-- 2276
Cdd:cd05904 187 vAQFVAGEGSNSD-SEDVFLCVLpmFHI---YGLSSFALGLLRlGATVVVMP---RFDLEELLAAIERYKVTHLPVVPpi 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2277 -----SHLAGLLAAaggtaVLPRECLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPEEWPVEQGvPV 2351
Cdd:cd05904 260 vlalvKSPIVDKYD-----LSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTGVVAMCFAPEKDRAKYG-SV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2352 GHPLAGNEAWVLD-RFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVahplaPDRLLyRSGDLARLDGEGRIVYLG 2430
Cdd:cd05904 334 GRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATID-----KEGWL-HTGDLCYIDEDGYLFIVD 407
|
410 420 430
....*....|....*....|....*....|....*..
gi 1246793773 2431 RGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALP 2467
Cdd:cd05904 408 RLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYP 444
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
2170-2525 |
6.54e-24 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 108.96 E-value: 6.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2170 PRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFT-ALFGALLSGRRVRL 2248
Cdd:cd05909 140 GVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTgCLWLPLLSGIKVVF 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2249 LPaelafdaqalaahlqaHPVDCLKIVPSHLAGLLAAAGGTAVLPR--------ECL------VTGGEALTGALVQQVRA 2314
Cdd:cd05909 220 HP----------------NPLDYKKIPELIYDKKATILLGTPTFLRgyaraahpEDFsslrlvVAGAEKLKDTLRQEFQE 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2315 LApTLRIVNHYGPTETTvGILTCTVPEEwPVEQGVpVGHPLAGNEAWVLDRFGL-PAPVGVAGELYLGGGNLSLGYWQRA 2393
Cdd:cd05909 284 KF-GIRILEGYGTTECS-PVISVNTPQS-PNKEGT-VGRPLPGMEVKIVSVETHeEVPIGEGGLLLVRGPNVMLGYLNEP 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2394 EQTAErfvahplAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPG--VEVAAVL---ALPG 2468
Cdd:cd05909 360 ELTSF-------AFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPedNEVAVVSvpdGRKG 432
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 2469 ANGVLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADL 2525
Cdd:cd05909 433 EKIVLLTTTTDTDPSSLNDILKNAGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKAL 489
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
2061-2465 |
6.87e-24 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 108.45 E-value: 6.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2061 SWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPR----TFAQLAAMAAvwhrGAAWLPLDPQHPdARQIA-VLDDSGAR 2135
Cdd:cd05907 5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNrpewTIADLAILAI----GAVPVPIYPTSS-AEQIAyILNDSEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2136 IVIgwgaapawvpasvrwldaesvldvvsayeepprVDvDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDL 2215
Cdd:cd05907 80 ALF---------------------------------VE-DPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2216 GEDASLAT---LSTVAADLgfTALFGALLSGRRVRLLP-AELAFDAQALAAHLQAHPVD------CLKIVPSHLAGLLAA 2285
Cdd:cd05907 126 TEGDRHLSflpLAHVFERR--AGLYVPLLAGARIYFASsAETLLDDLSEVRPTVFLAVPrvwekvYAAIKVKAVPGLKRK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2286 AGGTAVLPR-ECLVTGGEALTGALVQQVRALAPTLRIVnhYGPTETTvGILTCTVPEEWPVEQgvpVGHPLAGNEawvld 2364
Cdd:cd05907 204 LFDLAVGGRlRFAASGGAPLPAELLHFFRALGIPVYEG--YGLTETS-AVVTLNPPGDNRIGT---VGKPLPGVE----- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2365 rfglpAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAhplapDRLLyRSGDLARLDGEGRIVYLGR-GDHQVKIRGYRV 2443
Cdd:cd05907 273 -----VRIADDGEILVRGPNVMLGYYKNPEATAEALDA-----DGWL-HTGDLGEIDEDGFLHITGRkKDLIITSGGKNI 341
|
410 420
....*....|....*....|..
gi 1246793773 2444 ELGEVEQVLAQLPGVEVAAVLA 2465
Cdd:cd05907 342 SPEPIENALKASPLISQAVVIG 363
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
2053-2527 |
7.46e-24 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 108.79 E-value: 7.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2053 VAVEEGAASWTYAQLRAAAGRIAGAL-DAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDD 2131
Cdd:PRK06839 19 IAIITEEEEMTYKQLHEYVSKVAAYLiYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIV---------IGWGAAPAWVPASVRWLDAESVLDVVSAYEEPPrvdvDADTPAYLIYTSGSTGTPKGVVVSQGNL 2202
Cdd:PRK06839 99 SGTTVLfvektfqnmALSMQKVSYVQRVISITSLKEIEDRKIDNFVEK----NESASFIICYTSGTTGKPKGAVLTQENM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2203 A-NYVAGVLpVLDL-GEDASLATLSTVaaDLGFTALFG--ALLSGRRVrLLPAElaFDAQALAAHLQAHPVDCLKIVPS- 2277
Cdd:PRK06839 175 FwNALNNTF-AIDLtMHDRSIVLLPLF--HIGGIGLFAfpTLFAGGVI-IVPRK--FEPTKALSMIEKHKVTVVMGVPTi 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2278 HLAGLLAAAGGTAVLPR-ECLVTGGEALTGALVQQVRALAptLRIVNHYGPTET--TVGILTctvpEEWPVEQGVPVGHP 2354
Cdd:PRK06839 249 HQALINCSKFETTNLQSvRWFYNGGAPCPEELMREFIDRG--FLFGQGFGMTETspTVFMLS----EEDARRKVGSIGKP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2355 LAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFvahplaPDRLLYrSGDLARLDGEGRIVYLGRGDH 2434
Cdd:PRK06839 323 VLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI------QDGWLC-TGDLARVDEDGFVYIVGRKKE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2435 QVKIRGYRVELGEVEQVLAQLPGVEVAAVLA--------LPGANGVLQLGACIqgSLEGVAEALAQRLPEYLCPSRWRAV 2506
Cdd:PRK06839 396 MIISGGENIYPLEVEQVINKLSDVYEVAVVGrqhvkwgeIPIAFIVKKSSSVL--IEKDVIEHCRLFLAKYKIPKEIVFL 473
|
490 500
....*....|....*....|.
gi 1246793773 2507 ESMPRLGNGKIDRQALADLLQ 2527
Cdd:PRK06839 474 KELPKNATGKIQKAQLVNQLK 494
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
3529-4005 |
9.16e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 108.94 E-value: 9.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAV-SAEDGE-LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAA 3606
Cdd:PRK13390 7 AQIAPDRPAViVAETGEqVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3607 RRGFILEDSGVCLSVSQRAL--AVELPGTALCLDDPFTR-----AQLDAVEPGELPEVpTEAP--AYLIYTSGSTGTPKG 3677
Cdd:PRK13390 87 EADYIVGDSGARVLVASAALdgLAAKVGADLPLRLSFGGeidgfGSFEAALAGAGPRL-TEQPcgAVMLYSSGTTGFPKG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3678 VV--VTHRNVERLF--TAATQTGRFSFDEHDVWslFHSHAFDFAVWELWGAWLY--GGRAVLVPEAvcrQPDAFLDLLAE 3751
Cdd:PRK13390 166 IQpdLPGRDVDAPGdpIVAIARAFYDISESDIY--YSSAPIYHAAPLRWCSMVHalGGTVVLAKRF---DAQATLGHVER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3752 YGVTVLNQTPSAF---YALQSQAMRRELALNVRAVVFGGeALEPSRLQPWRERYPQAELVNMYGITEttVHVSFHRLSDE 3828
Cdd:PRK13390 241 YRITVTQMVPTMFvrlLKLDADVRTRYDVSSLRAVIHAA-APCPVDVKHAMIDWLGPIVYEYYSSTE--AHGMTFIDSPD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3829 DLQSPTSRIGSALPDLavHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAErfVERGGQRFYRS-GDLGRYRADG 3907
Cdd:PRK13390 318 WLAHPGSVGRSVLGDL--HICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAA--AQHPAHPFWTTvGDLGSVDEDG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3908 SLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSLREAL---RALLP 3983
Cdd:PRK13390 394 YLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIgVPDPEMGEQVKAVIQLVEGIRGSDELARELIdytRSRIA 473
|
490 500
....*....|....*....|..
gi 1246793773 3984 DYMLPRLIQLLPALPLTANGKL 4005
Cdd:PRK13390 474 HYKAPRSVEFVDELPRTPTGKL 495
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
539-1041 |
9.18e-24 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 109.08 E-value: 9.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 539 DAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGlsVIPLDTe 618
Cdd:COG1021 29 DLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAG--AIPVFA- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 619 WPQARRAE---VVAASGCDAVLTDAQ----GLAGFAPSVAIAVDELK----------------LDGAGENGSGENAAPNQ 675
Cdd:COG1021 106 LPAHRRAEishFAEQSEAVAYIIPDRhrgfDYRALARELQAEVPSLRhvlvvgdageftsldaLLAAPADLSEPRPDPDD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 676 LAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQ--ILAAWSRGACVVARPDelLEP 753
Cdd:COG1021 186 VAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHNFPLSSpgVLGVLYAGGTVVLAPD--PSP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 754 QRFLAFLSERAITVTDLAPAYANELVRASVADDWrDLA-LRCLVVGGDVLPVALAQRWF-ELGldrrCALINAYGPTEAT 831
Cdd:COG1021 264 DTAFPLIERERVTVTALVPPLALLWLDAAERSRY-DLSsLRVLQVGGAKLSPELARRVRpALG----CTLQQVFGMAEGL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 832 ISshYHRvqaIDAS---------RPV-PLGQLLpgriaaVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAp 901
Cdd:COG1021 339 VN--YTR---LDDPeevilttqgRPIsPDDEVR------IVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFT- 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 902 lrlPSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA-----GVVGEgaaqRLV 976
Cdd:COG1021 407 ---PDG----FYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVvampdEYLGE----RSC 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 977 AWVECAGEDgFGQADLNqtdsdqteserwhRALCER-LPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:COG1021 476 AFVVPRGEP-LTLAELR-------------RFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
2051-2528 |
1.02e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 108.98 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLD-PQHPDarQIAVL 2129
Cdd:PRK07470 22 DRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNfRQTPD--EVAYL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 -DDSGARIVIGWGAAPAWVPA---------SVRWLDA----ESVLDVVSAY--EEPPRVDVDADTPAYLIYTSGSTGTPK 2193
Cdd:PRK07470 100 aEASGARAMICHADFPEHAAAvraaspdltHVVAIGGaragLDYEALVARHlgARVANAAVDHDDPCWFFFTSGTTGRPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2194 GVVVSQGNLA----NYVAGVLPVLDlGEDASLatlstVAADLGFTALFGALLS---GRRVRLLPAElAFDAQALAAHLQA 2266
Cdd:PRK07470 180 AAVLTHGQMAfvitNHLADLMPGTT-EQDASL-----VVAPLSHGAGIHQLCQvarGAATVLLPSE-RFDPAEVWALVER 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2267 HPVDCLKIVPShlaGLLAAAGGTAVLPRE-----CLVTGGEALTGAlvQQVRALAPTLR-IVNHYGPTETTVGIltcTV- 2339
Cdd:PRK07470 253 HRVTNLFTVPT---ILKMLVEHPAVDRYDhsslrYVIYAGAPMYRA--DQKRALAKLGKvLVQYFGLGEVTGNI---TVl 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2340 ------PEEWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHplapdrlLYR 2413
Cdd:PRK07470 325 ppalhdAEDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDG-------WFR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2414 SGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPG--------ANGVLQLGACIQGslEG 2485
Cdd:PRK07470 398 TGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDpvwgevgvAVCVARDGAPVDE--AE 475
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1246793773 2486 VAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLLQQ 2528
Cdd:PRK07470 476 LLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREELEE 518
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
2053-2526 |
1.05e-23 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 108.13 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2053 VAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDpQHPDARQIAV-LDD 2131
Cdd:PRK03640 19 TAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLN-TRLSREELLWqLDD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVIGWGAAPA--WVPASVRWLDAESvldvvSAYEEP-PRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNlaNYVAG 2208
Cdd:PRK03640 98 AEVKCLITDDDFEAklIPGISVKFAELMN-----GPKEEAeIQEEFDLDEVATIMYTSGTTGKPKGVIQTYGN--HWWSA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2209 VLPVLDLG---EDASLATL-----StvaadlGFTALFGALLSGRRVRLLPaelAFDAQALAAHLQAHPVDCLKIVPShla 2280
Cdd:PRK03640 171 VGSALNLGlteDDCWLAAVpifhiS------GLSILMRSVIYGMRVVLVE---KFDAEKINKLLQTGGVTIISVVST--- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2281 gllAAAGGTAVLPRE-------CLVTGGEALTGALVQQVRalAPTLRIVNHYGPTETTVGIltCTVPEEWPVEQGVPVGH 2353
Cdd:PRK03640 239 ---MLQRLLERLGEGtypssfrCMLLGGGPAPKPLLEQCK--EKGIPVYQSYGMTETASQI--VTLSPEDALTKLGSAGK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2354 PLAGNEAWVLDRfGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVahplapDRLLYrSGDLARLDGEGRIVYLGRGD 2433
Cdd:PRK03640 312 PLFPCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQ------DGWFK-TGDIGYLDEEGFLYVLDRRS 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2434 HQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALP----GANGVlqlgACIQGSLEGVAEALAQ----RLPEYLCPSRWRA 2505
Cdd:PRK03640 384 DLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPddkwGQVPV----AFVVKSGEVTEEELRHfceeKLAKYKVPKRFYF 459
|
490 500
....*....|....*....|.
gi 1246793773 2506 VESMPRLGNGKIDRQALADLL 2526
Cdd:PRK03640 460 VEELPRNASGKLLRHELKQLV 480
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
3533-4010 |
2.56e-23 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 107.83 E-value: 2.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3533 PARIAVSAEDGE---LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDP-------- 3601
Cdd:PRK13295 41 TAVTAVRLGTGAprrFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPifrerels 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3602 ----HA-------PAARRGFILEDSGvclsvsqRALAVELP----------GTALCLDDPFTRAQLDAvEPGELPEVPTE 3660
Cdd:PRK13295 121 fmlkHAeskvlvvPKTFRGFDHAAMA-------RRLRPELPalrhvvvvggDGADSFEALLITPAWEQ-EPDAPAILARL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3661 AP-----AYLIYTSGSTGTPKGVVVTHRN--------VERL--------FTAAT---QTGrfsfdehdvwslfhshafdf 3716
Cdd:PRK13295 193 RPgpddvTQLIYTSGTTGEPKGVMHTANTlmanivpyAERLglgaddviLMASPmahQTG-------------------- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3717 avwelwgaWLYGGR-AVLVPEAVCRQ----PDAFLDLLAEYGVT-VLNQTPSAFYALQSQAMRRELALNVRAVVFGGEAL 3790
Cdd:PRK13295 253 --------FMYGLMmPVMLGATAVLQdiwdPARAAELIRTEGVTfTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3791 EPSRLQPWRERYpQAELVNMYGITETTVhVSFHRLSDEDLQSPTSRiGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDG 3870
Cdd:PRK13295 325 PGALVERARAAL-GAKIVSAWGMTENGA-VTLTKLDDPDERASTTD-GCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3871 VAQGYWQRPELTAERFverggQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTV-- 3948
Cdd:PRK13295 402 NFGGYLKRPQLNGTDA-----DGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAyp 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 3949 -EGQGEGAwlMAYAVAADGAEPDPQSLREALRA--LLPDYMLPRLIqLLPALPLTANGKLDRKAL 4010
Cdd:PRK13295 477 dERLGERA--CAFVVPRPGQSLDFEEMVEFLKAqkVAKQYIPERLV-VRDALPRTPSGKIQKFRL 538
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
1142-1371 |
3.31e-23 |
|
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380454 [Multi-domain] Cd Length: 427 Bit Score: 105.90 E-value: 3.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1142 LSPIQR--WFFDS-APAQPDrYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPaIQAQ 1218
Cdd:cd19531 4 LSFAQQrlWFLDQlEPGSAA-YNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLP-LPVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1219 DWRGAADLDSRVDAAFARMQEA-TP--LA-GPLVALTHAHCDDGE-RLLICAHHLIVDAVSWRLLLGELFDGLAALARGE 1293
Cdd:cd19531 82 DLSGLPEAEREAEAQRLAREEArRPfdLArGPLLRATLLRLGEDEhVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1294 AWTPSARGASYADYVEALREADDAQRFDA--GFWRE-LA-AQPMQALPQDRPVAladARQSNVGRIVQ-TLDAGLTADLL 1368
Cdd:cd19531 162 PSPLPPLPIQYADYAVWQREWLQGEVLERqlAYWREqLAgAPPVLELPTDRPRP---AVQSFRGARVRfTLPAELTAALR 238
|
...
gi 1246793773 1369 ERA 1371
Cdd:cd19531 239 ALA 241
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
2056-2517 |
4.21e-23 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 107.66 E-value: 4.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2056 EEGAAS--WTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSG 2133
Cdd:cd17634 77 DDTSQSrtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSS 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2134 ARIVIGW------------------------------------GAAPAWVPAsvRWLDAESVLDVVSAYEEPPRVDvdAD 2177
Cdd:cd17634 157 SRLLITAdggvragrsvplkknvddalnpnvtsvehvivlkrtGSDIDWQEG--RDLWWRDLIAKASPEHQPEAMN--AE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2178 TPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLP-VLDLGEdaslATLSTVAADLGFTA-----LFGALLSGRRVRLLPA 2251
Cdd:cd17634 233 DPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKyVFDYGP----GDIYWCTADVGWVTghsylLYGPLACGATTLLYEG 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2252 elafdaqalaAHLQAHPVDCLKIVPSHLAGLLAAAGgTAVlpRECLVTGGEALTGALVQQVRALAPT------------- 2318
Cdd:cd17634 309 ----------VPNWPTPARMWQVVDKHGVNILYTAP-TAI--RALMAAGDDAIEGTDRSSLRILGSVgepinpeayewyw 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2319 -------LRIVNHYGPTETTVGILTcTVPEEWPVEQGVPVgHPLAGNEAWVLDRFGLPAPVGVAGELYLGGG--NLSLGY 2389
Cdd:cd17634 376 kkigkekCPVVDTWWQTETGGFMIT-PLPGAIELKAGSAT-RPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTL 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2390 WQRAEqtaeRFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGA 2469
Cdd:cd17634 454 FGDHE----RFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHA 529
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 2470 -NG-------VLQLGACIQGSLEG-VAEALAQRLPEYLCPSRWRAVESMPRLGNGKI 2517
Cdd:cd17634 530 iKGqapyayvVLNHGVEPSPELYAeLRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
3515-4007 |
5.51e-23 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 107.01 E-value: 5.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3515 YACTG----NLVSRFAEIARRYPariavsaedgeldYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAIL 3590
Cdd:PRK09192 29 YAALGeagmNFYDRRGQLEEALP-------------YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3591 KTGAAYVPVDPHAPAARRGFILEDSGVCLSVSQRALA---------VELPGTALCLDDPFTRAQLDAVE--PGELPEVPT 3659
Cdd:PRK09192 96 YAGLVPVPLPLPMGFGGRESYIAQLRGMLASAQPAAIitpdellpwVNEATHGNPLLHVLSHAWFKALPeaDVALPRPTP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3660 EAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQTGrFSFDEHD---VW-SLFHshafDFAVWELWGAWLYGGRAV--L 3733
Cdd:PRK09192 176 DDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDG-LKVRPGDrcvSWlPFYH----DMGLVGFLLTPVATQLSVdyL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3734 VPEAVCRQPDAFLDLLAEYGVTVlNQTPSAFYALQSQAMR--RELALNV---RAVVFGGEALEPSRLQPWRERYPQA--- 3805
Cdd:PRK09192 251 PTRDFARRPLQWLDLISRNRGTI-SYSPPFGYELCARRVNskDLAELDLscwRVAGIGADMIRPDVLHQFAEAFAPAgfd 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3806 --ELVNMYGITETTVHVSF--------------HRLS----DEDLQSPTSRI------GSALPDLAVHVLDAAGQPVPLG 3859
Cdd:PRK09192 330 dkAFMPSYGLAEATLAVSFsplgsgivveevdrDRLEyqgkAVAPGAETRRVrtfvncGKALPGHEIEIRNEAGMPLPER 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3860 VVGELVVEGDGVAQGYWQRPEltAERFVERGGqrFYRSGDLGrYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLP 3939
Cdd:PRK09192 410 VVGHICVRGPSLMSGYFRDEE--SQDVLAADG--WLDTGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEP 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 3940 QV--SDAAV-TVEGQGEGAwlMAYAVAADGAEPDP-QSLREALRALLpdYM---LPRLIQLLP--ALPLTANGKLDR 4007
Cdd:PRK09192 485 ELrsGDAAAfSIAQENGEK--IVLLVQCRISDEERrGQLIHALAALV--RSefgVEAAVELVPphSLPRTSSGKLSR 557
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
3521-3952 |
6.19e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 106.95 E-value: 6.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3521 LVSRFAEIARRYPARIAVSAEDGELD---------YATLDRRSSQLATLLIRQGAgPGQRVGLCLPRGCDLLVALLAILK 3591
Cdd:PRK05850 3 VPSLLRERASLQPDDAAFTFIDYEQDpagvaetltWSQLYRRTLNVAEELRRHGS-TGDRAVILAPQGLEYIVAFLGALQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3592 TGAAYVPVDPHAPAA---RRGFILEDSG--VCLSVSQRALAVELPGTALCLDDPFTRAQLDAVE---PGELPEVPTEAP- 3662
Cdd:PRK05850 82 AGLIAVPLSVPQGGAhdeRVSAVLRDTSpsVVLTTSAVVDDVTEYVAPQPGQSAPPVIEVDLLDldsPRGSDARPRDLPs 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3663 -AYLIYTSGSTGTPKGVVVTHRNV----ERLFTA--ATQTGRFSFDEHDV-W-SLFHSHAFDFAVWelwgAWLYGGR-AV 3732
Cdd:PRK05850 162 tAYLQYTSGSTRTPAGVMVSHRNVianfEQLMSDyfGDTGGVPPPDTTVVsWlPFYHDMGLVLGVC----APILGGCpAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3733 LV-PEAVCRQPDAFLDLLAEYgvtvlnqtPSAFYALQSQAMrrELAL--------------NVRAVVFGGEALEPSRLQP 3797
Cdd:PRK05850 238 LTsPVAFLQRPARWMQLLASN--------PHAFSAAPNFAF--ELAVrktsdddmagldlgGVLGIISGSERVHPATLKR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3798 WRERY-----PQAELVNMYGITETTVHVS--------------FHRLSDEDLQSPTSRIGSAL------PDLAVHVLDA- 3851
Cdd:PRK05850 308 FADRFapfnlRETAIRPSYGLAEATVYVAtrepgqppesvrfdYEKLSAGHAKRCETGGGTPLvsygspRSPTVRIVDPd 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3852 AGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFverGGQ-----------RFYRSGDLGrYRADGSLEYRGRGDDQVK 3920
Cdd:PRK05850 388 TCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTF---GATlvdpspgtpegPWLRTGDLG-FISEGELFIVGRIKDLLI 463
|
490 500 510
....*....|....*....|....*....|..
gi 1246793773 3921 LRGYRIEPGEIAAKIASLPQVSDAAVTVEGQG 3952
Cdd:PRK05850 464 VDGRNHYPDDIEATIQEITGGRVAAISVPDDG 495
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
3529-4010 |
6.71e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 106.57 E-value: 6.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARR 3608
Cdd:PRK08162 28 AEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3609 GFILE--DSGVCL------SVSQRALAvELPGTALCL----DDPFTRAQL-------DAVEPGElPEVPTEAPA------ 3663
Cdd:PRK08162 108 AFMLRhgEAKVLIvdtefaEVAREALA-LLPGPKPLVidvdDPEYPGGRFigaldyeAFLASGD-PDFAWTLPAdewdai 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3664 YLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEHDV--WSL--FHSHAFDFAvWELwgawlyggrAVLVPEAVC 3739
Cdd:PRK08162 186 ALNYTSGTTGNPKGVVYHHRGA--YLNALSNILAWGMPKHPVylWTLpmFHCNGWCFP-WTV---------AARAGTNVC 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3740 -R--QPDAFLDLLAEYGVTVLNQTPSAFYALQS--QAMRRELALNVRAVVfGGEALEPSRLQPWRERypQAELVNMYGIT 3814
Cdd:PRK08162 254 lRkvDPKLIFDLIREHGVTHYCGAPIVLSALINapAEWRAGIDHPVHAMV-AGAAPPAAVIAKMEEI--GFDLTHVYGLT 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3815 ET----TV---HVSFHRLSDEDLQSPTSRIGSALPDL-AVHVLDAA-GQPVPLG--VVGELVVEGDGVAQGYWQRPELTA 3883
Cdd:PRK08162 331 ETygpaTVcawQPEWDALPLDERAQLKARQGVRYPLQeGVTVLDPDtMQPVPADgeTIGEIMFRGNIVMKGYLKNPKATE 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3884 ERFveRGGqrFYRSGDLGRYRADGSLEYRGRGDDQVklrgyrIEPGEiaaKIASL---------PQVSDAAVTV---EGQ 3951
Cdd:PRK08162 411 EAF--AGG--WFHTGDLAVLHPDGYIKIKDRSKDII------ISGGE---NISSIevedvlyrhPAVLVAAVVAkpdPKW 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 3952 GEGAwlMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPaLPLTANGKLDRKAL 4010
Cdd:PRK08162 478 GEVP--CAFVELKDGASATEEEIIAHCREHLAGFKVPKAVVFGE-LPKTSTGKIQKFVL 533
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
588-1036 |
7.83e-23 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 105.76 E-value: 7.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQGL-------AGFAPSVAIAVDELKLD 660
Cdd:cd05911 38 VGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDPDGLekvkeaaKELGPKDKIIVLDDKPD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 661 GAGENGSG---------------ENAAPNQLAYILYTSGSTGIPKGVEVGHAA--LAAHIDAAAEALALSADDRVL---- 719
Cdd:cd05911 118 GVLSIEDLlsptlgeededlpppLKDGKDDTAAILYSSGTTGLPKGVCLSHRNliANLSQVQTFLYGNDGSNDVILgflp 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 720 --HVAGLavDTTLEQILaawsRGACVVARPDelLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWrDLA-LRCLV 796
Cdd:cd05911 198 lyHIYGL--FTTLASLL----NGATVIIMPK--FDSELFLDLIEKYKITFLYLVPPIAAALAKSPLLDKY-DLSsLRVIL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 797 VGGDvlpvALAQRWFEL--GLDRRCALINAYGPTEAT-ISSHYHRVQAIDASrpvpLGQLLPGRIAAVLDAHGR-IVPRG 872
Cdd:cd05911 269 SGGA----PLSKELQELlaKRFPNATIKQGYGMTETGgILTVNPDGDDKPGS----VGRLLPNVEAKIVDDDGKdSLGPN 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 873 VCGELALGGIGLAEGYRGDAAASERRFAplrlPSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHC 952
Cdd:cd05911 341 EPGEICVRGPQVMKGYYNNPEATKETFD----EDG----WLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAV 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 953 LGQLPQVR-AAAAGVVGEGAAQRLVAWVECAgedgfgqadlnqtDSDQTESERWHRALCERLPAYM-----VptQFValP 1026
Cdd:cd05911 413 LLEHPGVAdAAVIGIPDEVSGELPRAYVVRK-------------PGEKLTEKEVKDYVAKKVASYKqlrggV--VFV--D 475
|
490
....*....|
gi 1246793773 1027 RLPRNASGKI 1036
Cdd:cd05911 476 EIPKSASGKI 485
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
2090-2531 |
8.10e-23 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 106.29 E-value: 8.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2090 ALCLPRTFAQL--AAMAAvwhrgaawlPLDPQHPDARQIAVLDDSGARIVIGWGAAPAWVPASvrwlDAESVLDvvsaye 2167
Cdd:PRK13295 130 VLVVPKTFRGFdhAAMAR---------RLRPELPALRHVVVVGGDGADSFEALLITPAWEQEP----DAPAILA------ 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2168 eppRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLanyVAGVLPV---LDLGEDASLATLSTVAADLGF----------- 2233
Cdd:PRK13295 191 ---RLRPGPDDVTQLIYTSGTTGEPKGVMHTANTL---MANIVPYaerLGLGADDVILMASPMAHQTGFmyglmmpvmlg 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2234 ----------TALFGALLSGRRVRLLPAELAF-DAQALAAHLQAHPVDCLKIvpshlagllaaaggtavlprecLVTGGE 2302
Cdd:PRK13295 265 atavlqdiwdPARAAELIRTEGVTFTMASTPFlTDLTRAVKESGRPVSSLRT----------------------FLCAGA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2303 ALTGALVQQVRALAPTlRIVNHYGPTETtvGILTCTVPEEWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGG 2382
Cdd:PRK13295 323 PIPGALVERARAALGA-KIVSAWGMTEN--GAVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRG 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2383 GNLSLGYWQRAEQTAERFVAhplapdrlLYRSGDLARLDGEGRIVYLGRgDHQVKIRG-YRVELGEVEQVLAQLPGVEVA 2461
Cdd:PRK13295 400 CSNFGGYLKRPQLNGTDADG--------WFDTGDLARIDADGYIRISGR-SKDVIIRGgENIPVVEIEALLYRHPAIAQV 470
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 2462 AVLALPGANgvLQLGACI-----QGS---LEGVAEAL-AQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLLQQDDA 2531
Cdd:PRK13295 471 AIVAYPDER--LGERACAfvvprPGQsldFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRGEDA 547
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
3545-4010 |
1.31e-22 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 105.69 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3545 LDYATLDRRSSQLATLLIRQ-GAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVCLSVSQ 3623
Cdd:PLN02574 67 ISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3624 -------RALAVELPGT--ALCLDD------PFTRAQLDAVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNverl 3688
Cdd:PLN02574 147 penveklSPLGVPVIGVpeNYDFDSkriefpKFYELIKEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRN---- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3689 FTAATQTG-RFSFDEHD----------VWSLFHSHAFDFAVWELwgawLYGGRAVLVpeavCRQPDA--FLDLLAEYGVT 3755
Cdd:PLN02574 223 LIAMVELFvRFEASQYEypgsdnvylaALPMFHIYGLSLFVVGL----LSLGSTIVV----MRRFDAsdMVKVIDRFKVT 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3756 VLNQTPSAFYAL--QSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVhVSFHRLSDEDLQSP 3833
Cdd:PLN02574 295 HFPVVPPILMALtkKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQGYGMTESTA-VGTRGFNTEKLSKY 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3834 TSrIGSALPDLAVHVLD-AAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYR 3912
Cdd:PLN02574 374 SS-VGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDG---WLRTGDIAYFDEDGYLYIV 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3913 GRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGE-GAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLI 3991
Cdd:PLN02574 450 DRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKEcGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKV 529
|
490
....*....|....*....
gi 1246793773 3992 QLLPALPLTANGKLDRKAL 4010
Cdd:PLN02574 530 VFVQSIPKSPAGKILRREL 548
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
2049-2523 |
1.43e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 104.69 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2049 PAQAVAVEEGAASWTYAQLRAAAGRIAGAL---DAVGVQPGAHVALCLPRTFAQLAAMAAVwhrgaawlPLDPQHPDARQ 2125
Cdd:PRK07787 13 ADIADAVRIGGRVLSRSDLAGAATAVAERVagaRRVAVLATPTLATVLAVVGALIAGVPVV--------PVPPDSGVAER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2126 IAVLDDSGARIVIGwgaAPAWVPASVRWLDAESVLDVVSAYEEPprvdvDADTPAYLIYTSGSTGTPKGVVVSQGNLAny 2205
Cdd:PRK07787 85 RHILADSGAQAWLG---PAPDDPAGLPHVPVRLHARSWHRYPEP-----DPDAPALIVYTSGTTGPPKGVVLSRRAIA-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2206 vagvlpvldlgedaslATLSTVAADLGFTA---------LF----------GALLSGRRVRLL----PAELAFDAQALAA 2262
Cdd:PRK07787 155 ----------------ADLDALAEAWQWTAddvlvhglpLFhvhglvlgvlGPLRIGNRFVHTgrptPEAYAQALSEGGT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2263 HLQAHPVDCLKIVpshlaglLAAAGGTAVLPRECLVTGGEALTGALVQQVRALApTLRIVNHYGPTETtvgILTCTVPEE 2342
Cdd:PRK07787 219 LYFGVPTVWSRIA-------ADPEAARALRGARLLVSGSAALPVPVFDRLAALT-GHRPVERYGMTET---LITLSTRAD 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2343 WPVEQGVpVGHPLAGNEAWVLDRFGLPAPVGVA--GELYLGGGNLSLGYWQRAEQTAERFVAHPLapdrllYRSGDLARL 2420
Cdd:PRK07787 288 GERRPGW-VGLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVV 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2421 DGEG--RIVylGRGDHQ-VKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQGSLEGVAEAL----AQR 2493
Cdd:PRK07787 361 DPDGmhRIV--GRESTDlIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAADELidfvAQQ 438
|
490 500 510
....*....|....*....|....*....|
gi 1246793773 2494 LPEYLCPSRWRAVESMPRLGNGKIDRQALA 2523
Cdd:PRK07787 439 LSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
2051-2529 |
1.84e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 105.51 E-value: 1.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLD 2130
Cdd:PRK06178 48 QRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELN 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2131 DSGARIVIGWG----------------------------AAPAW-VPASVR--------WLDAESVLDVVSAYEEPPRVD 2173
Cdd:PRK06178 128 DAGAEVLLALDqlapvveqvraetslrhvivtsladvlpAEPTLpLPDSLRaprlaaagAIDLLPALRACTAPVPLPPPA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2174 VDAdtPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVlDLGEDASLATLSTVA----ADLGFTALFgALLSGRRVRLL 2249
Cdd:PRK06178 208 LDA--LAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAV-AVVGGEDSVFLSFLPefwiAGENFGLLF-PLFSGATLVLL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2250 paelafdaqalaahLQAHPVDCLKIVPSHLAGLLAAAGGTAV---------------LPRECLVTGGEALTGALVQQVRA 2314
Cdd:PRK06178 284 --------------ARWDAVAFMAAVERYRVTRTVMLVDNAVelmdhprfaeydlssLRQVRVVSFVKKLNPDYRQRWRA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2315 LAPTLRIVNHYGPTET-TVGILTC--TVPEEWPVEQGVPVGHPLAGNEAWVLD-RFGLPAPVGVAGELYLGGGNLSLGYW 2390
Cdd:PRK06178 350 LTGSVLAEAAWGMTEThTCDTFTAgfQDDDFDLLSQPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYW 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2391 QRAEQTAERFVAHplapdrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLA----- 2465
Cdd:PRK06178 430 NKPEATAEALRDG-------WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGrpdpd 502
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 2466 ---LPGANGVLQLGACIqgSLEGVAEALAQRLPEYLCPSrWRAVESMPRLGNGKIDRQALADLLQQD 2529
Cdd:PRK06178 503 kgqVPVAFVQLKPGADL--TAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKVRKQDLQALAEEL 566
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
3529-4010 |
1.98e-22 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 104.38 E-value: 1.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARR 3608
Cdd:cd05929 2 EARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3609 GFILEdsgvclsVSQRALAVELPGTALCLDDPFTraqlDAVEPGELPEVPTE---APAYLIYTSGSTGTPKGVVVTH--- 3682
Cdd:cd05929 82 CAIIE-------IKAAALVCGLFTGGGALDGLED----YEAAEGGSPETPIEdeaAGWKMLYSGGTTGRPKGIKRGLpgg 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3683 -RNVERLFTAATQTGrFSFDEHDVWS--LFHSHAFDFAVwelwGAWLYGGRAVLVPEAvcrQPDAFLDLLAEYGVTVLNQ 3759
Cdd:cd05929 151 pPDNDTLMAAALGFG-PGADSVYLSPapLYHAAPFRWSM----TALFMGGTLVLMEKF---DPEEFLRLIERYRVTFAQF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3760 TPSAF---YALQSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAeLVNMYGITETtVHVSFHRlSDEDLQSPTSr 3836
Cdd:cd05929 223 VPTMFvrlLKLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPI-IWEYYGGTEG-QGLTIIN-GEEWLTHPGS- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3837 IGSALPDlAVHVLDAAGQPVPLGVVGELVVEGdGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGD 3916
Cdd:cd05929 299 VGRAVLG-KVHILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAARNEGG---WSTLGDVGYLDEDGYLYLTDRRS 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3917 DQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQ---SLREALRALLPDYMLPRLIQ 3992
Cdd:cd05929 374 DMIISGGVNIYPQEIENALIAHPKVLDAAVVgVPDEELGQRVHAVVQPAPGADAGTAlaeELIAFLRDRLSRYKCPRSIE 453
|
490
....*....|....*...
gi 1246793773 3993 LLPALPLTANGKLDRKAL 4010
Cdd:cd05929 454 FVAELPRDDTGKLYRRLL 471
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
3663-4010 |
3.27e-22 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 101.79 E-value: 3.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3663 AYLIYTSGSTGTPKgvVVTHRNVERLFTAATQTGRFSFDEHDV----WSLFHSHAfdfAVWELWGAWLYGGRAVLVPEAV 3738
Cdd:cd05944 5 AAYFHTGGTTGTPK--LAQHTHSNEVYNAWMLALNSLFDPDDVllcgLPLFHVNG---SVVTLLTPLASGAHVVLAGPAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3739 CRQPDAFLD---LLAEYGVTVLNQTPSAFYALQSQAMRRELAlNVRAVVFGGEALePSRLQPWRERYPQAELVNMYGITE 3815
Cdd:cd05944 80 YRNPGLFDNfwkLVERYRITSLSTVPTVYAALLQVPVNADIS-SLRFAMSGAAPL-PVELRARFEDATGLPVVEGYGLTE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3816 TTvhvSFHRLSDEDLQSPTSRIGSALPDLAVH--VLDAAGQ---PVPLGVVGELVVEGDGVAQGYWQRpELTAERFVERG 3890
Cdd:cd05944 158 AT---CLVAVNPPDGPKRPGSVGLRLPYARVRikVLDGVGRllrDCAPDEVGEICVAGPGVFGGYLYT-EGNKNAFVADG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3891 gqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGE---GAWLMAYAVAADGA 3967
Cdd:cd05944 234 ---WLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAV--GQPDahaGELPVAYVQLKPGA 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1246793773 3968 EPDPQSLREALRALLPDY-MLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:cd05944 309 VVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
513-1057 |
4.17e-22 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 104.07 E-value: 4.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 513 SWPWPADELALDDKREPAprtvgnvvdAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCL 592
Cdd:PRK06155 8 LAARAVDPLPPSERTLPA---------MLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 593 PRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQGLAGF--------------------APSVAI 652
Cdd:PRK06155 79 GNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALeaadpgdlplpavwlldapaSVSVPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 653 AVDELKLDGAGENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQ 732
Cdd:PRK06155 159 GWSTAPLPPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 733 ILAAWSRGACVVARPDelLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGdvLPVALAQRWFE 812
Cdd:PRK06155 239 FFQALLAGATYVLEPR--FSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPG--VPAALHAAFRE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 813 lgldrRC--ALINAYGPTEATISSHyhrvQAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGG---IGLAEG 887
Cdd:PRK06155 315 -----RFgvDLLDGYGSTETNFVIA----VTHGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRAdepFAFATG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 888 YRGDAAASERRFAPLrlpsgeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAAGVV 967
Cdd:PRK06155 386 YFGMPEKTVEAWRNL---------WFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPV 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 968 GEGAAQRLVAwVECAGEDGfgqadlnqTDSDQTESERWhralCE-RLPAYMVPTQFVALPRLPRNASGKIDRRALPAPPV 1046
Cdd:PRK06155 457 PSELGEDEVM-AAVVLRDG--------TALEPVALVRH----CEpRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGV 523
|
570
....*....|....*..
gi 1246793773 1047 LAQ------AERTPPRT 1057
Cdd:PRK06155 524 TADtwdreaAGVQLPRS 540
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1644-1906 |
5.63e-22 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380472 [Multi-domain] Cd Length: 430 Bit Score: 102.39 E-value: 5.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1644 TVRRQ-PMLRTAIVWEGlSVPHQIVLADAAAPWQTLDWSALDDAaqdaQLQRWLADDAAQGVDFAHAPLARMSLIGRGGG 1722
Cdd:cd20484 47 FVLEQhPILKSVIEEED-GVPFQKIEPSKPLSFQEEDISSLKES----EIIAYLREKAKEPFVLENGPLMRVHLFSRSEQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1723 RYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGATLRLPPAPG-FQAYLDWrERQDLARQRG-----WWRERLSGyaG 1796
Cdd:cd20484 122 EHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPTLASSPAsYYDFVAW-EQDMLAGAEGeehraYWKQQLSG--T 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1797 TAALPAPVAAAHHPVQR---EECERRLSAHDSERLRAFCRERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPPEl 1873
Cdd:cd20484 199 LPILELPADRPRSSAPSfegQTYTRRLPSELSNQIKSFARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEE- 277
|
250 260 270
....*....|....*....|....*....|...
gi 1246793773 1874 aGVESMVGVFINTLPLRLRIDAGQPALDLLSAL 1906
Cdd:cd20484 278 -RFDSLIGYFINMLPIRSRILGEETFSDFIRKL 309
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
3529-4029 |
1.00e-21 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 103.50 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVS--------AEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAyVPVD 3600
Cdd:PRK07529 35 AARHPDAPALSflldadplDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIA-NPIN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3601 PHAPAARRGFILEDSG----VCLS------VSQRALAV--ELPG--TALCLD------------DPFTR----------- 3643
Cdd:PRK07529 114 PLLEPEQIAELLRAAGakvlVTLGpfpgtdIWQKVAEVlaALPElrTVVEVDlarylpgpkrlaVPLIRrkaharildfd 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3644 AQLDAvEPGELPEVPTEA----PAYLIYTSGSTGTPKGVVVTHRN-VERLFTAATQTGrfsFDEHDV----WSLFHSHAf 3714
Cdd:PRK07529 194 AELAR-QPGDRLFSGRPIgpddVAAYFHTGGTTGMPKLAQHTHGNeVANAWLGALLLG---LGPGDTvfcgLPLFHVNA- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3715 dfAVWELWGAWLYGGRAVLVPEAVCRQP---DAFLDLLAEYGVTVLNQTPSAFYALqsqaMRREL-ALNVRAV--VFGGE 3788
Cdd:PRK07529 269 --LLVTGLAPLARGAHVVLATPQGYRGPgviANFWKIVERYRINFLSGVPTVYAAL----LQVPVdGHDISSLryALCGA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3789 ALEPSRLqpwRERYPQA---ELVNMYGITETTVHVSFHRLSDEdlqsptSRIGSA---LP--DLAVHVLDAAG---QPVP 3857
Cdd:PRK07529 343 APLPVEV---FRRFEAAtgvRIVEGYGLTEATCVSSVNPPDGE------RRIGSVglrLPyqRVRVVILDDAGrylRDCA 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3858 LGVVGELVVEGDGVAQGYwqrpeLTAERfvERG---GQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAK 3934
Cdd:PRK07529 414 VDEVGVLCIAGPNVFSGY-----LEAAH--NKGlwlEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEA 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3935 IASLPQVSDAAVTveGQGE---GAWLMAYAVAADGAEPDPQSLREALRALLPD-YMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK07529 487 LLRHPAVALAAAV--GRPDahaGELPVAYVQLKPGASATEAELLAFARDHIAErAAVPKHVRILDALPKTAVGKIFKPAL 564
|
570
....*....|....*....
gi 1246793773 4011 PKPETQDRDEGVLESASER 4029
Cdd:PRK07529 565 RRDAIRRVLRAALRDAGVE 583
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
2063-2634 |
2.12e-21 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 102.80 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2063 TYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQ-HPDARQIAVLDDSGARIVIGWG 2141
Cdd:PRK06060 32 THGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPElHRDDHALAARNTEPALVVTSDA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2142 AAPAWVPASVrwLDAESVLDVVSAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGV------LPVLDL 2215
Cdd:PRK06060 112 LRDRFQPSRV--AEAAELMSEAARVAPGGYEPMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMcrkalrLTPEDT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2216 GEDASLATLstvAADLGFTALFgALLSGRRVRLLPAELAFDAQALAAHLQAHPVdcLKIVPSHLAGLLAAAGGTAVLPRE 2295
Cdd:PRK06060 190 GLCSARMYF---AYGLGNSVWF-PLATGGSAVINSAPVTPEAAAILSARFGPSV--LYGVPNFFARVIDSCSPDSFRSLR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2296 CLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVpEEWPVEQgvpVGHPLAGNEAWVLDRFGLPAPVGVA 2375
Cdd:PRK06060 264 CVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTFVSNRV-DEWRLGT---LGRVLPPYEIRVVAPDGTTAGPGVE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2376 GELYLGGGNLSLGYWQRAEqtaerfvahPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQL 2455
Cdd:PRK06060 340 GDLWVRGPAIAKGYWNRPD---------SPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIED 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2456 PGVEVAAVLALPGANGVLQL--------GACIQGS-LEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL---- 2522
Cdd:PRK06060 411 EAVAEAAVVAVRESTGASTLqaflvatsGATIDGSvMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALrkqs 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2523 --------------ADLLQQDDADSSAEAID------ETPVNEVLRELWQ---------------KLLGREHIGAHDN-- 2565
Cdd:PRK06060 491 ptkpiwelsltepgSGVRAQRDDLSASNMTIaggndgGATLRERLVALRQerqrlvvdavcaeaaKMLGEPDPWSVDQdl 570
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 2566 -FFALGGDSILSLQLVAR-ARQAGLALMPRQLYDHPTLAGLS----AQVQASSPAPATikPATEAEQSFGLTPIQ 2634
Cdd:PRK06060 571 aFSELGFDSQMTVTLCKRlAAVTGLRLPETVGWDYGSISGLAqyleAELAGGHGRLKS--AGPVNSGATGLWAIE 643
|
|
| NRPS-para261 |
TIGR01720 |
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately ... |
1441-1585 |
2.13e-21 |
|
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately downstream from a condensation domain (pfam00668), and is followed primarily by the end of the molecule or another condensation domain (in a few cases it is followed by pfam00501, an AMP-binding module). The converse is not true, pfam00668 domains are not always followed by this domain. This implicates this domain in possible post-condensation modification events. This model is 171 amino acids long and contains three very highly conserved regions. At the N-terminus is a nearly invariant lysine (position 11) followed by xxxRxxPxxGxGYG in which the proline and the first glycine are invariant. This is followed approximately 22 residues later by the motif FNYLG. Near the C-terminus of the domain is the sequence TxSD where the serine and aspartate are nearly invariant.
Pssm-ID: 273774 [Multi-domain] Cd Length: 153 Bit Score: 93.49 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1441 AQIGALKEQIRALARRGLDYMPL----VASARIPALPAGQLLFNYHGVVDAGAHPAFeVEPRTLASGNGAD--NPPGALV 1514
Cdd:TIGR01720 4 RLIKAVKEQLRRIPNKGVGYGVLryltEPEEKLAASPQPEISFNYLGQFDADSNDEL-FQPSSYSPGEAISpeSPRPYAL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 1515 EINARVQAGRLGLVWNYAGEAYDAATIEAWSQAFAAELAALVAHCLQPGSGALTASDLPQARLQADEFALL 1585
Cdd:TIGR01720 83 EINAMIEDGELTLTWSYPTQLFSEDTIEQLADRFKEALEALIAHCAGKEGGGLTPSDFSLKDLTQDELDEL 153
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
2173-2525 |
2.53e-21 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 103.08 E-value: 2.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2173 DVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGE-DASLATLSTVAAdLGFTA-LFGALLSGRRVRLLP 2250
Cdd:PRK08633 778 TFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNdDVILSSLPFFHS-FGLTVtLWLPLLEGIKVVYHP 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2251 aelafdaqalaahlqaHPVDCLKIVPSHLAGLLAAAGGTAVLPRECL----------------VTGGEALTGALVQQVRa 2314
Cdd:PRK08633 857 ----------------DPTDALGIAKLVAKHRATILLGTPTFLRLYLrnkklhplmfaslrlvVAGAEKLKPEVADAFE- 919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2315 LAPTLRIVNHYGPTETTvGILTCTVPEEwpVEQGVP---------VGHPLAGNEAWVLD-RFGLPAPVGVAGELYLGGGN 2384
Cdd:PRK08633 920 EKFGIRILEGYGATETS-PVASVNLPDV--LAADFKrqtgskegsVGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQ 996
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2385 LSLGYWQRAEQTAErfVAHPLAPDRlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVE--VAA 2462
Cdd:PRK08633 997 VMKGYLGDPEKTAE--VIKDIDGIG-WYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEevVFA 1073
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 2463 VLALP----GANGVLqLGACIQGSLEGVAEALAQ-RLPEYLCPSRWRAVESMPRLGNGKIDRQALADL 2525
Cdd:PRK08633 1074 VTAVPdekkGEKLVV-LHTCGAEDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKEL 1140
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
2630-3043 |
3.03e-21 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380453 [Multi-domain] Cd Length: 427 Bit Score: 99.79 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2630 LTPIQ--HWFFEQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARFQRDAAGQWQQTLGDWQADRFA--- 2704
Cdd:cd19066 4 LSPMQrgMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVRFRIEiid 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2705 ---HREADAGQREDLLAQWQAGLSFDGALLRVLALPDPQDGDTRVLFAAHHLLVDAVSWGIIVDDLQHAY--AERRAGRS 2779
Cdd:cd19066 84 lrnLADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYdaAERQKPTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2780 PALAAEACGFGAWQAALRQLSA--ATLDGWRSYWRAQAADAEAIALPwQDSDNRYADTVHLHDRFERDWTERlLTQTARA 2857
Cdd:cd19066 164 PPPVGSYADYAAWLEKQLESEAaqADLAYWTSYLHGLPPPLPLPKAK-RPSQVASYEVLTLEFFLRSEETKR-LREVARE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2858 YGNEPQEVLLTALALALRDGGDAATLWVEMEGHGRDDlgagLDLSRTVGWFTARYPLALHLPAGEDLGAALRSTKDRMRA 2937
Cdd:cd19066 242 SGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPD----EAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSRE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2938 VPDRGLGFGVLRYLH----GELAELPVPQVCFNYLGQlraGERDGWALCEEPDGGGRAGGNRRRHLLDVNAM-LVDGELR 3012
Cdd:cd19066 318 AIEHQRVPFIELVRHlgvvPEAPKHPLFEPVFTFKNN---QQQLGKTGGFIFTTPVYTSSEGTVFDLDLEASeDPDGDLL 394
|
410 420 430
....*....|....*....|....*....|.
gi 1246793773 3013 LDWAWPQDAASREAMQALSRRYLAVLRELIA 3043
Cdd:cd19066 395 LRLEYSRGVYDERTIDRFAERYMTALRQLIE 425
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
3522-4009 |
3.28e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 101.73 E-value: 3.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3522 VSRFAE-----IARRYparIAVSAE-DG---ELDYATLDRRSSQLATLLiRQGAGPGQRVGLCLPRGCDLLVALLAILKT 3592
Cdd:PRK07769 27 VERWAKvrgdkLAYRF---LDFSTErDGvarDLTWSQFGARNRAVGARL-QQVTKPGDRVAILAPQNLDYLIAFFGALYA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3593 GAAYVPV-DPHAP--AARRGFILEDS--GVCLSVSQRALAVE-----LPGTalclDDPFTRAqLDAVePGEL------PE 3656
Cdd:PRK07769 103 GRIAVPLfDPAEPghVGRLHAVLDDCtpSAILTTTDSAEGVRkffraRPAK----ERPRVIA-VDAV-PDEVgatwvpPE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3657 VPTEAPAYLIYTSGSTGTPKGVVVTHRNVErlfTAATQT-GRFSFDEHD---VW-SLFHshafDFAVWELWGAWLYGGR- 3730
Cdd:PRK07769 177 ANEDTIAYLQYTSGSTRIPAGVQITHLNLP---TNVLQViDALEGQEGDrgvSWlPFFH----DMGLITVLLPALLGHYi 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3731 AVLVPEAVCRQPDAFLDLLA---EYGVTVLNQTPSafYALQSQAMR-----RELAL---NVRAVVFGGEALEPSRLQPWR 3799
Cdd:PRK07769 250 TFMSPAAFVRRPGRWIRELArkpGGTGGTFSAAPN--FAFEHAAARglpkdGEPPLdlsNVKGLLNGSEPVSPASMRKFN 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3800 ERY-----PQAELVNMYGITETTVHVSFHRLSDE-------------------DLQSPTS--RIGS---ALPDLAVHVLD 3850
Cdd:PRK07769 328 EAFapyglPPTAIKPSYGMAEATLFVSTTPMDEEptviyvdrdelnagrfvevPADAPNAvaQVSAgkvGVSEWAVIVDP 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3851 AAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGGQR--------------FYRSGDLGRYrADGSLEYRGRGD 3916
Cdd:PRK07769 408 ETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFQNILKSRlseshaegapddalWVRTGDYGVY-FDGELYITGRVK 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3917 DQVKLRGYR----------------IEPGEIAA---KIASLPQV----SDAAVTVEGQGEGAWLMAYAVAADGA-EPDPQ 3972
Cdd:PRK07769 487 DLVIIDGRNhypqdleytaqeatkaLRTGYVAAfsvPANQLPQVvfddSHAGLKFDPEDTSEQLVIVAERAPGAhKLDPQ 566
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1246793773 3973 SLREALRALLPDY--MLPRLIQLLPA--LPLTANGKLDRKA 4009
Cdd:PRK07769 567 PIADDIRAAIAVRhgVTVRDVLLVPAgsIPRTSSGKIARRA 607
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
2061-2522 |
3.64e-21 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 99.34 E-value: 3.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2061 SWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSgarivigw 2140
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDS-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2141 gaapawvpasvrwldaesvldvvsayeepprvDVDADTPAYLIYTSGSTGTPKGVVVSQGNlaNYVAGVLPVLDLG---E 2217
Cdd:cd05912 73 --------------------------------DVKLDDIATIMYTSGTTGKPKGVQQTFGN--HWWSAIGSALNLGlteD 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2218 DASLATLSTVAADlGFTALFGALLSGRRVRLLPaelAFDAQALAAHLQAHPVDCLKIVPShlagllAAAGGTAVLPR--- 2294
Cdd:cd05912 119 DNWLCALPLFHIS-GLSILMRSVIYGMTVYLVD---KFDAEQVLHLINSGKVTIISVVPT------MLQRLLEILGEgyp 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2295 ---ECLVTGGEALTGALVQQVRALAptLRIVNHYGPTETTVGILTCTvPEEWPVEQGvPVGHPLAGNEAWVLDRFGLPAP 2371
Cdd:cd05912 189 nnlRCILLGGGPAPKPLLEQCKEKG--IPVYQSYGMTETCSQIVTLS-PEDALNKIG-SAGKPLFPVELKIEDDGQPPYE 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2372 VgvaGELYLGGGNLSLGYWQRAEQTAERFVAHplapdrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQV 2451
Cdd:cd05912 265 V---GEILLKGPNVTKGYLNRPDATEESFENG-------WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEV 334
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 2452 LAQLPGVEVAAVLALP----GANGVLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:cd05912 335 LLSHPAIKEAGVVGIPddkwGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
2329-2616 |
4.28e-21 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 97.13 E-value: 4.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2329 ETTVGILTCTVPEEWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPD 2408
Cdd:COG3433 1 IAIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2409 RLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQGSLEGVAE 2488
Cdd:COG3433 81 QADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2489 ALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQA-----LADLLQQDDADSSAEAIDETPVNEVLRELWQKLLG--REHIG 2561
Cdd:COG3433 161 ALAALDKVPPDVVAASAVVALDALLLLALKVVAraapaLAAAEALLAAASPAPALETALTEEELRADVAELLGvdPEEID 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 2562 AHDNFFALGGDSILSLQLVARARQAGLALMPRQLYDHPTLAGLSAQVQASSPAPA 2616
Cdd:COG3433 241 PDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
2052-2518 |
5.07e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 100.34 E-value: 5.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDD 2131
Cdd:PRK07798 19 RVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGAR-------------------------IVIGWGAAPAWVPASVRWLDAesvldVVSAYEEPPRVDVDADTpAYLIYTS 2186
Cdd:PRK07798 99 SDAValvyerefaprvaevlprlpklrtlVVVEDGSGNDLLPGAVDYEDA-----LAAGSPERDFGERSPDD-LYLLYTG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2187 GSTGTPKGVV-------VSQGNLANYVAGVlPVLDLGEDASLATLST-----VAADL----GFTALFGALLSGRRVRLLP 2250
Cdd:PRK07798 173 GTTGMPKGVMwrqedifRVLLGGRDFATGE-PIEDEEELAKRAAAGPgmrrfPAPPLmhgaGQWAAFAALFSGQTVVLLP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2251 AElAFDaqalaahlqahPVDCLKIVPSHLAGLLAAA-------GGTAVLPRE--------CLVTGGEALTGALVQQVRAL 2315
Cdd:PRK07798 252 DV-RFD-----------ADEVWRTIEREKVNVITIVgdamarpLLDALEARGpydlsslfAIASGGALFSPSVKEALLEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2316 APTLRIVNHYGPTETTVGILTCTVPEEwpveqgVPVGHPL--AGNEAWVLDRFGLPAPVGVAGELYLG-GGNLSLGYWQR 2392
Cdd:PRK07798 320 LPNVVLTDSIGSSETGFGGSGTVAKGA------VHTGGPRftIGPRTVVLDEDGNPVEPGSGEIGWIArRGHIPLGYYKD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2393 AEQTAERFvahPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGAN-- 2470
Cdd:PRK07798 394 PEKTAETF---PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERwg 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 2471 ----GVLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKID 2518
Cdd:PRK07798 471 qevvAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
2054-2527 |
5.19e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 100.35 E-value: 5.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2054 AVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSG 2133
Cdd:PRK06145 20 ALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2134 ARIVI--GWGAAPAWVPASVRWLDAESVLDV---VSAYEEPPRVDVDADTPAY-LIYTSGSTGTPKGVVVSQGNLANYVA 2207
Cdd:PRK06145 100 AKLLLvdEEFDAIVALETPKIVIDAAAQADSrrlAQGGLEIPPQAAVAPTDLVrLMYTSGTTDRPKGVMHSYGNLHWKSI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2208 GVLPVLDLGEDASLATLSTV----AADL-GFTALF-GALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAG 2281
Cdd:PRK06145 180 DHVIALGLTASERLLVVGPLyhvgAFDLpGIAVLWvGGTLRIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2282 LLAAAGGTAVlpreclVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPEEwpVEQGVPVGHPLAGNEAW 2361
Cdd:PRK06145 260 RFDLDSLAWC------IGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGRE--IEKIGSTGRALAHVEIR 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2362 VLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHplapdrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGY 2441
Cdd:PRK06145 332 IADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGD-------WFRSGDVGYLDEEGFLYLTDRKKDMIISGGE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2442 RVELGEVEQVLAQLPGVEVAAVLALPGANG--------VLQLGACIqgSLEGVAEALAQRLPEYLCPSRWRAVESMPRLG 2513
Cdd:PRK06145 405 NIASSEVERVIYELPEVAEAAVIGVHDDRWgeritavvVLNPGATL--TLEALDRHCRQRLASFKVPRQLKVRDELPRNP 482
|
490
....*....|....
gi 1246793773 2514 NGKIDRQALADLLQ 2527
Cdd:PRK06145 483 SGKVLKRVLRDELN 496
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
598-1041 |
6.10e-21 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 100.43 E-value: 6.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 598 WYCLLLGAWRAGLSVIPLDTEwpQARRAE----VVAASGCDAVLTDAQGLAGFAP--------SVAIAVDELKLDGAGEN 665
Cdd:cd05906 82 WACVLAGFVPAPLTVPPTYDE--PNARLRklrhIWQLLGSPVVLTDAELVAEFAGletlsglpGIRVLSIEELLDTAADH 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 666 gSGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGL------AVDTTLEQI 733
Cdd:cd05906 160 -DLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLnwvpldHVGGLvelhlrAVYLGCQQV 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 734 LAAwsrgacvvarPDELL-EPQRFLAFLSERAITVTdLAPAYA----NELVRASVADDWRDLALRCLVVGGDVLPVALAQ 808
Cdd:cd05906 239 HVP----------TEEILaDPLRWLDLIDRYRVTIT-WAPNFAfallNDLLEEIEDGTWDLSSLRYLVNAGEAVVAKTIR 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 809 RWFEL----GLdRRCALINAYGPTE----ATISSHYHRVQAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALG 880
Cdd:cd05906 308 RLLRLlepyGL-PPDAIRPAFGMTEtcsgVIYSRSFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVR 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 881 GIGLAEGYRGDAAASERRFaplrLPSGeslrMYRSGDrVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR 960
Cdd:cd05906 387 GPVVTKGYYNNPEANAEAF----TEDG----WFRTGD-LGFLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVE 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 961 ---AAAAGVVGEGAAQRLVAWVECAGEDGFGQADLNQTDSDQTESERWHRAlcerlPAYMVPtqfvaLPR--LPRNASGK 1035
Cdd:cd05906 458 psfTAAFAVRDPGAETEELAIFFVPEYDLQDALSETLRAIRSVVSREVGVS-----PAYLIP-----LPKeeIPKTSLGK 527
|
....*.
gi 1246793773 1036 IDRRAL 1041
Cdd:cd05906 528 IQRSKL 533
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
2047-2517 |
6.41e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 100.24 E-value: 6.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2047 QMPAQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQI 2126
Cdd:PRK07786 28 LMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2127 AVLDDSGARIVIGwGAAPAWVPASVRwlDAESVLDVV-------------------SAYEEPPRVDVDADTPAYLIYTSG 2187
Cdd:PRK07786 108 FLVSDCGAHVVVT-EAALAPVATAVR--DIVPLLSTVvvaggssddsvlgyedllaEAGPAHAPVDIPNDSPALIMYTSG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2188 STGTPKGVVVSQGNLANYVAGVLPV--LDLGEDASLAT--LSTVAAdLGFTALFgaLLSGRRVRLLPAElAFDAQALAAH 2263
Cdd:PRK07786 185 TTGRPKGAVLTHANLTGQAMTCLRTngADINSDVGFVGvpLFHIAG-IGSMLPG--LLLGAPTVIYPLG-AFDPGQLLDV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2264 LQAHPVDCLKIVPSHLAGLLAAAGgtaVLPRE----CLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVgiLTCTV 2339
Cdd:PRK07786 261 LEAEKVTGIFLVPAQWQAVCAEQQ---ARPRDlalrVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSP--VTCML 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2340 PEEWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFvahplapDRLLYRSGDLAR 2419
Cdd:PRK07786 336 LGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF-------AGGWFHSGDLVR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2420 LDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPG-VEVA--------------AVLALPGANGVLqlgaciqgSLE 2484
Cdd:PRK07786 409 QDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDiVEVAvigradekwgevpvAVAAVRNDDAAL--------TLE 480
|
490 500 510
....*....|....*....|....*....|...
gi 1246793773 2485 GVAEALAQRLPEYLCPSRWRAVESMPRLGNGKI 2517
Cdd:PRK07786 481 DLAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1625-1934 |
7.32e-21 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380471 [Multi-domain] Cd Length: 430 Bit Score: 98.87 E-value: 7.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1625 VAELDGEIDAAALAQAWQQTVRRQPMLRTAIVwEGLSVPHQIVLADAAAPWQTLDWSalDDAAQDAQLQRWLADDAAQGV 1704
Cdd:cd20483 29 VCHIKGKPDVNLLQKALSELVRRHEVLRTAYF-EGDDFGEQQVLDDPSFHLIVIDLS--EAADPEAALDQLVRNLRRQEL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1705 DFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGATLRLPPAPGFQaYLD---WRER--QD 1779
Cdd:cd20483 106 DIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGRDLATVPPPPVQ-YIDftlWHNAllQS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1780 LARQR--GWWRERLSGYAGTAALPAPVAAAHHPV---QREECERRLSAHDSERLRAFCRERGCT-----LSDLIAMVWgl 1849
Cdd:cd20483 185 PLVQPllDFWKEKLEGIPDASKLLPFAKAERPPVkdyERSTVEATLDKELLARMKRICAQHAVTpfmflLAAFRAFLY-- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1850 anaRYGNHDDVVLGATRSGRP-PElagVESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAENEAVGLGEILadS 1928
Cdd:cd20483 263 ---RYTEDEDLTIGMVDGDRPhPD---FDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCLEAYEHSAVPFDYIV--D 334
|
....*.
gi 1246793773 1929 GLDADR 1934
Cdd:cd20483 335 ALDVPR 340
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
3529-4010 |
7.91e-21 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 100.05 E-value: 7.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIA-VSAEDGE-LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAA 3606
Cdd:PLN02330 38 AELYADKVAfVEAVTGKaVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALES 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3607 RRGFILEDSGVCLSVS-----QRALAVELPGTAL---CLDDPFTRAQL-----DAVEPGELPEVPTEAPAYLIYTSGSTG 3673
Cdd:PLN02330 118 EIKKQAEAAGAKLIVTndtnyGKVKGLGLPVIVLgeeKIEGAVNWKELleaadRAGDTSDNEEILQTDLCALPFSSGTTG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3674 TPKGVVVTHRNV-----ERLFTAATQT-------GRFSFdehdvwslFHShafdFAVWELWGAWLYG-GRAVLVPEAVCR 3740
Cdd:PLN02330 198 ISKGVMLTHRNLvanlcSSLFSVGPEMigqvvtlGLIPF--------FHI----YGITGICCATLRNkGKVVVMSRFELR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3741 qpdAFLDLLAEYGVTVLNQTPSAFYALQSQAMRREL---ALNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETT 3817
Cdd:PLN02330 266 ---TFLNALITQEVSFAPIVPPIILNLVKNPIVEEFdlsKLKLQAIMTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHS 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3818 VHVSFHrlSDEDLQSPTSR---IGSALPDLAVHVLDA-AGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqr 3893
Cdd:PLN02330 343 CITLTH--GDPEKGHGIAKknsVGFILPNLEVKFIDPdTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDG--- 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3894 FYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQ 3972
Cdd:PLN02330 418 WLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVpLPDEEAGEIPAACVVINPKAKESEE 497
|
490 500 510
....*....|....*....|....*....|....*...
gi 1246793773 3973 SLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PLN02330 498 DILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
3552-4009 |
8.07e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 100.07 E-value: 8.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3552 RRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVdpHAPAARRGFIL--EDSGVCLSVSQRALAVe 3629
Cdd:PRK07768 37 ERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTML--HQPTPRTDLAVwaEDTLRVIGMIGAKAVV- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3630 lpgtalcLDDPF---------------TRAQLDAVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVERlfTAATQ 3694
Cdd:PRK07768 114 -------VGEPFlaaapvleekgirvlTVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYA--NAEAM 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3695 TGRFSFD-EHDV---W-SLFHSHAFdfaVWELWGAWLYGGRAVLV-PEAVCRQPDAFLDLLAEYGVTVLnQTPSAFYALQ 3768
Cdd:PRK07768 185 FVAAEFDvETDVmvsWlPLFHDMGM---VGFLTVPMYFGAELVKVtPMDFLRDPLLWAELISKYRGTMT-AAPNFAYALL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3769 SQAMRR---ELALN---VRAVVFGGEALEPSRLQPW-----RERYPQAELVNMYGITETTVHVSFHRLS--------DED 3829
Cdd:PRK07768 261 ARRLRRqakPGAFDlssLRFALNGAEPIDPADVEDLldagaRFGLRPEAILPAYGMAEATLAVSFSPCGaglvvdevDAD 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3830 LQSPTSR--------------IGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYwqrpeLTAERFVE-RGGQRF 3894
Cdd:PRK07768 341 LLAALRRavpatkgntrrlatLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY-----LTMDGFIPaQDADGW 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3895 YRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQV-SDAAVTVE----GQGEGawlmaYAVAADGAEP 3969
Cdd:PRK07768 416 LDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVrPGNAVAVRldagHSREG-----FAVAVESNAF 490
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1246793773 3970 DPQSLREALRALLPDYML------PRLIQLLPA--LPLTANGKLDRKA 4009
Cdd:PRK07768 491 EDPAEVRRIRHQVAHEVVaevgvrPRNVVVLGPgsIPKTPSGKLRRAN 538
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
2056-2426 |
1.27e-20 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 99.24 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2056 EEGAASWTYAQLRAAAGRIAGALDAVGvQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPL---DPQHPDARQIAVLDDS 2132
Cdd:cd05931 19 GGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLpppTPGRHAERLAAILADA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2133 GARIVIGWGAAPAWVPASV---------RWLDAESVLDVVSAYEEPPrvDVDADTPAYLIYTSGSTGTPKGVVVSQGNLA 2203
Cdd:cd05931 98 GPRVVLTTAAALAAVRAFAasrpaagtpRLLVVDLLPDTSAADWPPP--SPDPDDIAYLQYTSGSTGTPKGVVVTHRNLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2204 NYVAGVLPVLDLGEDASLATLSTVAADLG-FTALFGALLSGRRVRLLPAE-------------------------LAFDA 2257
Cdd:cd05931 176 ANVRQIRRAYGLDPGDVVVSWLPLYHDMGlIGGLLTPLYSGGPSVLMSPAaflrrplrwlrlisryratisaapnFAYDL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2258 -QALAAHLQAHPVD--CLKIV-----PSHLAGLLAAAGGTAV--LPREC------------LVTGGEALTGALVQQVRAL 2315
Cdd:cd05931 256 cVRRVRDEDLEGLDlsSWRVAlngaePVRPATLRRFAEAFAPfgFRPEAfrpsyglaeatlFVSGGPPGTGPVVLRVDRD 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2316 APTLRIVNHYGPTETTVGILTCtvpeewpveqgvpvGHPLAGNEAWVLDRFGL-PAPVGVAGELYLGGGNLSLGYWQRAE 2394
Cdd:cd05931 336 ALAGRAVAVAADDPAARELVSC--------------GRPLPDQEVRIVDPETGrELPDGEVGEIWVRGPSVASGYWGRPE 401
|
410 420 430
....*....|....*....|....*....|....*..
gi 1246793773 2395 QTAERFVAHPLAPDRLLYRSGDLARL-DGE----GRI 2426
Cdd:cd05931 402 ATAETFGALAATDEGGWLRTGDLGFLhDGElyitGRL 438
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
544-1041 |
1.30e-20 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 98.85 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 544 AADEFPERAAL-ETAQGR-LSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDtewPQ 621
Cdd:cd05904 14 FASAHPSRPALiDAATGRaLTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTAN---PL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 622 ARRAEV---VAASGCDAVLTDAQG---LAGFAPSVaIAVDELKLDGAGE----NGSGENAAPNQ------LAYILYTSGS 685
Cdd:cd05904 91 STPAEIakqVKDSGAKLAFTTAELaekLASLALPV-VLLDSAEFDSLSFsdllFEADEAEPPVVvikqddVAALLYSSGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 686 TGIPKGVEVGHA--ALAAHIDAAAEALALSADDRVL------HVAGLAVDTtleqiLAAWSRGACVVARPDelLEPQRFL 757
Cdd:cd05904 170 TGRSKGVMLTHRnlIAMVAQFVAGEGSNSDSEDVFLcvlpmfHIYGLSSFA-----LGLLRLGATVVVMPR--FDLEELL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 758 AFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRwFElgldRR---CALINAYGPTEATISS 834
Cdd:cd05904 243 AAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEA-FR----AKfpnVDLGQGYGMTESTGVV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 835 HYHRVQAIDASRPVPLGQLLPGRIAAVLD-AHGRIVPRGVCGELALGGIGLAEGYRGDAAASERrfaplrlpSGESLRMY 913
Cdd:cd05904 318 AMCFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAA--------TIDKEGWL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 914 RSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVG---EGAAQRLVAWVecagedgfgqa 990
Cdd:cd05904 390 HTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAA--VIPypdEEAGEVPMAFV----------- 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 991 dLNQTDSDQTESErwhralcerlpaYMvptQFVA--------------LPRLPRNASGKIDRRAL 1041
Cdd:cd05904 457 -VRKPGSSLTEDE------------IM---DFVAkqvapykkvrkvafVDAIPKSPSGKILRKEL 505
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
2179-2519 |
2.24e-20 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 95.79 E-value: 2.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2179 PAYLIYTSGSTGTPKGVVVSQGNL-ANYVAGVLPVLDLGEDASLATLSTVAADLGF----TALF--GALLSGRRVRLLPA 2251
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANKTFfAVPDILQKEGLNWVVGDVTYLPLPATHIGGLwwilTCLIhgGLCVTGGENTTYKS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2252 ---ELAFDAqalaahlqahpVDCLKIVPSHLAGLLAAAGGT-AVLPR-ECLVTGGEALTGALVQqVRALAPTLRIVNHYG 2326
Cdd:cd17635 83 lfkILTTNA-----------VTTTCLVPTLLSKLVSELKSAnATVPSlRLIGYGGSRAIAADVR-FIEATGLTNTAQVYG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2327 PTETTVgilTCTVPEEWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVahpla 2406
Cdd:cd17635 151 LSETGT---ALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI----- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2407 pDRLLYrSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGAN--GVLQLGACIQGSLE 2484
Cdd:cd17635 223 -DGWVN-TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEfgELVGLAVVASAELD 300
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1246793773 2485 -----GVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDR 2519
Cdd:cd17635 301 enairALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
2053-2517 |
3.60e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 97.70 E-value: 3.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2053 VAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDpQHPDARQIA-VLDD 2131
Cdd:PRK08316 28 TALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVN-FMLTGEELAyILDH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVI---------------------GWGAAPAWVPASVRWLDAESVLDvvSAYEEPPRVDVDADTPAYLIYTSGSTG 2190
Cdd:PRK08316 107 SGARAFLvdpalaptaeaalallpvdtlILSLVLGGREAPGGWLDFADWAE--AGSVAEPDVELADDDLAQILYTSGTES 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2191 TPKGVVVSQGNL-ANYVAGVLpVLDLG-EDASLATLStvaadLGFTA-----LFGALLSGRRVRLLPAelafdaqalaah 2263
Cdd:PRK08316 185 LPKGAMLTHRALiAEYVSCIV-AGDMSaDDIPLHALP-----LYHCAqldvfLGPYLYVGATNVILDA------------ 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2264 lqAHPVDCLKIVPSHLAG------------LLAAAGGTAVLP--RECLVtGGEALTGALVQQVRALAPTLRIVNHYGPTE 2329
Cdd:PRK08316 247 --PDPELILRTIEAERITsffapptvwislLRHPDFDTRDLSslRKGYY-GASIMPVEVLKELRERLPGLRFYNCYGQTE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2330 ttVGILTcTV--PEEwPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHplap 2407
Cdd:PRK08316 324 --IAPLA-TVlgPEE-HLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGG---- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2408 drlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI---QGSLE 2484
Cdd:PRK08316 396 ---WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVvpkAGATV 472
|
490 500 510
....*....|....*....|....*....|....*.
gi 1246793773 2485 GVAEALA---QRLPEYLCPSRWRAVESMPRLGNGKI 2517
Cdd:PRK08316 473 TEDELIAhcrARLAGFKVPKRVIFVDELPRNPSGKI 508
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
2056-2535 |
3.97e-20 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 98.33 E-value: 3.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2056 EEGAA-SWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGA 2134
Cdd:cd05968 85 EDGTSrTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2135 RIVI-----------------------------------GWGAAPAWVPASVRWLDAEsvldVVSAYEEPPRVDvdADTP 2179
Cdd:cd05968 165 KALItadgftrrgrevnlkeeadkacaqcptvekvvvvrHLGNDFTPAKGRDLSYDEE----KETAGDGAERTE--SEDP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2180 AYLIYTSGSTGTPKGVV-VSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAq 2258
Cdd:cd05968 239 LMIIYTSGTTGKPKGTVhVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLYDGAPDHPK- 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2259 alaahlqahPVDCLKIVPSHLAGLLAAaggTAVLPRECLVTGGEALTGALVQQVRALAPT-------------------- 2318
Cdd:cd05968 318 ---------ADRLWRMVEDHEITHLGL---SPTLIRALKPRGDAPVNAHDLSSLRVLGSTgepwnpepwnwlfetvgkgr 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2319 LRIVNHYGPTETTVGILTCTvpeewPVEQGVPVGH--PLAGNEAWVLDRFGLPAPVGVaGELYLGGG--NLSLGYWQRAE 2394
Cdd:cd05968 386 NPIINYSGGTEISGGILGNV-----LIKPIKPSSFngPVPGMKADVLDESGKPARPEV-GELVLLAPwpGMTRGFWRDED 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2395 QTAERFVahplapDRL--LYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPG---- 2468
Cdd:cd05968 460 RYLETYW------SRFdnVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHpvkg 533
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 2469 ----ANGVLQLGACIQGSL-EGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL-ADLLQQDDADSSA 2535
Cdd:cd05968 534 eaivCFVVLKPGVTPTEALaEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIrAAYLGKELGDLSS 606
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
3082-3400 |
6.88e-20 |
|
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.
Pssm-ID: 380468 [Multi-domain] Cd Length: 440 Bit Score: 96.01 E-value: 6.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3082 PLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFavqglPSPRQLPHRQVSLPLAEQ 3161
Cdd:cd19546 6 PATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTF-----PGDGGDVHQRILDADAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3162 DWSGLEPAqARSRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAALRESR 3241
Cdd:cd19546 81 PELPVVPA-TEEELPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARREGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3242 TPQ-LPAAPPFRDYLHW----LRGQDEAAAR-----AFWREQLTGLEPAALPEATEPAEGYASstRRFDLAAASAWAQSH 3311
Cdd:cd19546 160 APErAPLPLQFADYALWerelLAGEDDRDSLigdqiAYWRDALAGAPDELELPTDRPRPVLPS--RRAGAVPLRLDAEVH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3312 ----------GLTASSLLQGALALVLQRYYGRDDFALGiTIAGRPPELAGVERMLGVFINSVPLRVTPAGEATPAPWLQA 3381
Cdd:cd19546 238 arlmeaaesaGATMFTVVQAALAMLLTRLGAGTDVTVG-TVLPRDDEEGDLEGMVGPFARPLALRTDLSGDPTFRELLGR 316
|
330
....*....|....*....
gi 1246793773 3382 LQQRNLDLRTHGYLPLAQI 3400
Cdd:cd19546 317 VREAVREARRHQDVPFERL 335
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
2063-2517 |
6.93e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 96.95 E-value: 6.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2063 TYAQLRAAAGRIAGAL-DAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVI--- 2138
Cdd:PRK08314 37 SYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIvgs 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2139 ------------------------------GWGAAPAW--VPASVRWLDAESVL---DVVSAYEEPPRVDVDADTPAYLI 2183
Cdd:PRK08314 117 elapkvapavgnlrlrhvivaqysdylpaePEIAVPAWlrAEPPLQALAPGGVVawkEALAAGLAPPPHTAGPDDLAVLP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2184 YTSGSTGTPKGVVVSQGNL-ANYVAGVLPVLDLGEDASLATLSTVAAdLGF-TALFGALLSGRRVRLLP---AELAFDAQ 2258
Cdd:PRK08314 197 YTSGTTGVPKGCMHTHRTVmANAVGSVLWSNSTPESVVLAVLPLFHV-TGMvHSMNAPIYAGATVVLMPrwdREAAARLI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2259 alaahlqahpvdclkivpSHLAGLLAAAGGTAVL-----PR---------ECLVTGGEALTGALVQQVRALApTLRIVNH 2324
Cdd:PRK08314 276 ------------------ERYRVTHWTNIPTMVVdflasPGlaerdlsslRYIGGGGAAMPEAVAERLKELT-GLDYVEG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2325 YGPTETTVGILTCtvPEEWPVEQGvpVGHPLAGNEAWVLD-RFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAh 2403
Cdd:PRK08314 337 YGLTETMAQTHSN--PPDRPKLQC--LGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFIE- 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2404 pLAPDRLLyRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPG--------ANGVLQL 2475
Cdd:PRK08314 412 -IDGKRFF-RTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDprrgetvkAVVVLRP 489
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1246793773 2476 GACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKI 2517
Cdd:PRK08314 490 EARGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
99-507 |
7.30e-20 |
|
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380464 [Multi-domain] Cd Length: 401 Bit Score: 95.45 E-value: 7.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 99 FLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHE------------------VLDRCiqgedsvaagggaAVE 160
Cdd:cd19542 11 MLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDilrtvfvessaegtflqvVLKSL-------------DPP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 161 SADLRGRGQDEIDALVEGFRLRpfELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSLGLLTQDLSRAYRvec 240
Cdd:cd19542 78 IEEVETDEDSLDALTRDLLDDP--TLFGQPPHRLTLLETSSG-----EVYLVLRISHALYDGVSLPIILRDLAAAYN--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 241 GLAAEPAPPlpcqYGDYARWQRDTldRLDASLRHHVEALSGAPHLHElpldherPAVLGQSGAKLRLAFPPGLSERVAAY 320
Cdd:cd19542 148 GQLLPPAPP----FSDYISYLQSQ--SQEESLQYWRKYLQGASPCAF-------PSLSPKRPAERSLSSTRRSLAKLEAF 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 321 AQASR---ATAFHVLQAAFAALLARCgagDDLLIGTPVAGR--VRPELDSLVGLFVNTVVLRTQLHDDPDFASLVARCRD 395
Cdd:cd19542 215 CASLGvtlASLFQAAWALVLARYTGS---RDVVFGYVVSGRdlPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 396 HQLAALEHQALPLERVIETLqveRSSRHAPLFQLMFALRHDADLALDLHGVQAHALTL-PEDVAKHELTLEVLVGAGGMS 474
Cdd:cd19542 292 QYLRSLPHQHLSLREIQRAL---GLWPSGTLFNTLVSYQNFEASPESELSGSSVFELSaAEDPTEYPVAVEVEPSGDSLK 368
|
410 420 430
....*....|....*....|....*....|...
gi 1246793773 475 AVWEYNTALWNPATVARWAERYFVALAAMLENP 507
Cdd:cd19542 369 VSLAYSTSVLSEEQAEELLEQFDDILEALLANP 401
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
3542-4020 |
7.46e-20 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 97.66 E-value: 7.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3542 DGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAY----------------VPVDPH--- 3602
Cdd:PLN02654 118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHsvvfagfsaeslaqriVDCKPKvvi 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3603 -APAARRGF-------ILEDS-----------GVCLSVSQRalavelpgTALCLDDPFTRAQLDAVEPGELPEVPT---- 3659
Cdd:PLN02654 198 tCNAVKRGPktinlkdIVDAAldesakngvsvGICLTYENQ--------LAMKREDTKWQEGRDVWWQDVVPNYPTkcev 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3660 -----EAPAYLIYTSGSTGTPKGVVVTHRNVeRLFTAATQTGRFSFDEHDV--------WSLFHSHAfdfavweLWGAWL 3726
Cdd:PLN02654 270 ewvdaEDPLFLLYTSGSTGKPKGVLHTTGGY-MVYTATTFKYAFDYKPTDVywctadcgWITGHSYV-------TYGPML 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3727 yGGRAVLVPEAVCRQPDA--FLDLLAEYGVTVLNQTPSAFYALQ---SQAMRRELALNVRAVVFGGEALEPSrlqPWRER 3801
Cdd:PLN02654 342 -NGATVLVFEGAPNYPDSgrCWDIVDKYKVTIFYTAPTLVRSLMrdgDEYVTRHSRKSLRVLGSVGEPINPS---AWRWF 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3802 YpqaelvNMYGITETTVhvsfhrlSDEDLQSPTS-------------RIGSA-LPDLAVhvldaagQPVplgVVGELVVE 3867
Cdd:PLN02654 418 F------NVVGDSRCPI-------SDTWWQTETGgfmitplpgawpqKPGSAtFPFFGV-------QPV---IVDEKGKE 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3868 GDGVAQGY------W-----------QRPELTaeRFVERGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGE 3930
Cdd:PLN02654 475 IEGECSGYlcvkksWpgafrtlygdhERYETT--YFKPFAG--YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAE 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3931 IAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGaEPDPQSLREAL----RALLPDYMLPRLIQLLPALPLTANGKL 4005
Cdd:PLN02654 551 VESALVSHPQCAEAAVVgIEHEVKGQGIYAFVTLVEG-VPYSEELRKSLiltvRNQIGAFAAPDKIHWAPGLPKTRSGKI 629
|
570
....*....|....*
gi 1246793773 4006 DRKALPKPETQDRDE 4020
Cdd:PLN02654 630 MRRILRKIASRQLDE 644
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
3111-3461 |
8.16e-20 |
|
Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380460 [Multi-domain] Cd Length: 395 Bit Score: 94.94 E-value: 8.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3111 LHGALDREAFAAAWQQALERHPILRSGFavqgLPSPRQlPHRQVSlplaeqdwsglEPAQARSRLSELQAQQcEAG--FD 3188
Cdd:cd19537 32 LSGDVDRDRLASAWNTVLARHRILRSRY----VPRDGG-LRRSYS-----------SSPPRVQRVDTLDVWK-EINrpFD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3189 LAAPPLMRLALLRRSadehwLVWTRHHLIVDGWSSALLLDEVWRLYAalresrtpQLPAAPPFRDYLHWLRGQDEAAA-- 3266
Cdd:cd19537 95 LEREDPIRVFISPDT-----LLVVMSHIICDLTTLQLLLREVSAAYN--------GKLLPPVRREYLDSTAWSRPASPed 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3267 RAFWREQLTGLEPAALPEATEPAeGYASSTRRFDLAAASA-----WAQSHGLTASSLLQGALALVLQRYYGRDDFALGIT 3341
Cdd:cd19537 162 LDFWSEYLSGLPLLNLPRRTSSK-SYRGTSRVFQLPGSLYrsllqFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3342 IAGRPPElaGVERMLGVFINSVPLRV--TPAGEATPAPWLQALQQRNLDLRTHgYLPLAQIQRAGAADAVSP----FDVL 3415
Cdd:cd19537 241 YLNRTSE--EDMETVGLFLEPLPIRIrfPSSSDASAADFLRAVRRSSQAALAH-AIPWHQLLEHLGLPPDSPnhplFDVM 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 3416 LVFEnlptESREERSGMRIEELDHRAH----SNYPLML--TAIPDAG-GLRIE 3461
Cdd:cd19537 318 VTFH----DDRGVSLALPIPGVEPLYTwaegAKFPLMFefTALSDDSlLLRLE 366
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
529-1041 |
9.58e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 96.41 E-value: 9.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 529 PAPRTVGNVVDAIARaadEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALclprgLDWYC-----LLL 603
Cdd:PRK06187 3 DYPLTIGRILRHGAR---KHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAV-----FDWNSheyleAYF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 604 GAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDA------QGLAGFAPSVA--IAVDELKLDGAGENGSG----ENA 671
Cdd:PRK06187 75 AVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSefvpllAAILPQLPTVRtvIVEGDGPAAPLAPEVGEyeelLAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 672 AP----------NQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVdttleqILA 735
Cdd:PRK06187 155 ASdtfdfpdideNDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLvivpmfHVHAWGL------PYL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 736 AWSRGACVVArPDElLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDwRDLA-LRCLVVGGDVLPVALAQRWFELg 814
Cdd:PRK06187 229 ALMAGAKQVI-PRR-FDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYF-VDFSsLRLVIYGGAALPPALLREFKEK- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 815 ldRRCALINAYGPTEA--TIS-SHYHRVQAIDASRPVPLGQLLPGRIAAVLDAHGRIVPR--GVCGELALGGIGLAEGYR 889
Cdd:PRK06187 305 --FGIDLVQGYGMTETspVVSvLPPEDQLPGQWTKRRSAGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYW 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 890 GDAAASERRFAplrlpSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVG- 968
Cdd:PRK06187 383 NRPEATAETID-----GG----WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVA--VIGv 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 969 --EGAAQRLVAWVECAGEDGFGQADLnqtdsdqtesERWhraLCERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK06187 452 pdEKWGERPVAVVVLKPGATLDAKEL----------RAF---LRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
537-1041 |
1.09e-19 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 96.04 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 537 VVDAIARAADEFPERAALETAQG--RLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIP 614
Cdd:cd05923 3 VFEMLRRAASRAPDACAIADPARglRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 615 LDtewPQARRAEVVA----ASGCDAVLT-DAQGLAGFAPSVAIAVDELKLDGAGENGSGENA------APNQLAYILYTS 683
Cdd:cd05923 83 IN---PRLKAAELAElierGEMTAAVIAvDAQVMDAIFQSGVRVLALSDLVGLGEPESAGPLiedpprEPEQPAFVFYTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 684 GSTGIPKGVEVGHAALAAHIDAAAEALALSADD--RVL------HVAG--------LAVDTTLeqilaawsrgaCVVarp 747
Cdd:cd05923 160 GTTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRhnVVLglmplyHVIGffavlvaaLALDGTY-----------VVV--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 748 dELLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFELGLDRRcalINAYGP 827
Cdd:cd05923 226 -EEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEK---VNIYGT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 828 TEATISSHYHRVQAIDASRPvplGQLLPGRIAAVLDAHGRIVPRGVCGELALggiglaegyrgDAAASERRFAPLRLP-- 905
Cdd:cd05923 302 TEAMNSLYMRDARTGTEMRP---GFFSEVRIVRIGGSPDEALANGEEGELIV-----------AAAADAAFTGYLNQPea 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 906 SGESLR--MYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQRLVAWVEca 982
Cdd:cd05923 368 TAKKLQdgWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTeVVVIGVADERWGQSVTACVV-- 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 983 gedgfgqadLNQTDSDQTESERWHRAlcERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05923 446 ---------PREGTLSADELDQFCRA--SELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
3544-3982 |
1.46e-19 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 95.61 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3544 ELDYATLDRRSSQLATLLIRQGAGPGQRVGLcLPRGC-DLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSG--VCL- 3619
Cdd:cd05932 6 EFTWGEVADKARRLAAALRALGLEPGSKIAL-ISKNCaEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSEskALFv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3620 ------SVSQRALAVELPGTALCLDDP----FTRAQLDAVEPGELPEVPTEAP--AYLIYTSGSTGTPKGVVVTHRNVEr 3687
Cdd:cd05932 85 gklddwKAMAPGVPEGLISISLPPPSAancqYQWDDLIAQHPPLEERPTRFPEqlATLIYTSGTTGQPKGVMLTFGSFA- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3688 lFTAATQTGRFSFDEHD--VWSLFHSHAFDFAVWElwGAWLYGGRAVLVPEAVcrqpDAFLDLLAEYGVTVLNQTPSAFY 3765
Cdd:cd05932 164 -WAAQAGIEHIGTEENDrmLSYLPLAHVTERVFVE--GGSLYGGVLVAFAESL----DTFVEDVQRARPTLFFSVPRLWT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3766 ALQ---------------------SQAMRRE----LALNVRAVVFGGEALEPSRLQPWRERYpQAELVNMYGITETTVHV 3820
Cdd:cd05932 237 KFQqgvqdkipqqklnlllkipvvNSLVKRKvlkgLGLDQCRLAGCGSAPVPPALLEWYRSL-GLNILEAYGMTENFAYS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3821 SFHRLSDEDlqspTSRIGSALPDLAVHVLDAagqpvplgvvGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDL 3900
Cdd:cd05932 316 HLNYPGRDK----IGTVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADG---FLRTGDK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3901 GRYRADGSLEYRGRGDDQVKL-RGYRIEPGEIAAKIASLPQVSdaAVTVEGQGEGAWLmayAVAADGAEPDPQSL---RE 3976
Cdd:cd05932 379 GELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVE--MVCVIGSGLPAPL---ALVVLSEEARLRADafaRA 453
|
....*.
gi 1246793773 3977 ALRALL 3982
Cdd:cd05932 454 ELEASL 459
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
588-1040 |
2.72e-19 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 95.38 E-value: 2.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 588 VALCLPRGLDWYCLLLGAWRAGLSVIPL--DTEWPQARRAEVVAA-SGCDAVLTDAQGLAGFAPSVA---------IAVD 655
Cdd:cd05931 51 VLLLAPPGLDFVAAFLGCLYAGAIAVPLppPTPGRHAERLAAILAdAGPRVVLTTAAALAAVRAFAAsrpaagtprLLVV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 656 ELKLDGAGENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------H----VAGLa 725
Cdd:cd05931 131 DLLPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVswlplyHdmglIGGL- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 726 vdttleqILAAWSRGACVVARP-DELLEPQRFLAFLSERAITVTdLAPAYANEL-VRASVADDWRDLAL---RCLVVGGD 800
Cdd:cd05931 210 -------LTPLYSGGPSVLMSPaAFLRRPLRWLRLISRYRATIS-AAPNFAYDLcVRRVRDEDLEGLDLsswRVALNGAE 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 801 vlPV------ALAQRWFELGLDRRcALINAYGPTEATI------------------SSHYHRVQAIDASRP-----VPLG 851
Cdd:cd05931 282 --PVrpatlrRFAEAFAPFGFRPE-AFRPSYGLAEATLfvsggppgtgpvvlrvdrDALAGRAVAVAADDPaarelVSCG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 852 QLLPG-RIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGEslRMYRSGDRVRLLdDGELQFL 930
Cdd:cd05931 359 RPLPDqEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALAATDEG--GWLRTGDLGFLH-DGELYIT 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 931 GRADFQVKLRGYRIELEEIEHCLGQLPQVR---AAAAGVVGEGAAQRLVAWVECAGedGFGQADLnqtdsdqteserwhR 1007
Cdd:cd05931 436 GRLKDLIIVRGRNHYPQDIEATAEEAHPALrpgCVAAFSVPDDGEERLVVVAEVER--GADPADL--------------A 499
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1246793773 1008 ALCERLPAY------MVPTQFVALPR--LPRNASGKIDRRA 1040
Cdd:cd05931 500 AIAAAIRAAvarehgVAPADVVLVRPgsIPRTSSGKIQRRA 540
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
3520-4010 |
2.72e-19 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 95.79 E-value: 2.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEIARRYPARIAVSAEDGE---LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAY 3596
Cdd:PRK10524 57 NAVDRHLAKRPEQLALIAVSTETDEertYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIH 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3597 VPV----DPHAPAARrgfiLEDSGVCLSVSQRA-------------------LAVELPGTALCLD---DPFT-------- 3642
Cdd:PRK10524 137 SVVfggfASHSLAAR----IDDAKPVLIVSADAgsrggkvvpykplldeaiaLAQHKPRHVLLVDrglAPMArvagrdvd 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3643 ----RAQ-LDAVEPGELpeVPTEAPAYLIYTSGSTGTPKGV--------VVTHRNVERLFTAatQTGRFSFDEHDV-WSL 3708
Cdd:PRK10524 213 yatlRAQhLGARVPVEW--LESNEPSYILYTSGTTGKPKGVqrdtggyaVALATSMDTIFGG--KAGETFFCASDIgWVV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3709 FHShafdFAVWelwgAWLYGGRAVLVPEAVCRQPDA--FLDLLAEYGVTVLNQTPSAFYALQSQ---AMRRELALNVRAV 3783
Cdd:PRK10524 289 GHS----YIVY----APLLAGMATIMYEGLPTRPDAgiWWRIVEKYKVNRMFSAPTAIRVLKKQdpaLLRKHDLSSLRAL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3784 VFGGEAL-EPSrlQPWRERYPQAELVNMYGITETTVHV-SFHRlsdeDLQSPTSRIGSalPDLAVH-----VLD-AAGQP 3855
Cdd:PRK10524 361 FLAGEPLdEPT--ASWISEALGVPVIDNYWQTETGWPIlAIAR----GVEDRPTRLGS--PGVPMYgynvkLLNeVTGEP 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3856 VPLGVVGELVVEG---DGVAQGYWQrpelTAERFV----ERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEP 3928
Cdd:PRK10524 433 CGPNEKGVLVIEGplpPGCMQTVWG----DDDRFVktywSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGT 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3929 GEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSLREALRALL---PDYML-----PRLIQLLPALPL 3999
Cdd:PRK10524 509 REIEESISSHPAVAEVAVVgVKDALKGQVAVAFVVPKDSDSLADREARLALEKEImalVDSQLgavarPARVWFVSALPK 588
|
570
....*....|.
gi 1246793773 4000 TANGKLDRKAL 4010
Cdd:PRK10524 589 TRSGKLLRRAI 599
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
115-506 |
3.01e-19 |
|
Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380460 [Multi-domain] Cd Length: 395 Bit Score: 93.40 E-value: 3.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 115 LFELRGELDAAALERAVHGLLIRHEVLdRCiqgeDSVAAGGGAA------------VESADLrgrgQDEIDalvegfrlR 182
Cdd:cd19537 29 ACRLSGDVDRDRLASAWNTVLARHRIL-RS----RYVPRDGGLRrsyssspprvqrVDTLDV----WKEIN--------R 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 183 PFELQRQRPLRM-----QLLrldgqgdgpvrhwlqVVVHHIACDGVSLGLLTQDLSRAYRvecglaAEPAPPLPCQYGDY 257
Cdd:cd19537 92 PFDLEREDPIRVfispdTLL---------------VVMSHIICDLTTLQLLLREVSAAYN------GKLLPPVRREYLDS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 258 ARWQRdtldRLDASLRHH-VEALSGAPHLHelplDHERPAVLGQSGAKLRLAFPPGLSERVAAYAQASRATaFHVLQAAF 336
Cdd:cd19537 151 TAWSR----PASPEDLDFwSEYLSGLPLLN----LPRRTSSKSYRGTSRVFQLPGSLYRSLLQFSTSSGIT-LHQLALAA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 337 AALLARCGAG-DDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQL--HDDPDFASLVARCRDHQLAALEHqALPLERVIE 413
Cdd:cd19537 222 VALALQDLSDrTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRIRFpsSSDASAADFLRAVRRSSQAALAH-AIPWHQLLE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 414 TLQVERSSRHAPLFQLM--FALRHDADLALDLHGVQAHaLTLPEDvAKHELTLE-VLVGAGGMSAVWEYNTALWNPATVA 490
Cdd:cd19537 301 HLGLPPDSPNHPLFDVMvtFHDDRGVSLALPIPGVEPL-YTWAEG-AKFPLMFEfTALSDDSLLLRLEYDTDCFSEEEID 378
|
410
....*....|....*.
gi 1246793773 491 RWAERYFVALAAMLEN 506
Cdd:cd19537 379 RIESLILAALELLVEG 394
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
3082-3384 |
3.44e-19 |
|
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380457 [Multi-domain] Cd Length: 428 Bit Score: 93.86 E-value: 3.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3082 PLAPLQEglLFHSLLNAEADPYiNQT-TVALHGALDREAFAAAWQQALERHPILRSGFA------VQGLPSPRQLPHRqv 3154
Cdd:cd19534 3 PLTPIQR--WFFEQNLAGRHHF-NQSvLLRVPQGLDPDALRQALRALVEHHDALRMRFRredggwQQRIRGDVEELFR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3155 slpLAEQDWSGLEPAQARsrlsELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLY 3234
Cdd:cd19534 78 ---LEVVDLSSLAQAAAI----EALAAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3235 AALRESRTPQLPAAPPFRDylhWLRGQDEAAA-------RAFWREQLTGlEPAALPEATEPAEGyASSTRRFDLAAAsaw 3307
Cdd:cd19534 151 EQALAGEPIPLPSKTSFQT---WAELLAEYAQspalleeLAYWRELPAA-DYWGLPKDPEQTYG-DARTVSFTLDEE--- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3308 aqshglTASSLLQG---------------ALALVLQRYYGRDDFALGITIAGRPPELAGVE--RMLGVFINSVPLRVTPA 3370
Cdd:cd19534 223 ------ETEALLQEanaayrteindlllaALALAFQDWTGRAPPAIFLEGHGREEIDPGLDlsRTVGWFTSMYPVVLDLE 296
|
330
....*....|....
gi 1246793773 3371 GEATpapWLQALQQ 3384
Cdd:cd19534 297 ASED---LGDTLKR 307
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
588-1041 |
4.13e-19 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 94.45 E-value: 4.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWP--------QARRAEVVAASgcDAVLTDAQGLAGFAPSVAIA--VDEL 657
Cdd:cd05928 70 VAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTakdilyrlQASKAKCIVTS--DELAPEVDSVASECPSLKTKllVSEK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 658 KLDGAG----------------ENGSGENAApnqlayILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRV--- 718
Cdd:cd05928 148 SRDGWLnfkellneastehhcvETGSQEPMA------IYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDImwn 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 719 LHVAGLAVdTTLEQILAAWSRGACVVARPDELLEPQRFLAFLSERAITVTDLAPAYANELVRASVADdWRDLALR-CLVV 797
Cdd:cd05928 222 TSDTGWIK-SAWSSLFEPWIQGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSS-YKFPSLQhCVTG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 798 GGDVLPVALAQRWFELGLDrrcaLINAYGPTEATISSHYHRVQAIdasRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGEL 877
Cdd:cd05928 300 GEPLNPEVLEKWKAQTGLD----IYEGYGQTETGLICANFKGMKI---KPGSMGKASPPYDVQIIDDNGNVLPPGTEGDI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 878 AL-----GGIGLAEGYRGD---AAASERRfaplrlpsgeslRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEI 949
Cdd:cd05928 373 GIrvkpiRPFGLFSGYVDNpekTAATIRG------------DFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEV 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 950 EHCLGQLPQVraAAAGVVGEGAAQR---LVAWVECAgedgfgqADLNQTDSDQTESERWHRALCERLPaYMVPTQFVALP 1026
Cdd:cd05928 441 ESALIEHPAV--VESAVVSSPDPIRgevVKAFVVLA-------PQFLSHDPEQLTKELQQHVKSVTAP-YKYPRKVEFVQ 510
|
490
....*....|....*
gi 1246793773 1027 RLPRNASGKIDRRAL 1041
Cdd:cd05928 511 ELPKTVTGKIQRNEL 525
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
588-1041 |
4.79e-19 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 93.31 E-value: 4.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCdavltdaqglagfapSVAIAVDELkldgagengs 667
Cdd:cd05935 29 VGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGA---------------KVAVVGSEL---------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 668 genaapNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLavdttLEQILAAWSRGA 741
Cdd:cd05935 84 ------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILaclplfHVTGF-----VGSLNTAVYVGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 742 CVV--ARPDELLEPQRFlaflSERAITVTDLAPAYANELVrASVADDWRDLA-LRCLVVGGDVLPVALAQRWFEL-GLDr 817
Cdd:cd05935 153 TYVlmARWDRETALELI----EKYKVTFWTNIPTMLVDLL-ATPEFKTRDLSsLKVLTGGGAPMPPAVAEKLLKLtGLR- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 818 rcaLINAYGPTEATISSHYHRVQAIDASrpvPLGQLLPGRIAAVLDAH-GRIVPRGVCGELALGGIGLAEGYRGDAAASE 896
Cdd:cd05935 227 ---FVEGYGLTETMSQTHTNPPLRPKLQ---CLGIP*FGVDARVIDIEtGRELPPNEVGEIVVRGPQIFKGYWNRPEETE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 897 RRFAPLrlpSGEslRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQRL 975
Cdd:cd05935 301 ESFIEI---KGR--RFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*eVCVISVPDERVGEEV 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 976 VAWV----ECAGEdgfgqadlnqtdSDQTESERWHRalcERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05935 376 KAFIvlrpEYRGK------------VTEEDIIEWAR---EQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
536-1041 |
5.07e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 93.80 E-value: 5.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 536 NVVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPL 615
Cdd:PRK06145 3 NLSASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 616 DTEWPQARRAEVVAASGCDAVLTDAQGLAGFAPSVAIAV-------DELKLDGAGENGSGENA-APNQLAYILYTSGSTG 687
Cdd:PRK06145 83 NYRLAADEVAYILGDAGAKLLLVDEEFDAIVALETPKIVidaaaqaDSRRLAQGGLEIPPQAAvAPTDLVRLMYTSGTTD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 688 IPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGL----AVDttLEQILAAWSRGACVVARPdelLEPQRFLAFLSER 763
Cdd:PRK06145 163 RPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLyhvgAFD--LPGIAVLWVGGTLRIHRE---FDPEAVLAAIERH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 764 AITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPvalAQRWFELG-LDRRCALINAYGPTEaTISSHYHRVQAI 842
Cdd:PRK06145 238 RLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTP---ESRIRDFTrVFTRARYIDAYGLTE-TCSGDTLMEAGR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 843 DASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPlrlpsgeslRMYRSGDRVRLL 922
Cdd:PRK06145 314 EIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYG---------DWFRSGDVGYLD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 923 DDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA-GVVGEGAAQRLVAWVEcagedgfgqadLNQTDSDQTE 1001
Cdd:PRK06145 385 EEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAViGVHDDRWGERITAVVV-----------LNPGATLTLE 453
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1246793773 1002 SERWHralCE-RLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK06145 454 ALDRH---CRqRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
588-1036 |
7.11e-19 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 92.83 E-value: 7.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 588 VALCLPRGLDWYCLLLGAWRAGLSVIPLdteWPQARRAEVVAasgcdaVLTDAQGLAGFAPSVAIAVDELkldgagengs 667
Cdd:cd05903 29 VAFQLPNWWEFAVLYLACLRIGAVTNPI---LPFFREHELAF------ILRRAKAKVFVVPERFRQFDPA---------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 668 genAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDT-TLEQILAAWSRGACVVAr 746
Cdd:cd05903 90 ---AMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTgFVYGFTLPLLLGAPVVL- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 747 pDELLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFELGLDRRCAlinAYG 826
Cdd:cd05903 166 -QDIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCS---AYG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 827 PTEatissHYHRVQAIDASRP----VPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGY--RGDAAASErrfa 900
Cdd:cd05903 242 STE-----CPGAVTSITPAPEdrrlYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYldRPDLTADA---- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 901 plrLPSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVG---EGAAQRLVA 977
Cdd:cd05903 313 ---APEG----WFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAA--VVAlpdERLGERACA 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 978 WVECAGEDGFGQADLNQTDSDQteserwhralceRLPAYMVPTQFVALPRLPRNASGKI 1036
Cdd:cd05903 384 VVVTKSGALLTFDELVAYLDRQ------------GVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1627-1934 |
8.40e-19 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380455 [Multi-domain] Cd Length: 421 Bit Score: 92.52 E-value: 8.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1627 ELDGEIDAAALAQAWQQTVRRQPMLRTAIVW-EGLSVPHQIVLADAAAPWQTLDWSALDDAAQdaqlqrwLADDAAQGV- 1704
Cdd:cd19532 31 RLTGPLDVARLERAVRAVGQRHEALRTCFFTdPEDGEPMQGVLASSPLRLEHVQISDEAEVEE-------EFERLKNHVy 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1705 DFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYtagaQGATLrlpPAPGFQaYLDWRERQDLARQR 1784
Cdd:cd19532 104 DLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAY----NGQPL---LPPPLQ-YLDFAARQRQDYES 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1785 G-------WWRERLSG---------YAGTAALPAPVAAAHHpvqreECERRLSAHDSERLRAFCRERGCT-----LSDLI 1843
Cdd:cd19532 176 GaldedlaYWKSEFSTlpeplpllpFAKVKSRPPLTRYDTH-----TAERRLDAALAARIKEASRKLRVTpfhfyLAALQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1844 AMVwglanARYGNHDDVVLGATRSGRPPElaGVESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAENEAVGLGE 1923
Cdd:cd19532 251 VLL-----ARLLDVDDICIGIADANRTDE--DFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDKAYAALAHSRVPFDV 323
|
330
....*....|.
gi 1246793773 1924 ILADsgLDADR 1934
Cdd:cd19532 324 LLDE--LGVPR 332
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
3498-3947 |
8.60e-19 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 93.36 E-value: 8.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3498 PLLPSQTRSAAwtSRERYActgnlVSRFAEIarryPARIA-VSAEDG-ELDYATLDRRSSQLATLLIRQGAGPGQRVGLC 3575
Cdd:cd17642 7 PFYPLEDGTAG--EQLHKA-----MKRYASV----PGTIAfTDAHTGvNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3576 LPRGCDLLVALLAILKTGAAYVPVDP--------HAPAARRGFILEDSGVCLsvsQRALAVE--LP--GTALCLD----- 3638
Cdd:cd17642 76 SENSLQFFLPVIAGLFIGVGVAPTNDiynereldHSLNISKPTIVFCSKKGL---QKVLNVQkkLKiiKTIIILDskedy 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3639 ------DPFTRAQLDAVEPGELPEVPT----EAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQT--GRFSFDEHDVW 3706
Cdd:cd17642 153 kgyqclYTFITQNLPPGFNEYDFKPPSfdrdEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPifGNQIIPDTAIL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3707 SL--FHsHAFdfAVWELWGAWLYGGRAVLVPEAvcrQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELAL-NVRAV 3783
Cdd:cd17642 233 TVipFH-HGF--GMFTTLGYLICGFRVVLMYKF---EEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLsNLHEI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3784 VFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSfhrLSDEDLQSPTSrIGSALPDLAVHVLDA-AGQPVPLGVVG 3862
Cdd:cd17642 307 ASGGAPLSKEVGEAVAKRFKLPGIRQGYGLTETTSAIL---ITPEGDDKPGA-VGKVVPFFYAKVVDLdTGKTLGPNERG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3863 ELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVS 3942
Cdd:cd17642 383 ELCVKGPMIMKGYVNNPEATKALIDKDG---WLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIF 459
|
....*
gi 1246793773 3943 DAAVT 3947
Cdd:cd17642 460 DAGVA 464
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
678-1039 |
9.31e-19 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 91.29 E-value: 9.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 678 YILYTSGSTGIPKGVEVGHA--ALAAHIDAAAEALALSADDRVLHVAGLAVDTTL---------EQILAAWS--RGACVV 744
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQEdiFRMLMGGADFGTGEFTPSEDAHKAAAAAAGTVMfpapplmhgTGSWTAFGglLGGQTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 745 ARPDELLEPQRFLAFLS-ERAITVTDLAPAYANELVRASVADDWRDL-ALRCLVVGGDVLPVALAQRWFELGLDRrcALI 822
Cdd:cd05924 87 VLPDDRFDPEEVWRTIEkHKVTSMTIVGDAMARPLIDALRDAGPYDLsSLFAISSGGALLSPEVKQGLLELVPNI--TLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 823 NAYGPTEATISSHYHRVQAIDASRPvplgQLLPGRIAAVLDAHGRIVP--RGVCGELALGGIgLAEGYRGDAAASERRFa 900
Cdd:cd05924 165 DAFGSSETGFTGSGHSAGSGPETGP----FTRANPDTVVLDDDGRVVPpgSGGVGWIARRGH-IPLGYYGDEAKTAETF- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 901 plrlPSGESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQRLVAWV 979
Cdd:cd05924 239 ----PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYdVLVVGRPDERWGQEVVAVV 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 980 ecAGEDGFGqADLNQTDsdqteserwhRALCERLPAYMVPTQFVALPRLPRNASGKIDRR 1039
Cdd:cd05924 315 --QLREGAG-VDLEELR----------EHCRTRIARYKLPKQVVFVDEIERSPAGKADYR 361
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
588-1051 |
9.79e-19 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 94.33 E-value: 9.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQGLAGFAPSVAIAVDELKLDGA-GENG 666
Cdd:PRK06060 58 VLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRFQPSRVAEAAELMSEAArVAPG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 667 SGENAAPNQLAYILYTSGSTGIPKGVEVGHA-------ALAAHIDAAAEALALSADDRVLHVAGLA------VDTTLEQI 733
Cdd:PRK06060 138 GYEPMGGDALAYATYTSGTTGPPKAAIHRHAdpltfvdAMCRKALRLTPEDTGLCSARMYFAYGLGnsvwfpLATGGSAV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 734 LAAWSRGACVVARPDELLEPqrflaflseraiTVTDLAPAYANELVRASVADDWRdlALRCLVVGGDVLPVALAQRWFEL 813
Cdd:PRK06060 218 INSAPVTPEAAAILSARFGP------------SVLYGVPNFFARVIDSCSPDSFR--SLRCVVSAGEALELGLAERLMEF 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 814 --GLdrrcALINAYGPTEA--TISSHyhrvqAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYR 889
Cdd:PRK06060 284 fgGI----PILDGIGSTEVgqTFVSN-----RVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYW 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 890 GdaaaserRFAPLrLPSGESLRmyrSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQV-RAAAAGVVG 968
Cdd:PRK06060 355 N-------RPDSP-VANEGWLD---TRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVaEAAVVAVRE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 969 EGAAQRLVAWVECAGEDGFgqadlnqtdsDQTESERWHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRAL----PAP 1044
Cdd:PRK06060 424 STGASTLQAFLVATSGATI----------DGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALrkqsPTK 493
|
....*....
gi 1246793773 1045 PV--LAQAE 1051
Cdd:PRK06060 494 PIweLSLTE 502
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
3524-4084 |
1.02e-18 |
|
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442548 [Multi-domain] Cd Length: 855 Bit Score: 94.38 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3524 RFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHA 3603
Cdd:COG3319 10 AAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAALALALA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3604 PAARRGFILEDSGVCLSVSQRALAVELPGTALCLDDPFTRAQLDAVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHR 3683
Cdd:COG3319 90 AAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAGVLVLVLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3684 NVERLFTAATQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSA 3763
Cdd:COG3319 170 ALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLLLAALLL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3764 FYALQSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQSPTSRIGSALPD 3843
Cdd:COG3319 250 LLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGGGPGLLVLLV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3844 LAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRG 3923
Cdd:COG3319 330 LLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRLRLQRLRRG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3924 YRIEPGEIAAKIASLPQVSDAAVTVEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANG 4003
Cdd:COG3319 410 LREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLLLLLLLLLLA 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 4004 KLDRKALPKPE-TQDRDEGVLESASERRLAELWRQLLGGELPGRGAHFFARGGHSLLVVRLAEAIRAEFAIAVPLKSLFE 4082
Cdd:COG3319 490 ALLLAAAAPAAaAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRLLLLLALLL 569
|
..
gi 1246793773 4083 QP 4084
Cdd:COG3319 570 AP 571
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
3547-4022 |
2.08e-18 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 91.72 E-value: 2.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3547 YATLDRRSSQLATLLIRQ-GAGPGQRVGLCLPRGCDLLVALLAILKTGAAyvpvdphaPAArrgfiledsgvclsvsqra 3625
Cdd:cd05937 8 YSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA--------PAF------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3626 LAVELPGTAL--CLDdpFTRAQLDAVEPgelpevptEAPAYLIYTSGSTGTPKGVVVTHRnveRLFTAATQTGR-FSFDE 3702
Cdd:cd05937 61 INYNLSGDPLihCLK--LSGSRFVIVDP--------DDPAILIYTSGTTGLPKAAAISWR---RTLVTSNLLSHdLNLKN 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3703 HDVW----SLFHSHAFDFAVWELWGAwlyGGRAVLVPEAVCRQpdaFLDLLAEYGVTVLNQTPSAF-YALQSQAMRRELA 3777
Cdd:cd05937 128 GDRTytcmPLYHGTAAFLGACNCLMS---GGTLALSRKFSASQ---FWKDVRDSGATIIQYVGELCrYLLSTPPSPYDRD 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3778 LNVRAVVfgGEALEPSRLQPWRERYPQAELVNMYGITE-------------TTVHVSFH----RLSDEDLQSPtsrigsa 3840
Cdd:cd05937 202 HKVRVAW--GNGLRPDIWERFRERFNVPEIGEFYAATEgvfaltnhnvgdfGAGAIGHHglirRWKFENQVVL------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3841 lpdlaVHVLDAAGQP-----------VPLGVVGELVV----EGDGVAQGYWQRPELTAERFVE---RGGQRFYRSGDLGR 3902
Cdd:cd05937 273 -----VKMDPETDDPirdpktgfcvrAPVGEPGEMLGrvpfKNREAFQGYLHNEDATESKLVRdvfRKGDIYFRTGDLLR 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3903 YRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDA---AVTV---EGQGEGAWLMAYAVAADGAEPDPQSLRE 3976
Cdd:cd05937 348 QDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEAnvyGVKVpghDGRAGCAAITLEESSAVPTEFTKSLLAS 427
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1246793773 3977 ALRALLPDYMLPRLIQLLPALPLTANGKLDRKALpkpetqdRDEGV 4022
Cdd:cd05937 428 LARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVL-------RDEGV 466
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2176-2524 |
2.43e-18 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 91.37 E-value: 2.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2176 ADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDL-GEDASLATLSTVA---ADLGFTALFGALLSGRRVRLLPA 2251
Cdd:cd05910 84 ADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIrPGEVDLATFPLFAlfgPALGLTSVIPDMDPTRPARADPQ 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2252 ELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAaggtavLPR-ECLVTGGEALTGALVQQVR-ALAPTLRIVNHYGPTE 2329
Cdd:cd05910 164 KLVGAIRQYGVSIVFGSPALLERVARYCAQHGIT------LPSlRRVLSAGAPVPIALAARLRkMLSDEAEILTPYGATE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2330 ----TTVG---ILTCTVPeewPVEQ--GVPVGHPLAGNEAWVL--DRFGLPA-------PVGVAGELYLGGGNLSLGYWQ 2391
Cdd:cd05910 238 alpvSSIGsreLLATTTA---ATSGgaGTCVGRPIPGVRVRIIeiDDEPIAEwddtlelPRGEIGEITVTGPTVTPTYVN 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2392 RAEQTAerFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLAL--PGA 2469
Cdd:cd05910 315 RPVATA--LAKIDDNSEGFWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVgkPGC 392
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 2470 N---GVLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRL-----GNGKIDRQALAD 2524
Cdd:cd05910 393 QlpvLCVEPLPGTITPRARLEQELRALAKDYPHTQRIGRFLIHPSFpvdirHNAKIFREKLAV 455
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
2630-2859 |
3.23e-18 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 87.02 E-value: 3.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2630 LTPIQHWFFEqALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARFQRDAaGQWQQTL---GDWQADRFAHR 2706
Cdd:COG4908 1 LSPAQKRFLF-LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEED-GEPVQRIdpdADLPLEVVDLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2707 EADAGQREDLLAQWQAGL---SFD---GALLRVLALPDPQDGDtRVLFAAHHLLVDAVSWGIIVDDLQHAYAERRAGRSP 2780
Cdd:COG4908 79 ALPEPEREAELEELVAEEasrPFDlarGPLLRAALIRLGEDEH-VLLLTIHHIISDGWSLGILLRELAALYAALLEGEPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2781 ALAAEACGFGAWQAALRQ-LSAATLDGWRSYWRAQ-AADAEAIALPW--QDSDNRYADTVHLHDRFERDWTERLLtQTAR 2856
Cdd:COG4908 158 PLPELPIQYADYAAWQRAwLQSEALEKQLEYWRQQlAGAPPVLELPTdrPRPAVQTFRGATLSFTLPAELTEALK-ALAK 236
|
...
gi 1246793773 2857 AYG 2859
Cdd:COG4908 237 AHG 239
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
2049-2431 |
4.04e-18 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 91.70 E-value: 4.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2049 PAQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLP-R---TFAQLAAMAAvwhrGAAWLPLDPQHPdAR 2124
Cdd:COG1022 28 VALREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDnRpewVIADLAILAA----GAVTVPIYPTSS-AE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2125 QIA-VLDDSGARIVI------------GWGAAPA----WV------PASVRWLDAESVLDVVSAYEEPPRVD-----VDA 2176
Cdd:COG1022 103 EVAyILNDSGAKVLFvedqeqldklleVRDELPSlrhiVVldprglRDDPRLLSLDELLALGREVADPAELEarraaVKP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2177 DTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASlaTLS------------------------------T 2226
Cdd:COG1022 183 DDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDR--TLSflplahvfertvsyyalaagatvafaespdT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2227 VAADLG------FTA---LFGALLSG--RRVRLLPA------ELAFDAQALAAHLQAHPVDclkivPSHLAGLLAAAGGT 2289
Cdd:COG1022 261 LAEDLRevkptfMLAvprVWEKVYAGiqAKAEEAGGlkrklfRWALAVGRRYARARLAGKS-----PSLLLRLKHALADK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2290 AVLPR---------ECLVTGGEALTGALVQQVRALAptLRIVNHYGPTETTvGILTCTVPEEwpVEQGVpVGHPLAGNEa 2360
Cdd:COG1022 336 LVFSKlrealggrlRFAVSGGAALGPELARFFRALG--IPVLEGYGLTETS-PVITVNRPGD--NRIGT-VGPPLPGVE- 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 2361 wvldrfglpapVGVA--GELYLGGGNLSLGYWQRAEQTAERFVAhplapDRLLyRSGDLARLDGEGRIVYLGR 2431
Cdd:COG1022 409 -----------VKIAedGEILVRGPNVMKGYYKNPEATAEAFDA-----DGWL-HTGDIGELDEDGFLRITGR 464
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
2047-2528 |
4.14e-18 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 90.70 E-value: 4.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2047 QMPAQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALC----LPRTFAQLAAMAAvwhrGAAWLPLDPQHPD 2122
Cdd:PRK09029 14 QVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRgknsPETLLAYLALLQC----GARVLPLNPQLPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2123 ARQIAVLDDSGARIvigwgaapAWVPASVRWLDAESVLdVVSAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVVS-QGN 2201
Cdd:PRK09029 90 PLLEELLPSLTLDF--------ALVLEGENTFSALTSL-HLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTaQAH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2202 LANyVAGVLPVLDLGEDAS-LATLstvaadlgftALFGA---------LLSGRRVrLLPAELAFDaqalaahlqahpvDC 2271
Cdd:PRK09029 161 LAS-AEGVLSLMPFTAQDSwLLSL----------PLFHVsgqgivwrwLYAGATL-VVRDKQPLE-------------QA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2272 LKIVpSHL-----------AGLLAAAGGTAVLpreclvTGGEALTGALVQQVRALAptLRIVNHYGPTE--TTVgiltCT 2338
Cdd:PRK09029 216 LAGC-THAslvptqlwrllDNRSEPLSLKAVL------LGGAAIPVELTEQAEQQG--IRCWCGYGLTEmaSTV----CA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2339 VPEEwpveqGVP-VGHPLAGNEAWVldrfglpapvgVAGELYLGGGNLSLGYWQRAEQTaerfvahPLAPDRLLYRSGDL 2417
Cdd:PRK09029 283 KRAD-----GLAgVGSPLPGREVKL-----------VDGEIWLRGASLALGYWRQGQLV-------PLVNDEGWFATRDR 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2418 ARLDGeGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGAN------GVLQLGAciQGSLEGVAEALA 2491
Cdd:PRK09029 340 GEWQN-GELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEfgqrpvAVVESDS--EAAVVNLAEWLQ 416
|
490 500 510
....*....|....*....|....*....|....*..
gi 1246793773 2492 QRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLLQQ 2528
Cdd:PRK09029 417 DKLARFQQPVAYYLLPPELKNGGIKISRQALKEWVAQ 453
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
3532-4010 |
1.04e-17 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 90.29 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3532 YPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFI 3611
Cdd:PLN02479 33 HPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3612 LEDSGVCL--------SVSQRAL---------AVELP-----GTALCLDDPFTRA-QLDAVEPGEL-----PEVPTEAPA 3663
Cdd:PLN02479 113 LEHSKSEVvmvdqeffTLAEEALkilaekkksSFKPPlliviGDPTCDPKSLQYAlGKGAIEYEKFletgdPEFAWKPPA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3664 ------YLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEHDV--WSL--FHSHAFDFAvWELwgawlyggrAVL 3733
Cdd:PLN02479 193 dewqsiALGYTSGTTASPKGVVLHHRGA--YLMALSNALIWGMNEGAVylWTLpmFHCNGWCFT-WTL---------AAL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3734 VPEAVC-RQ--PDAFLDLLAEYGVTVLNQTPSAFYALQSqAMRRELAL---NVRAVVFGGEALEPSRLQPWRERypQAEL 3807
Cdd:PLN02479 261 CGTNIClRQvtAKAIYSAIANYGVTHFCAAPVVLNTIVN-APKSETILplpRVVHVMTAGAAPPPSVLFAMSEK--GFRV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3808 VNMYGITET----TV---HVSFHRLSDEDLQSPTSRIG---SALPDLAVhVLDAAGQPVPL--GVVGELVVEGDGVAQGY 3875
Cdd:PLN02479 338 THTYGLSETygpsTVcawKPEWDSLPPEEQARLNARQGvryIGLEGLDV-VDTKTMKPVPAdgKTMGEIVMRGNMVMKGY 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3876 WQRPELTAERFveRGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTV---EGQG 3952
Cdd:PLN02479 417 LKNPKANEEAF--ANG--WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVArpdERWG 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 3953 EGAwlMAYAVAADGAE-PDPQSLREAL----RALLPDYMLPRLIQLLPaLPLTANGKLDRKAL 4010
Cdd:PLN02479 493 ESP--CAFVTLKPGVDkSDEAALAEDImkfcRERLPAYWVPKSVVFGP-LPKTATGKIQKHVL 552
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
2050-2522 |
1.13e-17 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 89.69 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2050 AQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVL 2129
Cdd:cd05920 29 PDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFC 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 DDSGARIVIGWGaapawvpasvRWLDAESVLDVVSAYEEPPrvdvdadTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGV 2209
Cdd:cd05920 109 AHAEAVAYIVPD----------RHAGFDHRALARELAESIP-------EVALFLLSGGTTGTPKLIPRTHNDYAYNVRAS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2210 LPVLDLGEDASLATLSTVAADLGFTA--LFGALLSGRRVRLLP---AELAFDAQALAAhlqahpVDCLKIVPSHLAG--L 2282
Cdd:cd05920 172 AEVCGLDQDTVYLAVLPAAHNFPLACpgVLGTLLAGGRVVLAPdpsPDAAFPLIEREG------VTVTALVPALVSLwlD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2283 LAAAGGTAVLPRECLVTGGEALTGALVQQVRA-LAPTLRIVnhYGPTEttvGILTCTV---PEEWPVE-QGVPVGhplAG 2357
Cdd:cd05920 246 AAASRRADLSSLRLLQVGGARLSPALARRVPPvLGCTLQQV--FGMAE---GLLNYTRlddPDEVIIHtQGRPMS---PD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2358 NEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFvahplAPDRLlYRSGDLARLDGEGRIVYLGRGDHQVK 2437
Cdd:cd05920 318 DEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAF-----TPDGF-YRTGDLVRRTPDGYLVVEGRIKDQIN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2438 IRGYRVELGEVEQVLAQLPGVEVAAVLALPgaNGVLQLGACI-------QGSLEGVAEALAQR-LPEYLCPSRWRAVESM 2509
Cdd:cd05920 392 RGGEKIAAEEVENLLLRHPAVHDAAVVAMP--DELLGERSCAfvvlrdpPPSAAQLRRFLRERgLAAYKLPDRIEFVDSL 469
|
490
....*....|...
gi 1246793773 2510 PRLGNGKIDRQAL 2522
Cdd:cd05920 470 PLTAVGKIDKKAL 482
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
2179-2519 |
1.18e-17 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 87.46 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2179 PAYLIYTSGSTGTPKGVVVSQGN-LANYVAGVLPVLDLGEDAsLATLSTVAADLGFTALFGALLSGRRVRLLPAelaFDA 2257
Cdd:cd17633 2 PFYIGFTSGTTGLPKAYYRSERSwIESFVCNEDLFNISGEDA-ILAPGPLSHSLFLYGAISALYLGGTFIGQRK---FNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2258 QALAAHLQAHPVDCLKIVPShlAGLLAAAGGTAVLPRECLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTvgILTC 2337
Cdd:cd17633 78 KSWIRKINQYNATVIYLVPT--MLQALARTLEPESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELS--FITY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2338 TVPEE-WPVEQgvpVGHPLAGNEAWVLDRFGlpapvGVAGELYLGGGNLSLGYWQRAEQTAERFvahplapdrllYRSGD 2416
Cdd:cd17633 154 NFNQEsRPPNS---VGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNPDGW-----------MSVGD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2417 LARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQG---SLEGVAEALAQR 2493
Cdd:cd17633 215 IGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGdklTYKQLKRFLKQK 294
|
330 340
....*....|....*....|....*.
gi 1246793773 2494 LPEYLCPSRWRAVESMPRLGNGKIDR 2519
Cdd:cd17633 295 LSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
3529-3982 |
1.35e-17 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 89.80 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGE-----LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDP-- 3601
Cdd:cd05921 5 ARQAPDRTWLAEREGNggwrrVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPay 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3602 ------HAPAARRGFILEDSGVCLSVS---QRAL-AVELPGTALCL-------DDPFTRAQLDAVEPGE-----LPEVPT 3659
Cdd:cd05921 85 slmsqdLAKLKHLFELLKPGLVFAQDAapfARALaAIFPLGTPLVVsrnavagRGAISFAELAATPPTAavdaaFAAVGP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3660 EAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQTGRFSFDEHDV------WS--LFHSHAFDFAVWElwGAWLY--GG 3729
Cdd:cd05921 165 DTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPPVlvdwlpWNhtFGGNHNFNLVLYN--GGTLYidDG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3730 RAVlvpeavcrqPDAF---LDLLAEYGVTVLNQTPSAFYALqSQAMRRELAL------NVRAVVFGGEALEPS---RLQP 3797
Cdd:cd05921 243 KPM---------PGGFeetLRNLREISPTVYFNVPAGWEML-VAALEKDEALrrrffkRLKLMFYAGAGLSQDvwdRLQA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3798 WR-----ERYPqaeLVNMYGITETTVHVSFhrlsdedLQSPTSR---IGSALPDLAVHVldaagqpVPLGVVGELVVEGD 3869
Cdd:cd05921 313 LAvatvgERIP---MMAGLGATETAPTATF-------THWPTERsglIGLPAPGTELKL-------VPSGGKYEVRVKGP 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3870 GVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYrADGS-----LEYRGRGDDQVKLRG---YRIEPGEIAAKIASLPQV 3941
Cdd:cd05921 376 NVTPGYWRQPELTAQAFDEEG---FYCLGDAAKL-ADPDdpakgLVFDGRVAEDFKLASgtwVSVGPLRARAVAACAPLV 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 3942 SDAAVTVEGQGE-GA--WLMAYAVAA--DGAEPDP------QSLREALRALL 3982
Cdd:cd05921 452 HDAVVAGEDRAEvGAlvFPDLLACRRlvGLQEASDaevlrhAKVRAAFRDRL 503
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
3662-4023 |
1.37e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 90.08 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3662 PAYLIYTSGSTGTPKGVVVTHRNVERLFTAAT---QTGRFSFdehDVWSL--FHSHAFDFAvwelWGAWLYGGRAVLVPE 3736
Cdd:PLN03102 188 PISLNYTSGTTADPKGVVISHRGAYLSTLSAIigwEMGTCPV---YLWTLpmFHCNGWTFT----WGTAARGGTSVCMRH 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3737 AVCrqPDAFLDlLAEYGVTVLNQTPSAFYALQsQAMRRELALNVRAV-VFGGEALEPSRLQPWRERYpQAELVNMYGITE 3815
Cdd:PLN03102 261 VTA--PEIYKN-IEMHNVTHMCCVPTVFNILL-KGNSLDLSPRSGPVhVLTGGSPPPAALVKKVQRL-GFQVMHAYGLTE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3816 TTVHVSFHRLSDEDLQSP-------TSRIGSALPDLA-VHVLDAAGQ---PVPLGVVGELVVEGDGVAQGYWQRPELTAE 3884
Cdd:PLN03102 336 ATGPVLFCEWQDEWNRLPenqqmelKARQGVSILGLAdVDVKNKETQesvPRDGKTMGEIVIKGSSIMKGYLKNPKATSE 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3885 RFvERGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQ---GEGAwlMAYA 3961
Cdd:PLN03102 416 AF-KHG---WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHptwGETP--CAFV 489
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 3962 VAADGAEPDPQ----------SLREALRALLPDYMLPRLIQLLPALPLTANGKldrkaLPKPETQDRDEGVL 4023
Cdd:PLN03102 490 VLEKGETTKEDrvdklvtrerDLIEYCRENLPHFMCPRKVVFLQELPKNGNGK-----ILKPKLRDIAKGLV 556
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
3529-3946 |
1.51e-17 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 88.78 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARR 3608
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3609 GFILEDsgvclsvsqraLAVELpgtALCLDDPFTRAQLDAVEPGELPEVPT-----EAPAYLIYTSGSTGTPKGVVVTHR 3683
Cdd:PRK09029 93 EELLPS-----------LTLDF---ALVLEGENTFSALTSLHLQLVEGAHAvawqpQRLATMTLTSGSTGLPKAAVHTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3684 NveRLFTAATQTGRFSFDEHDVW----SLFH--SHAFdfaVWElwgaWLYGGrAVLvpeaVCRQPDAFLDLLAeyGVTVL 3757
Cdd:PRK09029 159 A--HLASAEGVLSLMPFTAQDSWllslPLFHvsGQGI---VWR----WLYAG-ATL----VVRDKQPLEQALA--GCTHA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3758 NQTPSAFYALQSQamrRELALNVRAVVFGGEALEPSRLQpwrerypQAELVNM-----YGITE--TTVhvsFHRLSDEdl 3830
Cdd:PRK09029 223 SLVPTQLWRLLDN---RSEPLSLKAVLLGGAAIPVELTE-------QAEQQGIrcwcgYGLTEmaSTV---CAKRADG-- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3831 qspTSRIGSALPdlavhvldaaGQPVPLgVVGELVVEGDGVAQGYWQRPELTAerFVERGGqrFYRSGDLGRYRaDGSLE 3910
Cdd:PRK09029 288 ---LAGVGSPLP----------GREVKL-VDGEIWLRGASLALGYWRQGQLVP--LVNDEG--WFATRDRGEWQ-NGELT 348
|
410 420 430
....*....|....*....|....*....|....*.
gi 1246793773 3911 YRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAV 3946
Cdd:PRK09029 349 ILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFV 384
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
588-1041 |
1.63e-17 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 88.73 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEW-PQARrAEVVAASGCDAVLTDAQGLAgfapsvaiavdelKLDgageng 666
Cdd:cd05973 28 VAGLLPRTPELVVTILGIWRLGAVYQPLFTAFgPKAI-EHRLRTSGARLVVTDAANRH-------------KLD------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 667 sgenaapNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGlavdttleqilAAWSRGA-CVVA 745
Cdd:cd05973 88 -------SDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAAD-----------PGWAYGLyYAIT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 746 RPDELLEPQRFLA--FLSE------RAITVTDLA--PAYANELVRASVADDWR-DLALRCLVVGGDVLPVALAqRWFE-- 812
Cdd:cd05973 150 GPLALGHPTILLEggFSVEstwrviERLGVTNLAgsPTAYRLLMAAGAEVPARpKGRLRRVSSAGEPLTPEVI-RWFDaa 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 813 LGLdrrcALINAYGPTE--ATISSHYHRVQAIDASrpvPLGQLLPGRIAAVLDAHGRIVPRGVCGELALggiglaegyrg 890
Cdd:cd05973 229 LGV----PIHDHYGQTElgMVLANHHALEHPVHAG---SAGRAMPGWRVAVLDDDGDELGPGEPGRLAI----------- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 891 DAAASERRF------APLRLPSGeslRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAa 964
Cdd:cd05973 291 DIANSPLMWfrgyqlPDTPAIDG---GYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAA- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 965 gVVGEGAAQR---LVAWVE-CAGEDGfgqadlnqTDSDQTESERWHRalcERLPAYMVPTQFVALPRLPRNASGKIDRRA 1040
Cdd:cd05973 367 -VIGVPDPERtevVKAFVVlRGGHEG--------TPALADELQLHVK---KRLSAHAYPRTIHFVDELPKTPSGKIQRFL 434
|
.
gi 1246793773 1041 L 1041
Cdd:cd05973 435 L 435
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
3542-4015 |
2.11e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 88.17 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3542 DGELDYATLDRRSSQLATLLIRQGAgPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAP--AARRgfiledsgvcl 3619
Cdd:PRK08308 6 DEEYSKSDFDLRLQRYEEMEQFQEA-AGNRFAVCLKDPFDIITLVFFLKEKGASVLPIHPDTPkeAAIR----------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3620 svsqraLAVELPGTALCLDDP-FTRaqldavepGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQtgRF 3698
Cdd:PRK08308 74 ------MAKRAGCHGLLYGESdFTK--------LEAVNYLAEEPSLLQYSSGTTGEPKLIRRSWTEIDREIEAYNE--AL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3699 SFDEHDV----WSLFHSHAFDFAVwelwgawLYGGRAVLVPEAVCRQ-PDAFLDLLAEYGVTVLNQTPSAFYALQSQAMR 3773
Cdd:PRK08308 138 NCEQDETpivaCPVTHSYGLICGV-------LAALTRGSKPVIITNKnPKFALNILRNTPQHILYAVPLMLHILGRLLPG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3774 RElalNVRAVVFGGEALEPSRLQPWRERYPQaeLVNMYGITETTVhVSFHrlsdEDLQSPTSrIGSALPDLAVHVLDAAG 3853
Cdd:PRK08308 211 TF---QFHAVMTSGTPLPEAWFYKLRERTTY--MMQQYGCSEAGC-VSIC----PDMKSHLD-LGNPLPHVSVSAGSDEN 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3854 QPvplgvvGELVVegdgvaqgywqrpeltaerfveRGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAA 3933
Cdd:PRK08308 280 AP------EEIVV----------------------KMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVED 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3934 KIASLPQVSDaAVTVEGQ----GEgawLMAYAVAADGaEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKA 4009
Cdd:PRK08308 332 VMLRLPGVQE-AVVYRGKdpvaGE---RVKAKVISHE-EIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKL 406
|
....*.
gi 1246793773 4010 LPKPET 4015
Cdd:PRK08308 407 LELGEV 412
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
3520-3903 |
2.15e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 89.72 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEIARRYPARIAVSAEDG------ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTG 3593
Cdd:PRK12582 50 SIPHLLAKWAAEAPDRPWLAQREPghgqwrKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3594 AAYVPVDP--------HAP------AARRGFILEDSGVCLSvsqRAL-AVELPG------TALCLDDPFTR-AQLDAVEP 3651
Cdd:PRK12582 130 VPAAPVSPayslmshdHAKlkhlfdLVKPRVVFAQSGAPFA---RALaALDLLDvtvvhvTGPGEGIASIAfADLAATPP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3652 GELPEVPTEA-----PAYLIYTSGSTGTPKGVVVTHRnverLFTA--ATQTGRFSFDEHDV------WSLFH-----SHA 3713
Cdd:PRK12582 207 TAAVAAAIAAitpdtVAKYLFTSGSTGMPKAVINTQR----MMCAniAMQEQLRPREPDPPppvsldWMPWNhtmggNAN 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3714 FDFAVWELWGAWLYGGRAVlvpeavcrqPDAF---LDLLAEYGVTVLNQTPSAFYAL-----QSQAMRRELALNVRAVVF 3785
Cdd:PRK12582 283 FNGLLWGGGTLYIDDGKPL---------PGMFeetIRNLREISPTVYGNVPAGYAMLaeameKDDALRRSFFKNLRLMAY 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3786 GGEALEP---SRLQPW--RERYPQAELVNMYGITETT-VHVSFHRlsdedlqsPTSR---IGSALPDLAVHVldaagqpV 3856
Cdd:PRK12582 354 GGATLSDdlyERMQALavRTTGHRIPFYTGYGATETApTTTGTHW--------DTERvglIGLPLPGVELKL-------A 418
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1246793773 3857 PLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRY 3903
Cdd:PRK12582 419 PVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEG---FYRLGDAARF 462
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2184-2519 |
2.79e-17 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 86.56 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2184 YTSGSTGTPKGVVVSQGNLAN--YVAG-----------VLPV-------LDLGEDASLATLST-VAADLGF--------- 2233
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNngYFIGerlglteqdrlCIPVplfhcfgSVLGVLACLTHGATmVFPSPSFdplavleai 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2234 -----TALFG------ALLSgrrvrlLPAELAFDaqalaahlqahpVDCLKivpshlagllaaaggTAVLpreclvtGGE 2302
Cdd:cd05917 89 ekekcTALHGvptmfiAELE------HPDFDKFD------------LSSLR---------------TGIM-------AGA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2303 ALTGALVQQVRALAPTLRIVNHYGPTETTVGIlTCTVPEEwPVEQGV-PVGHPLAGNEAWVLDRFGLP-APVGVAGELYL 2380
Cdd:cd05917 129 PCPPELMKRVIEVMNMKDVTIAYGMTETSPVS-TQTRTDD-SIEKRVnTVGRIMPHTEAKIVDPEGGIvPPVGVPGELCI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2381 GGGNLSLGYWQRAEQTAErfvahPLAPDRlLYRSGDLARLDGEGRIVYLGRgdhqVK---IRGyrvelG------EVEQV 2451
Cdd:cd05917 207 RGYSVMKGYWNDPEKTAE-----AIDGDG-WLHTGDLAVMDEDGYCRIVGR----IKdmiIRG-----GeniyprEIEEF 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 2452 LAQLPGVEVAAVLALPGANGVLQLGACIQG------SLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDR 2519
Cdd:cd05917 272 LHTHPKVSDVQVVGVPDERYGEEVCAWIRLkegaelTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
2078-2524 |
2.85e-17 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 88.60 E-value: 2.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2078 LDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDpQHPDARQIA-VLDDSGARIVIGW-----GAAPAwVPASV 2151
Cdd:PRK12406 28 LAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVN-WHFKPEEIAyILEDSGARVLIAHadllhGLASA-LPAGV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2152 RWLDAESVLDVVSAYE------EPPRVDVDADT---------------PAYLIYTSGSTGTPKGV-----VVSQGNLANY 2205
Cdd:PRK12406 106 TVLSVPTPPEIAAAYRispallTPPAGAIDWEGwlaqqepydgppvpqPQSMIYTSGTTGHPKGVrraapTPEQAAAAEQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2206 VAGVLPVLDLGEDASLATLSTVAADLGFtalfgALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAa 2285
Cdd:PRK12406 186 MRALIYGLKPGIRALLTGPLYHSAPNAY-----GLRAGRLGGVLVLQPRFDPEELLQLIERHRITHMHMVPTMFIRLLK- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2286 aggtavLPREC----------LVTGGEALTGALVQQ--VRALAPTlrIVNHYGPTETtvGILTCTVPEEWPVEQGVpVGH 2353
Cdd:PRK12406 260 ------LPEEVrakydvsslrHVIHAAAPCPADVKRamIEWWGPV--IYEYYGSTES--GAVTFATSEDALSHPGT-VGK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2354 PLAGNEAWVLDRFGLPAPVGVAGELYL-GGGNLSLGYWQRAEQTAErfvahplaPDRL-LYRSGDLARLDGEGRIVYLGR 2431
Cdd:PRK12406 329 AAPGAELRFVDEDGRPLPQGEIGEIYSrIAGNPDFTYHNKPEKRAE--------IDRGgFITSGDVGYLDADGYLFLCDR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2432 GDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGAN------GVLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRA 2505
Cdd:PRK12406 401 KRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEfgealmAVVEPQPGATLDEADIRAQLKARLAGYKVPKHIEI 480
|
490
....*....|....*....
gi 1246793773 2506 VESMPRLGNGKIDRQALAD 2524
Cdd:PRK12406 481 MAELPREDSGKIFKRRLRD 499
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
3544-3946 |
3.79e-17 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 88.50 E-value: 3.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3544 ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVCLSVSQ 3623
Cdd:PLN02246 50 VYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3624 -------RALAVELPGTALCLDDPFTR----AQLDAVEPGELPEV---PTEAPAyLIYTSGSTGTPKGVVVTHRNverLF 3689
Cdd:PLN02246 130 scyvdklKGLAEDDGVTVVTIDDPPEGclhfSELTQADENELPEVeisPDDVVA-LPYSSGTTGLPKGVMLTHKG---LV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3690 TAATQ-----TGRFSFDEHD----VWSLFHSHAFDFAVweLWGawLYGGRAVLvpeaVCRQPD--AFLDLLAEYGVTVLN 3758
Cdd:PLN02246 206 TSVAQqvdgeNPNLYFHSDDvilcVLPMFHIYSLNSVL--LCG--LRVGAAIL----IMPKFEigALLELIQRHKVTIAP 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3759 QTPSAFYAL-QSQAMRRELALNVRAVVFG----GEALEPSrlqpWRERYPQAELVNMYGITET----TVHVSFhrlSDED 3829
Cdd:PLN02246 278 FVPPIVLAIaKSPVVEKYDLSSIRMVLSGaaplGKELEDA----FRAKLPNAVLGQGYGMTEAgpvlAMCLAF---AKEP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3830 LQSPTSRIGSALPDLAVHVLDA-AGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGS 3908
Cdd:PLN02246 351 FPVKSGSCGTVVRNAELKIVDPeTGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDG---WLHTGDIGYIDDDDE 427
|
410 420 430
....*....|....*....|....*....|....*...
gi 1246793773 3909 LEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAV 3946
Cdd:PLN02246 428 LFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAV 465
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
1142-1558 |
3.79e-17 |
|
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380465 [Multi-domain] Cd Length: 423 Bit Score: 87.26 E-value: 3.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1142 LSPIQRWF-FDSAPAQ-PDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFE-RADGQWRQQVAAPGPAPaIQAQ 1218
Cdd:cd19543 4 LSPMQEGMlFHSLLDPgSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVwEGLGEPLQVVLKDRKLP-WREL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1219 DWRG--AADLDSRVDAAFARMQEAT--PLAGPLVALTHAHCDDGE-RLLICAHHLIVDAVSWRLLLGELFDGLAALARGE 1293
Cdd:cd19543 83 DLSHlsEAEQEAELEALAEEDRERGfdLARAPLMRLTLIRLGDDRyRLVWSFHHILLDGWSLPILLKELFAIYAALGEGQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1294 AwTPSARGASYADYVEAL--READDAQRfdagFWRE-LAAQPMQA-LPQDRPVALADARQsnVGRIVQTLDAGLTADLLE 1369
Cdd:cd19543 163 P-PSLPPVRPYRDYIAWLqrQDKEAAEA----YWREyLAGFEEPTpLPKELPADADGSYE--PGEVSFELSAELTARLQE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1370 RAgeayrcRTDEVllialaralatrTGRNRL---W---LDRERHGRDVL-----DGRDwSSVLGWYTAV----HPLPLDL 1434
Cdd:cd19543 236 LA------RQHGV------------TLNTVVqgaWallLSRYSGRDDVVfgttvSGRP-AELPGIETMVglfiNTLPVRV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1435 GVADGPAQIGALKE-QIRALARRGLDYMPLvasARIPAL-PAGQLLFNyHGVVdagahpaFEVEPRTLASGNGADNPPGA 1512
Cdd:cd19543 297 RLDPDQTVLELLKDlQAQQLELREHEYVPL---YEIQAWsEGKQALFD-HLLV-------FENYPVDESLEEEQDEDGLR 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 1513 LVEINARVQ-----------AGRLGLVWNYAGEAYDAATIEAWSQAFAAELAALVAH 1558
Cdd:cd19543 366 ITDVSAEEQtnypltvvaipGEELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAAN 422
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
3547-3989 |
6.42e-17 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 87.90 E-value: 6.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3547 YATLDRRSSQLATLL-IRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSG---VCLSVS 3622
Cdd:cd17632 70 YAELWERVGAVAAAHdPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEprlLAVSAE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3623 QRALAVEL------PGTALCLD----DPFTRAQLDA------------------------VEPGEL--PEVPTEAPAYLI 3666
Cdd:cd17632 150 HLDLAVEAvleggtPPRLVVFDhrpeVDAHRAALESarerlaavgipvttltliavrgrdLPPAPLfrPEPDDDPLALLI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3667 YTSGSTGTPKGVVVTHRNVERLFTAATQT-GRFSFDEHDVWSLFHSHAFDFAVweLWGAWLYGGRAVLVPE--------- 3736
Cdd:cd17632 230 YTSGSTGTPKGAMYTERLVATFWLKVSSIqDIRPPASITLNFMPMSHIAGRIS--LYGTLARGGTAYFAAAsdmstlfdd 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3737 -AVCRQPDAFL-----DLL-----AEYGVTVLNQTPSAFYALQSQAMRRELALNVR-AVVFGGEALEPSRLQPWRERYPQ 3804
Cdd:cd17632 308 lALVRPTELFLvprvcDMLfqryqAELDRRSVAGADAETLAERVKAELRERVLGGRlLAAVCGSAPLSAEMKAFMESLLD 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3805 AELVNMYGITETTV----------HVSFHRLSDedlqsptsrigsaLPDLAVHVLDaagQPVPLgvvGELVVEGDGVAQG 3874
Cdd:cd17632 388 LDLHDGYGSTEAGAvildgvivrpPVLDYKLVD-------------VPELGYFRTD---RPHPR---GELLVKTDTLFPG 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3875 YWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKL-RGYRIEPGEIAAKIASLPQVSDaaVTVEGQGE 3953
Cdd:cd17632 449 YYKRPEVTAEVFDEDG---FYRTGDVMAELGPDRLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVRQ--IFVYGNSE 523
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1246793773 3954 GAWLMAYAVAADGA---EPDPQ---SLREALRAL-----LPDYMLPR 3989
Cdd:cd17632 524 RAYLLAVVVPTQDAlagEDTARlraALAESLQRIareagLQSYEIPR 570
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
2047-2522 |
7.45e-17 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 87.51 E-value: 7.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2047 QMPAQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVAL-CLPRtfaqlAAMAAVWhRGAAWLP--LDPQHPDA 2123
Cdd:PRK06155 32 ERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALmCGNR-----IEFLDVF-LGCAWLGaiAVPINTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2124 R--QIA-VLDDSGAR-IVIGWGAAPAWVPASVRWLDAESV--LDVVSAYEEPPRVDV----------------DADTPAy 2181
Cdd:PRK06155 106 RgpQLEhILRNSGARlLVVEAALLAALEAADPGDLPLPAVwlLDAPASVSVPAGWSTaplppldapapaaavqPGDTAA- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2182 LIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALA 2261
Cdd:PRK06155 185 ILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVLEPRFSASGFWPAV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2262 AHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPRECLVTGGEAltgALVQQVRALApTLRIVNHYGPTETTVGILTctvpe 2341
Cdd:PRK06155 265 RRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPA---ALHAAFRERF-GVDLLDGYGSTETNFVIAV----- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2342 EWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGG---GNLSLGYWQRAEQTAErfvahplAPDRLLYRSGDLA 2418
Cdd:PRK06155 336 THGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRAdepFAFATGYFGMPEKTVE-------AWRNLWFHTGDRV 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2419 RLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIqGSLEGVA---EALAQ--- 2492
Cdd:PRK06155 409 VRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAV-VLRDGTAlepVALVRhce 487
|
490 500 510
....*....|....*....|....*....|.
gi 1246793773 2493 -RLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:PRK06155 488 pRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
3557-4007 |
7.65e-17 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 87.55 E-value: 7.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3557 LATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVD-----PHAPAAR---RGFILEDSGVCLSVSQRALAV 3628
Cdd:PLN02860 45 LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNyrwsfEEAKSAMllvRPVMLVTDETCSSWYEELQND 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3629 ELP--GTALCLDDPFTR---AQLDAVEPGELPE---VPTE-----AP--AYLI-YTSGSTGTPKGVVVTHRN--VERLFT 3690
Cdd:PLN02860 125 RLPslMWQVFLESPSSSvfiFLNSFLTTEMLKQralGTTEldyawAPddAVLIcFTSGTTGRPKGVTISHSAliVQSLAK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3691 AATqtgrFSFDEHDVW----SLFHSHAFDFAVWELwgawLYGGRAVLVPEAvcrQPDAFLDLLAEYGVTVLNQTPSAFYA 3766
Cdd:PLN02860 205 IAI----VGYGEDDVYlhtaPLCHIGGLSSALAML----MVGACHVLLPKF---DAKAALQAIKQHNVTSMITVPAMMAD 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3767 LQS---QAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQSP--TSRIGSAL 3841
Cdd:PLN02860 274 LISltrKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEACSSLTFMTLHDPTLESPkqTLQTVNQT 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3842 PDLAVHVLDAA--GQPVP---LGV-------VGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSL 3909
Cdd:PLN02860 354 KSSSVHQPQGVcvGKPAPhveLKIgldessrVGRILTRGPHVMLGYWGQNSETASVLSNDG---WLDTGDIGWIDKAGNL 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3910 EYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEgAWLMAYAVA----------ADGAEPD--------P 3971
Cdd:PLN02860 431 WLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVV--GVPD-SRLTEMVVAcvrlrdgwiwSDNEKENakknltlsS 507
|
490 500 510
....*....|....*....|....*....|....*...
gi 1246793773 3972 QSLREALRAL-LPDYMLPRLI-QLLPALPLTANGKLDR 4007
Cdd:PLN02860 508 ETLRHHCREKnLSRFKIPKLFvQWRKPFPLTTTGKIRR 545
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
542-1044 |
8.17e-17 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 87.12 E-value: 8.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 542 ARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQ 621
Cdd:PRK13382 50 AIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 622 ARRAEVVAASGCDAVLTDAQglagFAPSVAIAVD----------------ELKLDGAGENGSGEN--AAPNQLAYILYTS 683
Cdd:PRK13382 130 PALAEVVTREGVDTVIYDEE----FSATVDRALAdcpqatrivawtdedhDLTVEVLIAAHAGQRpePTGRKGRVILLTS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 684 GSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARpdELLEPQRFLAFLSER 763
Cdd:PRK13382 206 GTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWGFSQLVLAASLACTIVTR--RRFDPEATLDLIDRH 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 764 AITVTDLAPAYANELVR--ASVADDWRDLALRCLVVGGDVLPVALAQRWFELGLDrrcALINAYGPTEA---TISSHYHR 838
Cdd:PRK13382 284 RATGLAVVPVMFDRIMDlpAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGD---VIYNNYNATEAgmiATATPADL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 839 VQAID-ASRPvPLGQLLpgriaAVLDAHGRIVPRGVCGELALGGIGLAEGYrgdAAASERRFAplrlpSGeslrMYRSGD 917
Cdd:PRK13382 361 RAAPDtAGRP-AEGTEI-----RILDQDFREVPTGEVGTIFVRNDTQFDGY---TSGSTKDFH-----DG----FMASGD 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 918 RVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQV-RAAAAGVVGEGAAQRLVAWVECAGEDGFGQADLNQTD 996
Cdd:PRK13382 423 VGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVaEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHV 502
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1246793773 997 SDQteserwhralcerLPAYMVPTQFVALPRLPRNASGKIDRRALPAP 1044
Cdd:PRK13382 503 RDN-------------LANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
2052-2528 |
8.58e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 87.11 E-value: 8.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPR------TFAQLAAMAA----VWHR------------ 2109
Cdd:PRK06164 26 AVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNciewvvLFLACARLGAtviaVNTRyrshevahilgr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2110 -GAAWLPLDPQH-----------------PDARQIAVLDDSGArivigwgAAPAWVPASVRWLDAESVLDVVSAYEEPPR 2171
Cdd:PRK06164 106 gRARWLVVWPGFkgidfaailaavppdalPPLRAIAVVDDAAD-------ATPAPAPGARVQLFALPDPAPPAAAGERAA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2172 vdvDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPA 2251
Cdd:PRK06164 179 ---DPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEPV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2252 elaFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPRECLVtGGEALTGA---LVQQVRALAPTLRIVnhYGPT 2328
Cdd:PRK06164 256 ---FDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLF-GFASFAPAlgeLAALARARGVPLTGL--YGSS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2329 EttVGILTCTVPEEWPVEQGVPVGHPLAGNEAWVLDR---FGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPL 2405
Cdd:PRK06164 330 E--VQALVALQPATDPVSVRIEGGGRPASPEARVRARdpqDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGY 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2406 apdrllYRSGDLARLDGEGRIVYLGR-GDHqVKIRGYRVELGEVEQVLAQLPGVEVAAVLAL-------PGANGVLQLGA 2477
Cdd:PRK06164 408 ------FRTGDLGYTRGDGQFVYQTRmGDS-LRLGGFLVNPAEIEHALEALPGVAAAQVVGAtrdgktvPVAFVIPTDGA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 2478 ciQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRL--GNG-KIDRQALADLLQQ 2528
Cdd:PRK06164 481 --SPDEAGLMAACREALAGFKVPARVQVVEAFPVTesANGaKIQKHRLREMAQA 532
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
1142-1557 |
8.75e-17 |
|
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380462 [Multi-domain] Cd Length: 427 Bit Score: 86.28 E-value: 8.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1142 LSPIQR--WFFDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERAD-GQWRQQVAAPGPAPAIQAQ 1218
Cdd:cd19539 4 LSFAQErlWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDgGVPRQEILPPGPAPLEVRD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1219 DWRGAADLDsRVDAAFARMQEATP--LAG--PLVALTHAHCDDGERLLICAHHLIVDAVSWRLLLGELFDGLAALARGEA 1294
Cdd:cd19539 84 LSDPDSDRE-RRLEELLRERESRGfdLDEepPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1295 WTPSARGASYADYVEALREADDAQRFDA--GFWRE-LAAQPMQALPQDRPVALADARQSNVGRIVqtLDAGLTADLLERA 1371
Cdd:cd19539 163 APLPELRQQYKEYAAWQREALAAPRAAEllDFWRRrLRGAEPTALPTDRPRPAGFPYPGADLRFE--LDAELVAALRELA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1372 GEAyRCRTDEVLLIALARALATRTGRNRLWLDRERHGRDvldgRDW-SSVLGWYTAVHPLPLDLGvadgpaQIGALKEQI 1450
Cdd:cd19539 241 KRA-RSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRN----HPRfESTVGFFVNLLPLRVDVS------DCATFRDLI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1451 RALARRgldympLVASARIPALPAGQLLFNYHGVVDAGAHPAFEV---------EPRTLASGN----GADNPPGALVEIN 1517
Cdd:cd19539 310 ARVRKA------LVDAQRHQELPFQQLVAELPVDRDAGRHPLVQIvfqvtnapaGELELAGGLsyteGSDIPDGAKFDLN 383
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1246793773 1518 ARV--QAGRLGLVWNYAGEAYDAATIEAWSQAFAAELAALVA 1557
Cdd:cd19539 384 LTVteEGTGLRGSLGYATSLFDEETIQGFLADYLQVLRQLLA 425
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
3540-4033 |
1.13e-16 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 87.12 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3540 AEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPV----DPHAPAAR------RG 3609
Cdd:PRK00174 94 GDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVfggfSAEALADRiidagaKL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3610 FILEDSGV------------------CLSVsQRALAVELPGTALCLDDP-------FTRAQLDAVEPgelPEVPTEAPAY 3664
Cdd:PRK00174 174 VITADEGVrggkpiplkanvdealanCPSV-EKVIVVRRTGGDVDWVEGrdlwwheLVAGASDECEP---EPMDAEDPLF 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3665 LIYTSGSTGTPKGVVVThrnverlfTA-----ATQTGRFSFDEH---------DV-WSLFHSHAfdfavwelwgawLYG- 3728
Cdd:PRK00174 250 ILYTSGSTGKPKGVLHT--------TGgylvyAAMTMKYVFDYKdgdvywctaDVgWVTGHSYI------------VYGp 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3729 ---GRAVLVPEAVCRQPDA--FLDLLAEYGVTVLNQTPSAFYALqsqaMR--------RELA-LNVRAVVfgGEALEPsr 3794
Cdd:PRK00174 310 lanGATTLMFEGVPNYPDPgrFWEVIDKHKVTIFYTAPTAIRAL----MKegdehpkkYDLSsLRLLGSV--GEPINP-- 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3795 lQPWR--------ERYPqaeLVNMYGITETTVHvsfhrlsdedLQSPT-----SRIGSA---LPDLAVHVLDAAGQPVPL 3858
Cdd:PRK00174 382 -EAWEwyykvvggERCP---IVDTWWQTETGGI----------MITPLpgatpLKPGSAtrpLPGIQPAVVDEEGNPLEG 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3859 GVVGELVVEGD--GVAQGYWQRPeltaERFVERGGQRF---YRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAA 3933
Cdd:PRK00174 448 GEGGNLVIKDPwpGMMRTIYGDH----ERFVKTYFSTFkgmYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIES 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3934 KIASLPQVSDAAVT-----VEGQGegawLMAYAVAADGAEPDPQsLREALRALLPDYM----LPRLIQLLPALPLTANGK 4004
Cdd:PRK00174 524 ALVAHPKVAEAAVVgrpddIKGQG----IYAFVTLKGGEEPSDE-LRKELRNWVRKEIgpiaKPDVIQFAPGLPKTRSGK 598
|
570 580 590
....*....|....*....|....*....|....*...
gi 1246793773 4005 LDRKALPK-----PETQD----RDEGVLESASERRLAE 4033
Cdd:PRK00174 599 IMRRILRKiaegeEILGDtstlADPSVVEKLIEARQNR 636
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
530-1038 |
1.48e-16 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 86.40 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 530 APRTVGNVVDAIARAADEFPERAAL-----ETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLD-WYCLLl 603
Cdd:cd05970 12 VPENFNFAYDVVDAMAKEYPDKLALvwcddAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEfWYSLL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 604 GAWRAGLSVIPL-------DTEWpQARRAEV--VAASGCDAVLTDAQGLAGFAPSVAIAV-------------DELKLDG 661
Cdd:cd05970 91 ALHKLGAIAIPAthqltakDIVY-RIESADIkmIVAIAEDNIPEEIEKAAPECPSKPKLVwvgdpvpegwidfRKLIKNA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 662 AG--ENGSGENAAPNQLAYILY-TSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVA----GLAVdttLEQIL 734
Cdd:cd05970 170 SPdfERPTANSYPCGEDILLVYfSSGTTGMPKMVEHDFTYPLGHIVTAKYWQNVREGGLHLTVAdtgwGKAV---WGKIY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 735 AAWSRGACVVARPDELLEPQRFLAFLSERAITVTDLAPAYANELVRASVADdwRDLA-LRCLVVGGDVLPVALAQRWFEL 813
Cdd:cd05970 247 GQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSR--YDLSsLRYCTTAGEALNPEVFNTFKEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 814 -GLDrrcaLINAYGPTEATISshyhrVQAIDASRPVP--LGQLLPGRIAAVLDAHGRIVPRGVCGELALG-----GIGLA 885
Cdd:cd05970 325 tGIK----LMEGFGQTETTLT-----IATFPWMEPKPgsMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRtskgkPVGLF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 886 EGYRGDAAASERRFAplrlpSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQV-RAAAA 964
Cdd:cd05970 396 GGYYKDAEKTAEVWH-----DG----YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVlECAVT 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 965 GVVGEGAAQRLVAWVECAgedgfgqadlnqtdSDQTESERWHRAL---CERLPA-YMVPTQFVALPRLPRNASGKIDR 1038
Cdd:cd05970 467 GVPDPIRGQVVKATIVLA--------------KGYEPSEELKKELqdhVKKVTApYKYPRIVEFVDELPKTISGKIRR 530
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
2063-2522 |
2.18e-16 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 85.76 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2063 TYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQ-HPDarQIA-VLDDSGARIV--- 2137
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRlFPE--QIAyIINHAEDRVVfvd 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2138 -----IGWGAAPAW----------------VPASVRWLDAESVLDVVSAYEEPPrvDVDADTPAYLIYTSGSTGTPKGVV 2196
Cdd:cd12119 105 rdflpLLEAIAPRLptvehvvvmtddaampEPAGVGVLAYEELLAAESPEYDWP--DFDENTAAAICYTSGTTGNPKGVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2197 VSQGNLANYVAGVLPVLDLGEDASLATLSTV------AADLGFTA-LFGA--LLSGRrvRLLPAELAfdaqalaAHLQAH 2267
Cdd:cd12119 183 YSHRSLVLHAMAALLTDGLGLSESDVVLPVVpmfhvnAWGLPYAAaMVGAklVLPGP--YLDPASLA-------ELIERE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2268 PVDCLKIVPS--HLAGLLAAAGGTAVLPRECLVTGGEALTGALVQqvRALAPTLRIVNHYGPTET----TVGILTCTVPE 2341
Cdd:cd12119 254 GVTFAAGVPTvwQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIE--AFEERGVRVIHAWGMTETsplgTVARPPSEHSN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2342 EwPVEQGVPV----GHPLAGNEAWVLDRFG--LPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVahplapDRLLyRSG 2415
Cdd:cd12119 332 L-SEDEQLALrakqGRPVPGVELRIVDDDGreLPWDGKAVGELQVRGPWVTKSYYKNDEESEALTE------DGWL-RTG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2416 DLARLDGEG--RIVylGRGDHQVKIRG---YRVELgevEQVLAQLPGVEVAAVLALPG--------ANGVLQLGAciQGS 2482
Cdd:cd12119 404 DVATIDEDGylTIT--DRSKDVIKSGGewiSSVEL---ENAIMAHPAVAEAAVIGVPHpkwgerplAVVVLKEGA--TVT 476
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1246793773 2483 LEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:cd12119 477 AEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
673-1041 |
2.26e-16 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 85.46 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 673 PNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVDTTLEQILaawsrGACVVAR 746
Cdd:cd05909 146 PDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFgalpffHSFGLTGCLWLPLLS-----GIKVVFH 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 747 PDElLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRdlALRCLVVGGDVLPVALAQRWFEL-GLdrrcALINAY 825
Cdd:cd05909 221 PNP-LDYKKIPELIYDKKATILLGTPTFLRGYARAAHPEDFS--SLRLVVAGAEKLKDTLRQEFQEKfGI----RILEGY 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 826 GPTEATISSHYHRVQAidASRPVPLGQLLPGRIAAVLDAHGRI-VPRGVCGELALGGIGLAEGYrgdaaaserrfapLRL 904
Cdd:cd05909 294 GTTECSPVISVNTPQS--PNKEGTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLVRGPNVMLGY-------------LNE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 905 PSGESLRM----YRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQL--PQVRAAAAGVVGEGAAQRLVAW 978
Cdd:cd05909 359 PELTSFAFgdgwYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlpEDNEVAVVSVPDGRKGEKIVLL 438
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 979 VecagedgfgqadlnqTDSDQTESErWHRALCE-RLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05909 439 T---------------TTTDTDPSS-LNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
1645-1977 |
2.70e-16 |
|
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380463 [Multi-domain] Cd Length: 433 Bit Score: 84.78 E-value: 2.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1645 VRRQPMLRTAIVwEGLSVPHQIVLADAAAPwqtLDWSALDDAAQDaqLQRWLADDAAQGVDFAHAPLARMSLIGRGGGRY 1724
Cdd:cd19540 49 VARHESLRTVFP-EDDGGPYQVVLPAAEAR---PDLTVVDVTEDE--LAARLAEAARRGFDLTAELPLRARLFRLGPDEH 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1725 WLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGATLRLPPAPgFQaYLD---WRERQ---------DLARQRGWWRERLS 1792
Cdd:cd19540 123 VLVLVVHHIAADGWSMAPLARDLATAYAARRAGRAPDWAPLP-VQ-YADyalWQRELlgdeddpdsLAARQLAYWRETLA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1793 G------------------YAGtaalpapvaaAHHPVqreecerRLSAHDSERLRAFCRERGCTLSdliaMVW--GLAN- 1851
Cdd:cd19540 201 GlpeelelptdrprpavasYRG----------GTVEF-------TIDAELHARLAALAREHGATLF----MVLhaALAVl 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1852 -ARYGNHDDVVLGATRSGRP-PELagvESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAENEAVGLgEILADSg 1929
Cdd:cd19540 260 lSRLGAGDDIPIGTPVAGRGdEAL---DDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLAAFAHQDVPF-ERLVEA- 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 1930 LDADR------LFASLLVVENFPAmAPAQLPfALRVRETRAANHYA---LTLRVSER 1977
Cdd:cd19540 335 LNPPRstarhpLFQVMLAFQNTAA-ATLELP-GLTVEPVPVDTGVAkfdLSFTLTER 389
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2181-2518 |
3.40e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 83.59 E-value: 3.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2181 YLIYTSGSTGTPKGVV-------VSQGNLANYVAGVLPVLDLGEDASLATLSTV---AADL----GFTALFGALLSGRRV 2246
Cdd:cd05924 7 YILYTGGTTGMPKGVMwrqedifRMLMGGADFGTGEFTPSEDAHKAAAAAAGTVmfpAPPLmhgtGSWTAFGGLLGGQTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2247 rLLPaELAFDAQALAAHLQAHPVDCLKIVpSHLAGLLAAAGGTAVLPREC-----LVTGGEALTGALVQQVRALAPTLRI 2321
Cdd:cd05924 87 -VLP-DDRFDPEEVWRTIEKHKVTSMTIV-GDAMARPLIDALRDAGPYDLsslfaISSGGALLSPEVKQGLLELVPNITL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2322 VNHYGPTETtvGILTCTVPEEWPVEQGVPVghpLAGNEAWVLDRFGLPAPVGVAGELYLG-GGNLSLGYWQRAEQTAERF 2400
Cdd:cd05924 164 VDAFGSSET--GFTGSGHSAGSGPETGPFT---RANPDTVVLDDDGRVVPPGSGGVGWIArRGHIPLGYYGDEAKTAETF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2401 vahPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGV---------------EVAAVLA 2465
Cdd:cd05924 239 ---PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVydvlvvgrpderwgqEVVAVVQ 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 2466 LPGANGVlqlgaciqgSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKID 2518
Cdd:cd05924 316 LREGAGV---------DLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
535-1043 |
3.42e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 85.36 E-value: 3.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 535 GNVVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALcLPRGLDWYCL-LLGAWRAGLSVI 613
Cdd:PRK07788 49 GPFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAV-LARNHRGFVLaLYAAGKVGARII 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 614 PLDTEWPQARRAEVVAASGCDAVLTDAQ--GLAGFAP-------SVAIAVDELKLDGAG--------ENGSGEN--AAPN 674
Cdd:PRK07788 128 LLNTGFSGPQLAEVAAREGVKALVYDDEftDLLSALPpdlgrlrAWGGNPDDDEPSGSTdetlddliAGSSTAPlpKPPK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 675 QLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARpdELLEPQ 754
Cdd:PRK07788 208 PGGIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLAMALGSTVVLR--RRFDPE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 755 RFLAFLSERAITVTDLAPAYANELVRasVADDWR---DL-ALRCLVVGGDVLPVALAQRWFELGLDRRCaliNAYGPTE- 829
Cdd:PRK07788 286 ATLEDIAKHKATALVVVPVMLSRILD--LGPEVLakyDTsSLKIIFVSGSALSPELATRALEAFGPVLY---NLYGSTEv 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 830 --ATISSHYHRVQAidasrPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDaaaserrfaplrlPSG 907
Cdd:PRK07788 361 afATIATPEDLAEA-----PGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDG-------------RDK 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 908 ESLR-MYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQRLVAWVecAGED 985
Cdd:PRK07788 423 QIIDgLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVeAAVIGVDDEEFGQRLRAFV--VKAP 500
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 986 GfgqADLnqtDSDQTesERWHRalcERLPAYMVPTQFVALPRLPRNASGKIDRRALPA 1043
Cdd:PRK07788 501 G---AAL---DEDAI--KDYVR---DNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
2320-2522 |
3.51e-16 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 85.12 E-value: 3.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2320 RIVNHYGPTETTVGILTCTVPEE--WPveqgvPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGG---GNLSLGYWQRAE 2394
Cdd:PRK08008 314 RLLTSYGMTETIVGIIGDRPGDKrrWP-----SIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2395 QTAErfvahPLAPDRLLYrSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPG------ 2468
Cdd:PRK08008 389 ATAK-----VLEADGWLH-TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDsirdea 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 2469 --ANGVLQLGACIqgSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:PRK08008 463 ikAFVVLNEGETL--SEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
2134-2528 |
3.78e-16 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 85.34 E-value: 3.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2134 ARIVIGWGAAPA--WVPASVRWLDAESVLD---VVSAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYV-- 2206
Cdd:PRK09274 126 ARRLFGWGKPSVrrLVTVGGRLLWGGTTLAtllRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIea 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2207 -----------------------------AGVLPVLDLGEDASL--ATLSTVAADLGFTALFG--ALLSgrrvRLLPAEL 2253
Cdd:PRK09274 206 lredygiepgeidlptfplfalfgpalgmTSVIPDMDPTRPATVdpAKLFAAIERYGVTNLFGspALLE----RLGRYGE 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2254 AfdaqalaahlQAHPVDCLKIVPShlagllaaaggtavlpreclvtGGEALTGALVQQVRA-LAPTLRIVNHYGPTE--- 2329
Cdd:PRK09274 282 A----------NGIKLPSLRRVIS----------------------AGAPVPIAVIERFRAmLPPDAEILTPYGATEalp 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2330 -TTVG---ILTCTVpEEWPVEQGVPVGHPLAGNE------------AWVLDrfgLPAPVGVAGELYLGGGNLSLGYWQRA 2393
Cdd:PRK09274 330 iSSIEsreILFATR-AATDNGAGICVGRPVDGVEvriiaisdapipEWDDA---LRLATGEIGEIVVAGPMVTRSYYNRP 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2394 EQTAERFVAHPLAPDRllYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVL 2473
Cdd:PRK09274 406 EATRLAKIPDGQGDVW--HRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVPGAQR 483
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 2474 --------QLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMP---RlGNGKIDRQALADLLQQ 2528
Cdd:PRK09274 484 pvlcvelePGVACSKSALYQELRALAAAHPHTAGIERFLIHPSFPvdiR-HNAKIFREKLAVWAAK 548
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
2062-2528 |
5.16e-16 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 84.64 E-value: 5.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2062 WTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDP----QHPDAR-----QIAVLDDS 2132
Cdd:cd05906 40 QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVpptyDEPNARlrklrHIWQLLGS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2133 gARIVIGWGAAPAWVPASVRWLDAESVLDVVSAYEEPPR----VDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAG 2208
Cdd:cd05906 120 -PVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAAdhdlPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2209 VLPVLDLGEDAslATLSTVAAD----LGFTALFGALLSGRRVRLLPAELAFDaqalaahlqahPVDCLKIVPSH------ 2278
Cdd:cd05906 199 KIQHNGLTPQD--VFLNWVPLDhvggLVELHLRAVYLGCQQVHVPTEEILAD-----------PLRWLDLIDRYrvtitw 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2279 ---------LAGLLAAAGGTAVLPR-ECLVTGGEALTGALVQQ-VRALAPT-LR---IVNHYGPTETTVGILTCTVPEEW 2343
Cdd:cd05906 266 apnfafallNDLLEEIEDGTWDLSSlRYLVNAGEAVVAKTIRRlLRLLEPYgLPpdaIRPAFGMTETCSGVIYSRSFPTY 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2344 PVEQG---VPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPlapdrlLYRSGDLARL 2420
Cdd:cd05906 346 DHSQAlefVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDG------WFRTGDLGFL 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2421 DgEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGV-----------------EVAAVLALPGANGVLQLGACIQgSL 2483
Cdd:cd05906 420 D-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVepsftaafavrdpgaetEELAIFFVPEYDLQDALSETLR-AI 497
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1246793773 2484 EGVAEALAQRLPEYLCPSrwrAVESMPRLGNGKIDRQALADLLQQ 2528
Cdd:cd05906 498 RSVVSREVGVSPAYLIPL---PKEEIPKTSLGKIQRSKLKAAFEA 539
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
2062-2524 |
6.98e-16 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 84.47 E-value: 6.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2062 WTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLP----LDP-------QHPDARQIAVLD 2130
Cdd:cd05970 48 FTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPathqLTAkdivyriESADIKMIVAIA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2131 DSGARIVIGwGAAP--------AWVPASVR--WLDAESVLDVVSAYEEPPRVDVDA--DTPAYLIYTSGSTGTPKgvVVS 2198
Cdd:cd05970 128 EDNIPEEIE-KAAPecpskpklVWVGDPVPegWIDFRKLIKNASPDFERPTANSYPcgEDILLVYFSSGTTGMPK--MVE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2199 QGNLanYVAGVLPVLDLGEDASLATLSTVAADLGFTA-----LFGALLSGRRVRLLPAELaFDAQALAAHLQAHPVDCLK 2273
Cdd:cd05970 205 HDFT--YPLGHIVTAKYWQNVREGGLHLTVADTGWGKavwgkIYGQWIAGAAVFVYDYDK-FDPKALLEKLSKYGVTTFC 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2274 IVPSHLAGLLAAAGGTAVLP--REClVTGGEALTGALVQQVRALApTLRIVNHYGPTETTVGILTCTVPEEWPVEqgvpV 2351
Cdd:cd05970 282 APPTIYRFLIREDLSRYDLSslRYC-TTAGEALNPEVFNTFKEKT-GIKLMEGFGQTETTLTIATFPWMEPKPGS----M 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2352 GHPLAGNEAWVLDRFGLPAPVGVAGELYL---GGGNLSL--GYWQRAEQTAERFVAHplapdrlLYRSGDLARLDGEGRI 2426
Cdd:cd05970 356 GKPAPGYEIDLIDREGRSCEAGEEGEIVIrtsKGKPVGLfgGYYKDAEKTAEVWHDG-------YYHTGDAAWMDEDGYL 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2427 VYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPG--------ANGVLQLGACIQGSLEGVAEALAQRLPE-Y 2497
Cdd:cd05970 429 WFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDpirgqvvkATIVLAKGYEPSEELKKELQDHVKKVTApY 508
|
490 500
....*....|....*....|....*..
gi 1246793773 2498 LCPSRWRAVESMPRLGNGKIDRQALAD 2524
Cdd:cd05970 509 KYPRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
2050-2529 |
1.45e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 83.28 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2050 AQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVL 2129
Cdd:PRK12583 34 REALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 DDSGARIVI------------------------GWGA---------------APAWVPASVRWLDAESVLDVVSAYEEPP 2170
Cdd:PRK12583 114 GQSGVRWVIcadafktsdyhamlqellpglaegQPGAlacerlpelrgvvslAPAPPPGFLAWHELQARGETVSREALAE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2171 R-VDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLAT-------LSTVAADLGFTALfGALLs 2242
Cdd:PRK12583 194 RqASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVpvplyhcFGMVLANLGCMTV-GACL- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2243 grrvrLLPAElAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAvLPRECLVTG---GEALTGALVQQVRALAPTL 2319
Cdd:PRK12583 272 -----VYPNE-AFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGN-FDLSSLRTGimaGAPCPIEVMRRVMDEMHMA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2320 RIVNHYGPTETT-VGILTCTvpeEWPVEQGV-PVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTA 2397
Cdd:PRK12583 345 EVQIAYGMTETSpVSLQTTA---ADDLERRVeTVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATA 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2398 ERFVAhplapDRLLYrSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGA 2477
Cdd:PRK12583 422 ESIDE-----DGWMH-TGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVA 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 2478 CI------QGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLLQQD 2529
Cdd:PRK12583 496 WVrlhpghAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREISIEE 553
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
512-1043 |
1.54e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 83.12 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 512 LSWPWPADELALddKREpAPRTVGNVVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALC 591
Cdd:PRK13383 15 LNPPSPRAVLRL--LRE-ASRGGTNPYTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 592 LPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTD---AQGLAGFAPSVAIaVDELKLDGAGENGSG 668
Cdd:PRK13383 92 CRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADnefAERIAGADDAVAV-IDPATAGAEESGGRP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 669 ENAAPNQLayILYTSGSTGIPKGVE--------VGHAALAAHIDAAAEALALSADDRVLHVAGLAVdttleqILAAWSRG 740
Cdd:PRK13383 171 AVAAPGRI--VLLTSGTTGKPKGVPrapqlrsaVGVWVTILDRTRLRTGSRISVAMPMFHGLGLGM------LMLTIALG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 741 ACVVARPDellepqrflaFLSERAITVTDLAPAYANELVRASVA------DDWRDL----ALRCLVVGGDVLPVALAQRW 810
Cdd:PRK13383 243 GTVLTHRH----------FDAEAALAQASLHRADAFTAVPVVLArilelpPRVRARnplpQLRVVMSSGDRLDPTLGQRF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 811 FELGLDrrcALINAYGPTEATISSHYHRVQAIDAsrPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRG 890
Cdd:PRK13383 313 MDTYGD---ILYNGYGSTEVGIGALATPADLRDA--PETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTD 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 891 DAAASerrfaplrLPSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQV-RAAAAGVVGE 969
Cdd:PRK13383 388 GGGKA--------VVDG----MTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVaDNAVIGVPDE 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 970 GAAQRLVAWVecAGEDGFGqadlnqTDSDQTESerwhrALCERLPAYMVPTQFVALPRLPRNASGKIDRRALPA 1043
Cdd:PRK13383 456 RFGHRLAAFV--VLHPGSG------VDAAQLRD-----YLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELPG 516
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
2052-2528 |
1.57e-15 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 83.27 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRT-------FAQLAA-----MAAVWHR---------- 2109
Cdd:COG1021 41 RIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVaefvivfFALFRAgaipvFALPAHRraeishfaeq 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2110 -GAAWLPLDPQHP--DARQIA--VLDD-SGARIVIGWGAAPAWVPasvrwLDAesvldVVSAYEEPPRVDVDADTPAYLI 2183
Cdd:COG1021 121 sEAVAYIIPDRHRgfDYRALAreLQAEvPSLRHVLVVGDAGEFTS-----LDA-----LLAAPADLSEPRPDPDDVAFFQ 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2184 YTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGED-ASLATLsTVA--ADLGFTALFGALLSGRRVRLLP---AELAFDA 2257
Cdd:COG1021 191 LSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADtVYLAAL-PAAhnFPLSSPGVLGVLYAGGTVVLAPdpsPDTAFPL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2258 QALAAhlqahpVDCLKIVPSHLAGLLAAAGGTAVLPR--ECLVTGGEALTGALVQQVR-ALAPTLRIVnhYGPTEttvGI 2334
Cdd:COG1021 270 IERER------VTVTALVPPLALLWLDAAERSRYDLSslRVLQVGGAKLSPELARRVRpALGCTLQQV--FGMAE---GL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2335 LTCTVPEEwPVE-----QGVPVGhplAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFvahplAPDR 2409
Cdd:COG1021 339 VNYTRLDD-PEEvilttQGRPIS---PDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAF-----TPDG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2410 LlYRSGDLARLDGEGRIVYLGRGDHQVkIRGyrvelGE------VEQVLAQLPGVEVAAVLALPGAngvlQLG----ACI 2479
Cdd:COG1021 410 F-YRTGDLVRRTPDGYLVVEGRAKDQI-NRG-----GEkiaaeeVENLLLAHPAVHDAAVVAMPDE----YLGerscAFV 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 2480 QG-----SLEGVAEALAQR-LPEYLCPSRWRAVESMPRLGNGKIDRQALADLLQQ 2528
Cdd:COG1021 479 VPrgeplTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALAA 533
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
2082-2524 |
1.59e-15 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 82.81 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2082 GVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGwgAAPAWvPASVRWLDAESVLD 2161
Cdd:cd05929 38 GVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEACAIIEIKAAALVCG--LFTGG-GALDGLEDYEAAEG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2162 vvsAYEEPPRVDVDAdtPAYLIYTSGSTGTPKGVVVS-QGNLANYVAGVLPVLDLGEDASLATLSTV----AAdlGFTAL 2236
Cdd:cd05929 115 ---GSPETPIEDEAA--GWKMLYSGGTTGRPKGIKRGlPGGPPDNDTLMAAALGFGPGADSVYLSPAplyhAA--PFRWS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2237 FGALLSGRRVRLLPAelaFDAQALAAHLQAHPVDCLKIVPSHLAGLlaaaggtAVLPREclVTGGEALTG---------- 2306
Cdd:cd05929 188 MTALFMGGTLVLMEK---FDPEEFLRLIERYRVTFAQFVPTMFVRL-------LKLPEA--VRNAYDLSSlkrvihaaap 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2307 ---ALVQQVRALAPTlRIVNHYGPTETtVGiLTCTVPEEWPVEQGvPVGHPLAGnEAWVLDRFGLPAPVGVAGELYLGGG 2383
Cdd:cd05929 256 cppWVKEQWIDWGGP-IIWEYYGGTEG-QG-LTIINGEEWLTHPG-SVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2384 NLSLgYWQRAEQTAERFVAHPlapdrllYRS-GDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAA 2462
Cdd:cd05929 331 PGFE-YTNDPEKTAAARNEGG-------WSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAA 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 2463 VLALPGANGVLQLGACIQGSLEGV-----AEALA----QRLPEYLCPSRWRAVESMPRLGNGKIDRQALAD 2524
Cdd:cd05929 403 VVGVPDEELGQRVHAVVQPAPGADagtalAEELIaflrDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
3521-4010 |
1.86e-15 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 83.13 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3521 LVSRFAEIARRYPARIAVSAEDG--ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVP 3598
Cdd:PRK05857 16 VLDRVFEQARQQPEAIALRRCDGtsALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3599 VDPHAPAA---RRGFILEDSGVCLSVSQRALAVELPGTALCL---------DDPFTRAQLDAVEPGELPEVPTEAPAYLI 3666
Cdd:PRK05857 96 ADGNLPIAaieRFCQITDPAAALVAPGSKMASSAVPEALHSIpviavdiaaVTRESEHSLDAASLAGNADQGSEDPLAMI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3667 YTSGSTGTPKGVVVTHRNverlFTAATQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAW------LYGGRAVLVPEavcr 3740
Cdd:PRK05857 176 FTSGTTGEPKAVLLANRT----FFAVPDILQKEGLNWVTWVVGETTYSPLPATHIGGLWwiltclMHGGLCVTGGE---- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3741 QPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELAL-NVRAVVFGGealepSRLQPWRERYPQAELV---NMYGITET 3816
Cdd:PRK05857 248 NTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVpSLRLVGYGG-----SRAIAADVRFIEATGVrtaQVYGLSET 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3817 TVHVSFHRLSDEDLQS-PTSRIGSALPDLAVHVLDAAG------QPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVEr 3889
Cdd:PRK05857 323 GCTALCLPTDDGSIVKiEAGAVGRPYPGVDVYLAATDGigptapGAGPSASFGTLWIKSPANMLGYWNNPERTAEVLID- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3890 ggqRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEGAWLMAYAVAAdGAEP 3969
Cdd:PRK05857 402 ---GWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVA-SAEL 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1246793773 3970 DPQSLREALRALLPDY-------MLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK05857 478 DESAARALKHTIAARFrresepmARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
3525-4004 |
2.14e-15 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 83.09 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAE--IARRYPARIAV--SAEDG---ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYV 3597
Cdd:cd05943 72 YAEnlLRHADADDPAAiyAAEDGertEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3598 PVDP----HAPAARRG-----FILEDSGV-------CLSVSQRALAVELPGT--ALCLDDPFTRAQLDA----------- 3648
Cdd:cd05943 152 SCSPdfgvPGVLDRFGqiepkVLFAVDAYtyngkrhDVREKVAELVKGLPSLlaVVVVPYTVAAGQPDLskiakaltled 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3649 -VEPGELPE-----VPTEAPAYLIYTSGSTGTPK-------GVVVTHRNVERLFTAATQTGRFSFdehdvwslfhshaFD 3715
Cdd:cd05943 232 fLATGAAGElefepLPFDHPLYILYSSGTTGLPKcivhgagGTLLQHLKEHILHCDLRPGDRLFY-------------YT 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3716 FAVWELWGaWLYGGRA-----VLVPEA-VCRQPDAFLDLLAEYGVTVLNqTPSAFYALQSQA---MRRELALN-VRAVVF 3785
Cdd:cd05943 299 TCGWMMWN-WLVSGLAvgatiVLYDGSpFYPDTNALWDLADEEGITVFG-TSAKYLDALEKAglkPAETHDLSsLRTILS 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3786 GGEALEPSrLQPW--RERYPQAELVNMYGITE-------TTVHVSFHRlsdEDLQSPTsrIGsalpdLAVHVLDAAGQPV 3856
Cdd:cd05943 377 TGSPLKPE-SFDYvyDHIKPDVLLASISGGTDiiscfvgGNPLLPVYR---GEIQCRG--LG-----MAVEAFDEEGKPV 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3857 PlGVVGELVVEGDGVAQ--GYWQRPELTAER---FVERGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEI 3931
Cdd:cd05943 446 W-GEKGELVCTKPFPSMpvGFWNDPDGSRYRaayFAKYPG--VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEI 522
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 3932 AAKIASLPQVSDA-AVTVEGQGEGAWLMAYAVAADGAEPDP---QSLREALRALLPDYMLPRLIQLLPALPLTANGK 4004
Cdd:cd05943 523 YRVVEKIPEVEDSlVVGQEWKDGDERVILFVKLREGVELDDelrKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGK 599
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
3656-3921 |
3.35e-15 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 82.17 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3656 EVPTEAPAYLIYTSGSTGTPKGVVVTHRNVerlftAATQTGRFSF---DEHDVWSLFHS--HAFDFAVWELWgAWLYGGR 3730
Cdd:PRK06334 179 DKDPEDVAVILFTSGTEKLPKGVPLTHANL-----LANQRACLKFfspKEDDVMMSFLPpfHAYGFNSCTLF-PLLSGVP 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3731 AVLVPEAVcrQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELAL-NVRAVVFGGEALEPSRLQPWRERYPQAELVN 3809
Cdd:PRK06334 253 VVFAYNPL--YPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLpSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQ 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3810 MYGITETTVHVSfhrLSDEDLQSPTSRIGSALPDLAVHVLDAAGQ-PVPLGVVGELVVEGDGVAQGYWQRPEltAERFVE 3888
Cdd:PRK06334 331 GYGTTECSPVIT---INTVNSPKHESCVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLGEDF--GQGFVE 405
|
250 260 270
....*....|....*....|....*....|...
gi 1246793773 3889 RGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKL 3921
Cdd:PRK06334 406 LGGETWYVTGDLGYVDRHGELFLKGRLSRFVKI 438
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
3663-3921 |
4.36e-15 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 81.49 E-value: 4.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3663 AYLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFS--FDEHDVW--SLFHSHAFDFAVwEL----WGAWL-YGGRAVL 3733
Cdd:cd17639 91 ACIMYTSGSTGNPKGVMLTHGNL--VAGIAGLGDRVPelLGPDDRYlaYLPLAHIFELAA-ENvclyRGGTIgYGSPRTL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3734 VPeAVCRQPDAflDLLaEY------GV---------TVLNQTPSA-------F---YALQSQAM---------------- 3772
Cdd:cd17639 168 TD-KSKRGCKG--DLT-EFkptlmvGVpaiwdtirkGVLAKLNPMgglkrtlFwtaYQSKLKALkegpgtplldelvfkk 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3773 -RRELALNVRAVVFGGEALEPSrlqpwrerypQAELVNM--------YGITETTVHVSFHRLSDEDlqspTSRIGSALPD 3843
Cdd:cd17639 244 vRAALGGRLRYMLSGGAPLSAD----------TQEFLNIvlcpviqgYGLTETCAGGTVQDPGDLE----TGRVGPPLPC 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3844 LAVHVLD------AAGQPVPLGvvgELVVEGDGVAQGYWQRPELTAERFVergGQRFYRSGDLGRYRADGSLEYRGRGDD 3917
Cdd:cd17639 310 CEIKLVDweeggySTDKPPPRG---EILIRGPNVFKGYYKNPEKTKEAFD---GDGWFHTGDIGEFHPDGTLKIIDRKKD 383
|
....
gi 1246793773 3918 QVKL 3921
Cdd:cd17639 384 LVKL 387
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
2170-2524 |
4.39e-15 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 81.85 E-value: 4.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2170 PRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLanyvagvlpvldlgedasLATLSTVAADLGFTalfGALLSGRRVRL- 2248
Cdd:PRK08751 201 PTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNL------------------VANMQQAHQWLAGT---GKLEEGCEVVIt 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2249 -LPA---------ELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPRECLVTGG----------EALTGAL 2308
Cdd:PRK08751 260 aLPLyhifaltanGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGfdqidfsslkMTLGGGM 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2309 VQQvRALAPT------LRIVNHYGPTETTVGilTCTVPEEWPVEQGvPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGG 2382
Cdd:PRK08751 340 AVQ-RSVAERwkqvtgLTLVEAYGLTETSPA--ACINPLTLKEYNG-SIGLPIPSTDACIKDDAGTVLAIGEIGELCIKG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2383 GNLSLGYWQRAEQTAERFVAHPLapdrllYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGV-EVA 2461
Cdd:PRK08751 416 PQVMKGYWKRPEETAKVMDADGW------LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVlEVA 489
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 2462 AVlALPGANGVLQLGACIQG-----SLEGVAEALAQRLPEYLCPsrwRAVE---SMPRLGNGKIDRQALAD 2524
Cdd:PRK08751 490 AV-GVPDEKSGEIVKVVIVKkdpalTAEDVKAHARANLTGYKQP---RIIEfrkELPKTNVGKILRRELRD 556
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
1143-1361 |
4.85e-15 |
|
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380464 [Multi-domain] Cd Length: 401 Bit Score: 80.43 E-value: 4.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1143 SPIQRWFFDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASF--ERADGQWRQQVAAPGPAPAIQAQDw 1220
Cdd:cd19542 5 TPMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFveSSAEGTFLQVVLKSLDPPIEEVET- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1221 rgaaDLDSRVDAAFARMQEATPLAGPLVALTHAHCDDGE-RLLICAHHLIVDAVSWRLLLGElfdgLAALARGeawTPSA 1299
Cdd:cd19542 84 ----DEDSLDALTRDLLDDPTLFGQPPHRLTLLETSSGEvYLVLRISHALYDGVSLPIILRD----LAAAYNG---QLLP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 1300 RGASYADYVEALREADDAQRFDagFWRE-LAAQPMQALPQDRPVALADARQSNVGRIVQTLDA 1361
Cdd:cd19542 153 PAPPFSDYISYLQSQSQEESLQ--YWRKyLQGASPCAFPSLSPKRPAERSLSSTRRSLAKLEA 213
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
601-1041 |
5.22e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 81.39 E-value: 5.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 601 LLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQGLAGFAPSVAIAVDELKLDGAgENGSGENAAPNQLAYIL 680
Cdd:PRK09088 63 LHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDDAVAAGRTDVEDLAAFIASADAL-EPADTPSIPPERVSLIL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 681 YTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAvdTTLEQILAawsRGACVVARPDelLEPQ 754
Cdd:PRK09088 142 FTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLcdapmfHIIGLI--TSVRPVLA---VGGSILVSNG--FEPK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 755 RFLAFLSERAITVTDL--APAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFELGLdrrcALINAYGPTEATI 832
Cdd:PRK09088 215 RTLGRLGDPALGITHYfcVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEDILGWLDDGI----PMVDGFGMSEAGT 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 833 SSHYHRVQAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFaplrlpsgESLRM 912
Cdd:PRK09088 291 VFGMSVDCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF--------TGDGW 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 913 YRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVGEGAAQrlvaWVECagedgfGQADL 992
Cdd:PRK09088 363 FRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECA--VVGMADAQ----WGEV------GYLAI 430
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1246793773 993 NQTDSDQTESERWHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK09088 431 VPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
679-1036 |
5.75e-15 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 79.47 E-value: 5.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 679 ILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVDttleqILAAWSRGACVVarPDELLE 752
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLiinpffHTFGYKAG-----IVACLLTGATVV--PVAVFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 753 PQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRWF-ELGLDrrcALINAYGPTEAT 831
Cdd:cd17638 78 VDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRsELGFE---TVLTAYGLTEAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 832 ISShyhrvqaidASRP--------VPLGQLLPGRIAAVLDAhgrivprgvcGELALGGIGLAEGYRGDAAASERRFaplr 903
Cdd:cd17638 155 VAT---------MCRPgddaetvaTTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAI---- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 904 lpsgESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQRLVAWVECA 982
Cdd:cd17638 212 ----DADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAqVAVIGVPDERMGEVGKAFVVAR 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 983 GEDGFGQADLNQtdsdqteserWHRalcERLPAYMVPTQFVALPRLPRNASGKI 1036
Cdd:cd17638 288 PGVTLTEEDVIA----------WCR---ERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
533-1039 |
5.78e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 81.47 E-value: 5.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 533 TVGNVVDAIARAadeFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSV 612
Cdd:PRK07798 4 NIADLFEAVADA---VPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 613 IPLDTEWPQARRAEVVAASGCDAVLTDAQglagFAPSVAIAVDEL-KL-------DGAGENGSG---------ENAAPNQ 675
Cdd:PRK07798 81 VNVNYRYVEDELRYLLDDSDAVALVYERE----FAPRVAEVLPRLpKLrtlvvveDGSGNDLLPgavdyedalAAGSPER 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 676 LA--------YILYTSGSTGIPKGVEVGHA-ALAAHIDAAAEALALSADDRVLHVAGLAVD--------------TTLEQ 732
Cdd:PRK07798 157 DFgerspddlYLLYTGGTTGMPKGVMWRQEdIFRVLLGGRDFATGEPIEDEEELAKRAAAGpgmrrfpapplmhgAGQWA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 733 ILAAWSRGACVVARPDELLEPQRFLAFLS-ERAITVTDLAPAYANELVRASVADDWRDL-ALRCLVVGGDVLPVALAQRW 810
Cdd:PRK07798 237 AFAALFSGQTVVLLPDVRFDADEVWRTIErEKVNVITIVGDAMARPLLDALEARGPYDLsSLFAIASGGALFSPSVKEAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 811 FELGLDRrcALINAYGPTEATISSHyhrvqAIDASRPVPLGQLL--PGRIAAVLDAHGRIVPRG--VCGELALGG-IGLa 885
Cdd:PRK07798 317 LELLPNV--VLTDSIGSSETGFGGS-----GTVAKGAVHTGGPRftIGPRTVVLDEDGNPVEPGsgEIGWIARRGhIPL- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 886 eGYRGDAAASERRFaplrlPSGESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAA 964
Cdd:PRK07798 389 -GYYKDPEKTAETF-----PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVAdALVV 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 965 GVVGEGAAQRLVAWVECAGEDGFGQADLnqtdsdqteserwhRALC-ERLPAYMVPTQFVALPRLPRNASGKIDRR 1039
Cdd:PRK07798 463 GVPDERWGQEVVAVVQLREGARPDLAEL--------------RAHCrSSLAGYKVPRAIWFVDEVQRSPAGKADYR 524
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
3524-3980 |
6.15e-15 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 81.46 E-value: 6.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3524 RFAEIARRYPARIAVSAEDG-----ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVP 3598
Cdd:PRK08180 44 RLVHWAQEAPDRVFLAERGAdggwrRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3599 VDP------HAPAARR--------GFILEDSGvclSVSQRAL-AVELPGTALC-----LDDPFTRAQLDAVEPGELPEVP 3658
Cdd:PRK08180 124 VSPayslvsQDFGKLRhvlelltpGLVFADDG---AAFARALaAVVPADVEVVavrgaVPGRAATPFAALLATPPTAAVD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3659 T-------EAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQTGRFSFDEHDV------WSlfH----SHAFDFAVWel 3721
Cdd:PRK08180 201 AahaavgpDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEPPVlvdwlpWN--HtfggNHNLGIVLY-- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3722 WGAWLY--GGRAVlvpeavcrqPDAF---LDLLAEYGVTVLNQTPSAFYALqSQAMRRELAL------NVRAVVFGGEAL 3790
Cdd:PRK08180 277 NGGTLYidDGKPT---------PGGFdetLRNLREISPTVYFNVPKGWEML-VPALERDAALrrrffsRLKLLFYAGAAL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3791 EPS---RLQPWRERYpQAELVNM---YGITETTVHVSF-HRlsdedlqsPTSR---IGSALPDLAVHVldaagqpVPLGV 3860
Cdd:PRK08180 347 SQDvwdRLDRVAEAT-CGERIRMmtgLGMTETAPSATFtTG--------PLSRagnIGLPAPGCEVKL-------VPVGG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3861 VGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRY----RADGSLEYRGRGDDQVKL-RGYRIEPGEIAAKI 3935
Cdd:PRK08180 411 KLEVRVKGPNVTPGYWRAPELTAEAFDEEG---YYRSGDAVRFvdpaDPERGLMFDGRIAEDFKLsSGTWVSVGPLRARA 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3936 ASL--PQVSDAAVTVEGQGE-GA--WLMAYAVAADGAEPDPQSLREALRA 3980
Cdd:PRK08180 488 VSAgaPLVQDVVITGHDRDEiGLlvFPNLDACRRLAGLLADASLAEVLAH 537
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
831-1120 |
6.69e-15 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 78.64 E-value: 6.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 831 TISSHYHRVQAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGESL 910
Cdd:COG3433 1 IAIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 911 RMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAAGVVGEGAAQRLVAWVECAGEDGFGQA 990
Cdd:COG3433 81 QADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 991 DLNQTDsdqteserwhralcERLPAYMVPTQFVALPRLPRNASGKIDRRALPAPPVLAQAERTPPRTAEESA-----LCE 1065
Cdd:COG3433 161 ALAALD--------------KVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALETAlteeeLRA 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 1066 VWAEVLQC---EVGIHDSFFRLGGDSIRSLQVVARLRERGYAVTPKLMYQYQSAAELA 1120
Cdd:COG3433 227 DVAELLGVdpeEIDPDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWW 284
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
3541-4005 |
6.74e-15 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 81.18 E-value: 6.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3541 EDGELDYATLDRRSSQLATLLIRQ-GAGPGQRVGLCLPRGCDLLVALLAILKTG--AAYVPvdphaPAARRGFIL---ED 3614
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGcpVAFLN-----TNIRSKSLLhcfRC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3615 SG----------------VCLSVSQRALAV-------ELPGTAlCLDDPFTRAQLDAVePGELPEVPT-EAPAYLIYTSG 3670
Cdd:cd05938 77 CGakvlvvapelqeaveeVLPALRADGVSVwylshtsNTEGVI-SLLDKVDAASDEPV-PASLRAHVTiKSPALYIYTSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3671 STGTPKGVVVTHrnvERLFTAATQTGRFSFDEHDV----WSLFHSHAFdfaVWELWGAWLYGGRAVLVPEAVCRQpdaFL 3746
Cdd:cd05938 155 TTGLPKAARISH---LRVLQCSGFLSLCGVTADDViyitLPLYHSSGF---LLGIGGCIELGATCVLKPKFSASQ---FW 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3747 DLLAEYGVTVL-----------NQTPSAfyalqsqamrRELALNVRAVVfgGEALepsRLQPWRE---RYPQAELVNMYG 3812
Cdd:cd05938 226 DDCRKHNVTVIqyigellrylcNQPQSP----------NDRDHKVRLAI--GNGL---RADVWREflrRFGPIRIREFYG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3813 ITETTVhvSFHRLsdedlqspTSRIG-----SALPDLAVH-------------VLDAAGQ--PVPLGVVGELVVEgdgVA 3872
Cdd:cd05938 291 STEGNI--GFFNY--------TGKIGavgrvSYLYKLLFPfelikfdvekeepVRDAQGFciPVAKGEPGLLVAK---IT 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3873 Q-----GYWQRPELTAE---RFVERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDA 3944
Cdd:cd05938 358 QqspflGYAGDKEQTEKkllRDVFKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEV 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 3945 ---AVTVEGQgEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKL 4005
Cdd:cd05938 438 nvyGVTVPGH-EGRIGMAAVKLKPGHEFDGKKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQ 500
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1142-1558 |
8.54e-15 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 81.83 E-value: 8.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1142 LSPIQRWFFDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQ----VAAPGPAPAIQA 1217
Cdd:COG1020 22 AAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQViqpvVAAPLPVVVLLV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1218 QDWRGAADLDSRVDAAFARMQEATPLAGPLVALTHAHCDDGERLLICAHHLIVDAVSWRLLLGELFDGLAALARGEAWTP 1297
Cdd:COG1020 102 DLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYAGAPLPL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1298 SARGASYADYVEALREADDAQRFDAG----FWRELAAQPMQALPQDRPvaLADARQSNVGRIVQTLDAGLTADLLERAGE 1373
Cdd:COG1020 182 PPLPIQYADYALWQREWLQGEELARQlaywRQQLAGLPPLLELPTDRP--RPAVQSYRGARVSFRLPAELTAALRALARR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1374 -----------AYrcrtdevllialaralatrtgrnRLWLDRERHGRDVL--------DGRDWSSVLGWYTAVHPLPLDL 1434
Cdd:COG1020 260 hgvtlfmvllaAF-----------------------ALLLARYSGQDDVVvgtpvagrPRPELEGLVGFFVNTLPLRVDL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1435 gvaDGPAQIGALKEQIRALARRGLDY--MP---LVASARIPALPAGQLLFNYHGVVDAGAHPAFEVEPRTLASGNGADNP 1509
Cdd:COG1020 317 ---SGDPSFAELLARVRETLLAAYAHqdLPferLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGT 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1246793773 1510 PGALVEINARVQAGRLGLVWNYAGEAYDAATIEAWSQAFAAELAALVAH 1558
Cdd:COG1020 394 AKFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAAD 442
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
2063-2522 |
2.76e-14 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 78.38 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2063 TYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPldpqhpdARQIAVLDDSGARIVIGWGa 2142
Cdd:cd05974 2 SFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP-------ATTLLTPDDLRDRVDRGGA- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2143 apawvpasvrwldaesvldVVSAYEEPPRvdvdADTPAYLIYTSGSTGTPKGVVVSQ-----GNLAN-YVAGVLPvldlg 2216
Cdd:cd05974 74 -------------------VYAAVDENTH----ADDPMLLYFTSGTTSKPKLVEHTHrsypvGHLSTmYWIGLKP----- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2217 EDASLATLSTVAADLGFTALFGALLSGRRVRLLpAELAFDAQALAAHLQAHPVDCLKIVPS-HLAGLLAAAGGTAVLPRE 2295
Cdd:cd05974 126 GDVHWNISSPGWAKHAWSCFFAPWNAGATVFLF-NYARFDAKRVLAALVRYGVTTLCAPPTvWRMLIQQDLASFDVKLRE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2296 cLVTGGEALTGALVQQVRAlAPTLRIVNHYGPTETTVgiLTCTVPEEwPVEQGvPVGHPLAGNEAWVLDRFGLPAPvgvA 2375
Cdd:cd05974 205 -VVGAGEPLNPEVIEQVRR-AWGLTIRDGYGQTETTA--LVGNSPGQ-PVKAG-SMGRPLPGYRVALLDPDGAPAT---E 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2376 GELYLGGGN-----LSLGYWQRAEQTAErfvahplAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQ 2450
Cdd:cd05974 276 GEVALDLGDtrpvgLMKGYAGDPDKTAH-------AMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELES 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2451 VLAQLPGVEVAAV--------LALPGANGVLqlgacIQGSLEGVAEALA--QRLPEYLCP-SRWRAVE--SMPRLGNGKI 2517
Cdd:cd05974 349 VLIEHPAVAEAAVvpspdpvrLSVPKAFIVL-----RAGYEPSPETALEifRFSRERLAPyKRIRRLEfaELPKTISGKI 423
|
....*
gi 1246793773 2518 DRQAL 2522
Cdd:cd05974 424 RRVEL 428
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
604-1044 |
3.22e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 78.49 E-value: 3.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 604 GAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQGLAGFAPSVAIAVDelkldgAGENGSGENAAPNQLAYILYTS 683
Cdd:PRK07787 64 GALIAGVPVVPVPPDSGVAERRHILADSGAQAWLGPAPDDPAGLPHVPVRLH------ARSWHRYPEPDPDAPALIVYTS 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 684 GSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVDttleqILAAWSRGACVV--ARPDellePQR 755
Cdd:PRK07787 138 GTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVhglplfHVHGLVLG-----VLGPLRIGNRFVhtGRPT----PEA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 756 FLAFLSERAiTVTDLAPAyanelVRASVADDwRDLAL-----RCLVVGGDVLPVALAQRWFELGLDRrcaLINAYGPTEA 830
Cdd:PRK07787 209 YAQALSEGG-TLYFGVPT-----VWSRIAAD-PEAARalrgaRLLVSGSAALPVPVFDRLAALTGHR---PVERYGMTET 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 831 TISShyhRVQAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRGV--CGELALGGIGLAEGYRGDAAASERRFAplrlPSGe 908
Cdd:PRK07787 279 LITL---STRADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGetVGELQVRGPTLFDGYLNRPDATAAAFT----ADG- 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 909 slrMYRSGDRVRLLDDGELQFLGRADFQ-VKLRGYRIELEEIEHCLGQLPQVRAAAagVVGEGAA---QRLVAWVecAGE 984
Cdd:PRK07787 351 ---WFRTGDVAVVDPDGMHRIVGRESTDlIKSGGYRIGAGEIETALLGHPGVREAA--VVGVPDDdlgQRIVAYV--VGA 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 985 DGFGQADLnqTDsdqteserwHRAlcERLPAYMVPTQFVALPRLPRNASGKIDRRALPAP 1044
Cdd:PRK07787 424 DDVAADEL--ID---------FVA--QQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSE 470
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
3539-4010 |
6.02e-14 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 78.29 E-value: 6.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3539 SAEDGELDYATLDRRSSQLATLLIRQ-GAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGV 3617
Cdd:PRK05620 33 GAEQEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAED 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3618 CLSVSQRALAVEL-------PGTALCL---DDPFTRAQLDAVEPGEL----------------PEVPTEAPAYLIYTSGS 3671
Cdd:PRK05620 113 EVIVADPRLAEQLgeilkecPCVRAVVfigPSDADSAAAHMPEGIKVysyealldgrstvydwPELDETTAAAICYSTGT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3672 TGTPKGVVVTHRNverLFTAAtqtgrFSFDEHDVWSLFHSHAFDFAV--WEL--WG----AWLYGGRAVLVPEAVcrQPD 3743
Cdd:PRK05620 193 TGAPKGVVYSHRS---LYLQS-----LSLRTTDSLAVTHGESFLCCVpiYHVlsWGvplaAFMSGTPLVFPGPDL--SAP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3744 AFLDLLAEYGVTVLNQTPSAFYALQSQAMR---RELALnvRAVVFGGEALEPSRLQPWRERYpQAELVNMYGITET---- 3816
Cdd:PRK05620 263 TLAKIIATAMPRVAHGVPTLWIQLMVHYLKnppERMSL--QEIYVGGSAVPPILIKAWEERY-GVDVVHVWGMTETspvg 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3817 TVHVSFHRLSDE---DLQSPTSRIGSALPDLAV---HVLDAAGQPVplgvvGELVVEGDGVAQGYWQRPELT----AERF 3886
Cdd:PRK05620 340 TVARPPSGVSGEarwAYRVSQGRFPASLEYRIVndgQVMESTDRNE-----GEIQVRGNWVTASYYHSPTEEgggaASTF 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3887 ----VERGGQRF-----YRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEGAWL 3957
Cdd:PRK05620 415 rgedVEDANDRFtadgwLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVI--GYPDDKWG 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 3958 ---MAYAVAADGAEPD---PQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK05620 493 erpLAVTVLAPGIEPTretAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
2182-2517 |
7.80e-14 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 76.00 E-value: 7.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2182 LIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFTA-LFGALLSGRRVrlLPaELAFDAQAL 2260
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAgIVACLLTGATV--VP-VAVFDVDAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2261 AAHLQAHPVDCLKIVPS--HLAGLLAAAGGTAVLPRECLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVGilTCT 2338
Cdd:cd17638 82 LEAIERERITVLPGPPTlfQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGVA--TMC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2339 VPEEWPVEQGVPVGHPLAGNEAWVLDrfglpapvgvAGELYLGGGNLSLGYWQRAEQTAERFVAhplapDRLLYrSGDLA 2418
Cdd:cd17638 160 RPGDDAETVATTCGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEATAEAIDA-----DGWLH-TGDVG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2419 RLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALP----GANG----VLQLGACIqgSLEGVAEAL 2490
Cdd:cd17638 224 ELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPdermGEVGkafvVARPGVTL--TEEDVIAWC 301
|
330 340
....*....|....*....|....*..
gi 1246793773 2491 AQRLPEYLCPSRWRAVESMPRLGNGKI 2517
Cdd:cd17638 302 RERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
2325-2519 |
9.23e-14 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 75.77 E-value: 9.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2325 YGPTETTvGILTCTVPEEWPVEqgvpVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFvahp 2404
Cdd:cd17637 143 YGQTETS-GLVTLSPYRERPGS----AGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF---- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2405 lapDRLLYRSGDLARLDGEGRIVYLGRGDHQ--VKIRGYRVELGEVEQVLAQLPGVEVAAVLALP------GANGVLQLG 2476
Cdd:cd17637 214 ---RNGWHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPdpkwgeGIKAVCVLK 290
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1246793773 2477 ACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDR 2519
Cdd:cd17637 291 PGATLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
596-1041 |
9.53e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 77.21 E-value: 9.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 596 LDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDA---------QGLAGFAPSVAIA----VDELKLDGA 662
Cdd:PRK06839 64 LEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVEKtfqnmalsmQKVSYVQRVISITslkeIEDRKIDNF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 663 gENGSGENAApnqlaYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDR------VLHVAGLAVDTtleqiLAA 736
Cdd:PRK06839 144 -VEKNESASF-----IICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRsivllpLFHIGGIGLFA-----FPT 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 737 WSRGACVVArPDELlEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFELGLd 816
Cdd:PRK06839 213 LFAGGVIIV-PRKF-EPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDRGF- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 817 rrcALINAYGPTEAT-----ISSHYHRVQAIDASRPVPLGQLlpgriaAVLDAHGRIVPRGVCGELALGGIGLAEGYRGD 891
Cdd:PRK06839 290 ---LFGQGFGMTETSptvfmLSEEDARRKVGSIGKPVLFCDY------ELIDENKNKVEVGEVGELLIRGPNVMKEYWNR 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 892 AAASErrfaplrlpsgESLR--MYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVGe 969
Cdd:PRK06839 361 PDATE-----------ETIQdgWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVA--VVG- 426
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 970 gaaQRLVAWVECAGedgfgQADLNQTDSDQTESERwhRALCE-RLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK06839 427 ---RQHVKWGEIPI-----AFIVKKSSSVLIEKDV--IEHCRlFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
107-511 |
1.04e-13 |
|
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380467 [Multi-domain] Cd Length: 395 Bit Score: 76.57 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 107 GHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIqgeDSVAAGGG--AAVESADLRGRGQDEIDALVEGFRLRPF 184
Cdd:cd19545 19 PGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRI---VQSDSGGLlqVVVKESPISWTESTSLDEYLEEDRAAPM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 185 ELQrQRPLRMQLLRldgqgDGPVRHWLQVVVHHIACDGVSLGLLTQDLSRAYRvecglaaEPAPPLPCQYGDYARWQRDT 264
Cdd:cd19545 96 GLG-GPLVRLALVE-----DPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQ-------GEPVPQPPPFSRFVKYLRQL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 265 ldRLDASLRHHVEALSGAPHLHELPLDHERPAVLGQSGAKLRLAFPPGLSERV--AAYAQA------SRATafhvlqaaf 336
Cdd:cd19545 163 --DDEAAAEFWRSYLAGLDPAVFPPLPSSRYQPRPDATLEHSISLPSSASSGVtlATVLRAawalvlSRYT--------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 337 aallarcgAGDDLLIGTPVAGR---VrPELDSLVGLFVNTVVLRTQLHDDPDFASLVARCRDHQLAALEHQALPLERVie 413
Cdd:cd19545 232 --------GSDDVVFGVTLSGRnapV-PGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQNI-- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 414 tLQVERSSRHAPLFQLMFALRHDADLALDlhgvQAHALTLPEDVAKHE------LTLEVLVGAGGMSAvweynTALWNPA 487
Cdd:cd19545 301 -RRLGPDARAACNFQTLLVVQPALPSSTS----ESLELGIEEESEDLEdfssygLTLECQLSGSGLRV-----RARYDSS 370
|
410 420
....*....|....*....|....*
gi 1246793773 488 TVARW-AERYFVALAAMLENPHEPA 511
Cdd:cd19545 371 VISEEqVERLLDQFEHVLQQLASAP 395
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
1142-1374 |
1.09e-13 |
|
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380463 [Multi-domain] Cd Length: 433 Bit Score: 76.69 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1142 LSPIQR--WF---FDsaPAQPDrYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPA-PAI 1215
Cdd:cd19540 4 LSFAQQrlWFlnrLD--GPSAA-YNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLPAAEArPDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1216 QAQDwRGAADLDSRVDAAFAR---MQEATPLAGPLVALThahcDDGERLLICAHHLIVDAVSWRLLLGELFDGLAALARG 1292
Cdd:cd19540 81 TVVD-VTEDELAARLAEAARRgfdLTAELPLRARLFRLG----PDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1293 EA--WTPSArgASYADYV----EALREADDAQRFDA---GFWRE-LAAQPMQ-ALPQDRPVAladARQSNVGRIVQ-TLD 1360
Cdd:cd19540 156 RApdWAPLP--VQYADYAlwqrELLGDEDDPDSLAArqlAYWREtLAGLPEElELPTDRPRP---AVASYRGGTVEfTID 230
|
250
....*....|....
gi 1246793773 1361 AGLTADLLERAGEA 1374
Cdd:cd19540 231 AELHARLAALAREH 244
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1598-1927 |
1.13e-13 |
|
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380458 [Multi-domain] Cd Length: 423 Bit Score: 76.37 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1598 FPLTPLQRGVLL-----ESLRGDGADPYFqqtvaELDGE-IDAAALAQAWQQTVRRQPMLRTAIVWEGlsvpHQIVLADA 1671
Cdd:cd19535 2 FPLTDVQYAYWIgrqddQELGGVGCHAYL-----EFDGEdLDPDRLERAWNKLIARHPMLRAVFLDDG----TQQILPEV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1672 AAP-WQTLDWSALDDAAQDAQLQRWLADDAAQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQR 1750
Cdd:cd19535 73 PWYgITVHDLRGLSEEEAEAALEELRERLSHRVLDVERGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1751 YtagaQGATLRLPPAP-GFQAYL-DWRERQDLARQRG--WWRERLS---GYAGTAALPAPVAAAHHPVQReeCERRLSAH 1823
Cdd:cd19535 153 Y----EDPGEPLPPLElSFRDYLlAEQALRETAYERAraYWQERLPtlpPAPQLPLAKDPEEIKEPRFTR--REHRLSAE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1824 DSERLRAFCRERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPPELAGVESMVGVFINTLPLRLRIDAGQPALDLL 1903
Cdd:cd19535 227 QWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRFLLNLTLFNRLPLHPDVNDVVGDFTSLLLLEVDGSEGQSFLERA 306
|
330 340
....*....|....*....|....
gi 1246793773 1904 SALRSQSLEVAENEAVGLGEILAD 1927
Cdd:cd19535 307 RRLQQQLWEDLDHSSYSGVVVVRR 330
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
3521-4006 |
1.23e-13 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 78.08 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3521 LVSRFAEIARRYPARiAVSAEDGE---LDYATLDRRSSQLATLLiRQGAGPGQRVGLCLPRGCDLLVALLAILKTGaaYV 3597
Cdd:PRK06814 633 LFEALIEAAKIHGFK-KLAVEDPVngpLTYRKLLTGAFVLGRKL-KKNTPPGENVGVMLPNANGAAVTFFALQSAG--RV 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3598 P-----------VDPHAPAAR-------RGFI----LEDSGVCLSVSQRALAVELPGTALCLDDpftraQLDAVEPGELP 3655
Cdd:PRK06814 709 PaminfsagianILSACKAAQvktvltsRAFIekarLGPLIEALEFGIRIIYLEDVRAQIGLAD-----KIKGLLAGRFP 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3656 EVPT-----EAPAYLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEHD----VWSLFHShaFDFAVWELWGAwL 3726
Cdd:PRK06814 784 LVYFcnrdpDDPAVILFTSGSEGTPKGVVLSHRNL--LANRAQVAARIDFSPEDkvfnALPVFHS--FGLTGGLVLPL-L 858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3727 YGGRAVL---------VPEAVCRQ-------PDAFLDLLAEYGvtvlnqTPSAFYALqsqamrrelalnvRAVVFGGEAL 3790
Cdd:PRK06814 859 SGVKVFLypsplhyriIPELIYDTnatilfgTDTFLNGYARYA------HPYDFRSL-------------RYVFAGAEKV 919
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3791 EPSRLQPWRERYpQAELVNMYGITETTVHVSfhrlsdedLQSPT-SRIGSA---LPDlavhvLDAAGQPVPlGVV--GEL 3864
Cdd:PRK06814 920 KEETRQTWMEKF-GIRILEGYGVTETAPVIA--------LNTPMhNKAGTVgrlLPG-----IEYRLEPVP-GIDegGRL 984
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3865 VVEGDGVAQGYwqrpeLTAER--FVERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASL-PQV 3941
Cdd:PRK06814 985 FVRGPNVMLGY-----LRAENpgVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELwPDA 1059
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 3942 SDAAVTVEGQGEGAWLMAYAVAADGAEPDPQslREALRALLPDYMLPRLIQLLPALPLTANGKLD 4006
Cdd:PRK06814 1060 LHAAVSIPDARKGERIILLTTASDATRAAFL--AHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
2152-2479 |
1.33e-13 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 77.15 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2152 RWLDAESVLDVVSAYEEpprvdvdadtpAYLI-YTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAAD 2230
Cdd:PLN02860 157 QRALGTTELDYAWAPDD-----------AVLIcFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHI 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2231 LGFTALFGALLSGRRVRLLP---AELAFDAQALAAhlqahpVDCLKIVP-------SHLAGLLAAAGGTAVLPrecLVTG 2300
Cdd:PLN02860 226 GGLSSALAMLMVGACHVLLPkfdAKAALQAIKQHN------VTSMITVPammadliSLTRKSMTWKVFPSVRK---ILNG 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2301 GEALTGALVQQVRALAPTLRIVNHYGPTET-------TVGILTCTVPEEWPVE------------QGVPVGHPLAGNEAw 2361
Cdd:PLN02860 297 GGSLSSRLLPDAKKLFPNAKLFSAYGMTEAcssltfmTLHDPTLESPKQTLQTvnqtksssvhqpQGVCVGKPAPHVEL- 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2362 vldRFGLPAPVGVaGELYLGGGNLSLGYWQRAEQTAErfvahpLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGY 2441
Cdd:PLN02860 376 ---KIGLDESSRV-GRILTRGPHVMLGYWGQNSETAS------VLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGE 445
|
330 340 350
....*....|....*....|....*....|....*...
gi 1246793773 2442 RVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI 2479
Cdd:PLN02860 446 NVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACV 483
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
1604-1919 |
1.71e-13 |
|
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380461 [Multi-domain] Cd Length: 432 Bit Score: 76.15 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1604 QRGVLLESLRGDGAdPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGlSVPHQIVLADAAApwqTLDWSAL 1683
Cdd:cd19538 9 RRLWFLHQLEGPSA-TYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEED-GVPYQLILEEDEA---TPKLEIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1684 DdaAQDAQLQRWLADDAAQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGATLRLP 1763
Cdd:cd19538 84 E--VDEEELESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAPELA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1764 PAP-GFQAYLDWRERQ---------DLARQRGWWRERLsgyAGTAALPAPVAAAHHPVQREECERRLS----AHDSERLR 1829
Cdd:cd19538 162 PLPvQYADYALWQQELlgdesdpdsLIARQLAYWKKQL---AGLPDEIELPTDYPRPAESSYEGGTLTfeidSELHQQLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1830 AFCRERGCTLsdliAMVW--GLAN--ARYGNHDDVVLGATRSGRppELAGVESMVGVFINTLPlrLRID-AGQPA-LDLL 1903
Cdd:cd19538 239 QLAKDNNVTL----FMVLqaGFAAllTRLGAGTDIPIGSPVAGR--NDDSLEDLVGFFVNTLV--LRTDtSGNPSfRELL 310
|
330
....*....|....*.
gi 1246793773 1904 SALRSQSLEVAENEAV 1919
Cdd:cd19538 311 ERVKETNLEAYEHQDI 326
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
612-1041 |
1.90e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 76.62 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 612 VIPLDTEWPQAR--RAEV----VAASGCDAVLTDA------QGLAGFAPSVAIAVDELK-LDGAGENGSGENAAPNQLAY 678
Cdd:PRK06178 134 LLALDQLAPVVEqvRAETslrhVIVTSLADVLPAEptlplpDSLRAPRLAAAGAIDLLPaLRACTAPVPLPPPALDALAA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 679 ILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL-------HVAGlaVDTTLeqILAAWSrGACVV--ARPDe 749
Cdd:PRK06178 214 LNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFlsflpefWIAG--ENFGL--LFPLFS-GATLVllARWD- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 750 llePQRFLAFLSERAITVTDLAPAYANELVRASvadDWRDLALRCLVVGGDV-----LPVALAQRWFEL-GLDRRCAlin 823
Cdd:PRK06178 288 ---AVAFMAAVERYRVTRTVMLVDNAVELMDHP---RFAEYDLSSLRQVRVVsfvkkLNPDYRQRWRALtGSVLAEA--- 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 824 AYGPTEATISSHYHR-VQAID---ASRPVPLGQLLPGRIAAVLD-AHGRIVPRGVCGELALGGIGLAEGYRGDAAASerr 898
Cdd:PRK06178 359 AWGMTETHTCDTFTAgFQDDDfdlLSQPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEAT--- 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 899 faplrlpsGESLR--MYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVraAAAGVVG---EGAAQ 973
Cdd:PRK06178 436 --------AEALRdgWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAV--LGSAVVGrpdPDKGQ 505
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 974 RLVAWVECAGEDGFGQADLnqtdsdqteserwhRALC-ERLPAYMVPTQFVaLPRLPRNASGKIDRRAL 1041
Cdd:PRK06178 506 VPVAFVQLKPGADLTAAAL--------------QAWCrENMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
3542-4012 |
2.10e-13 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 75.92 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3542 DGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAyvpvdphAPAARRGFILEDSGVCLSV 3621
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVE-------TALINSNLRLESLLHCITV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3622 SQ-RALAVELpgtalcLDDPFTRAQLdavEPGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHrnVERLFTAATQTGRFSF 3700
Cdd:cd05939 74 SKaKALIFNL------LDPLLTQSST---EPPSQDDVNFRDKLFYIYTSGTTGLPKAAVIVH--SRYYRIAAGAYYAFGM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3701 DEHDVW----SLFHSHAFDFAVwelwGAWLYGGRAVlvpeaVCRQ---PDAFLDLLAEYGVTV-----------LNQTPS 3762
Cdd:cd05939 143 RPEDVVydclPLYHSAGGIMGV----GQALLHGSTV-----VIRKkfsASNFWDDCVKYNCTIvqyigeicrylLAQPPS 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3763 afyalqsqamRRELALNVRAVVfgGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHrlsDEDLQSP--TSRIGSA 3840
Cdd:cd05939 214 ----------EEEQKHNVRLAV--GNGLRPQIWEQFVRRFGIPQIGEFYGATEGNSSLVNI---DNHVGACgfNSRILPS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3841 L-PDLAVHVLDAAGQPV--PLGVV--------GELV---VEGDGVAQ--GYWQRPElTAE---RFVERGGQRFYRSGDLG 3901
Cdd:cd05939 279 VyPIRLIKVDEDTGELIrdSDGLCipcqpgepGLLVgkiIQNDPLRRfdGYVNEGA-TNKkiaRDVFKKGDSAFLSGDVL 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3902 RYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAV-TVE-GQGEGAWLMAyAVAADGAEPDPQSLREALR 3979
Cdd:cd05939 358 VMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVyGVEvPGVEGRAGMA-AIVDPERKVDLDRFSAVLA 436
|
490 500 510
....*....|....*....|....*....|...
gi 1246793773 3980 ALLPDYMLPRLIQLLPALPLTANGKLDRKALPK 4012
Cdd:cd05939 437 KSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
2176-2523 |
2.28e-13 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 75.59 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2176 ADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLP-VLDLGEDASLATLstvaADLGFTALFGALL-----SGRRVRLL 2249
Cdd:cd05958 96 SDDICILAFTSGTTGAPKATMHFHRDPLASADRYAVnVLRLREDDRFVGS----PPLAFTFGLGGVLlfpfgVGASGVLL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2250 PAELAFDaqALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLP--REClVTGGEALTGALVQQVRAlAPTLRIVNHYGP 2327
Cdd:cd05958 172 EEATPDL--LLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSslRKC-VSAGEALPAALHRAWKE-ATGIPIIDGIGS 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2328 TETTVGILTCTVPEEWPVEQGVPVghplAGNEAWVLDRFGLPAPVGVAGELYLGGgnlSLGYWQRAEQTAERFVAhplap 2407
Cdd:cd05958 248 TEMFHIFISARPGDARPGATGKPV----PGYEAKVVDDEGNPVPDGTIGRLAVRG---PTGCRYLADKRQRTYVQ----- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2408 DRLLYrSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI-----QGS 2482
Cdd:cd05958 316 GGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVvlrpgVIP 394
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1246793773 2483 LEGVAEALAQRLPEYLCPSRW-RAVE---SMPRLGNGKIDRQALA 2523
Cdd:cd05958 395 GPVLARELQDHAKAHIAPYKYpRAIEfvtELPRTATGKLQRFALR 439
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
1143-1327 |
3.06e-13 |
|
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380467 [Multi-domain] Cd Length: 395 Bit Score: 75.03 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1143 SPIQRWFFDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASF-ERADGQWRQQVAAPGPapaiqaQDWR 1221
Cdd:cd19545 5 TPLQEGLMALTARQPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIvQSDSGGLLQVVVKESP------ISWT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1222 GAADLDSRVDAAfarMQEATPLAGPLVALTHAHCDDGER-LLICAHHLIVDAVSWRLLLGELfdgLAALARgeawTPSAR 1300
Cdd:cd19545 79 ESTSLDEYLEED---RAAPMGLGGPLVRLALVEDPDTERyFVWTIHHALYDGWSLPLILRQV---LAAYQG----EPVPQ 148
|
170 180
....*....|....*....|....*..
gi 1246793773 1301 GASYADYVEALREADDAQRfdAGFWRE 1327
Cdd:cd19545 149 PPPFSRFVKYLRQLDDEAA--AEFWRS 173
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
529-1062 |
3.88e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 75.55 E-value: 3.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 529 PAPRTVGNVVDAIARAAdefPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRA 608
Cdd:PRK06164 7 PRADTLASLLDAHARAR---PDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 609 GLSVIPLDTEWPQARRAEVVAASGCD----------------------AVLTDAQGLAGF--------APSVAIAVDELK 658
Cdd:PRK06164 84 GATVIAVNTRYRSHEVAHILGRGRARwlvvwpgfkgidfaailaavppDALPPLRAIAVVddaadatpAPAPGARVQLFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 659 L-DGAGENGSGENAAPNQLAYILY-TSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAA 736
Cdd:PRK06164 164 LpDPAPPAAAGERAADPDAGALLFtTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 737 WSRGACVVARPdeLLEPQRFLAFLSERAITVTdlapAYANELVR--ASVADDWRDLALRCLVVGGDVLPvalaqRWFEL- 813
Cdd:PRK06164 244 LAGGAPLVCEP--VFDAARTARALRRHRVTHT----FGNDEMLRriLDTAGERADFPSARLFGFASFAP-----ALGELa 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 814 --GLDRRCALINAYGPTEATISSHYHRVQAIDASRPVPLGQLL--PGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYR 889
Cdd:PRK06164 313 alARARGVPLTGLYGSSEVQALVALQPATDPVSVRIEGGGRPAspEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 890 GDAAASERRFAplrlPSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAAGVVGE 969
Cdd:PRK06164 393 DNPDATARALT----DDG----YFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATR 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 970 GAAQRLVAWVEcagedgfgqadlnQTDSDQTESERWHRALCERLPAYMVPTQFVALPRLPRNASG---KIDRRALPAppv 1046
Cdd:PRK06164 465 DGKTVPVAFVI-------------PTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLRE--- 528
|
570
....*....|....*.
gi 1246793773 1047 LAQAertppRTAEESA 1062
Cdd:PRK06164 529 MAQA-----RLAAERA 539
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
2084-2426 |
4.73e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 75.54 E-value: 4.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2084 QPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPL-DPQHPD--ARQIAVLDDSGARIVIGWGAAPAWVPASVRWLDA---- 2156
Cdd:PRK07769 77 KPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPGhvGRLHAVLDDCTPSAILTTTDSAEGVRKFFRARPAkerp 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2157 -----ESVLDVVSAYEEPPrvDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADL 2231
Cdd:PRK07769 157 rviavDAVPDEVGATWVPP--EANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDM 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2232 GF-TALFGALLSGRRVRLLPA-----------ELAFDAQALAAHLQAHPvdclKIVPSHLAGLLaaaggtavLPRE---- 2295
Cdd:PRK07769 235 GLiTVLLPALLGHYITFMSPAafvrrpgrwirELARKPGGTGGTFSAAP----NFAFEHAAARG--------LPKDgepp 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2296 -------CLVTGGEALTGALVQQV-RALAP-TLR---IVNHYGPTETTVGILTCTVPEE----------------WPVEQ 2347
Cdd:PRK07769 303 ldlsnvkGLLNGSEPVSPASMRKFnEAFAPyGLPptaIKPSYGMAEATLFVSTTPMDEEptviyvdrdelnagrfVEVPA 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2348 GVP--VGHPLAGNEA---W---VLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERF---VAHPLAP--------D 2408
Cdd:PRK07769 383 DAPnaVAQVSAGKVGvseWaviVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqniLKSRLSEshaegapdD 462
|
410 420
....*....|....*....|...
gi 1246793773 2409 RLLYRSGDL-ARLDGE----GRI 2426
Cdd:PRK07769 463 ALWVRTGDYgVYFDGElyitGRV 485
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
2136-2530 |
5.10e-13 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 75.43 E-value: 5.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2136 IVIGWGAAPAWVPASVRWLDAESVLdvvSAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLA---NY------- 2205
Cdd:cd05967 192 LVLNRPQVPADLTKPGRDLDWSELL---AKAEPVDCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAvalNWsmrniyg 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2206 ---------------------------VAGVLPVLDLGE-----DASlaTLSTVAADLGFTALFGALLSGRRVRLLPAEL 2253
Cdd:cd05967 269 ikpgdvwwaasdvgwvvghsyivygplLHGATTVLYEGKpvgtpDPG--AFWRVIEKYQVNALFTAPTAIRAIRKEDPDG 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2254 AFdaqalaahLQAHPVDCLKIvpshlagllaaaggtavlprecLVTGGEALTGALVQQVRALAPTLrIVNHYGPTETTVG 2333
Cdd:cd05967 347 KY--------IKKYDLSSLRT----------------------LFLAGERLDPPTLEWAENTLGVP-VIDHWWQTETGWP 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2334 ILT-CTVPEEWPVEQGVPvGHPLAGNEAWVLDRFGLPAPVGVAGELYLGG----GNLsLGYWQraeqTAERFVAHPLAPD 2408
Cdd:cd05967 396 ITAnPVGLEPLPIKAGSP-GKPVPGYQVQVLDEDGEPVGPNELGNIVIKLplppGCL-LTLWK----NDERFKKLYLSKF 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2409 RLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGA-NGVLQLGACI-QGSLEGV 2486
Cdd:cd05967 470 PGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDElKGQVPLGLVVlKEGVKIT 549
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 2487 AEALAQRLPEYL--------CPSRWRAVESMPRLGNGKIDRQALADLLQQDD 2530
Cdd:cd05967 550 AEELEKELVALVreqigpvaAFRLVIFVKRLPKTRSGKILRRTLRKIADGED 601
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
539-1038 |
5.25e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 75.19 E-value: 5.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 539 DAIARAADEFPERAAL---ETAQgRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPL 615
Cdd:PRK12583 22 DAFDATVARFPDREALvvrHQAL-RYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 616 DtewPQARRAEVVAA---SGCDAVLTdaqgLAGFAPSVAIA-----VDELKLDGAGENGS------------GENAAPNQ 675
Cdd:PRK12583 101 N---PAYRASELEYAlgqSGVRWVIC----ADAFKTSDYHAmlqelLPGLAEGQPGALACerlpelrgvvslAPAPPPGF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 676 LAY-----------------------------ILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------H 720
Cdd:PRK12583 174 LAWhelqargetvsrealaerqasldrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCvpvplyH 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 721 VAGLAVDTtleqiLAAWSRGACVVArPDELLEPQRFL-AFLSERAITVTDLAPAYANELVRASVADdwRDL-ALRCLVVG 798
Cdd:PRK12583 254 CFGMVLAN-----LGCMTVGACLVY-PNEAFDPLATLqAVEEERCTALYGVPTMFIAELDHPQRGN--FDLsSLRTGIMA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 799 GDVLPVALAQRWFElglDRRCALIN-AYGPTEATISSHYHRVQAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGEL 877
Cdd:PRK12583 326 GAPCPIEVMRRVMD---EMHMAEVQiAYGMTETSPVSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGEL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 878 ALGGIGLAEGYRGDAAASerrfaplRLPSGESLRMYrSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLP 957
Cdd:PRK12583 403 CTRGYSVMKGYWNNPEAT-------AESIDEDGWMH-TGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHP 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 958 QVRAAAA-GVVGEGAAQRLVAWVECAGedgfGQAdlnqtdSDQTESERWHRAlceRLPAYMVPTQFVALPRLPRNASGKI 1036
Cdd:PRK12583 475 AVADVQVfGVPDEKYGEEIVAWVRLHP----GHA------ASEEELREFCKA---RIAHFKVPRYFRFVDEFPMTVTGKV 541
|
..
gi 1246793773 1037 DR 1038
Cdd:PRK12583 542 QK 543
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
677-1041 |
5.99e-13 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 74.31 E-value: 5.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 677 AYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVdtTLEQILAAWSrgACVVARPDEl 750
Cdd:cd05912 80 ATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLcalplfHISGLSI--LMRSVIYGMT--VYLVDKFDA- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 751 lepQRFLAFLSERAITVTDLAPAYANELvrASVADDWRDLALRCLVVGGDVLPVALAQRWFELGLdrrcALINAYGPTE- 829
Cdd:cd05912 155 ---EQVLHLINSGKVTIISVVPTMLQRL--LEILGEGYPNNLRCILLGGGPAPKPLLEQCKEKGI----PVYQSYGMTEt 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 830 ----ATISSHYHRVQAIDASRPVPLGQLlpgRIAavldaHGRIVPRGVcGELALGGIGLAEGYRGDAAASERRFAplrlp 905
Cdd:cd05912 226 csqiVTLSPEDALNKIGSAGKPLFPVEL---KIE-----DDGQPPYEV-GEILLKGPNVTKGYLNRPDATEESFE----- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 906 SGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVraAAAGVVGEGAA---QRLVAWVECA 982
Cdd:cd05912 292 NG----WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAI--KEAGVVGIPDDkwgQVPVAFVVSE 365
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 983 GEdgFGQADLnqtdsdqteserwhRALC-ERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05912 366 RP--ISEEEL--------------IAYCsEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
3655-3976 |
6.53e-13 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 74.94 E-value: 6.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3655 PEVPT-EAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAA--TQTGRFSFDEHDVWSLF--HSHAFDFAVweLWGAWLYGG 3729
Cdd:cd05927 108 PPPPKpEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVfkILEILNKINPTDVYISYlpLAHIFERVV--EALFLYHGA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3730 R---------------AVLVPEAVCRQPDAFLDLLAEYGVTVLNQTP-----------SAFYALQSQAMRRE-------- 3775
Cdd:cd05927 186 KigfysgdirlllddiKALKPTVFPGVPRVLNRIYDKIFNKVQAKGPlkrklfnfalnYKLAELRSGVVRASpfwdklvf 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3776 ------LALNVRAVVFGGEALEPSRLQPWRErYPQAELVNMYGITETTVHVSFHRLSDEDlqspTSRIGSALPDLAVHVL 3849
Cdd:cd05927 266 nkikqaLGGNVRLMLTGSAPLSPEVLEFLRV-ALGCPVLEGYGQTECTAGATLTLPGDTS----VGHVGGPLPCAEVKLV 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3850 DA------AGQPVPlgvVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKL-R 3922
Cdd:cd05927 341 DVpemnydAKDPNP---RGEVCIRGPNVFSGYYKDPEKTAEALDEDG---WLHTGDIGEWLPNGTLKIIDRKKNIFKLsQ 414
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 3923 GYRIEPGEIAAKIASLPQVSDaaVTVEGQGEGAWLMAYAVaadgaePDPQSLRE 3976
Cdd:cd05927 415 GEYVAPEKIENIYARSPFVAQ--IFVYGDSLKSFLVAIVV------PDPDVLKE 460
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
2053-2517 |
8.60e-13 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 74.26 E-value: 8.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2053 VAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHpDARQIAV-LDD 2131
Cdd:cd12118 21 TSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRL-DAEEIAFiLRH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVIgwgaapawvpasvrwldaesvLDVVSAYEE---------PPRVDVDADTPAYLIYTSGSTGTPKGVVVSqgNL 2202
Cdd:cd12118 100 SEAKVLF---------------------VDREFEYEDllaegdpdfEWIPPADEWDPIALNYTSGTTGRPKGVVYH--HR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2203 ANYVAGVLPVLDLGEDASLATLSTV----AADLGF----TALFGALLSGRRVRllpAELAFDAQALAAhlqahpVDCLKI 2274
Cdd:cd12118 157 GAYLNALANILEWEMKQHPVYLWTLpmfhCNGWCFpwtvAAVGGTNVCLRKVD---AKAIYDLIEKHK------VTHFCG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2275 VPS-HLAGLLAAAGGTAVLPRECLV-TGGEALTGALVQQVRALAptLRIVNHYGPTETTVGILTCTVPEEW---PVE--- 2346
Cdd:cd12118 228 APTvLNMLANAPPSDARPLPHRVHVmTAGAPPPAAVLAKMEELG--FDVTHVYGLTETYGPATVCAWKPEWdelPTEera 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2347 -----QGVPVghpLAGNEAWVLDRFGL---PAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHplapdrlLYRSGDLA 2418
Cdd:cd12118 306 rlkarQGVRY---VGLEEVDVLDPETMkpvPRDGKTIGEIVFRGNIVMKGYLKNPEATAEAFRGG-------WFHSGDLA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2419 RLDGEGRIvylgrgdhQVKIR--------GYRVELGEVEQVLAQLPGVEVAAVLALPG--------ANGVLQLGACIQGs 2482
Cdd:cd12118 376 VIHPDGYI--------EIKDRskdiiisgGENISSVEVEGVLYKHPAVLEAAVVARPDekwgevpcAFVELKEGAKVTE- 446
|
490 500 510
....*....|....*....|....*....|....*..
gi 1246793773 2483 lEGVAEALAQRLPEYLCPsrwRAVE--SMPRLGNGKI 2517
Cdd:cd12118 447 -EEIIAFCREHLAGFMVP---KTVVfgELPKTSTGKI 479
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
3930-4004 |
9.29e-13 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 66.03 E-value: 9.29e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 3930 EIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGK 4004
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVgVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
602-1036 |
9.43e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 74.43 E-value: 9.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 602 LLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQgLAGFAPSVAIAVDELKL----DGAGENGS-------GEN 670
Cdd:PRK07786 84 VLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAA-LAPVATAVRDIVPLLSTvvvaGGSSDDSVlgyedllAEA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 671 AAPNQL--------AYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRV-------LHVAGLAvdttleQILA 735
Cdd:PRK07786 163 GPAHAPvdipndspALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVgfvgvplFHIAGIG------SMLP 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 736 AWSRGACVVARPDELLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDwRDLALRCLVVGGDVLPVALAQRWFELGL 815
Cdd:PRK07786 237 GLLLGAPTVIYPLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARP-RDLALRVLSWGAAPASDTLLRQMAATFP 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 816 DrrCALINAYGPTEatISSHYHRVQAIDASRPV-PLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAA 894
Cdd:PRK07786 316 E--AQILAAFGQTE--MSPVTCMLLGEDAIRKLgSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEA 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 895 SERRFAplrlpSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVGEGAAQr 974
Cdd:PRK07786 392 TAEAFA-----GG----WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVA--VIGRADEK- 459
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 975 lvaWvecaGEDGFGQADLNQTDSDQT--ESERWhraLCERLPAYMVPTQFVALPRLPRNASGKI 1036
Cdd:PRK07786 460 ---W----GEVPVAVAAVRNDDAALTleDLAEF---LTDRLARYKHPKALEIVDALPRNPAGKV 513
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
87-294 |
1.13e-12 |
|
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380457 [Multi-domain] Cd Length: 428 Bit Score: 73.44 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 87 PAPLSLGQErlWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLD-RCIQGEDSV------AAGGGAAV 159
Cdd:cd19534 1 EVPLTPIQR--WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRmRFRREDGGWqqrirgDVEELFRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 160 ESADLRGRGQDE-IDALVEGFRlRPFELQRQRPLRMQLLRLDGQGDgpvRHWLqvVVHHIACDGVSLGLLTQDLSRAYRv 238
Cdd:cd19534 79 EVVDLSSLAQAAaIEALAAEAQ-SSLDLEEGPLLAAALFDGTDGGD---RLLL--VIHHLVVDGVSWRILLEDLEAAYE- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 239 ecGLAAEPAPPLP--CQYGDYARWQRD--TLDRLDASLRHHVEALsgAPHLHELPLDHER 294
Cdd:cd19534 152 --QALAGEPIPLPskTSFQTWAELLAEyaQSPALLEELAYWRELP--AADYWGLPKDPEQ 207
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
679-1038 |
1.16e-12 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 72.68 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 679 ILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTtleqILAAWSR------GACVVARpdELLE 752
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHI----GGLWWILtclihgGLCVTGG--ENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 753 PQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDvLPVALAQRWFELGLDRRCAliNAYGPTEATI 832
Cdd:cd17635 80 YKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGS-RAIAADVRFIEATGLTNTA--QVYGLSETGT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 833 SS--HYHRvQAIDASrpvPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDaaaserrfaPLRLPSGESL 910
Cdd:cd17635 157 ALclPTDD-DSIEIN---AVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNN---------PERTAEVLID 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 911 RMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQRLVAWVECAGEDgfgq 989
Cdd:cd17635 224 GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQeCACYEISDEEFGELVGLAVVASAEL---- 299
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1246793773 990 aDLNQTdSDQTESERwhralcERLPAYMVPTQFVALPRLPRNASGKIDR 1038
Cdd:cd17635 300 -DENAI-RALKHTIR------RELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
3646-3946 |
1.47e-12 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 73.61 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3646 LDAVEPG----ELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVerlftAATQTGRFSFDEHdvwslfhsHAFDFAVWEL 3721
Cdd:cd17641 140 LDRRDPGlyerEVAAGKGEDVAVLCTTSGTTGKPKLAMLSHGNF-----LGHCAAYLAADPL--------GPGDEYVSVL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3722 WGAW-----------LYGGRAVLVPEAVCR--------QPDAFL----------------------------DLLAEYGV 3754
Cdd:cd17641 207 PLPWigeqmysvgqaLVCGFIVNFPEEPETmmedlreiGPTFVLlpprvwegiaadvrarmmdatpfkrfmfELGMKLGL 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3755 TVLNQTPSA-------------FYALQSQAMRRELAL-NVRAVVFGGEALEPSRLqpwreRYPQAELVNM---YGITETT 3817
Cdd:cd17641 287 RALDRGKRGrpvslwlrlaswlADALLFRPLRDRLGFsRLRSAATGGAALGPDTF-----RFFHAIGVPLkqlYGQTELA 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3818 VHVSFHRLSDEDLQSptsrIGSALPDLAVHVLDaagqpvplgvVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRS 3897
Cdd:cd17641 362 GAYTVHRDGDVDPDT----VGVPFPGTEVRIDE----------VGEILVRSPGVFVGYYKNPEATAEDFDEDG---WLHT 424
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3898 GDLGRYRADGSLEYRGRGDDQVKL-RGYRIEPGEIAAKIASLPQVSDAAV 3946
Cdd:cd17641 425 GDAGYFKENGHLVVIDRAKDVGTTsDGTRFSPQFIENKLKFSPYIAEAVV 474
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
3663-3931 |
1.57e-12 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 73.29 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3663 AYLIYTSGSTGTPKGVVVTHRN-VERLFTAATQTGRFSFDEHDVWsLFHSHAFDFAVWELwgAWLYGG-RAVLVPEAV-C 3739
Cdd:cd05908 109 AFIQFSSGSTGDPKGVMLTHENlVHNMFAILNSTEWKTKDRILSW-MPLTHDMGLIAFHL--APLIAGmNQYLMPTRLfI 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3740 RQPDAFLDLLAEYGVTVLNqTPSAFYALQSQAMRRELALN-----VRAVVFGGEALEP-------SRLQPWRERypQAEL 3807
Cdd:cd05908 186 RRPILWLKKASEHKATIVS-SPNFGYKYFLKTLKPEKANDwdlssIRMILNGAEPIDYelcheflDHMSKYGLK--RNAI 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3808 VNMYGITETTVHVSFHRLsDEDLQSPT-------------------------SRIGSALPDLAVHVLDAAGQPVPLGVVG 3862
Cdd:cd05908 263 LPVYGLAEASVGASLPKA-QSPFKTITlgrrhvthgepepevdkkdsecltfVEVGKPIDETDIRICDEDNKILPDGYIG 341
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 3863 ELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRaDGSLEYRGRGDDQVKLRGYRIEPGEI 3931
Cdd:cd05908 342 HIQIRGKNVTPGYYNNPEATAKVFTDDG---WLKTGDLGFIR-NGRLVITGREKDIIFVNGQNVYPHDI 406
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
535-1045 |
1.79e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 73.48 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 535 GNVVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIP 614
Cdd:PRK06188 12 ATYGHLLVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 615 LDTEWPQARRAEVVAASGCDAVLTD-------AQGLAGFAPS---------VAIAVDELKLDGAGENGSGENAA-PNQLA 677
Cdd:PRK06188 92 LHPLGSLDDHAYVLEDAGISTLIVDpapfverALALLARVPSlkhvltlgpVPDGVDLLAAAAKFGPAPLVAAAlPPDIA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 678 YILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVDTTLeqilaawSRGACVVARPDelL 751
Cdd:PRK06188 172 GLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLmctplsHAGGAFFLPTL-------LRGGTVIVLAK--F 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 752 EPQRFLAFLSERAITVTDLAPAYANELVRASVADDwRDL-ALRCLVVGGD-VLPVALAQrwfelGLDR-RCALINAYGPT 828
Cdd:PRK06188 243 DPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRT-RDLsSLETVYYGASpMSPVRLAE-----AIERfGPIFAQYYGQT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 829 EATISSHYHRVQAIDASRPVPL---GQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLp 905
Cdd:PRK06188 317 EAPMVITYLRKRDHDPDDPKRLtscGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDGWL- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 906 sgeslrmyRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVraAAAGVVGegaaqrlvawvecAGED 985
Cdd:PRK06188 396 --------HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAV--AQVAVIG-------------VPDE 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 986 GFGQA----DLNQTDSDQTESErWHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRALPAPP 1045
Cdd:PRK06188 453 KWGEAvtavVVLRPGAAVDAAE-LQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRARY 515
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
2061-2524 |
2.04e-12 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 72.85 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2061 SWTYAQLRAAAGRIAGAL-DAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIg 2139
Cdd:cd05937 5 TWTYSETYDLVLRYAHWLhDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVI- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2140 wgaapawvpasvrwldaesvldvvsayeepprvdVDADTPAYLIYTSGSTGTPKGVVVSqgNLANYVAGVLPVLDLGEDA 2219
Cdd:cd05937 84 ----------------------------------VDPDDPAILIYTSGTTGLPKAAAIS--WRRTLVTSNLLSHDLNLKN 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2220 SLATLSTVA---ADLGFTALFGALLSGRRVRLLPaelafdaqalaahlqahpvdclKIVPSHLAGLLAAAGGTAVL---- 2292
Cdd:cd05937 128 GDRTYTCMPlyhGTAAFLGACNCLMSGGTLALSR----------------------KFSASQFWKDVRDSGATIIQyvge 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2293 --------PRE-------CLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPE-------------EWP 2344
Cdd:cd05937 186 lcryllstPPSpydrdhkVRVAWGNGLRPDIWERFRERFNVPEIGEFYAATEGVFALTNHNVGDfgagaighhglirRWK 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2345 VE-QGVPVGHPLAGNEAWVLDR--FGLPAPVGVAGELY--LGGGNLSL--GYWQRAEQTAERFVAHPLAPDRLLYRSGDL 2417
Cdd:cd05937 266 FEnQVVLVKMDPETDDPIRDPKtgFCVRAPVGEPGEMLgrVPFKNREAfqGYLHNEDATESKLVRDVFRKGDIYFRTGDL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2418 ARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAV--LALPGANGVLQLGACI--QGSLEGVAEALA-- 2491
Cdd:cd05937 346 LRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygVKVPGHDGRAGCAAITleESSAVPTEFTKSll 425
|
490 500 510
....*....|....*....|....*....|....*...
gi 1246793773 2492 -----QRLPEYLCPSRWRAVESMPRLGNGKIDRQALAD 2524
Cdd:cd05937 426 aslarKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
537-1041 |
2.77e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 72.50 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 537 VVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARsVALCLPRGLDWYCLLLGAWRAGLSVIPLD 616
Cdd:PRK07638 3 ITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKT-IAILLENRIEFLQLFAGAAMAGWTCVPLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 617 TEWPQARRAEVVAASGCDAVLTDAQGLAGF--APSVAIAVDELK--LDGAGENGSGENAAPNQLAYILYTSGSTGIPKGV 692
Cdd:PRK07638 82 IKWKQDELKERLAISNADMIVTERYKLNDLpdEEGRVIEIDEWKrmIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPKAF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 693 EVGHAALAAHIDAAAEALALSADDRVLhVAGLAVDTT-LEQILAAWSRGACVVARPDelLEPQRFLAFLSERAITVTDLA 771
Cdd:PRK07638 162 LRAQQSWLHSFDCNVHDFHMKREDSVL-IAGTLVHSLfLYGAISTLYVGQTVHLMRK--FIPNQVLDKLETENISVMYTV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 772 PAYANELVRasvADDWRDLALRCLVVGGDVLPVA---LAQRWFELgldrrcALINAYGPTEATISSHYHRVQAidASRPV 848
Cdd:PRK07638 239 PTMLESLYK---ENRVIENKMKIISSGAKWEAEAkekIKNIFPYA------KLYEFYGASELSFVTALVDEES--ERRPN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 849 PLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAaserrfAPLRLPSGESLRMYRSG--DRvrlldDGE 926
Cdd:PRK07638 308 SVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGV------LARELNADGWMTVRDVGyeDE-----EGF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 927 LQFLGRADFQVKLRGYRIELEEIEHCLGQLPQV-RAAAAGVVGEGAAQRLVAWVEcagedgfGQADLNQTdsdqteserw 1005
Cdd:PRK07638 377 IYIVGREKNMILFGGINIFPEEIESVLHEHPAVdEIVVIGVPDSYWGEKPVAIIK-------GSATKQQL---------- 439
|
490 500 510
....*....|....*....|....*....|....*..
gi 1246793773 1006 hRALC-ERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK07638 440 -KSFClQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1170-1327 |
2.89e-12 |
|
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380458 [Multi-domain] Cd Length: 423 Bit Score: 72.14 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1170 QPLDAQHLAQVWDALWRRHDLLRASFErADGQwrQQVAAPGPAPAIQAQDWRGAADLDsrVDAAFARMQEAT------PL 1243
Cdd:cd19535 35 EDLDPDRLERAWNKLIARHPMLRAVFL-DDGT--QQILPEVPWYGITVHDLRGLSEEE--AEAALEELRERLshrvldVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1244 AGPLVALTHAHCDDGE-RLLICAHHLIVDAVSWRLLLGElfdgLAALARGEAWTPSARGASYADYVEALREADDAQR-FD 1321
Cdd:cd19535 110 RGPLFDIRLSLLPEGRtRLHLSIDLLVADALSLQILLRE----LAALYEDPGEPLPPLELSFRDYLLAEQALRETAYeRA 185
|
....*.
gi 1246793773 1322 AGFWRE 1327
Cdd:cd19535 186 RAYWQE 191
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
2168-2536 |
3.44e-12 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 73.08 E-value: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2168 EPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGedaslatlstvAADLGFTAL-----FG---- 2238
Cdd:PRK06814 784 LVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFS-----------PEDKVFNALpvfhsFGltgg 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2239 ---ALLSGRRVRLLPAELAFdaqalaahlqahpvdclKIVPShlagLLAAAGGTAVLPRECLVT---------------- 2299
Cdd:PRK06814 853 lvlPLLSGVKVFLYPSPLHY-----------------RIIPE----LIYDTNATILFGTDTFLNgyaryahpydfrslry 911
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2300 ---GGEALTGAlVQQVRALAPTLRIVNHYGPTETTvGILTCTVPEEWPVEQgvpVGHPLAGNEaWVLDrfglPAPvGV-- 2374
Cdd:PRK06814 912 vfaGAEKVKEE-TRQTWMEKFGIRILEGYGVTETA-PVIALNTPMHNKAGT---VGRLLPGIE-YRLE----PVP-GIde 980
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2375 AGELYLGGGNLSLGYWqRAEQTAerfVAHPLAPDrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQ 2454
Cdd:PRK06814 981 GGRLFVRGPNVMLGYL-RAENPG---VLEPPADG--WYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAE 1054
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2455 L-PGVEVAAVlALP----GANGVLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLLQQD 2529
Cdd:PRK06814 1055 LwPDALHAAV-SIPdarkGERIILLTTASDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKIDYVAVTKLAEEA 1133
|
....*..
gi 1246793773 2530 DADSSAE 2536
Cdd:PRK06814 1134 AAKPEAA 1140
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
604-1040 |
3.47e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 72.34 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 604 GAWRAGLSVIPLDTEWPQ---ARRAE----VVAASGCDAVLTDA--QGLAGFAPSVAIAVDELKLDGAGENGSGENAAPN 674
Cdd:PRK07768 73 GLWMRGASLTMLHQPTPRtdlAVWAEdtlrVIGMIGAKAVVVGEpfLAAAPVLEEKGIRVLTVADLLAADPIDPVETGED 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 675 QLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL-------H----VAGLAVDTTleqilaawsRGACV 743
Cdd:PRK07768 153 DLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMvswlplfHdmgmVGFLTVPMY---------FGAEL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 744 V-ARPDELL-EPQRFLAFLSERAITVTdLAPAYANELVR---ASVADDWR-DL-ALRCLVVGGDVLPVALAQRWFE---- 812
Cdd:PRK07768 224 VkVTPMDFLrDPLLWAELISKYRGTMT-AAPNFAYALLArrlRRQAKPGAfDLsSLRFALNGAEPIDPADVEDLLDagar 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 813 LGLdRRCALINAYGPTEATISSHYH------RVQAIDA-----------------SRPVPLGQLLPGRIAAVLDAHGRIV 869
Cdd:PRK07768 303 FGL-RPEAILPAYGMAEATLAVSFSpcgaglVVDEVDAdllaalrravpatkgntRRLATLGPPLPGLEVRVVDEDGQVL 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 870 P-RGVcGELALGGIGLAEGYRGDAAaserrFAPLRLPSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEE 948
Cdd:PRK07768 382 PpRGV-GVIELRGESVTPGYLTMDG-----FIPAQDADG----WLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTD 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 949 IEHCLGQLPQVRAAAAGVVGEGAAQRlvawvecagEDGFGQADLNQTDSDQTESERWHRALCERLPAY--MVPTQFVALP 1026
Cdd:PRK07768 452 IERAAARVEGVRPGNAVAVRLDAGHS---------REGFAVAVESNAFEDPAEVRRIRHQVAHEVVAEvgVRPRNVVVLG 522
|
490
....*....|....*.
gi 1246793773 1027 --RLPRNASGKIDRRA 1040
Cdd:PRK07768 523 pgSIPKTPSGKLRRAN 538
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
636-1041 |
3.64e-12 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 72.28 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 636 VLTDAQGLAGFAPSVAIAVDELKLDGAGENG---SGENAApnqlAYILYTSGSTGIPKGVEVGHAALaahidaaaealal 712
Cdd:cd12119 126 VMTDDAAMPEPAGVGVLAYEELLAAESPEYDwpdFDENTA----AAICYTSGTTGNPKGVVYSHRSL------------- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 713 saddrVLH-VAGLAVDTT-LEQ-------------------ILAAWSrGACVVArPDELLEPQRFLAFLSERAITVTDLA 771
Cdd:cd12119 189 -----VLHaMAALLTDGLgLSEsdvvlpvvpmfhvnawglpYAAAMV-GAKLVL-PGPYLDPASLAELIEREGVTFAAGV 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 772 PAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFELGLDrrcaLINAYGPTE----ATISSHYHRVQAIDASRP 847
Cdd:cd12119 262 PTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEERGVR----VIHAWGMTEtsplGTVARPPSEHSNLSEDEQ 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 848 VPL----GQLLPGRIAAVLDAHGRIVPR--GVCGELALGGIGLAEGYRGDAAASERRFAPLRLpsgeslrmyRSGDRVRL 921
Cdd:cd12119 338 LALrakqGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEESEALTEDGWL---------RTGDVATI 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 922 LDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVG---EGAAQRLVAWVECAGEDGFGQADLNQTdsd 998
Cdd:cd12119 409 DEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAA--VIGvphPKWGERPLAVVVLKEGATVTAEELLEF--- 483
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1246793773 999 qteserwhraLCERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd12119 484 ----------LADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
2299-2525 |
4.07e-12 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 72.16 E-value: 4.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2299 TGGEALTGALVQQVRALApTLRIVNHYGPTETTVgiLTCTVPEEWPVEQGVpVGHPLAGNEAWVLDRFGLPAPVGVAGEL 2378
Cdd:PRK12492 340 SGGTALVKATAERWEQLT-GCTIVEGYGLTETSP--VASTNPYGELARLGT-VGIPVPGTALKVIDDDGNELPLGERGEL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2379 YLGGGNLSLGYWQRAEQTAERFVAHPlapdrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGV 2458
Cdd:PRK12492 416 CIKGPQVMKGYWQQPEATAEALDAEG------WFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKV 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 2459 EVAAVLALP----GANGVLQLGACIQG-SLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADL 2525
Cdd:PRK12492 490 ANCAAIGVPdersGEAVKLFVVARDPGlSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
89-385 |
4.64e-12 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.
Pssm-ID: 380469 [Multi-domain] Cd Length: 422 Bit Score: 71.57 E-value: 4.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 89 PLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQGEDS------VAAGGGAAVESA 162
Cdd:cd19547 3 PLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRaeplqyVRDDLAPPWALL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 163 DLRGRGQDEIDALVEGF----RLRPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSLGLLTQDLSRAYRv 238
Cdd:cd19547 83 DWSGEDPDRRAELLERLladdRAAGLSLADCPLYRLTLVRLGGG-----RHYLLWSHHHILLDGWCLSLIWGDVFRVYE- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 239 ecGLAAEPAPPL-PCQ-YGDYARWQRDTLDRLDAS---LRHHVEALSGAPhLHELPLDHErpavlGQSGAKLRlAFPPGL 313
Cdd:cd19547 157 --ELAHGREPQLsPCRpYRDYVRWIRARTAQSEESerfWREYLRDLTPSP-FSTAPADRE-----GEFDTVVH-EFPEQL 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 314 SERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRvRPELDS---LVGLFVNTVVLRTQLhdDPD 385
Cdd:cd19547 228 TRLVNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGR-PPELEGsehMVGIFINTIPLRIRL--DPD 299
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
2063-2519 |
4.97e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 71.70 E-value: 4.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2063 TYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQ-HPDARQiAVLDDSgarivigwg 2141
Cdd:cd05914 9 TYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEfTADEVH-HILNHS--------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2142 aapawvpasvrwldaESVLDVVSayeepprvdvDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGE-DAS 2220
Cdd:cd05914 79 ---------------EAKAIFVS----------DEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKgDKI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2221 LATLSTVAA-DLGFTALFGALLSGRRVRL--LPAELAFDAQALAAHLQA---HPVDCLKI-----VPSHLAGLLAAAGGT 2289
Cdd:cd05914 134 LSILPLHHIyPLTFTLLLPLLNGAHVVFLdkIPSAKIIALAFAQVTPTLgvpVPLVIEKIfkmdiIPKLTLKKFKFKLAK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2290 AVLPRECL------------------VTGGEALTGALVQQVRALAPTLRIvnHYGPTETTvGILTCTVPEEwpvEQGVPV 2351
Cdd:cd05914 214 KINNRKIRklafkkvheafggnikefVIGGAKINPDVEEFLRTIGFPYTI--GYGMTETA-PIISYSPPNR---IRLGSA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2352 GHPLAGNEAWVLDrfglPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVahplaPDRLLyRSGDLARLDGEGRIVYLGR 2431
Cdd:cd05914 288 GKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFD-----KDGWF-HTGDLGKIDAEGYLYIRGR 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2432 GDHQ-VKIRGYRVELGEVEQVLAQLPGV-----------EVAAVLALPGANGVLQLG--ACIQGSLEGVAEALAQRLPEY 2497
Cdd:cd05914 358 KKEMiVLSSGKNIYPEEIEAKINNMPFVleslvvvqekkLVALAYIDPDFLDVKALKqrNIIDAIKWEVRDKVNQKVPNY 437
|
490 500
....*....|....*....|...
gi 1246793773 2498 LCPSRWRAV-ESMPRLGNGKIDR 2519
Cdd:cd05914 438 KKISKVKIVkEEFEKTPKGKIKR 460
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
529-1041 |
5.01e-12 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 71.84 E-value: 5.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 529 PAPRTVG-NVVDAIARAADEFPERAALETAQGR--LSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGA 605
Cdd:PRK05852 9 PMASDFGpRIADLVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 606 WRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQGLAGFAP--------SVAIAVDELKLDGAGENGSGENAAPNQL- 676
Cdd:PRK05852 89 SRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADGPHDRAEpttrwwplTVNVGGDSGPSGGTLSVHLDAATEPTPAt 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 677 ----------AYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTL-EQILAAWSRGACVVA 745
Cdd:PRK05852 169 stpeglrpddAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLiAALLATLASGGAVLL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 746 RPDELLEPQRFLAFLSERAITVTDLAPAYANELV-RASVADDWRD-LALRCLVVGGDVLPVALAQrwfelGLDRRCA--L 821
Cdd:PRK05852 249 PARGRFSAHTFWDDIKAVGATWYTAVPTIHQILLeRAATEPSGRKpAALRFIRSCSAPLTAETAQ-----ALQTEFAapV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 822 INAYGPTEATISSHYHRVQAIDASRPVPLGQLLPGRIAA----VLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASER 897
Cdd:PRK05852 324 VCAFGMTEATHQVTTTQIEGIGQTENPVVSTGLVGRSTGaqirIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 898 RFAPLRLpsgeslrmyRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA-----GVVGEGAA 972
Cdd:PRK05852 404 NFTDGWL---------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVfgvpdQLYGEAVA 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 973 QRLVAwvecagedgfgQADLNQTDSDQTESERwhralcERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK05852 475 AVIVP-----------RESAPPTAEELVQFCR------ERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
2169-2522 |
5.08e-12 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 71.79 E-value: 5.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2169 PPRVDVDADTpAYLIYTSGSTGTPKGVVVSQGNL-ANYVAGVLPVLDLGEDASLATLSTVAADLGF--TALFGALLSGRR 2245
Cdd:cd17642 177 PPSFDRDEQV-ALIMNSSGSTGLPKGVQLTHKNIvARFSHARDPIFGNQIIPDTAILTVIPFHHGFgmFTTLGYLICGFR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2246 VRLLPAelaFDAQALAAHLQAHPVDCLKIVPShlagllaaagGTAVLPRECLV------------TGGEALTGALVQQV- 2312
Cdd:cd17642 256 VVLMYK---FEEELFLRSLQDYKVQSALLVPT----------LFAFFAKSTLVdkydlsnlheiaSGGAPLSKEVGEAVa 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2313 -RALAPTLRivNHYGPTETTVGILTctVPEEWpVEQGVpVGHPLAGNEAWVLD-RFGLPAPVGVAGELYLGGGNLSLGYW 2390
Cdd:cd17642 323 kRFKLPGIR--QGYGLTETTSAILI--TPEGD-DKPGA-VGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGPMIMKGYV 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2391 QRAEQTAERFVAhplapDRLLyRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLA----- 2465
Cdd:cd17642 397 NNPEATKALIDK-----DGWL-HSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGipded 470
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 2466 ---LPGANGVLQLGACIqgslegVAEALAQRLPEYLCPSRW-----RAVESMPRLGNGKIDRQAL 2522
Cdd:cd17642 471 ageLPAAVVVLEAGKTM------TEKEVMDYVASQVSTAKRlrggvKFVDEVPKGLTGKIDRRKI 529
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
588-970 |
5.11e-12 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 71.47 E-value: 5.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAqglagfapsvaiavdelkldgagengs 667
Cdd:cd05907 33 VAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVED--------------------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 668 genaaPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAvdTTLEQILAAW---SRGACVV 744
Cdd:cd05907 86 -----PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLA--HVFERRAGLYvplLAGARIY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 745 -ARPDELL-------EPQRFLAFLS--ER--AITVTDLAPAYANELVRASVADDwrdlaLRCLVVGGDVLPVALAQRWFE 812
Cdd:cd05907 159 fASSAETLlddlsevRPTVFLAVPRvwEKvyAAIKVKAVPGLKRKLFDLAVGGR-----LRFAASGGAPLPAELLHFFRA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 813 LGLDrrcaLINAYGPTEATISSHYHRVQAIDASRPvplGQLLPGriaavldAHGRIVPRgvcGELALGGIGLAEGYRGDA 892
Cdd:cd05907 234 LGIP----VYEGYGLTETSAVVTLNPPGDNRIGTV---GKPLPG-------VEVRIADD---GEILVRGPNVMLGYYKNP 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 893 AASERRFaplrLPSGEslrmYRSGDRVRLLDDGELQFLGRA-DFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVGEG 970
Cdd:cd05907 297 EATAEAL----DADGW----LHTGDLGEIDEDGFLHITGRKkDLIITSGGKNISPEPIENALKASPLISQAV--VIGDG 365
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
3547-4010 |
5.38e-12 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 71.71 E-value: 5.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3547 YATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFIL---EDSGVCLSVS- 3622
Cdd:PRK06018 42 YAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIInhaEDRVVITDLTf 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3623 ---QRALAVELPGT-------------------ALCLDDPFTRAQLDaVEPGELPEvptEAPAYLIYTSGSTGTPKGVVV 3680
Cdd:PRK06018 122 vpiLEKIADKLPSVeryvvltdaahmpqttlknAVAYEEWIAEADGD-FAWKTFDE---NTAAGMCYTSGTTGDPKGVLY 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3681 THR-NVerLFT-AATQTGRFSFDEHD----VWSLFHSHAFDFAvwelWGAWLYGGRAVLvpeavcrqPDAFLD------L 3748
Cdd:PRK06018 198 SHRsNV--LHAlMANNGDALGTSAADtmlpVVPLFHANSWGIA----FSAPSMGTKLVM--------PGAKLDgasvyeL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3749 LAEYGVTVLNQTPSAFYALQsQAMRRE-LAL-NVRAVVFGGEALEPSRLQPWRERypQAELVNMYGITETTVHVSFHRLS 3826
Cdd:PRK06018 264 LDTEKVTFTAGVPTVWLMLL-QYMEKEgLKLpHLKMVVCGGSAMPRSMIKAFEDM--GVEVRHAWGMTEMSPLGTLAALK 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3827 DEDLQSPtsrigsalPDLAVHVLDAAGQPvPLGV------------------VGELVVEGDGVAQGYWQrpeLTAERFVE 3888
Cdd:PRK06018 341 PPFSKLP--------GDARLDVLQKQGYP-PFGVemkitddagkelpwdgktFGRLKVRGPAVAAAYYR---VDGEILDD 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3889 RGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEGAW---LMAYAVAAD 3965
Cdd:PRK06018 409 DG---FFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVI--GVYHPKWderPLLIVQLKP 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1246793773 3966 GAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK06018 484 GETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
2052-2524 |
6.24e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 71.47 E-value: 6.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDpQHPDARQIA-VLD 2130
Cdd:PRK08276 2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPIN-WHLTAAEIAyIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2131 DSGARIVIGWGA-------APAWVP--ASVRWLDAESVlDVVSAYEEppRVDVDADTP-------AYLIYTSGSTGTPKG 2194
Cdd:PRK08276 81 DSGAKVLIVSAAladtaaeLAAELPagVPLLLVVAGPV-PGFRSYEE--ALAAQPDTPiadetagADMLYSSGTTGRPKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2195 VVVSQGNLANYVAG----VLPVLDLGEDASLATLSTV----AADLGFTAlfGALLSGRRVRLLPaelAFDAQALAAHLQA 2266
Cdd:PRK08276 158 IKRPLPGLDPDEAPgmmlALLGFGMYGGPDSVYLSPAplyhTAPLRFGM--SALALGGTVVVME---KFDAEEALALIER 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2267 HPVDCLKIVPSHLAGLLAaaggtavLPREclvtggealtgalvqqVRAL--APTLRIVNH-------------------- 2324
Cdd:PRK08276 233 YRVTHSQLVPTMFVRMLK-------LPEE----------------VRARydVSSLRVAIHaaapcpvevkramidwwgpi 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2325 ----YGPTETtvGILTCTVPEEWPVEQGvPVGHPLAGnEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERF 2400
Cdd:PRK08276 290 iheyYASSEG--GGVTVITSEDWLAHPG-SVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAAR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2401 VAHPLAPdrllyrSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGAN------GVLQ 2474
Cdd:PRK08276 366 NPHGWVT------VGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEmgervkAVVQ 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 2475 LGACIQGSLEGVAEALA---QRLPEYLCPSRWRAVESMPRLGNGKIDRQALAD 2524
Cdd:PRK08276 440 PADGADAGDALAAELIAwlrGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRD 492
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
679-1038 |
6.61e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 70.38 E-value: 6.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 679 ILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRV------LHVAGLAVDttleqILAAWSRGACVVArPDELLE 752
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLcipvplFHCFGSVLG-----VLACLTHGATMVF-PSPSFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 753 PQRFLAFLSERAITVTDLAPA-YANELVRASVADDwrDLA-LRCLVVGGDVLPVALAQRWFE-LGLDrrcALINAYGPTE 829
Cdd:cd05917 81 PLAVLEAIEKEKCTALHGVPTmFIAELEHPDFDKF--DLSsLRTGIMAGAPCPPELMKRVIEvMNMK---DVTIAYGMTE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 830 ATISSHYHRVQAIDASRPVPLGQLLPGRIAAVLDAHGRIVP-RGVCGELALGGIGLAEGYRGDAAASERRFaplrlpSGE 908
Cdd:cd05917 156 TSPVSTQTRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEKTAEAI------DGD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 909 slRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQRLVAWVecAGEDGf 987
Cdd:cd05917 230 --GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSdVQVVGVPDERYGEEVCAWI--RLKEG- 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 988 gqadlnqtdSDQTESERwhRALC-ERLPAYMVPTQFVALPRLPRNASGKIDR 1038
Cdd:cd05917 305 ---------AELTEEDI--KAYCkGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
584-1041 |
8.34e-12 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 70.87 E-value: 8.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 584 QARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPqaRRAEVVAASGCDAVLTDAQGLAGFAPSvAIAVDELKLDGAG 663
Cdd:cd05929 41 IADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAP--RAEACAIIEIKAAALVCGLFTGGGALD-GLEDYEAAEGGSP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 664 ENGSGENAAPNqlaYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALAL---SADDRVLHVAGLAVDTTLEQILAAWSRG 740
Cdd:cd05929 118 ETPIEDEAAGW---KMLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAALGfgpGADSVYLSPAPLYHAAPFRWSMTALFMG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 741 ACVVARpdELLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWR-DLA-LRCLVVGGDVLPVALAQRWFELGLDRr 818
Cdd:cd05929 195 GTLVLM--EKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAyDLSsLKRVIHAAAPCPPWVKEQWIDWGGPI- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 819 caLINAYGPTEATISShyhrvqAIDA----SRPVPLGQLLPGRIaAVLDAHGRIVPRGVCGELalggiglaegYRGDAAA 894
Cdd:cd05929 272 --IWEYYGGTEGQGLT------IINGeewlTHPGSVGRAVLGKV-HILDEDGNEVPPGEIGEV----------YFANGPG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 895 SERRFAPLRLPSGESLRMYRS-GDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA-GVVGEGAA 972
Cdd:cd05929 333 FEYTNDPEKTAAARNEGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVvGVPDEELG 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 973 QRLVAWVECAGEDGFGQADLNQTdsdqteserwhRALC-ERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05929 413 QRVHAVVQPAPGADAGTALAEEL-----------IAFLrDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
2545-2602 |
1.03e-11 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 62.58 E-value: 1.03e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 2545 EVLRELWQKLLGREH--IGAHDNFFALGGDSILSLQLVARARQA-GLALMPRQLYDHPTLA 2602
Cdd:pfam00550 1 ERLRELLAEVLGVPAeeIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLA 61
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
2052-2523 |
1.04e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 70.80 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASwtYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDD 2131
Cdd:PRK13383 53 AIIDDDGALS--YRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVIgwgAAPAWVPASVRWLDAESVLD--VVSAYEEPPRVDVDADTPAYLIyTSGSTGTPKGVVvSQGNLANYVAGV 2209
Cdd:PRK13383 131 HHISTVV---ADNEFAERIAGADDAVAVIDpaTAGAEESGGRPAVAAPGRIVLL-TSGTTGKPKGVP-RAPQLRSAVGVW 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2210 LPVLD-----LGEDASLATLSTVAADLGF----TALFGALLSGRRvrllpaelaFDAQALAAHLQAHPVDCLKIVPSHLA 2280
Cdd:PRK13383 206 VTILDrtrlrTGSRISVAMPMFHGLGLGMlmltIALGGTVLTHRH---------FDAEAALAQASLHRADAFTAVPVVLA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2281 GLLAAAGGT-AVLPRECL---VTGGEALTGALVQQVRALAPTLrIVNHYGPTETTVGIL-TCTVPEEWPVEqgvpVGHPL 2355
Cdd:PRK13383 277 RILELPPRVrARNPLPQLrvvMSSGDRLDPTLGQRFMDTYGDI-LYNGYGSTEVGIGALaTPADLRDAPET----VGKPV 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2356 AGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYwqraEQTAERFVAHPLApdrllyRSGDLARLDGEGRIVYLGRGDHQ 2435
Cdd:PRK13383 352 AGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRY----TDGGGKAVVDGMT------STGDMGYLDNAGRLFIVGREDDM 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2436 VKIRGYRVELGEVEQVLAQLPGVEVAAVLALP--------GANGVLQLGACIQGslEGVAEALAQRLPEYLCPSRWRAVE 2507
Cdd:PRK13383 422 IISGGENVYPRAVENALAAHPAVADNAVIGVPderfghrlAAFVVLHPGSGVDA--AQLRDYLKDRVSRFEQPRDINIVS 499
|
490
....*....|....*.
gi 1246793773 2508 SMPRLGNGKIDRQALA 2523
Cdd:PRK13383 500 SIPRNPTGKVLRKELP 515
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
3498-4005 |
1.06e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 70.89 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3498 PLLPSQTRSAAwtsrERYACTGNLVSRFAE-IARRYpariavsaedgelDYATLDRRSSQLATLLIRQGAGPGQRVGLCL 3576
Cdd:PRK07008 9 PLLISSLIAHA----ARHAGDTEIVSRRVEgDIHRY-------------TYRDCERRAKQLAQALAALGVEPGDRVGTLA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3577 PRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFIL---EDSGVCLSVS----QRALAVELPGT----ALCLDDPFTRAQ 3645
Cdd:PRK07008 72 WNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVnhaEDRYVLFDLTflplVDALAPQCPNVkgwvAMTDAAHLPAGS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3646 LD--------AVEPG--ELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQTGRFSFDEHD----VWSLFHS 3711
Cdd:PRK07008 152 TPllcyetlvGAQDGdyDWPRFDENQASSLCYTSGTTGNPKGALYSHRSTVLHAYGAALPDAMGLSARDavlpVVPMFHV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3712 HAfdfavWEL-WGAWLYGGRAVLvpeavcrqPDAFLD------LLAEYGVTVLNQTPSAFYALQSQAMRRELALN-VRAV 3783
Cdd:PRK07008 232 NA-----WGLpYSAPLTGAKLVL--------PGPDLDgkslyeLIEAERVTFSAGVPTVWLGLLNHMREAGLRFStLRRT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3784 VFGGEALEPSRLQPWRERYpQAELVNMYGITE-------TTVHVSFHRLSDEDLQSPTSRIGSALPDLAVHVLDAAGQPV 3856
Cdd:PRK07008 299 VIGGSACPPAMIRTFEDEY-GVEVIHAWGMTEmsplgtlCKLKWKHSQLPLDEQRKLLEKQGRVIYGVDMKIVGDDGREL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3857 PL-GVV-GELVVEGDGVAQGYWQRpelTAERFVerggQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAK 3934
Cdd:PRK07008 378 PWdGKAfGDLQVRGPWVIDRYFRG---DASPLV----DGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENV 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 3935 IASLPQVSDAAVTveGQGEGAW----LMAyAVAADGAEpdpqSLREALRAL----LPDYMLPRLIQLLPALPLTANGKL 4005
Cdd:PRK07008 451 AVAHPAVAEAACI--ACAHPKWderpLLV-VVKRPGAE----VTREELLAFyegkVAKWWIPDDVVFVDAIPHTATGKL 522
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
3637-3982 |
1.15e-11 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 70.18 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3637 LDD----PFTRAQ-LDAVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVVT-------HRNVERLFTAAtqtGrfsFDEHD 3704
Cdd:COG1541 55 LEDlaklPFTTKEdLRDNYPFGLFAVPLEEIVRIHASSGTTGKPTVVGYTrkdldrwAELFARSLRAA---G---VRPGD 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3705 VwslFHsHAFDFAVWelWGAWL--YGGRAV---LVPEAVcRQPDAFLDLLAEYGVTVLNQTPSafYALQ-SQAMRRE--- 3775
Cdd:COG1541 129 R---VQ-NAFGYGLF--TGGLGlhYGAERLgatVIPAGG-GNTERQLRLMQDFGPTVLVGTPS--YLLYlAEVAEEEgid 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3776 -LALNVRAVVFGGEALEPSrlqpWRERYPQ---AELVNMYGITETTVHVSFhrlsdedlQSPTSRiGSALPDLAVHV--L 3849
Cdd:COG1541 200 pRDLSLKKGIFGGEPWSEE----MRKEIEErwgIKAYDIYGLTEVGPGVAY--------ECEAQD-GLHIWEDHFLVeiI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3850 D-AAGQPVPLGVVGELVVEGdgvaqgywqrpeLTAE-----RfverggqrfYRSGDLGRYRADGS--------LEY-RGR 3914
Cdd:COG1541 267 DpETGEPVPEGEEGELVVTT------------LTKEampliR---------YRTGDLTRLLPEPCpcgrthprIGRiLGR 325
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 3915 GDDQVKLRGYRIEPGEIAAKIASLPQVSDAA-VTVEGQGEGAWLMAYAVAADGAEPDP--QSLREALRALL 3982
Cdd:COG1541 326 ADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYqIVVDREGGLDELTVRVELAPGASLEAlaEAIAAALKAVL 396
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
1181-1723 |
1.19e-11 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 71.44 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1181 WDALW-----RRHDLLRASFEradgqwRQQVAAPGPAPAIQAQDWRGAADLDSRVDAAFARMQEATPLAGPLVALTHAHC 1255
Cdd:COG3321 849 WSALYpgrgrRRVPLPTYPFQ------REDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALA 922
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1256 DDGERLLICAHHLIVDAVSWRLLLGELFDGLAALARGEAWTPSARGAsyadyveALREADDAQRFDAGFWRELAAQPMQA 1335
Cdd:COG3321 923 AAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAA-------AAAAAAAAAAAAAAAAAAAAAAAAAA 995
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1336 LPQDRPVALADARQSNVGRIVQTLDAGLTADLLERAGEAYRCRTDEVLLIALARALATRTGRNRLWLDRERHGRDVLDGR 1415
Cdd:COG3321 996 LAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALA 1075
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1416 DWSSVLGWYTAVHPLPLDLGVADGPAQIGALKEQIRALARRGLDYMPLVASARIPALPAGQLLFNYHGVVDAGAHPAFEV 1495
Cdd:COG3321 1076 ELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAA 1155
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1496 EPRTLASGNGADNPPGALVEINARVQAGRLGLVWNYAGEAYDAATIEAWSQAFAAELAALVAHCLQPGSGALTASDLPQA 1575
Cdd:COG3321 1156 AAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALAL 1235
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1576 RLQADEFALLAAREDARAIEHAFPLTPLQRGVLLESLRGDGADPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAI 1655
Cdd:COG3321 1236 LALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAA 1315
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 1656 VWEGLSVPHQIVLADAAAPWQTLDWSALDDAAQDAQLQRWLADDAAQGVDFAHAPLARMSLIGRGGGR 1723
Cdd:COG3321 1316 AAAAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAA 1383
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
3653-4017 |
1.23e-11 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 71.28 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3653 ELPEVPTEApAYLIYTSGSTGTPKGVVVTHR----NVERLFTAATQTGRFSFdeHDVWSLFHshAFDFAVwELWGAWLYG 3728
Cdd:PRK08043 359 QVKQQPEDA-ALILFTSGSEGHPKGVVHSHKsllaNVEQIKTIADFTPNDRF--MSALPLFH--SFGLTV-GLFTPLLTG 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3729 GRAVL---------VPEavcrqpdafldLLAEYGVTVLNQTpSAF---YAlqSQAMRRELAlNVRAVVFGGEALEPSRLQ 3796
Cdd:PRK08043 433 AEVFLypsplhyriVPE-----------LVYDRNCTVLFGT-STFlgnYA--RFANPYDFA-RLRYVVAGAEKLQESTKQ 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3797 PWRERYpQAELVNMYGITETTVHVSFhrlsDEDLQSPTSRIGSALPDLAVHVLdaagqPVPlGVV--GELVVEGDGVAQG 3874
Cdd:PRK08043 498 LWQDKF-GLRILEGYGVTECAPVVSI----NVPMAAKPGTVGRILPGMDARLL-----SVP-GIEqgGRLQLKGPNIMNG 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3875 YW--QRP-ELTAERFVERGGQR---FYRSGDLGRYRADGSLEYRGRGDDQVKlrgyriepgeIAAKIASLPQVSDAAVTV 3948
Cdd:PRK08043 567 YLrvEKPgVLEVPTAENARGEMergWYDTGDIVRFDEQGFVQIQGRAKRFAK----------IAGEMVSLEMVEQLALGV 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3949 EGQGEgawlMAYAVAADGAE--------PDPQSLREALRAL-----LPDYMLPRLIQLLPALPLTANGKLD----RKALP 4011
Cdd:PRK08043 637 SPDKQ----HATAIKSDASKgealvlftTDSELTREKLQQYarehgVPELAVPRDIRYLKQLPLLGSGKPDfvtlKSMVD 712
|
....*.
gi 1246793773 4012 KPETQD 4017
Cdd:PRK08043 713 EPEQHD 718
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
643-1039 |
1.43e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 70.41 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 643 LAGFAPSvAIAVDELKLDGAGENGSGEN---AAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAE--ALALSADDR 717
Cdd:PRK05605 186 LTGPAPG-TVPWETLVDAAIGGDGSDVShprPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAwvPGLGDGPER 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 718 VL------HVAGLAVDTTLeqilaAWSRGACVVARPDelLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLA 791
Cdd:PRK05605 265 VLaalpmfHAYGLTLCLTL-----AVSIGGELVLLPA--PDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSG 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 792 LRCLVVGGDVLPVALAQRWFEL--GLdrrcaLINAYGPTEAT-------ISSHyhrvqaidaSRPVPLGQLLPGRIAAVL 862
Cdd:PRK05605 338 VRNAFSGAMALPVSTVELWEKLtgGL-----LVEGYGLTETSpiivgnpMSDD---------RRPGYVGVPFPDTEVRIV 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 863 DAH--GRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPlrlpsgeslRMYRSGDRVRLLDDGELQFLGRADFQVKLR 940
Cdd:PRK05605 404 DPEdpDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLD---------GWFRTGDVVVMEEDGFIRIVDRIKELIITG 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 941 GYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQRLVAWVECAGEDGFGQADLnqtdsdqteserwhRALC-ERLPAYMV 1018
Cdd:PRK05605 475 GFNVYPAEVEEVLREHPGVEdAAVVGLPREDGSEEVVAAVVLEPGAALDPEGL--------------RAYCrEHLTRYKV 540
|
410 420
....*....|....*....|.
gi 1246793773 1019 PTQFVALPRLPRNASGKIDRR 1039
Cdd:PRK05605 541 PRRFYHVDELPRDQLGKVRRR 561
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
677-1041 |
1.54e-11 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 70.48 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 677 AYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHV-AGLAVDTTLEQILAAWSRGACVVarpdeLLEPQR 755
Cdd:PRK08008 176 AEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVmPAFHIDCQCTAAMAAFSAGATFV-----LLEKYS 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 756 FLAFLSE----RAiTVTDLAPAYANELVRASVADDWRDLALRclvvggDV---LPVALAQRW-FELGLDRRcaLINAYGP 827
Cdd:PRK08008 251 ARAFWGQvckyRA-TITECIPMMIRTLMVQPPSANDRQHCLR------EVmfyLNLSDQEKDaFEERFGVR--LLTSYGM 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 828 TEaTIsshyhrVQAI-----DASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGI---GLAEGYRGDAAASERRF 899
Cdd:PRK08008 322 TE-TI------VGIIgdrpgDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYYLDPKATAKVL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 900 AplrlPSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVG------EGAAQ 973
Cdd:PRK08008 395 E----ADG----WLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIV--VVGikdsirDEAIK 464
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 974 RLVAWVEcaGEdgfgqadlnqtdsdqTESERWHRALCE-RLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK08008 465 AFVVLNE--GE---------------TLSEEEFFAFCEqNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
3638-4010 |
1.60e-11 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 69.30 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3638 DDPFTRAQLDAVEPGElpevPTEAP-AYLIYTSGSTGTPKGVVVTHRNverLFTAATQTGRFSFDEHDvW--SLFHSHAF 3714
Cdd:PRK07824 16 DERRAALLRDALRVGE----PIDDDvALVVATSGTTGTPKGAMLTAAA---LTASADATHDRLGGPGQ-WllALPAHHIA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3715 DFAVweLWGAWLYGGRAVLVPEAVCRQPDAFLDLLAE------YGVTVLNQTPSAFYALQSQAMRRELAlnvrAVVFGGE 3788
Cdd:PRK07824 88 GLQV--LVRSVIAGSEPVELDVSAGFDPTALPRAVAElgggrrYTSLVPMQLAKALDDPAATAALAELD----AVLVGGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3789 ALEPsrlqPWRERYPQA--ELVNMYGITETTVHVSFHrlsdedlqsptsriGSALPDLAVHVLDaagqpvplgvvGELVV 3866
Cdd:PRK07824 162 PAPA----PVLDAAAAAgiNVVRTYGMSETSGGCVYD--------------GVPLDGVRVRVED-----------GRIAL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3867 EGDGVAQGYWQRPELTAerFVERGgqrFYRSGDLGRYrADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAV 3946
Cdd:PRK07824 213 GGPTLAKGYRNPVDPDP--FAEPG---WFRTDDLGAL-DDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAV 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 3947 T-VEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK07824 287 FgLPDDRLGQRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
677-1041 |
1.77e-11 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 69.80 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 677 AYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLhvAGLAVDTTLEQILAAWSRGACVVARPDELLEPQRF 756
Cdd:cd05910 88 AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDL--ATFPLFALFGPALGLTSVIPDMDPTRPARADPQKL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 757 LAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRwFELGLDRRCALINAYGPTEA----TI 832
Cdd:cd05910 166 VGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAAR-LRKMLSDEAEILTPYGATEAlpvsSI 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 833 SSH---YHRVQAIDASRPVPLGQLLPG---RIAAVLDA------HGRIVPRGVCGELALGGIGLAEGYRGDAAASerRFA 900
Cdd:cd05910 245 GSRellATTTAATSGGAGTCVGRPIPGvrvRIIEIDDEpiaewdDTLELPRGEIGEITVTGPTVTPTYVNRPVAT--ALA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 901 PLRLPSGESLrmYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAAGVVGEGAAQRLVAWVE 980
Cdd:cd05910 323 KIDDNSEGFW--HRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPVLCVE 400
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 981 cagedgfgqaDLNQTDSDQTESERWHRALCERLPAYMVPTQFVALPRLP----RNAsgKIDRRAL 1041
Cdd:cd05910 401 ----------PLPGTITPRARLEQELRALAKDYPHTQRIGRFLIHPSFPvdirHNA--KIFREKL 453
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
2298-2524 |
2.02e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 70.18 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2298 VTGGEALTGALVQQVRALApTLRIVNHYGPTETTvgiltctvpeewPVEQGVPVGH--------PLAGNEAWVLDRFGLP 2369
Cdd:PRK05677 332 LSGGMALQLATAERWKEVT-GCAICEGYGMTETS------------PVVSVNPSQAiqvgtigiPVPSTLCKVIDDDGNE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2370 APVGVAGELYLGGGNLSLGYWQRAEQTAERFVAhplapDRLLyRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVE 2449
Cdd:PRK05677 399 LPLGEVGELCVKGPQVMKGYWQRPEATDEILDS-----DGWL-KTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELE 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2450 QVLAQLPGVEVAAVLALPGANG--------VLQLGACIqgSLEGVAEALAQRLPEYLCPsrwRAVE---SMPRLGNGKID 2518
Cdd:PRK05677 473 DVLAALPGVLQCAAIGVPDEKSgeaikvfvVVKPGETL--TKEQVMEHMRANLTGYKVP---KAVEfrdELPTTNVGKIL 547
|
....*.
gi 1246793773 2519 RQALAD 2524
Cdd:PRK05677 548 RRELRD 553
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
2063-2493 |
2.40e-11 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 69.31 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2063 TYAQLRAAAGRIAGALDAVGVQPGAHVALCL---PR-TFAQLAAMAAvwhrGAAWLPLDPQHP--DARQIavLDDSGARI 2136
Cdd:cd17640 7 TYKDLYQEILDFAAGLRSLGVKAGEKVALFAdnsPRwLIADQGIMAL----GAVDVVRGSDSSveELLYI--LNHSESVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2137 VIgwgaapawvpasvrwldaesvldvvsayeepprVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLG 2216
Cdd:cd17640 81 LV---------------------------------VENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2217 E-DASLATL----------STVAADLGFTALFGAllsgrrVRLLPAELAfdaqalaahlqAHPVDCLKIVP--------- 2276
Cdd:cd17640 128 PgDRFLSILpiwhsyersaEYFIFACGCSQAYTS------IRTLKDDLK-----------RVKPHYIVSVPrlweslysg 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2277 -----SHLAGLLAAAGGTAVLPRE--CLVTGGealtGALVQQVRAL--APTLRIVNHYGPTETTvGILTCTVPeeWPVEQ 2347
Cdd:cd17640 191 iqkqvSKSSPIKQFLFLFFLSGGIfkFGISGG----GALPPHVDTFfeAIGIEVLNGYGLTETS-PVVSARRL--KCNVR 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2348 GVpVGHPLAGNEAWVLDRFG-LPAPVGVAGELYLGGGNLSLGYWQRAEQTAErfvahPLAPDRLLyRSGDLARLDGEGRI 2426
Cdd:cd17640 264 GS-VGRPLPGTEIKIVDPEGnVVLPPGEKGIVWVRGPQVMKGYYKNPEATSK-----VLDSDGWF-NTGDLGWLTCGGEL 336
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2427 VYLGRG-DHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLalpganGVLQ--LGACIQGSLEGVAEALAQR 2493
Cdd:cd17640 337 VLTGRAkDTIVLSNGENVEPQPIEEALMRSPFIEQIMVV------GQDQkrLGALIVPNFEELEKWAKES 400
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
3662-4012 |
2.68e-11 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 69.38 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3662 PAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQTGRFSFDEHDVW----SLFHSHAFDFavweLWGAWLYGGRAVLVPEA 3737
Cdd:cd05915 155 ACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKDVVlpvvPMFHVNAWCL----PYAATLVGAKQVLPGPR 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3738 vcRQPDAFLDLLAEYGVTVLNQTPSAFYALQS--QAMRRELALNVRaVVFGGEAlePSRLQPWRERYPQAELVNMYGITE 3815
Cdd:cd05915 231 --LDPASLVELFDGEGVTFTAGVPTVWLALADylESTGHRLKTLRR-LVVGGSA--APRSLIARFERMGVEVRQGYGLTE 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3816 T----TVHV---SFHRLSDEDLQSPTSRIGSALPDLAVHVLDAAGQPVPLG--VVGELVVEGDGVAQGYWQRPELTaERF 3886
Cdd:cd05915 306 TspvvVQNFvksHLESLSEEEKLTLKAKTGLPIPLVRLRVADEEGRPVPKDgkALGEVQLKGPWITGGYYGNEEAT-RSA 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3887 VERGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT---VEGQGEGawlMAYAVA 3963
Cdd:cd05915 385 LTPDG--FFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVaipHPKWQER---PLAVVV 459
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3964 ADGAEPDPQSLREALRALLPDY-MLPRLIQLLPALPLTANGKLDRKALPK 4012
Cdd:cd05915 460 PRGEKPTPEELNEHLLKAGFAKwQLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
2175-2550 |
2.93e-11 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 69.66 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2175 DADTPAYLIYTSGSTGTPKGVVVSQ--------GNLANYVAGVLPVLdlgedasLATLSTVAADlGFTALFGALLSGRRV 2246
Cdd:PLN03102 184 DEHDPISLNYTSGTTADPKGVVISHrgaylstlSAIIGWEMGTCPVY-------LWTLPMFHCN-GWTFTWGTAARGGTS 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2247 RLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPRECLvTGGEALTGALVQQVRALAptLRIVNHYG 2326
Cdd:PLN03102 256 VCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVL-TGGSPPPAALVKKVQRLG--FQVMHAYG 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2327 PTETTVGILTCTVPEEW-----------PVEQGVPVghpLAGNEAWVLDRFGL---PAPVGVAGELYLGGGNLSLGYWQR 2392
Cdd:PLN03102 333 LTEATGPVLFCEWQDEWnrlpenqqmelKARQGVSI---LGLADVDVKNKETQesvPRDGKTMGEIVIKGSSIMKGYLKN 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2393 AEQTAERFVAHPLapdrllyRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALP----- 2467
Cdd:PLN03102 410 PKATSEAFKHGWL-------NTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPhptwg 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2468 -----------GANGVLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADL---LQQDDADS 2533
Cdd:PLN03102 483 etpcafvvlekGETTKEDRVDKLVTRERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIakgLVVEDEDN 562
|
410
....*....|....*..
gi 1246793773 2534 SAEAIDETPVNEVLREL 2550
Cdd:PLN03102 563 VIKKVHQRPVEHFSSRL 579
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
3655-4012 |
3.20e-11 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 69.76 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3655 PEVPTEAP-AYLIYTSGSTGTPKGVVVTHRNVerLFT-AATQTGRFSFDEHDVW--SLFHSHAFDFA----VWELWGAWL 3726
Cdd:PLN02387 244 PDLPSPNDiAVIMYTSGSTGLPKGVMMTHGNI--VATvAGVMTVVPKLGKNDVYlaYLPLAHILELAaesvMAAVGAAIG 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3727 YG-----------------GRA-VLVP--------------EAVCRQPDA-------FLDLLAEYGVTVLNQTPSAFYAL 3767
Cdd:PLN02387 322 YGspltltdtsnkikkgtkGDAsALKPtlmtavpaildrvrDGVRKKVDAkgglakkLFDIAYKRRLAAIEGSWFGAWGL 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3768 QS--------QAMRRELALNVRAVVFGGEALEPSRlqpwrERYPQ----AELVNMYGITETTVHVSFHRLSDedlqSPTS 3835
Cdd:PLN02387 402 EKllwdalvfKKIRAVLGGRIRFMLSGGAPLSGDT-----QRFINiclgAPIGQGYGLTETCAGATFSEWDD----TSVG 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3836 RIGSALPDLAVHVLD-------AAGQPVPLGvvgELVVEGDGVAQGYWQRPELTAERF-VERGGQRFYRSGDLGRYRADG 3907
Cdd:PLN02387 473 RVGPPLPCCYVKLVSweeggylISDKPMPRG---EIVIGGPSVTLGYFKNQEKTDEVYkVDERGMRWFYTGDIGQFHPDG 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3908 SLEYRGRGDDQVKLR-GYRIEPGEIAAKIASLPQVSD-------------AAVTVEGQGEGAWLMAYAVA-ADGAE--PD 3970
Cdd:PLN02387 550 CLEIIDRKKDIVKLQhGEYVSLGKVEAALSVSPYVDNimvhadpfhsycvALVVPSQQALEKWAKKAGIDySNFAElcEK 629
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 3971 PQSLREALRAL--------LPDYMLPRLIQLLPAL--P----LTANGKLDRKALPK 4012
Cdd:PLN02387 630 EEAVKEVQQSLskaakaarLEKFEIPAKIKLLPEPwtPesglVTAALKLKREQIRK 685
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
2050-2524 |
3.44e-11 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 69.24 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2050 AQAVAVEEGAA--SWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRT----FAQLAAMAAvwhrGAAWLPLDP----- 2118
Cdd:PLN02330 42 ADKVAFVEAVTgkAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVaeygIVALGIMAA----GGVFSGANPtales 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2119 ------QHPDARQIaVLDDSGARIVIGWGAaPAWV------PASVRW---LDAESVLDVVSAYEEPPRVDVDAdtpayLI 2183
Cdd:PLN02330 118 eikkqaEAAGAKLI-VTNDTNYGKVKGLGL-PVIVlgeekiEGAVNWkelLEAADRAGDTSDNEEILQTDLCA-----LP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2184 YTSGSTGTPKGVVVSQGNL-ANYVAGVLPVLD--LGEDASLATLSTVAAdLGFTALFGALL--SGRRVrllpAELAFDAQ 2258
Cdd:PLN02330 191 FSSGTTGISKGVMLTHRNLvANLCSSLFSVGPemIGQVVTLGLIPFFHI-YGITGICCATLrnKGKVV----VMSRFELR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2259 ALAAHLQAHPVDCLKIVP----SHLAGLLAAAGGTAVLPRECLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVGI 2334
Cdd:PLN02330 266 TFLNALITQEVSFAPIVPpiilNLVKNPIVEEFDLSKLKLQAIMTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHSCIT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2335 LTCTVPEEwpvEQGVP----VGHPLAGNEAWVLD-RFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAhplapDR 2409
Cdd:PLN02330 346 LTHGDPEK---GHGIAkknsVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDE-----DG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2410 LLYrSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI------QGSL 2483
Cdd:PLN02330 418 WLH-TGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVvinpkaKESE 496
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1246793773 2484 EGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALAD 2524
Cdd:PLN02330 497 EDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
2079-2467 |
3.54e-11 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 69.03 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2079 DAVGVQPGAHVALCLPRT----FAQLAAMAAvwhrGAAWLPLDPQHPDARQIAVLDDSGAR-IVIGWGAAPA-------- 2145
Cdd:cd05928 60 GACGLQRGDRVAVILPRVpewwLVNVACIRT----GLVFIPGTIQLTAKDILYRLQASKAKcIVTSDELAPEvdsvasec 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2146 -------WVPASVR--WLDAESVLDvvSAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLA-NYVAGVLPVLDL 2215
Cdd:cd05928 136 pslktklLVSEKSRdgWLNFKELLN--EASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGlGLKVNGRYWLDL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2216 GE-DASLATLSTVAADLGFTALFGALLSGRRV--RLLPAelaFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVL 2292
Cdd:cd05928 214 TAsDIMWNTSDTGWIKSAWSSLFEPWIQGACVfvHHLPR---FDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2293 P--RECLvTGGEALTGALVQQVRALApTLRIVNHYGPTETtvgILTCTVPEEWPVEQGvPVGHPLAGNEAWVLDRFGLPA 2370
Cdd:cd05928 291 PslQHCV-TGGEPLNPEVLEKWKAQT-GLDIYEGYGQTET---GLICANFKGMKIKPG-SMGKASPPYDVQIIDDNGNVL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2371 PVGVAGELYLGGG-----NLSLGYWQRAEQTAERFVAHplapdrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVEL 2445
Cdd:cd05928 365 PPGTEGDIGIRVKpirpfGLFSGYVDNPEKTAATIRGD-------FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGP 437
|
410 420
....*....|....*....|..
gi 1246793773 2446 GEVEQVLAQLPGVEVAAVLALP 2467
Cdd:cd05928 438 FEVESALIEHPAVVESAVVSSP 459
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
2061-2467 |
3.64e-11 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 69.15 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2061 SWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPL----DPQHPDARqiavLDDSGARI 2136
Cdd:PRK04319 73 KYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLfeafMEEAVRDR----LEDSEAKV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2137 VIGWGAAPAWVPA----SVRWL-----DAESVLDVVS-------AYEEPPRVDVDADTPAYLIYTSGSTGTPKGVV-VSQ 2199
Cdd:PRK04319 149 LITTPALLERKPAddlpSLKHVllvgeDVEEGPGTLDfnalmeqASDEFDIEWTDREDGAILHYTSGSTGKPKGVLhVHN 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2200 GNLANYVAGVLpVLDLGEDaslaTLSTVAADLGFTA-----LFGALLSGrrVRLLPAELAFDAQALAAHLQAHPVDCLKI 2274
Cdd:PRK04319 229 AMLQHYQTGKY-VLDLHED----DVYWCTADPGWVTgtsygIFAPWLNG--ATNVIDGGRFSPERWYRILEDYKVTVWYT 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2275 VPshlagllaaaggTAV---------------LPRECLVTG-GEALTG-ALVQQVRALAptLRIVNHYGPTETTvGILTC 2337
Cdd:PRK04319 302 AP------------TAIrmlmgagddlvkkydLSSLRHILSvGEPLNPeVVRWGMKVFG--LPIHDNWWMTETG-GIMIA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2338 TVPEEwPVEQGvPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSL--GYWQRAEQTAERFvahplAPDrlLYRSG 2415
Cdd:PRK04319 367 NYPAM-DIKPG-SMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGWPSMmrGIWNNPEKYESYF-----AGD--WYVSG 437
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 2416 DLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALP 2467
Cdd:PRK04319 438 DSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKP 489
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
531-1041 |
5.50e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 68.45 E-value: 5.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 531 PRTvgNVVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQA--RsVALCLPRGLDWYCLLLGAWRA 608
Cdd:PRK08314 8 PET--SLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQECGVRKgdR-VLLYMQNSPQFVIAYYAILRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 609 GLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQGLAGFAPS----------VAIAVDELKLDG----------------- 661
Cdd:PRK08314 85 NAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAvgnlrlrhviVAQYSDYLPAEPeiavpawlraepplqal 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 662 -------------AGENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVA 722
Cdd:PRK08314 165 apggvvawkealaAGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLavlplfHVT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 723 G--------LAVDTTLeQILAAWSRGAcvvARpdELLEPQRflaflseraITVTDLAPAYANELVrASVADDWRDLA-LR 793
Cdd:PRK08314 245 GmvhsmnapIYAGATV-VLMPRWDREA---AA--RLIERYR---------VTHWTNIPTMVVDFL-ASPGLAERDLSsLR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 794 CLVVGGDVLPVALAQRWFEL-GLDrrcaLINAYGPTEaTIS-SHyhrVQAIDASRPVPLGQLLPGRIAAVLD-AHGRIVP 870
Cdd:PRK08314 309 YIGGGGAAMPEAVAERLKELtGLD----YVEGYGLTE-TMAqTH---SNPPDRPKLQCLGIPTFGVDARVIDpETLEELP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 871 RGVCGELALGGIGLAEGYRGDAAASERRFAPLrlpsgESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIE 950
Cdd:PRK08314 381 PGEVGEIVVHGPQVFKGYWNRPEATAEAFIEI-----DGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 951 HCLGQLPQVRAAAagVVGEGAAQRlvawvecaGEDGFGQADLNQTDSDQTESER---WHRalcERLPAYMVP--TQFVAl 1025
Cdd:PRK08314 456 NLLYKHPAIQEAC--VIATPDPRR--------GETVKAVVVLRPEARGKTTEEEiiaWAR---EHMAAYKYPriVEFVD- 521
|
570
....*....|....*.
gi 1246793773 1026 pRLPRNASGKIDRRAL 1041
Cdd:PRK08314 522 -SLPKSGSGKILWRQL 536
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
2052-2524 |
5.85e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 68.56 E-value: 5.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDD 2131
Cdd:PRK13391 15 AVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVIGWGA-------APAWVPASVRWL--DAESVLDVVSAYEE-----PPRVDVDADTPAYLIYTSGSTGTPKGVVV 2197
Cdd:PRK13391 95 SGARALITSAAkldvaraLLKQCPGVRHRLvlDGDGELEGFVGYAEavaglPATPIADESLGTDMLYSSGTTGRPKGIKR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2198 SQGNLAnyVAGVLPVLDLGE-----DASLATLSTV----AADLGFTALFGALlsGRRVRLLPAelaFDAQALAAHLQAHP 2268
Cdd:PRK13391 175 PLPEQP--PDTPLPLTAFLQrlwgfRSDMVYLSPAplyhSAPQRAVMLVIRL--GGTVIVMEH---FDAEQYLALIEEYG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2269 VDCLKIVPSHLAGLLAaaggtavLPREclvtggealtgalvQQVRALAPTLRIVNH------------------------ 2324
Cdd:PRK13391 248 VTHTQLVPTMFSRMLK-------LPEE--------------VRDKYDLSSLEVAIHaaapcppqvkeqmidwwgpiihey 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2325 YGPTETtVGILTCTvPEEWPVEQGVpVGHPLAGnEAWVLDRFGLPAPVGVAGELYLGGGnLSLGYWQRAEQTAErfvAHp 2404
Cdd:PRK13391 307 YAATEG-LGFTACD-SEEWLAHPGT-VGRAMFG-DLHILDDDGAELPPGEPGTIWFEGG-RPFEYLNDPAKTAE---AR- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2405 lAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPG------ANGVLQLGAC 2478
Cdd:PRK13391 378 -HPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNedlgeeVKAVVQPVDG 456
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1246793773 2479 IQGSLEGVAEALA---QRLPEYLCPSRWRAVESMPRLGNGKIDRQALAD 2524
Cdd:PRK13391 457 VDPGPALAAELIAfcrQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRD 505
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
2052-2517 |
6.24e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 68.50 E-value: 6.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDD 2131
Cdd:PRK13390 15 AVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVIGWGA-----APAWVPASVRwLDAESVLDVVSAYEEP-----PRVdvdADTP--AYLIYTSGSTGTPKGV---- 2195
Cdd:PRK13390 95 SGARVLVASAAldglaAKVGADLPLR-LSFGGEIDGFGSFEAAlagagPRL---TEQPcgAVMLYSSGTTGFPKGIqpdl 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2196 ----VVSQGNLANYVAGVLpvLDLGEDASLATLSTV--AADLGFTALFGALlsGRRVRLLPAelaFDAQALAAHLQAHPV 2269
Cdd:PRK13390 171 pgrdVDAPGDPIVAIARAF--YDISESDIYYSSAPIyhAAPLRWCSMVHAL--GGTVVLAKR---FDAQATLGHVERYRI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2270 DCLKIVPSHLAGLLAAAGGTAV---LPRECLVTGGEALTGALVQQ--VRALAPTlrIVNHYGPTEttVGILTCTVPEEWP 2344
Cdd:PRK13390 244 TVTQMVPTMFVRLLKLDADVRTrydVSSLRAVIHAAAPCPVDVKHamIDWLGPI--VYEYYSSTE--AHGMTFIDSPDWL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2345 VEQGvPVGHPLAGNeAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAErfVAHPLAPdrLLYRSGDLARLDGEG 2424
Cdd:PRK13390 320 AHPG-SVGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAA--AQHPAHP--FWTTVGDLGSVDEDG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2425 RIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPG------ANGVLQLGACIQGSLEGVAEAL---AQRLP 2495
Cdd:PRK13390 394 YLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDpemgeqVKAVIQLVEGIRGSDELARELIdytRSRIA 473
|
490 500
....*....|....*....|..
gi 1246793773 2496 EYLCPSRWRAVESMPRLGNGKI 2517
Cdd:PRK13390 474 HYKAPRSVEFVDELPRTPTGKL 495
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
2636-3043 |
6.63e-11 |
|
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380462 [Multi-domain] Cd Length: 427 Bit Score: 67.79 E-value: 6.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2636 WFFEQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARFQRDAAGQWQQTLGDWQADRFAHREADAG---- 2711
Cdd:cd19539 12 WFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGPAPLEVRDLSDPdsdr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2712 -QREDLLAQWQAGLSFDGA---LLRVLALPDPQDgDTRVLFAAHHLLVDAVSWGIIVDDLQHAYAERRAGRS---PALAA 2784
Cdd:cd19539 92 eRRLEELLRERESRGFDLDeepPIRAVLGRFDPD-DHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGPAaplPELRQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2785 EACGFGAWQAalRQLSAATLDGWRSYWRAQAADAEAIALPWQD--SDNRYADTVHLHDRFERDWTERlLTQTARAYGNEP 2862
Cdd:cd19539 171 QYKEYAAWQR--EALAAPRAAELLDFWRRRLRGAEPTALPTDRprPAGFPYPGADLRFELDAELVAA-LRELAKRARSSL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2863 QEVLLtalalalrdggdAATLWVEMEGHGRDDLGAGL--------DLSRTVGWFTARYPLALHLPAGEDLGAALRSTkdr 2934
Cdd:cd19539 248 FMVLL------------AAYCVLLRRYTGQTDIVVGTpvagrnhpRFESTVGFFVNLLPLRVDVSDCATFRDLIARV--- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2935 MRAVPDrglgfgvlRYLHGEL------AELPVP---------QVCFNYLgQLRAGERDGWALCEEPDGGGRAGGNrrrhL 2999
Cdd:cd19539 313 RKALVD--------AQRHQELpfqqlvAELPVDrdagrhplvQIVFQVT-NAPAGELELAGGLSYTEGSDIPDGA----K 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1246793773 3000 LDVNAMLVD--GELRLDWAWPQDAASREAMQALSRRYLAVLRELIA 3043
Cdd:cd19539 380 FDLNLTVTEegTGLRGSLGYATSLFDEETIQGFLADYLQVLRQLLA 425
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
670-1041 |
8.77e-11 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 67.85 E-value: 8.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 670 NAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTT-LEQILAAWSRGACVVARpd 748
Cdd:PRK06087 183 TTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGfLHGVTAPFLIGARSVLL-- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 749 ELLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFELGLdrrcALINAYGPT 828
Cdd:PRK06087 261 DIFTPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKVARECQQRGI----KLLSVYGST 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 829 EatisSHYHRVQAIDasRPVPL-----GQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFaplr 903
Cdd:PRK06087 337 E----SSPHAVVNLD--DPLSRfmhtdGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARAL---- 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 904 lpsgESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVG---EGAAQRLVAWVE 980
Cdd:PRK06087 407 ----DEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDAC--VVAmpdERLGERSCAYVV 480
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 981 CAGEdgfgqaDLNQTDSDQTESerwhraLCE-RLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK06087 481 LKAP------HHSLTLEEVVAF------FSRkRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
675-1041 |
1.00e-10 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 67.94 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 675 QLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAE---ALALSADDRVLHVA----GLAVDTTLEQILAawsrGACVVARP 747
Cdd:cd17642 185 QVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDpifGNQIIPDTAILTVIpfhhGFGMFTTLGYLIC----GFRVVLMY 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 748 DelLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWrDLA-LRCLVVGGDVLPV----ALAQRwFELGLDRRcali 822
Cdd:cd17642 261 K--FEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKY-DLSnLHEIASGGAPLSKevgeAVAKR-FKLPGIRQ---- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 823 nAYGPTEATISShyhRVQAIDASRPVPLGQLLPGRIAAVLDAH-GRIVPRGVCGELALGGIGLAEGYRGDAAASErrfaP 901
Cdd:cd17642 333 -GYGLTETTSAI---LITPEGDDKPGAVGKVVPFFYAKVVDLDtGKTLGPNERGELCVKGPMIMKGYVNNPEATK----A 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 902 LRLPSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQRLVAWVE 980
Cdd:cd17642 405 LIDKDG----WLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFdAGVAGIPDEDAGELPAAVVV 480
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 981 CAGEDGFGQADLNQTDSDQTESERWHRAlcerlpaymvPTQFValPRLPRNASGKIDRRAL 1041
Cdd:cd17642 481 LEAGKTMTEKEVMDYVASQVSTAKRLRG----------GVKFV--DEVPKGLTGKIDRRKI 529
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
1142-1349 |
1.04e-10 |
|
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380459 [Multi-domain] Cd Length: 419 Bit Score: 67.09 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1142 LSPIQRWFFDSAPAQP--DRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPAIQAQD 1219
Cdd:cd19536 4 LSSLQEGMLFHSLLNPggSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQAQVPVTELD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1220 WRGAADLDSRVDAAFAR-MQEATPLAG-PLVALTHAHCDDGER--LLICAHHLIVDAVSWRLLLGELFDGLAALARGEAW 1295
Cdd:cd19536 84 LTPLEEQLDPLRAYKEEtKIRRFDLGRaPLVRAALVRKDERERflLVISDHHSILDGWSLYLLVKEILAVYNQLLEYKPL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 1296 TPSARgASYADYVeALREADDAQRFDAGFWRE-LAAQPMQALPQDRPVALADARQ 1349
Cdd:cd19536 164 SLPPA-QPYRDFV-AHERASIQQAASERYWREyLAGATLATLPALSEAVGGGPEQ 216
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
2307-2529 |
1.05e-10 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 67.33 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2307 ALVQQVRA----LAPTlrivnhYGPTETTVGILTCTvPEEWpveqgvpvghpLAGNeawvlDRFGLPAP-------VGVA 2375
Cdd:PRK07445 245 SLLEQARQlqlrLAPT------YGMTETASQIATLK-PDDF-----------LAGN-----NSSGQVLPhaqitipANQT 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2376 GELYLGGGNLSLGYWQRAEQTAERFVahplapdrllyrSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQL 2455
Cdd:PRK07445 302 GNITIQAQSLALGYYPQILDSQGIFE------------TDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILAT 369
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 2456 PGVEVAAVLALPGANGVLQLGACI-----QGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLLQQD 2529
Cdd:PRK07445 370 GLVQDVCVLGLPDPHWGEVVTAIYvpkdpSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQR 448
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
2171-2463 |
1.56e-10 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 67.39 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2171 RVDVDADTPAYLIYTSGSTGTPKGVVVSQGNL------ANYVAG------------VLPV-------------LDLGEDA 2219
Cdd:PRK08974 200 KPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMlanleqAKAAYGpllhpgkelvvtALPLyhifaltvncllfIELGGQN 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2220 SLAT----LSTVAADLG---FTA------LFGALLSGRRVRllpaELAFDAqalaahlqahpvdcLKIVpshlagllaaa 2286
Cdd:PRK08974 280 LLITnprdIPGFVKELKkypFTAitgvntLFNALLNNEEFQ----ELDFSS--------------LKLS----------- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2287 ggtavlpreclVTGGEALTGALVQQVRALAPTlRIVNHYGPTETTvGILTCTvPEEWPVEQGvPVGHPLAGNEAWVLDRF 2366
Cdd:PRK08974 331 -----------VGGGMAVQQAVAERWVKLTGQ-YLLEGYGLTECS-PLVSVN-PYDLDYYSG-SIGLPVPSTEIKLVDDD 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2367 GLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLApdrllyrSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELG 2446
Cdd:PRK08974 396 GNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVIKDGWLA-------TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPN 468
|
330
....*....|....*...
gi 1246793773 2447 EVEQVLAQLPGV-EVAAV 2463
Cdd:PRK08974 469 EIEDVVMLHPKVlEVAAV 486
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
735-975 |
1.58e-10 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 66.82 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 735 AAWSRGACVVARPDELLEPQRFLAFLSERAITVTDLAPAYANELVRASVADdwRDLALRCLVVGGDVL-PVALAQRWFEL 813
Cdd:cd05974 147 APWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLAS--FDVKLREVVGAGEPLnPEVIEQVRRAW 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 814 GLDRRcaliNAYGPTEATISSHYHRVQAIdasRPVPLGQLLPGRIAAVLDAHGRIVPRG-VCGEL-ALGGIGLAEGYRGD 891
Cdd:cd05974 225 GLTIR----DGYGQTETTALVGNSPGQPV---KAGSMGRPLPGYRVALLDPDGAPATEGeVALDLgDTRPVGLMKGYAGD 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 892 aaaserrfaPLRLPSGESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVraAAAGVVGEGA 971
Cdd:cd05974 298 ---------PDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAV--AEAAVVPSPD 366
|
....
gi 1246793773 972 AQRL 975
Cdd:cd05974 367 PVRL 370
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
2539-2610 |
1.85e-10 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 59.87 E-value: 1.85e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 2539 DETPVNEVLRELWQKLLG--REHIGAHDNFFA-LGGDSILSLQLVARARQA-GLALMPRQLYDHPTLAGLSAQVQA 2610
Cdd:COG0236 2 PREELEERLAEIIAEVLGvdPEEITPDDSFFEdLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADLADYLEE 77
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
601-1059 |
1.87e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 67.01 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 601 LLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTD---AQGLAGFAPSVAI------AVDELKLDGAGENGSGENA 671
Cdd:PRK07867 70 LLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTEsahAELLDGLDPGVRVinvdspAWADELAAHRDAEPPFRVA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 672 APNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGlavdttleqILAAWSRGACVVA 745
Cdd:PRK07867 150 DPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYvsmplfHSNA---------VMAGWAVALAAGA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 746 rpdELLEPQRFLA--FLSE-RAITVTdlapaYANELVRA--------SVADDwRDLALRcLVVGGDVLPVALAQrwFElg 814
Cdd:PRK07867 221 ---SIALRRKFSAsgFLPDvRRYGAT-----YANYVGKPlsyvlatpERPDD-ADNPLR-IVYGNEGAPGDIAR--FA-- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 815 ldRR--CALINAYGPTEATISshyhrVQAIDASRPVPLGQLLPG-RI----------AAVLDAHGRIVPRGVCGELA-LG 880
Cdd:PRK07867 287 --RRfgCVVVDGFGSTEGGVA-----ITRTPDTPPGALGPLPPGvAIvdpdtgtecpPAEDADGRLLNADEAIGELVnTA 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 881 GIGLAEGYRGDAAASERRfaplrlpsgesLR--MYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQ 958
Cdd:PRK07867 360 GPGGFEGYYNDPEADAER-----------MRggVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPD 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 959 VRAAAA-GVVGEGAAQRLVAWVECAGEDGFGQADLNQTDSDQTEserwhralcerLPAYMVPTQFVALPRLPRNASGKID 1037
Cdd:PRK07867 429 ATEVAVyAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLAAQPD-----------LGPKQWPSYVRVCAELPRTATFKVL 497
|
490 500
....*....|....*....|....*...
gi 1246793773 1038 RRALPA------PPVLAQAERTPPRTAE 1059
Cdd:PRK07867 498 KRQLSAegvdcaDPVWWIRRLTPSDYAA 525
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
2141-2523 |
1.91e-10 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 65.84 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2141 GAAPAWVPASVRWLD-AESVLDVVSAYEEpprvdVDADTpAYLIYTSGSTGTPKGVVVSQGNLA---------------- 2203
Cdd:PRK07824 4 GRAPALLPVPAQDERrAALLRDALRVGEP-----IDDDV-ALVVATSGTTGTPKGAMLTAAALTasadathdrlggpgqw 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2204 -----------------NYVAGVLPV-LDLGEDASLATLSTVAADLGftalfgallSGRR-VRLLPAEL--AFDaqalaa 2262
Cdd:PRK07824 78 llalpahhiaglqvlvrSVIAGSEPVeLDVSAGFDPTALPRAVAELG---------GGRRyTSLVPMQLakALD------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2263 hlqahpvdclkivpsHLAGLLAAAGGTAVLpreclvTGGEALTGALVQQVRALAptLRIVNHYGPTETTVGiltCtvpee 2342
Cdd:PRK07824 143 ---------------DPAATAALAELDAVL------VGGGPAPAPVLDAAAAAG--INVVRTYGMSETSGG---C----- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2343 wpVEQGVpvghPLAGNEAWVLDrfglpapvgvaGELYLGGGNLSLGYwqraeqtaERFVAHPLAPDRLLYRSGDLARLDg 2422
Cdd:PRK07824 192 --VYDGV----PLDGVRVRVED-----------GRIALGGPTLAKGY--------RNPVDPDPFAEPGWFRTDDLGALD- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2423 EGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQGS------LEGVAEALAQRLPE 2496
Cdd:PRK07824 246 DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDggpaptLEALRAHVARTLDR 325
|
410 420
....*....|....*....|....*..
gi 1246793773 2497 YLCPSRWRAVESMPRLGNGKIDRQALA 2523
Cdd:PRK07824 326 TAAPRELHVVDELPRRGIGKVDRRALV 352
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
673-1041 |
2.01e-10 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 65.96 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 673 PNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVdttleQILAAWSRGACVV-A 745
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLcglplfHVNGSVV-----TLLTPLASGAHVVlA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 746 RPDELLEPQRFLAF--LSE--RAITVTDLAPAYAnelVRASVADDwRDL-ALRCLVVGGDVLPVALAQRwFE--LGLdrr 818
Cdd:cd05944 76 GPAGYRNPGLFDNFwkLVEryRITSLSTVPTVYA---ALLQVPVN-ADIsSLRFAMSGAAPLPVELRAR-FEdaTGL--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 819 cALINAYGPTEATISSHyhRVQAIDASRPVPLGQLLP---GRIAaVLDAHGRIVPR---GVCGELALGGIGLAEGYRGDA 892
Cdd:cd05944 148 -PVVEGYGLTEATCLVA--VNPPDGPKRPGSVGLRLPyarVRIK-VLDGVGRLLRDcapDEVGEICVAGPGVFGGYLYTE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 893 AASERRFAPLRLpsgeslrmyRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVraAAAGVVGEGAA 972
Cdd:cd05944 224 GNKNAFVADGWL---------NTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAV--AFAGAVGQPDA 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 973 QrlvawvecAGEDGFGQADLNQ-TDSDQTESERWHRalcERLPAY-MVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05944 293 H--------AGELPVAYVQLKPgAVVEEEELLAWAR---DHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
2180-2532 |
2.61e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 66.60 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2180 AYLIYTSGSTGTPKGVVVSQGNL-ANYVAGVLPVLDL--GEDASLATLSTVAAdLGFTALFG-ALLSGRRVRLLPaelAF 2255
Cdd:PRK06710 209 ALLQYTGGTTGFPKGVMLTHKNLvSNTLMGVQWLYNCkeGEEVVLGVLPFFHV-YGMTAVMNlSIMQGYKMVLIP---KF 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2256 DAQALAAHLQAHPVDCLKIVPShlagLLAAAGGTAVLP-------RECLvtGGEALTGALVQQVRALAPTLRIVNHYGPT 2328
Cdd:PRK06710 285 DMKMVFEAIKKHKVTLFPGAPT----IYIALLNSPLLKeydissiRACI--SGSAPLPVEVQEKFETVTGGKLVEGYGLT 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2329 ETTVgiltcTVPEEWPVEQGVP--VGHPLAGNEAWVLD-RFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAerfvahPL 2405
Cdd:PRK06710 359 ESSP-----VTHSNFLWEKRVPgsIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQIMKGYWNKPEETA------AV 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2406 APDRLLYrSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPG--------ANGVLQLGA 2477
Cdd:PRK06710 428 LQDGWLH-TGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDpyrgetvkAFVVLKEGT 506
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 2478 -CIQGSLEGVAEalaQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLLQQDDAD 2532
Cdd:PRK06710 507 eCSEEELNQFAR---KYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEKRKNED 559
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
2352-2528 |
3.18e-10 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 66.17 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2352 GHPLAGN-EAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLapdrllYRSGDLARLDGEGRIVYLG 2430
Cdd:PRK10946 356 GRPMSPDdEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF------YCSGDLVSIDPDGYITVVG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2431 RGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGAngvlQLG----ACI--QGSLEGVA---EALAQRLPEYLCPS 2501
Cdd:PRK10946 430 REKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDE----LMGekscAFLvvKEPLKAVQlrrFLREQGIAEFKLPD 505
|
170 180
....*....|....*....|....*..
gi 1246793773 2502 RWRAVESMPRLGNGKIDRQALADLLQQ 2528
Cdd:PRK10946 506 RVECVDSLPLTAVGKVDKKQLRQWLAS 532
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1598-1828 |
4.22e-10 |
|
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380457 [Multi-domain] Cd Length: 428 Bit Score: 65.35 E-value: 4.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1598 FPLTPLQRgvLLESLRGDGADPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGLSvpHQIVLADAAAPWQT 1677
Cdd:cd19534 2 VPLTPIQR--WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGG--WQQRIRGDVEELFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1678 LDWSALDDAAQDAQLQRwLADDAAQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQG 1757
Cdd:cd19534 78 LEVVDLSSLAQAAAIEA-LAAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 1758 ATLRLPPAPGFQaylDWRERQ-------DLARQRGWWRERLSGYAGTAALPAPVAAAHhpvqREECERRLSAHDSERL 1828
Cdd:cd19534 157 EPIPLPSKTSFQ---TWAELLaeyaqspALLEELAYWRELPAADYWGLPKDPEQTYGD----ARTVSFTLDEEETEAL 227
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
3540-3946 |
6.38e-10 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 65.45 E-value: 6.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3540 AEDGELDYATLDRRSSQLA-TLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVC 3618
Cdd:cd05905 10 KEATTLTWGKLLSRAEKIAaVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3619 LSVSQRALAVELP------GTALCLDDP--------------FTRAQLDAVEPGELPEVPTEapAYLIYTSGSTGTPKGV 3678
Cdd:cd05905 90 VALTVEACLKGLPkkllksKTAAEIAKKkgwpkildfvkipkSKRSKLKKWGPHPPTRDGDT--AYIEYSFSSDGSLSGV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3679 VVTHRNVERLFTAATQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLyGGRAVLVPEA-VCRQPDAFLDLLAEYGVTVL 3757
Cdd:cd05905 168 AVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYS-GHHTILIPPElMKTNPLLWLQTLSQYKVRDA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3758 NQTPSAFYALQSQAMRRELALNVRAVVFGG------EALEP---SRLQPWRERY-------------------PQAELVN 3809
Cdd:cd05905 247 YVKLRTLHWCLKDLSSTLASLKNRDVNLSSlrmcmvPCENRpriSSCDSFLKLFqtlglspravstefgtrvnPFICWQG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3810 MYGITETTVHVSFHRLSdEDLQSPTSR----------IGSALPDLAVHVLDAAGQPvPLGV--VGELVVEGDGVAQGYWQ 3877
Cdd:cd05905 327 TSGPEPSRVYLDMRALR-HGVVRLDERdkpnslplqdSGKVLPGAQVAIVNPETKG-LCKDgeIGEIWVNSPANASGYFL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3878 RPELTAERFVER---------GGQRFYRSGDLGRYR---------ADGSLEYR-GRGDDQVKLRGYRIEPGEIAAKI-AS 3937
Cdd:cd05905 405 LDGETNDTFKVFpstrlstgiTNNSYARTGLLGFLRptkctdlnvEEHDLLFVvGSIDETLEVRGLRHHPSDIEATVmRV 484
|
....*....
gi 1246793773 3938 LPQVSDAAV 3946
Cdd:cd05905 485 HPYRGRCAV 493
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
615-1041 |
8.70e-10 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 64.69 E-value: 8.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 615 LDTEWPQARRAEVVAASGCDavltdaqglaGFAPSVAIAVDELKLDgAGENGSGENAAPNQLAYILYTSGSTGIPKGVEV 694
Cdd:PRK13295 149 LRPELPALRHVVVVGGDGAD----------SFEALLITPAWEQEPD-APAILARLRPGPDDVTQLIYTSGTTGEPKGVMH 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 695 GHAALAAHIDAAAEALALSADDRVL------HVAGLAVDTTLEQILaawsrGACVVARpdELLEPQRFLAFLSERAITVT 768
Cdd:PRK13295 218 TANTLMANIVPYAERLGLGADDVILmaspmaHQTGFMYGLMMPVML-----GATAVLQ--DIWDPARAAELIRTEGVTFT 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 769 DLAPAYANELVRAsVADDWRDLA-LRCLVVGGDVLPVALAQR-WFELGLdrrcALINAYGPTE---ATISSHYHRVQAID 843
Cdd:PRK13295 291 MASTPFLTDLTRA-VKESGRPVSsLRTFLCAGAPIPGALVERaRAALGA----KIVSAWGMTEngaVTLTKLDDPDERAS 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 844 ASRPVPlgqlLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYrgdaaaserrFAPLRLPSGESLRMYRSGDRVRLLD 923
Cdd:PRK13295 366 TTDGCP----LPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGY----------LKRPQLNGTDADGWFDTGDLARIDA 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 924 DGELQFLGRADfQVKLRG-YRIELEEIEHCLGQLPQVRAAAagVVG---EGAAQRLVAWVECAGEDGFGQADLnqtdsdq 999
Cdd:PRK13295 432 DGYIRISGRSK-DVIIRGgENIPVVEIEALLYRHPAIAQVA--IVAypdERLGERACAFVVPRPGQSLDFEEM------- 501
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1246793773 1000 tesERWHRAlcERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK13295 502 ---VEFLKA--QKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
785-1041 |
8.80e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 64.78 E-value: 8.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 785 DDWRDL---ALRCLVVGGDVLPVALAQRWFELgldRRCALINAYGPTEAtisSHYHRVQAIDASRPVPLGQLLPGRIAAV 861
Cdd:PRK05677 318 EAFRKLdfsALKLTLSGGMALQLATAERWKEV---TGCAICEGYGMTET---SPVVSVNPSQAIQVGTIGIPVPSTLCKV 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 862 LDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFaplrlpsgESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRG 941
Cdd:PRK05677 392 IDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEIL--------DSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSG 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 942 YRIELEEIEHCLGQLPQV-RAAAAGVVGEGAAQRLVAWVecagedgfgqadLNQTDSDQTESE--RWHRAlceRLPAYMV 1018
Cdd:PRK05677 464 FNVYPNELEDVLAALPGVlQCAAIGVPDEKSGEAIKVFV------------VVKPGETLTKEQvmEHMRA---NLTGYKV 528
|
250 260
....*....|....*....|...
gi 1246793773 1019 PTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK05677 529 PKAVEFRDELPTTNVGKILRREL 551
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
549-1041 |
9.56e-10 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 64.60 E-value: 9.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 549 PERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVV 628
Cdd:PRK03640 16 PDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 629 AASGCDAVLTDAQGLAGFAPSVAIAVDELkldgagENGSGENAAP------NQLAYILYTSGSTGIPKGVEVGHAALAAH 702
Cdd:PRK03640 96 DDAEVKCLITDDDFEAKLIPGISVKFAEL------MNGPKEEAEIqeefdlDEVATIMYTSGTTGKPKGVIQTYGNHWWS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 703 IDAAAEALALSADDRVL------HVAGLAVdtTLEQILaawsRGACVVARpdELLEPQRFLAFLSERAITVTDLAPAYAN 776
Cdd:PRK03640 170 AVGSALNLGLTEDDCWLaavpifHISGLSI--LMRSVI----YGMRVVLV--EKFDAEKINKLLQTGGVTIISVVSTMLQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 777 ELVrASVADDWRDLALRCLVVGGDVLPVALAQRWFELGLdrrcALINAYGPTE-----ATISSHYHRVQAIDASRPvplg 851
Cdd:PRK03640 242 RLL-ERLGEGTYPSSFRCMLLGGGPAPKPLLEQCKEKGI----PVYQSYGMTEtasqiVTLSPEDALTKLGSAGKP---- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 852 qLLPGRIAAVLDahGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAplrlpSGeslrMYRSGDRVRLLDDGELQFLG 931
Cdd:PRK03640 313 -LFPCELKIEKD--GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQ-----DG----WFKTGDIGYLDEEGFLYVLD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 932 RADFQVKLRGYRIELEEIEHCLGQLPQVraAAAGVVGEGAA---QRLVAWVECAGEdgFGQADLnqtdsdqteserwhRA 1008
Cdd:PRK03640 381 RRSDLIISGGENIYPAEIEEVLLSHPGV--AEAGVVGVPDDkwgQVPVAFVVKSGE--VTEEEL--------------RH 442
|
490 500 510
....*....|....*....|....*....|....
gi 1246793773 1009 LC-ERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK03640 443 FCeEKLAKYKVPKRFYFVEELPRNASGKLLRHEL 476
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
3779-4018 |
1.04e-09 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 64.25 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3779 NVRAVVFGGEALEPSRLQpwRERYPQAELVNMYGITETTvhvsfhrlsdedlqsptSRIGSALPDLAVHVLDAAGQPVP- 3857
Cdd:PRK07445 231 QFRTILLGGAPAWPSLLE--QARQLQLRLAPTYGMTETA-----------------SQIATLKPDDFLAGNNSSGQVLPh 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3858 ------LGVVGELVVEGDGVAQGYWqrPELTAErfverggQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEI 3931
Cdd:PRK07445 292 aqitipANQTGNITIQAQSLALGYY--PQILDS-------QGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEV 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3932 AAKIASLPQVSDaaVTVEGQGEGAW---LMAYAVAADGaEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRK 4008
Cdd:PRK07445 363 EAAILATGLVQD--VCVLGLPDPHWgevVTAIYVPKDP-SISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQ 439
|
250
....*....|
gi 1246793773 4009 ALPKPETQDR 4018
Cdd:PRK07445 440 QLQQIAVQRL 449
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
3654-4007 |
1.24e-09 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 64.40 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3654 LPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQtgRFSFDE-HDV---W-SLFHSHAFDFAVWELWGawlyG 3728
Cdd:PRK05851 146 LTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNA--RVGLDAaTDVgcsWlPLYHDMGLAFLLTAALA----G 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3729 GRAVLVPE-AVCRQPDAFLDLLAEYGVTvLNQTPSAFYALQSQAMRR--ELAL-NVRAVVFGGE------------ALEP 3792
Cdd:PRK05851 220 APLWLAPTtAFSASPFRWLSWLSDSRAT-LTAAPNFAYNLIGKYARRvsDVDLgALRVALNGGEpvdcdgferfatAMAP 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3793 SRLQPwrerypqAELVNMYGITETTVHVS---------FHRLSDEDLQSPT--SRIGSALPDLAVHVlDAAGQPVPLGV- 3860
Cdd:PRK05851 299 FGFDA-------GAAAPSYGLAESTCAVTvpvpgiglrVDEVTTDDGSGARrhAVLGNPIPGMEVRI-SPGDGAAGVAGr 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3861 -VGELVVEGDGVAQGYWQRPELTAerfverggQRFYRSGDLGrYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLP 3939
Cdd:PRK05851 371 eIGEIEIRGASMMSGYLGQAPIDP--------DDWFPTGDLG-YLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVR 441
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 3940 QVSDAAVTVEGQGEGAWLMAYAVAADGAEPDPQSLREAL--RALLPDYMLPRLIQLLP--ALPLTANGKLDR 4007
Cdd:PRK05851 442 GVREGAVVAVGTGEGSARPGLVIAAEFRGPDEAGARSEVvqRVASECGVVPSDVVFVApgSLPRTSSGKLRR 513
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
678-1038 |
1.95e-09 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 62.42 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 678 YILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVArpDELLEPQRFL 757
Cdd:cd17633 4 YIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIG--QRKFNPKSWI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 758 AFLSERAITVTDLAPAYANELVRASVAddwrDLALRCLVVGGDVLPVALAQ---RWFElgldrRCALINAYGPTEATISS 834
Cdd:cd17633 82 RKINQYNATVIYLVPTMLQALARTLEP----ESKIKSIFSSGQKLFESTKKklkNIFP-----KANLIEFYGTSELSFIT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 835 hYHRVQaiDASRPVPLGQLLPGRIAAVLDAHGRIVPR-GVCGELALGGIGLAEGYRGDAaaserrfaplrlpsgeslrMY 913
Cdd:cd17633 153 -YNFNQ--ESRPPNSVGRPFPNVEIEIRNADGGEIGKiFVKSEMVFSGYVRGGFSNPDG-------------------WM 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 914 RSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRaaAAGVVGEGAAqrlvawvecagedGFGQADLN 993
Cdd:cd17633 211 SVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIE--EAIVVGIPDA-------------RFGEIAVA 275
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1246793773 994 QTDSDQTESERWHRALCERLPAYMVPTQFVALPRLPRNASGKIDR 1038
Cdd:cd17633 276 LYSGDKLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1160-1370 |
1.95e-09 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380472 [Multi-domain] Cd Length: 430 Bit Score: 63.10 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1160 YHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPaPAIQAQDwrgAADLDSRVDAAFARMQE 1239
Cdd:cd20484 24 YNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKP-LSFQEED---ISSLKESEIIAYLREKA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1240 ATPLA---GPLVALTHAHCDDGER-LLICAHHLIVDAVSWRLLLGELFDGLAALARGEAWTPSARGASYADYVE----AL 1311
Cdd:cd20484 100 KEPFVlenGPLMRVHLFSRSEQEHfVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPTLASSPASYYDFVAweqdML 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 1312 READDAQRFdaGFWREL--AAQPMQALPQDRPVALAdarQSNVGrivQTLDAGLTADLLER 1370
Cdd:cd20484 180 AGAEGEEHR--AYWKQQlsGTLPILELPADRPRSSA---PSFEG---QTYTRRLPSELSNQ 232
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
533-1041 |
2.08e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 63.41 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 533 TVGnvvDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALcLPRGLDWYCLL-LGAWRAGLS 611
Cdd:PRK08316 12 TIG---DILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAA-LGHNSDAYALLwLACARAGAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 612 VIPLDTEWPQARRAEVVAASGCDAVLTDaqglAGFAPSVAIAVDELK-------------------LDGAGENGSGENAA 672
Cdd:PRK08316 88 HVPVNFMLTGEELAYILDHSGARAFLVD----PALAPTAEAALALLPvdtlilslvlggreapggwLDFADWAEAGSVAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 673 P------NQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGL----AVDTTLEQILAAWSRGAc 742
Cdd:PRK08316 164 PdveladDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLyhcaQLDVFLGPYLYVGATNV- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 743 VVARPDellePQRFLAFLSERAITVTDLAPAYANELVRASVADDwRDL-ALRCLVVGGDVLPVALAQRwfelgLDRR--- 818
Cdd:PRK08316 243 ILDAPD----PELILRTIEAERITSFFAPPTVWISLLRHPDFDT-RDLsSLRKGYYGASIMPVEVLKE-----LRERlpg 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 819 CALINAYGPTE----ATI-SSHYHRVQAIDASRPVPLGQllpgriAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAA 893
Cdd:PRK08316 313 LRFYNCYGQTEiaplATVlGPEEHLRRPGSAGRPVLNVE------TRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 894 ASERRFAplrlpSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVGEGAAQ 973
Cdd:PRK08316 387 KTAEAFR-----GG----WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVA--VIGLPDPK 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 974 rlvaWVEC--------AGEdgfgqadlnqtdsDQTESERWhrALC-ERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK08316 456 ----WIEAvtavvvpkAGA-------------TVTEDELI--AHCrARLAGFKVPKRVIFVDELPRNPSGKILKREL 513
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
2325-2531 |
2.21e-09 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 63.29 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2325 YGPTETTVGIlTCTVPEEwPVEQGV-PVGHPLAGNEAWVLDRF-GLPAPVGVAGELYLGGGNLSLGYWQRAEQTAErfva 2402
Cdd:PRK08315 348 YGMTETSPVS-TQTRTDD-PLEKRVtTVGRALPHLEVKIVDPEtGETVPRGEQGELCTRGYSVMKGYWNDPEKTAE---- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2403 hPLAPDRLLyRSGDLARLDGEG--RIVylGRgdhqVK---IRG----Y-RvelgEVEQVLAQLPGVEVAAVLALPGANGV 2472
Cdd:PRK08315 422 -AIDADGWM-HTGDLAVMDEEGyvNIV--GR----IKdmiIRGgeniYpR----EIEEFLYTHPKIQDVQVVGVPDEKYG 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 2473 LQLGACI------QGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKID----RQALADLLQQDDA 2531
Cdd:PRK08315 490 EEVCAWIilrpgaTLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQkfkmREMMIEELGLQAA 558
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
672-1036 |
2.29e-09 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 63.36 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 672 APNQLAYILYTSGSTGIPKGV-EVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQIL-AAWSRGACVV---AR 746
Cdd:cd17634 230 NAEDPLFILYTSGTTGKPKGVlHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLyGPLACGATTLlyeGV 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 747 PDELlEPQRFLAFLSERAITVTDLAPAYANELVRASvaDDW---RDLA-LRCLVVGGDVL-PVALAQRWFELGlDRRCAL 821
Cdd:cd17634 310 PNWP-TPARMWQVVDKHGVNILYTAPTAIRALMAAG--DDAiegTDRSsLRILGSVGEPInPEAYEWYWKKIG-KEKCPV 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 822 INAYGPTEA-----TISSHYHRVQAIDASRPVPlgqllpGRIAAVLDAHGRIVPRGVCGELALGgIGLAEGYRGDAAASE 896
Cdd:cd17634 386 VDTWWQTETggfmiTPLPGAIELKAGSATRPVF------GVQPAVVDNEGHPQPGGTEGNLVIT-DPWPGQTRTLFGDHE 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 897 RRFAP-LRLPSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQV-RAAAAGVVGEGAAQR 974
Cdd:cd17634 459 RFEQTyFSTFKG----MYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVaEAAVVGIPHAIKGQA 534
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 975 LVAWVEC-AGEdgfgqadlnqTDSDQTESERWHRaLCERLPAYMVPTQFVALPRLPRNASGKI 1036
Cdd:cd17634 535 PYAYVVLnHGV----------EPSPELYAELRNW-VRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1142-1337 |
2.44e-09 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380455 [Multi-domain] Cd Length: 421 Bit Score: 62.86 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1142 LSPIQR--WFFDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASF--ERADGQWRQQVAAPgPAPAIQA 1217
Cdd:cd19532 4 MSFGQSrfWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFftDPEDGEPMQGVLAS-SPLRLEH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1218 QDWRGAADldsrVDAAFARMQEAT--PLAGPLVALTHAHCDDGE-RLLICAHHLIVDAVSWRLLLGElfdgLAALARGEA 1294
Cdd:cd19532 83 VQISDEAE----VEEEFERLKNHVydLESGETMRIVLLSLSPTEhYLIFGYHHIAMDGVSFQIFLRD----LERAYNGQP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1246793773 1295 WTPSARgaSYADYVEALREADDAQRFDAG--FWRELAAQPMQALP 1337
Cdd:cd19532 155 LLPPPL--QYLDFAARQRQDYESGALDEDlaYWKSEFSTLPEPLP 197
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
1141-1347 |
2.45e-09 |
|
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380456 [Multi-domain] Cd Length: 419 Bit Score: 62.77 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1141 GLSPIQR--WFFDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPaIQAQ 1218
Cdd:cd19533 3 PLTSAQRgvWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVP-IRHI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1219 DWRGAADLDSrvdAAFARMQEAT----PLAG-PLVALTHAHCDDGERLL-ICAHHLIVDAVSWRLLLGELFDGLAALARG 1292
Cdd:cd19533 82 DLSGDPDPEG---AAQQWMQEDLrkplPLDNdPLFRHALFTLGDNRHFWyQRVHHIVMDGFSFALFGQRVAEIYTALLKG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 1293 EAWTPSARGaSYADYVEALREADDAQRF--DAGFWRELAAQPMQalpqdrPVALADA 1347
Cdd:cd19533 159 RPAPPAPFG-SFLDLVEEEQAYRQSERFerDRAFWTEQFEDLPE------PVSLARR 208
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
2413-2522 |
2.62e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 62.75 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2413 RSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVL----ALPGANGVLQLGACIQGSLEGVAE 2488
Cdd:PRK08308 294 FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYrgkdPVAGERVKAKVISHEEIDPVQLRE 373
|
90 100 110
....*....|....*....|....*....|....
gi 1246793773 2489 ALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:PRK08308 374 WCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
602-1038 |
3.50e-09 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 62.86 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 602 LLGAWRAG--LSVIP------LDTEWPQARrAEVVAASGCDAVLTDAQGLAGFAPSV-AIAVDELKLDG-AGENGSGENA 671
Cdd:PRK05851 71 IQGAWLAGaaVSILPgpvrgaDDGRWADAT-LTRFAGIGVRTVLSHGSHLERLRAVDsSVTVHDLATAAhTNRSASLTPP 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 672 APNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSAD-DRVLHVAGLAVDTTLEQILAAWSRGACVVARPDEL 750
Cdd:PRK05851 150 DSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAAtDVGCSWLPLYHDMGLAFLLTAALAGAPLWLAPTTA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 751 LE--PQRFLAFLSERAITVTDlAPAYANELV--RASVADDWRDLALRCLVVGGDVLPVALAQRWFE----LGLDRRcALI 822
Cdd:PRK05851 230 FSasPFRWLSWLSDSRATLTA-APNFAYNLIgkYARRVSDVDLGALRVALNGGEPVDCDGFERFATamapFGFDAG-AAA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 823 NAYGPTEAT---------ISSHYHRVQAIDAS---RPVPLGQLLPG---RIAAVlDAHGRIVPRGVcGELALGGIGLAEG 887
Cdd:PRK05851 308 PSYGLAESTcavtvpvpgIGLRVDEVTTDDGSgarRHAVLGNPIPGmevRISPG-DGAAGVAGREI-GEIEIRGASMMSG 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 888 YRGDAaaserrfaPLRlpSGEslrMYRSGDRVRLLDDGeLQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAAGVV 967
Cdd:PRK05851 386 YLGQA--------PID--PDD---WFPTGDLGYLVDGG-LVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAV 451
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 968 G--EGAA-QRLVAWVECAGedgfgqadlnqTDSDQTESERWHR--ALCERLPAYMVptqFVALPRLPRNASGKIDR 1038
Cdd:PRK05851 452 GtgEGSArPGLVIAAEFRG-----------PDEAGARSEVVQRvaSECGVVPSDVV---FVAPGSLPRTSSGKLRR 513
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
2051-2523 |
5.08e-09 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 62.33 E-value: 5.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVE--EGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCL---PRTFAQLAAMAAVwhrGAAWLPLDPQHPDA-- 2123
Cdd:PRK05857 29 EAIALRrcDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISdngPETYLSVLACAKL---GAIAVMADGNLPIAai 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2124 -RQIAVLDDSGARIVIGWGAAPAWVPASVRWLDAESVLDVVSAYEEPPRVDVD---------ADTPAYLIYTSGSTGTPK 2193
Cdd:PRK05857 106 eRFCQITDPAAALVAPGSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAAslagnadqgSEDPLAMIFTSGTTGEPK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2194 GVVvsqgnLANYVAGVLPvlDLGEDASLATLSTVAADLGFTAL----FGAL---LSGrrvrLLPAELAFDAQALAAHLQA 2266
Cdd:PRK05857 186 AVL-----LANRTFFAVP--DILQKEGLNWVTWVVGETTYSPLpathIGGLwwiLTC----LMHGGLCVTGGENTTSLLE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2267 HPVD------CLkiVPS--HLAGLLAAAGGTAVLPRECLVTGGEALTGALVQQVRALAptLRIVNHYGPTETTVGILTCT 2338
Cdd:PRK05857 255 ILTTnavattCL--VPTllSKLVSELKSANATVPSLRLVGYGGSRAIAADVRFIEATG--VRTAQVYGLSETGCTALCLP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2339 VPEE--WPVEQGVpVGHPLAGNEAWVLDRFG------LPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHplapdrl 2410
Cdd:PRK05857 331 TDDGsiVKIEAGA-VGRPYPGVDVYLAATDGigptapGAGPSASFGTLWIKSPANMLGYWNNPERTAEVLIDG------- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2411 LYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQGSLE---GVA 2487
Cdd:PRK05857 403 WVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAEldeSAA 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1246793773 2488 EALAQRL-------PEYLC-PSRWRAVESMPRLGNGKIDRQALA 2523
Cdd:PRK05857 483 RALKHTIaarfrreSEPMArPSTIVIVTDIPRTQSGKVMRASLA 526
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
3637-3942 |
7.15e-09 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 61.49 E-value: 7.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3637 LDD----PFTRAQ-LDAVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVE-------RLFTAATQTGrfsfdeHD 3704
Cdd:cd05913 50 LDDlrklPFTTKEdLRDNYPFGLFAVPREKVVRIHASSGTTGKPTVVGYTKNDLDvwaelvaRCLDAAGVTP------GD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3705 VWSLFHSHAFDFAVWEL-WGAWLYGgraVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSafYALQ--SQAMRREL---AL 3778
Cdd:cd05913 124 RVQNAYGYGLFTGGLGFhYGAERLG---ALVIPAGGGNTERQLQLIKDFGPTVLCCTPS--YALYlaEEAEEEGIdprEL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3779 NVRAVVFGGEA-LEPSRLQpwRERYPQAELVNMYGITE---------TTVHVSFHRLSDEdlqsptsrigsalpdLAVHV 3848
Cdd:cd05913 199 SLKVGIFGAEPwTEEMRKR--IERRLGIKAYDIYGLTEiigpgvafeCEEKDGLHIWEDH---------------FIPEI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3849 LD-AAGQPVPLGVVGELVVEgdgvaqgywqrpELTaerfVERGGQRFYRSGDLGRYRADGSLEYR---------GRGDDQ 3918
Cdd:cd05913 262 IDpETGEPVPPGEVGELVFT------------TLT----KEAMPLIRYRTRDITRLLPGPCPCGRthrridritGRSDDM 325
|
330 340
....*....|....*....|....
gi 1246793773 3919 VKLRGYRIEPGEIAAKIASLPQVS 3942
Cdd:cd05913 326 LIIRGVNVFPSQIEDVLLKIPGLG 349
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
2108-2522 |
8.84e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 61.33 E-value: 8.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2108 HRGAAWLPLDPQHPDARQIaVLDDSGARIVIGWGAAPA-W--VPASVRWLDAE-------SVLDVV--SAY-------EE 2168
Cdd:PRK07638 37 CKVANWLNEKESKNKTIAI-LLENRIEFLQLFAGAAMAgWtcVPLDIKWKQDElkerlaiSNADMIvtERYklndlpdEE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2169 PPRVDVD---------ADTPA----------YLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAA 2229
Cdd:PRK07638 116 GRVIEIDewkrmiekyLPTYApienvqnapfYMGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVH 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2230 DLgFtaLFGA---LLSGRRVRLLPAelaFDAQALAAHLQAHPVDCLKIVPShlaGLLAAAGGTAVLPRECLVTGGEALTG 2306
Cdd:PRK07638 196 SL-F--LYGAistLYVGQTVHLMRK---FIPNQVLDKLETENISVMYTVPT---MLESLYKENRVIENKMKIISSGAKWE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2307 AL-VQQVRALAPTLRIVNHYGPTEttVGILTCTVPEEwPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNL 2385
Cdd:PRK07638 267 AEaKEKIKNIFPYAKLYEFYGASE--LSFVTALVDEE-SERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2386 SLGYWQRAEQTAErfvahplAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLA 2465
Cdd:PRK07638 344 FMGYIIGGVLARE-------LNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIG 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 2466 LPGANGVLQLGACIQGS--LEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:PRK07638 417 VPDSYWGEKPVAIIKGSatKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
2170-2526 |
1.04e-08 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 61.40 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2170 PRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAgvlpvLDLGEDASL----ATLSTVAADLGFTALFG------A 2239
Cdd:PLN02574 191 PKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVE-----LFVRFEASQyeypGSDNVYLAALPMFHIYGlslfvvG 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2240 LLS-GRRVRLLPAelaFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPRECLV---TGGEALTGALVQQVRAL 2315
Cdd:PLN02574 266 LLSlGSTIVVMRR---FDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLKSLKqvsCGAAPLSGKFIQDFVQT 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2316 APTLRIVNHYGPTETT-VGILTCTVPEewpVEQGVPVGHpLAGN-EAWVLD-RFGLPAPVGVAGELYLGGGNLSLGYWQR 2392
Cdd:PLN02574 343 LPHVDFIQGYGMTESTaVGTRGFNTEK---LSKYSSVGL-LAPNmQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNN 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2393 AEQTAERFVAhplapDRLLyRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLA------- 2465
Cdd:PLN02574 419 PKATQSTIDK-----DGWL-RTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAvpdkecg 492
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 2466 -LPGANGVLQLGACIqgSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLL 2526
Cdd:PLN02574 493 eIPVAFVVRRQGSTL--SQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSL 552
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
2062-2497 |
1.68e-08 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 60.56 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2062 WTYAQLRAAAGRIAGALDAVGVQPGAHVALcLPRTFAQ-LAAMAAVWHRGAAWLPLDPQ-HPD-ARQIavLDDSGARIVI 2138
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIAL-ISKNCAEwFITDLAIWMAGHISVPLYPTlNPDtIRYV--LEHSESKALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2139 -----GWGAAPAWVPASV--RWLDAESVL-------DVVSAY----EEPPRvdvDADTPAYLIYTSGSTGTPKGVVVSQG 2200
Cdd:cd05932 84 vgkldDWKAMAPGVPEGLisISLPPPSAAncqyqwdDLIAQHppleERPTR---FPEQLATLIYTSGTTGQPKGVMLTFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2201 NLANYVAGVLPVLDLGEDASLATLSTVAADLGFTALF-GALLSGRRV--------------RLLPAeLAFDAQALAAHLQ 2265
Cdd:cd05932 161 SFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEgGSLYGGVLVafaesldtfvedvqRARPT-LFFSVPRLWTKFQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2266 AHPVDclKIVPSHLAGLLAAAGGTAVLPR---------ECLVTGGEA--LTGALVQQVRALAptLRIVNHYGPTEtTVGI 2334
Cdd:cd05932 240 QGVQD--KIPQQKLNLLLKIPVVNSLVKRkvlkglgldQCRLAGCGSapVPPALLEWYRSLG--LNILEAYGMTE-NFAY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2335 LTCTVPEEwpvEQGVPVGHPLAGNEAWVLDRfglpapvgvaGELYLGGGNLSLGYWQRAEQTAERFVAhplapDRLLyRS 2414
Cdd:cd05932 315 SHLNYPGR---DKIGTVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTA-----DGFL-RT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2415 GDLARLDGEGRIVYLGRGDHQVKI-RGYRVELGEVEQVLAQLPGVEVAAVLA--LPGANGVLQLGAciqgslEGVAEALA 2491
Cdd:cd05932 376 GDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVIGsgLPAPLALVVLSE------EARLRADA 449
|
....*.
gi 1246793773 2492 QRLPEY 2497
Cdd:cd05932 450 FARAEL 455
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
2173-2525 |
1.80e-08 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 60.60 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2173 DVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGE-DASLATLSTVAAdLGFT--ALFgALLSGrrvrlL 2249
Cdd:PRK06334 179 DKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEdDVMMSFLPPFHA-YGFNscTLF-PLLSG-----V 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2250 PAELAFDaqalaahlqahPVDCLKIVPSHLAGLLAAAGGTAVL----------PRECL------VTGGEALTGALVQQVR 2313
Cdd:PRK06334 252 PVVFAYN-----------PLYPKKIVEMIDEAKVTFLGSTPVFfdyilktakkQESCLpslrfvVIGGDAFKDSLYQEAL 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2314 ALAPTLRIVNHYGPTETTVGILTCTvpEEWPVEQGVpVGHPLAGNEAWVL-DRFGLPAPVGVAGELYLGGGNLSLGYWqr 2392
Cdd:PRK06334 321 KTFPHIQLRQGYGTTECSPVITINT--VNSPKHESC-VGMPIRGMDVLIVsEETKVPVSSGETGLVLTRGTSLFSGYL-- 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2393 AEQTAERFVAhpLAPDrLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLA------QLPGVEVAAVLAL 2466
Cdd:PRK06334 396 GEDFGQGFVE--LGGE-TWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMegfgqnAADHAGPLVVCGL 472
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2467 PGANGVLQLGACIQGSLEGVAEALAQ-RLPEYLCPSRWRAVESMPRLGNGKIDRQALADL 2525
Cdd:PRK06334 473 PGEKVRLCLFTTFPTSISEVNDILKNsKTSSILKISYHHQVESIPMLGTGKPDYCSLNAL 532
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
2321-2522 |
2.33e-08 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 60.16 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2321 IVNHYGPTEttVGILTCTVPEEWpveQGVP--VGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQ-RAEQTA 2397
Cdd:PRK13382 340 IYNNYNATE--AGMIATATPADL---RAAPdtAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSgSTKDFH 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2398 ERFVAhplapdrllyrSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGA 2477
Cdd:PRK13382 415 DGFMA-----------SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAA 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 2478 CI--QGSLEGVAEALAQ----RLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:PRK13382 484 FVvlKPGASATPETLKQhvrdNLANYKVPRDIVVLDELPRGATGKILRREL 534
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
1061-1118 |
2.46e-08 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 52.95 E-value: 2.46e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 1061 SALCEVWAEVLQC---EVGIHDSFFRLGGDSIRSLQVVARLRER-GYAVTPKLMYQYQSAAE 1118
Cdd:pfam00550 1 ERLRELLAEVLGVpaeEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
2173-2490 |
2.69e-08 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 59.92 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2173 DVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLD--LGEDASLATLSTVAADLGFTALFGALLSGRR----- 2245
Cdd:cd17639 84 DGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPelLGPDDRYLAYLPLAHIFELAAENVCLYRGGTigygs 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2246 VRLL----------------PAELA-----FDAQALAAHLQAHPVDCLK-----IVPSHLAGLLAAAGGTAVL------- 2292
Cdd:cd17639 164 PRTLtdkskrgckgdltefkPTLMVgvpaiWDTIRKGVLAKLNPMGGLKrtlfwTAYQSKLKALKEGPGTPLLdelvfkk 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2293 PREclVTGGealtgalvqQVRAL--------APTLR--------IVNHYGPTETtVGILTCTVPEEWpvEQGVpVGHPLA 2356
Cdd:cd17639 244 VRA--ALGG---------RLRYMlsggaplsADTQEflnivlcpVIQGYGLTET-CAGGTVQDPGDL--ETGR-VGPPLP 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2357 GNEAWVLD--RFG----LPAPvgvAGELYLGGGNLSLGYWQRAEQTAERFvahplAPDRLLyRSGDLARLDGEGRIVYLG 2430
Cdd:cd17639 309 CCEIKLVDweEGGystdKPPP---RGEILIRGPNVFKGYYKNPEKTKEAF-----DGDGWF-HTGDIGEFHPDGTLKIID 379
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 2431 RGDHQVKIR-GYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQGSLEGVAEAL 2490
Cdd:cd17639 380 RKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYADPDKSYPVAIVVPNEKHLTKLAEKH 440
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
3657-3941 |
2.97e-08 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 60.14 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3657 VPTEA--PAYLIYTSGSTGTPKGVV----------------VTHRNVERLFTAATQTGrfsfdehdvWSLFHSHafdfav 3718
Cdd:PTZ00237 249 VPVESshPLYILYTSGTTGNSKAVVrsngphlvglkyywrsIIEKDIPTVVFSHSSIG---------WVSFHGF------ 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3719 weLWGAWLYGGRAVLVPEAVCRQP---DAFLDLLAEYGVTVLNQTPSAFYAL-----QSQAMRRELAL-NVRAVVFGGEA 3789
Cdd:PTZ00237 314 --LYGSLSLGNTFVMFEGGIIKNKhieDDLWNTIEKHKVTHTLTLPKTIRYLiktdpEATIIRSKYDLsNLKEIWCGGEV 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3790 LEPSrLQPWRERYPQAELVNMYGITET--TVHVSFHRLSdedlqSPTSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVE 3867
Cdd:PTZ00237 392 IEES-IPEYIENKLKIKSSRGYGQTEIgiTYLYCYGHIN-----IPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFK 465
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 3868 ---GDGVAQGYWQRPELTAERFVERGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQV 3941
Cdd:PTZ00237 466 lpmPPSFATTFYKNDEKFKQLFSKFPG--YYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLV 540
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
2676-2810 |
3.48e-08 |
|
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380465 [Multi-domain] Cd Length: 423 Bit Score: 59.14 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2676 HPMLRARFQRDAAGQWQQ------TLGDWQADRfahREADAGQREDLLAQWQAG---LSFD---GALLRVLALPDPqDGD 2743
Cdd:cd19543 52 HPILRTSFVWEGLGEPLQvvlkdrKLPWRELDL---SHLSEAEQEAELEALAEEdreRGFDlarAPLMRLTLIRLG-DDR 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 2744 TRVLFAAHHLLVDAVSWGIIVDDLQHAYAERRAGRSPALAAEAcGFGAWQAAL-RQLSAATLDGWRSY 2810
Cdd:cd19543 128 YRLVWSFHHILLDGWSLPILLKELFAIYAALGEGQPPSLPPVR-PYRDYIAWLqRQDKEAAEAYWREY 194
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
2321-2463 |
3.65e-08 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 59.65 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2321 IVNHYGPTETTvGILTCTvPEEWPVEQGVpVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAErf 2400
Cdd:PRK07059 355 ITEGYGLSETS-PVATCN-PVDATEFSGT-IGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAK-- 429
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 2401 vahPLAPDRlLYRSGDLARLDGEG--RIVylGRGDHQVKIRGYRVELGEVEQVLAQLPGV-EVAAV 2463
Cdd:PRK07059 430 ---VMTADG-FFRTGDVGVMDERGytKIV--DRKKDMILVSGFNVYPNEIEEVVASHPGVlEVAAV 489
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
588-696 |
3.77e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 59.57 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTewPQA-----RRAEVVAASGCDAVLT------------DAQGLAGfAPSV 650
Cdd:PRK05850 62 AVILAPQGLEYIVAFLGALQAGLIAVPLSV--PQGgahdeRVSAVLRDTSPSVVLTtsavvddvteyvAPQPGQS-APPV 138
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1246793773 651 aIAVDELKLDGAGENGSGENAAPNqLAYILYTSGSTGIPKGVEVGH 696
Cdd:PRK05850 139 -IEVDLLDLDSPRGSDARPRDLPS-TAYLQYTSGSTRTPAGVMVSH 182
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
1599-1919 |
4.07e-08 |
|
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.
Pssm-ID: 380468 [Multi-domain] Cd Length: 440 Bit Score: 59.03 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1599 PLTPLQRGVLLESLRGDGADPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGLSVPHQIVLADAAAPWQTL 1678
Cdd:cd19546 6 PATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRILDADAARPELPV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1679 dwsaldDAAQDAQLQRWLADDAAQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQG- 1757
Cdd:cd19546 86 ------VPATEEELPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARREGr 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1758 ATLRLPPAPGFQAYLDW--------RERQDLA-RQRGWWRERLSGYAGTAALPAPVAAAHHPVQRE-ECERRLSAHDSER 1827
Cdd:cd19546 160 APERAPLPLQFADYALWerellageDDRDSLIgDQIAYWRDALAGAPDELELPTDRPRPVLPSRRAgAVPLRLDAEVHAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1828 LRAFCRERGCTLSDLIAMVWGLANARYGNHDDVVLGaTRSGRPPELAGVESMVGVFINTLPLRLRIDAGQPALDLLSALR 1907
Cdd:cd19546 240 LMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVG-TVLPRDDEEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVR 318
|
330
....*....|..
gi 1246793773 1908 SQSLEVAENEAV 1919
Cdd:cd19546 319 EAVREARRHQDV 330
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
2109-2524 |
4.73e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 58.92 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2109 RGAAwLPLDPQHPDArQIAVLDDSGARIVIGwgaapawVPASVRWLDAESVL--DVVSAY--EEPPRVDVDADTPAYLIY 2184
Cdd:PRK07867 89 RGAA-LARDIAHADC-QLVLTESAHAELLDG-------LDPGVRVINVDSPAwaDELAAHrdAEPPFRVADPDDLFMLIF 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2185 TSGSTGTPKGVVVSQGNLAnyVAGVLPVLDLG---EDASLATL-----STVAADLGFTALFGALLSGRR----VRLLPAE 2252
Cdd:PRK07867 160 TSGTSGDPKAVRCTHRKVA--SAGVMLAQRFGlgpDDVCYVSMplfhsNAVMAGWAVALAAGASIALRRkfsaSGFLPDV 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2253 LAFDAQALaahlqahpvdclkivpSHLAGLLAAAGGTAVLPREC-----LVTGGEALTGALVQQVRALAptLRIVNHYGP 2327
Cdd:PRK07867 238 RRYGATYA----------------NYVGKPLSYVLATPERPDDAdnplrIVYGNEGAPGDIARFARRFG--CVVVDGFGS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2328 TETTVGIL-TCTVPEE--WPVEQGVPVGHPLAGNE--AWVLDRFGLPAPVGVAGELY-LGGGNLSLGYWQRAEQTAERFV 2401
Cdd:PRK07867 300 TEGGVAITrTPDTPPGalGPLPPGVAIVDPDTGTEcpPAEDADGRLLNADEAIGELVnTAGPGGFEGYYNDPEADAERMR 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2402 AHplapdrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQg 2481
Cdd:PRK07867 380 GG-------VYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALV- 451
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 2482 sLEGVAEALAQRLPEYLC----------PSRWRAVESMPRLGNGKIDRQALAD 2524
Cdd:PRK07867 452 -LAPGAKFDPDAFAEFLAaqpdlgpkqwPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
672-1038 |
5.17e-08 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 59.04 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 672 APNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARPdell 751
Cdd:PLN02860 170 APDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLP---- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 752 epqRFLAFLSERAIT---VTDL--APAYANELV---RASVADDWRDlALRCLVVGGDVLPVALAQRWFELGldRRCALIN 823
Cdd:PLN02860 246 ---KFDAKAALQAIKqhnVTSMitVPAMMADLIsltRKSMTWKVFP-SVRKILNGGGSLSSRLLPDAKKLF--PNAKLFS 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 824 AYGPTEA--------------------------TISSHYHRVQAIDASRPVPLGQLlpgRIAAVLDAH-GRIVPRGVcge 876
Cdd:PLN02860 320 AYGMTEAcssltfmtlhdptlespkqtlqtvnqTKSSSVHQPQGVCVGKPAPHVEL---KIGLDESSRvGRILTRGP--- 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 877 lalggiGLAEGYRGD-AAASERRFAPLRLPSGEslrmyrsgdrVRLLDD-GELQFLGRADFQVKLRGYRIELEEIEHCLG 954
Cdd:PLN02860 394 ------HVMLGYWGQnSETASVLSNDGWLDTGD----------IGWIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLS 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 955 QLPQV-RAAAAGVVGEGAAQRLVAWVECagEDGFGQADlnqtdsDQTESERWHRALCE----------RLPAYMVPTQFV 1023
Cdd:PLN02860 458 QHPGVaSVVVVGVPDSRLTEMVVACVRL--RDGWIWSD------NEKENAKKNLTLSSetlrhhcrekNLSRFKIPKLFV 529
|
410
....*....|....*.
gi 1246793773 1024 ALPR-LPRNASGKIDR 1038
Cdd:PLN02860 530 QWRKpFPLTTTGKIRR 545
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
667-1080 |
6.03e-08 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 58.81 E-value: 6.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 667 SGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVdttleQILAAWSRG 740
Cdd:PRK07529 206 SGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFcglplfHVNALLV-----TGLAPLARG 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 741 ACVV------ARPDELLepQRFLAFLSERAITVTDLAP-AYAnelVRASVADDWRDL-ALRCLVVGGDVLPVALAQRwFE 812
Cdd:PRK07529 281 AHVVlatpqgYRGPGVI--ANFWKIVERYRINFLSGVPtVYA---ALLQVPVDGHDIsSLRYALCGAAPLPVEVFRR-FE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 813 --LGLdrrcALINAYGPTEATISShyhRVQAID-ASRPVPLGQLLPG---RIaAVLDAHGRIV---PRGVCGELALGGIG 883
Cdd:PRK07529 355 aaTGV----RIVEGYGLTEATCVS---SVNPPDgERRIGSVGLRLPYqrvRV-VILDDAGRYLrdcAVDEVGVLCIAGPN 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 884 LAEGYRGDAAASERRFAPlrlpsgeslRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVraAA 963
Cdd:PRK07529 427 VFSGYLEAAHNKGLWLED---------GWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAV--AL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 964 AGVVGEG---AAQRLVAWVECAGEDGFGQADLNQTDSDQTeSERwhralcerlpaYMVPTQFVALPRLPRNASGKIDRRA 1040
Cdd:PRK07529 496 AAAVGRPdahAGELPVAYVQLKPGASATEAELLAFARDHI-AER-----------AAVPKHVRILDALPKTAVGKIFKPA 563
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1246793773 1041 LpappvlaqaERTPPRTAEESALCEVWAEVLQCEVGIHDS 1080
Cdd:PRK07529 564 L---------RRDAIRRVLRAALRDAGVEAEVVDVVEDGR 594
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
668-1041 |
6.14e-08 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 59.17 E-value: 6.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 668 GENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVDTTLEQILaawsrGA 741
Cdd:PRK08633 776 GPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILsslpffHSFGLTVTLWLPLLE-----GI 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 742 CVVARPDELlepqrflaflseRAITVTDLAPAYanelvRASV-----------ADDWR----DLA-LRCLVVGGDVLPVA 805
Cdd:PRK08633 851 KVVYHPDPT------------DALGIAKLVAKH-----RATIllgtptflrlyLRNKKlhplMFAsLRLVVAGAEKLKPE 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 806 LAQRwFELGLDRRcaLINAYGPTE----ATISSHYHRVQAID---ASRPVPLGQLLPGRIAAVLDAH-GRIVPRGVCGEL 877
Cdd:PRK08633 914 VADA-FEEKFGIR--ILEGYGATEtspvASVNLPDVLAADFKrqtGSKEGSVGMPLPGVAVRIVDPEtFEELPPGEDGLI 990
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 878 ALGGIGLAEGYRGDAaasERRFAPLRLPSGesLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQL- 956
Cdd:PRK08633 991 LIGGPQVMKGYLGDP---EKTAEVIKDIDG--IGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKAl 1065
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 957 --PQVRAAAAGVVGEGAAQRLVAWVECAGEDGfgqadlnqtdsdqtesERWHRALCE-RLPAYMVPTQFVALPRLPRNAS 1033
Cdd:PRK08633 1066 ggEEVVFAVTAVPDEKKGEKLVVLHTCGAEDV----------------EELKRAIKEsGLPNLWKPSRYFKVEALPLLGS 1129
|
....*...
gi 1246793773 1034 GKIDRRAL 1041
Cdd:PRK08633 1130 GKLDLKGL 1137
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
588-1040 |
6.32e-08 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 58.98 E-value: 6.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 588 VALCLPRGLDWYCLLLGAWRAGLSVIPL-DTEWP-QARRAEVVAAsgcDA----VLTD---AQGLAGF--------APSV 650
Cdd:PRK12476 95 VAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPgHAERLDTALR---DAeptvVLTTtaaAEAVEGFlrnlprlrRPRV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 651 aIAVDELKlDGAGENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSadDRVLHVAG---LAVD 727
Cdd:PRK12476 172 -IAIDAIP-DSAGESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLL--DRNTHGVSwlpLYHD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 728 TTLEQI-LAAWSRGACVVARPDELL-EPQRFLAFLSE--RAITVTDLAPAYANELVRA-SVADDWRDLALR--CLVVGGD 800
Cdd:PRK12476 248 MGLSMIgFPAVYGGHSTLMSPTAFVrRPQRWIKALSEgsRTGRVVTAAPNFAYEWAAQrGLPAEGDDIDLSnvVLIIGSE 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 801 vlPVALAQ-RWFE-----LGLdRRCALINAYGPTEATIS------------SHYHRVQ------------AIDASRPVPL 850
Cdd:PRK12476 328 --PVSIDAvTTFNkafapYGL-PRTAFKPSYGIAEATLFvatiapdaepsvVYLDREQlgagravrvaadAPNAVAHVSC 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 851 GQLLPGRIAAVLDAH-GRIVPRGVCGELALGGIGLAEGYRGDAAASERRF-APL--RLPSG-------ESLRMYRSGDRV 919
Cdd:PRK12476 405 GQVARSQWAVIVDPDtGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFgAKLqsRLAEGshadgaaDDGTWLRTGDLG 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 920 RLLdDGELQFLGRADFQVKLRGYRIELEEIEHCLGQL-PQVRA---AAAGVVGEGaAQRLVAWVECAGedGFGQADlnqt 995
Cdd:PRK12476 485 VYL-DGELYITGRIADLIVIDGRNHYPQDIEATVAEAsPMVRRgyvTAFTVPAED-NERLVIVAERAA--GTSRAD---- 556
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1246793773 996 dsDQTESERWHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRA 1040
Cdd:PRK12476 557 --PAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRA 599
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1142-1365 |
7.74e-08 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380471 [Multi-domain] Cd Length: 430 Bit Score: 58.04 E-value: 7.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1142 LSPIQR--WFFDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAapgPAPAIQ--A 1217
Cdd:cd20483 4 MSTFQRrlWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVL---DDPSFHliV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1218 QDWRGAADLDSRVDaAFARMQEATPL---AGPLVALTHAHCDDGE-RLLICAHHLIVDAVSWRLLLGE---LFDGLaaLA 1290
Cdd:cd20483 81 IDLSEAADPEAALD-QLVRNLRRQELdieEGEVIRGWLVKLPDEEfALVLASHHIAWDRGSSKSIFEQftaLYDAL--RA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1291 RGEAWTPSARGASYADYV---EALREADDAQRfDAGFWREL---AAQPMQALP---QDRPValadARQSNVGRIVQTLDA 1361
Cdd:cd20483 158 GRDLATVPPPPVQYIDFTlwhNALLQSPLVQP-LLDFWKEKlegIPDASKLLPfakAERPP----VKDYERSTVEATLDK 232
|
....
gi 1246793773 1362 GLTA 1365
Cdd:cd20483 233 ELLA 236
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
2078-2467 |
7.95e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 58.47 E-value: 7.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2078 LDAVGVQPGAHVALclprtfaqLAAMA--------AVWHRGAAWLPLdpQHPDAR---------QIAVLDDSGARIVIGw 2140
Cdd:PRK07768 46 LAAAGVGPGDAVAV--------LAGAPveiaptaqGLWMRGASLTML--HQPTPRtdlavwaedTLRVIGMIGAKAVVV- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2141 gAAPAWVPASVRWLDAESVLDVVSAYEEPP--RVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGV--------- 2209
Cdd:PRK07768 115 -GEPFLAAAPVLEEKGIRVLTVADLLAADPidPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMfvaaefdve 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2210 -------LPVL-DLGEDASLATLSTVAAD---------LGFTALFGALLS-----------------GRRVRLLPAELAF 2255
Cdd:PRK07768 194 tdvmvswLPLFhDMGMVGFLTVPMYFGAElvkvtpmdfLRDPLLWAELISkyrgtmtaapnfayallARRLRRQAKPGAF 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2256 DaqalaahlqahpVDCLKIVpshlagllaaaggtavlpreclVTGGEALTGALVQQ-VRALAP-TLR---IVNHYGPTET 2330
Cdd:PRK07768 274 D------------LSSLRFA----------------------LNGAEPIDPADVEDlLDAGARfGLRpeaILPAYGMAEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2331 TV---------GILTCTV-------------PEEWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLG 2388
Cdd:PRK07768 320 TLavsfspcgaGLVVDEVdadllaalrravpATKGNTRRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPG 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 2389 YwqraeQTAERFVahPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALP 2467
Cdd:PRK07768 400 Y-----LTMDGFI--PAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVR 471
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
846-1043 |
8.45e-08 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 58.37 E-value: 8.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 846 RPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELAL--GGIGLAEGYRGDAAASERRFAPlrlpsgeslRMYRSGDRVRLLD 923
Cdd:PRK04319 374 KPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIkkGWPSMMRGIWNNPEKYESYFAG---------DWYVSGDSAYMDE 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 924 DGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVraAAAGVVG---EGAAQRLVAWVecAGEDGFgqadlNQTDSDQT 1000
Cdd:PRK04319 445 DGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAV--AEAGVIGkpdPVRGEIIKAFV--ALRPGY-----EPSEELKE 515
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1246793773 1001 ESERWHRalcERLPAYMVPTQFVALPRLPRNASGKIDRRALPA 1043
Cdd:PRK04319 516 EIRGFVK---KGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKA 555
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
2123-2431 |
1.38e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 57.75 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2123 ARQIAVLDDSGARIVIGWGAAPAwvPASVRWldAESVLDVVSAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNL 2202
Cdd:PRK12582 170 ARALAALDLLDVTVVHVTGPGEG--IASIAF--ADLAATPPTAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQRMM 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2203 ANYVAGVLPVLDLGEDASLATL-------STVAADLGFTALF--GALLSGRRVRLLPAELAfdaQALAAHLQAHPVDCLK 2273
Cdd:PRK12582 246 CANIAMQEQLRPREPDPPPPVSldwmpwnHTMGGNANFNGLLwgGGTLYIDDGKPLPGMFE---ETIRNLREISPTVYGN 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2274 iVPSHLAGLLAAAGGTAVLPR------ECLVTGGEALTGALVQQVRALAptLRIVNH-------YGPTETTvGILTCTvp 2340
Cdd:PRK12582 323 -VPAGYAMLAEAMEKDDALRRsffknlRLMAYGGATLSDDLYERMQALA--VRTTGHripfytgYGATETA-PTTTGT-- 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2341 eEWPVEQGVPVGHPLAGNEAWVldrfglpAPVGVAGELYLGGGNLSLGYWQRAEQTAERFvahplaPDRLLYRSGDLARL 2420
Cdd:PRK12582 397 -HWDTERVGLIGLPLPGVELKL-------APVGDKYEVRVKGPNVTPGYHKDPELTAAAF------DEEGFYRLGDAARF 462
|
330
....*....|....*
gi 1246793773 2421 ----DGEGRIVYLGR 2431
Cdd:PRK12582 463 vdpdDPEKGLIFDGR 477
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
2176-2531 |
1.42e-07 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 57.80 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2176 ADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDL-GEDASLATLSTVAAdLGFT-ALFGALLSGRRVRLLPAEL 2253
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFtPNDRFMSALPLFHS-FGLTvGLFTPLLTGAEVFLYPSPL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2254 AFdaqalaahlqahpvdclKIVPShlagllaaaggtAVLPRECLVTGGEA---------------------LTGA--LVQ 2310
Cdd:PRK08043 443 HY-----------------RIVPE------------LVYDRNCTVLFGTStflgnyarfanpydfarlryvVAGAekLQE 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2311 QVRALAPT---LRIVNHYGPTETT--VGIltcTVPEEWPVEQgvpVGHPLAGNEAWVLdrfglPAPvGVA--GELYLGGG 2383
Cdd:PRK08043 494 STKQLWQDkfgLRILEGYGVTECApvVSI---NVPMAAKPGT---VGRILPGMDARLL-----SVP-GIEqgGRLQLKGP 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2384 NLSLGYWqRAEQTAErfVAHPLAPD------RLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQL-P 2456
Cdd:PRK08043 562 NIMNGYL-RVEKPGV--LEVPTAENargemeRGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVsP 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2457 GVEVAAVLALPGANG---VL-----QLGaciQGSLEGVAEALAqrLPEYLCPSRWRAVESMPRLGNGKIDRQALADLLQQ 2528
Cdd:PRK08043 639 DKQHATAIKSDASKGealVLfttdsELT---REKLQQYAREHG--VPELAVPRDIRYLKQLPLLGSGKPDFVTLKSMVDE 713
|
...
gi 1246793773 2529 DDA 2531
Cdd:PRK08043 714 PEQ 716
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
2183-2467 |
1.62e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 57.24 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2183 IYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFTAL-----FGALLSGRRVrllpaelaFDA 2257
Cdd:PRK07788 213 ILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLtlamaLGSTVVLRRR--------FDP 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2258 QALAAHLQAHPVDCLKIVPSHLAGLLAAAGgtAVLPR------ECLVTGGEALTGALVQQV-RALAPTLriVNHYGPTEt 2330
Cdd:PRK07788 285 EATLEDIAKHKATALVVVPVMLSRILDLGP--EVLAKydtsslKIIFVSGSALSPELATRAlEAFGPVL--YNLYGSTE- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2331 tVGILTCTVPEEWPVEQGVpVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYwqraeqTAERfvaHPLAPDRL 2410
Cdd:PRK07788 360 -VAFATIATPEDLAEAPGT-VGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY------TDGR---DKQIIDGL 428
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 2411 LyRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALP 2467
Cdd:PRK07788 429 L-SSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVD 484
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
669-957 |
1.82e-07 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 56.98 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 669 ENAaPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGL--AVDTTLEQILAAWSrGAC---- 742
Cdd:cd17640 84 END-SDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIwhSYERSAEYFIFACG-CSQayts 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 743 VVARPDEL--LEPQRFLAF------LSERAITVTDLAPAYANELVRASVADDwrdlALRCLVVGGDVLPVALaQRWFE-L 813
Cdd:cd17640 162 IRTLKDDLkrVKPHYIVSVprlwesLYSGIQKQVSKSSPIKQFLFLFFLSGG----IFKFGISGGGALPPHV-DTFFEaI 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 814 GLDrrcaLINAYGPTEATISSHYHRVqaidaSRPV--PLGQLLPGRIAAVLDAHGR-IVPRGVCGELALGGIGLAEGYRG 890
Cdd:cd17640 237 GIE----VLNGYGLTETSPVVSARRL-----KCNVrgSVGRPLPGTEIKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYK 307
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 891 DAAASERRFAplrlPSGeslrMYRSGDRVRLLDDGELQFLGRA-DFQVKLRGYRIELEEIEHCLGQLP 957
Cdd:cd17640 308 NPEATSKVLD----SDG----WFNTGDLGWLTCGGELVLTGRAkDTIVLSNGENVEPQPIEEALMRSP 367
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
1055-1120 |
1.89e-07 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 51.01 E-value: 1.89e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 1055 PRTAEESALCEVWAEVLQC---EVGIHDSFFR-LGGDSIRSLQVVARLRER-GYAVTPKLMYQYQSAAELA 1120
Cdd:COG0236 2 PREELEERLAEIIAEVLGVdpeEITPDDSFFEdLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADLA 72
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
791-1041 |
2.45e-07 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 56.75 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 791 ALRCLVVGGDVLPVALAQRWFELgldRRCALINAYGPTEAT--ISSHYHRVQAidasRPVPLGQLLPGRIAAVLDAHGRI 868
Cdd:PRK12492 334 ALKLTNSGGTALVKATAERWEQL---TGCTIVEGYGLTETSpvASTNPYGELA----RLGTVGIPVPGTALKVIDDDGNE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 869 VPRGVCGELALGGIGLAEGYRGDAAASErrfaplrlpsgESLRM---YRSGDRVRLLDDGELQFLGRADFQVKLRGYRIE 945
Cdd:PRK12492 407 LPLGERGELCIKGPQVMKGYWQQPEATA-----------EALDAegwFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVY 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 946 LEEIEHCLGQLPQVRAAAA-GVVGEGAAQRLVAWVeCAGEDGFGQADLnqtdsdqteserwhRALC-ERLPAYMVPTQFV 1023
Cdd:PRK12492 476 PNEIEDVVMAHPKVANCAAiGVPDERSGEAVKLFV-VARDPGLSVEEL--------------KAYCkENFTGYKVPKHIV 540
|
250
....*....|....*...
gi 1246793773 1024 ALPRLPRNASGKIDRRAL 1041
Cdd:PRK12492 541 LRDSLPMTPVGKILRREL 558
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
875-1041 |
2.47e-07 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 56.21 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 875 GELALGGIGLAEGYRG----DAAASERRFAPlrlpsgeslrmyrsgDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIE 950
Cdd:PRK07824 208 GRIALGGPTLAKGYRNpvdpDPFAEPGWFRT---------------DDLGALDDGVLTVLGRADDAISTGGLTVLPQVVE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 951 HCLGQLPQVRAAAA-GVVGEGAAQRLVAWVECAGEDGFGQADLnqtdsdqteseRWHRAlcERLPAYMVPTQFVALPRLP 1029
Cdd:PRK07824 273 AALATHPAVADCAVfGLPDDRLGQRVVAAVVGDGGPAPTLEAL-----------RAHVA--RTLDRTAAPRELHVVDELP 339
|
170
....*....|..
gi 1246793773 1030 RNASGKIDRRAL 1041
Cdd:PRK07824 340 RRGIGKVDRRAL 351
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
2060-2207 |
2.56e-07 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 56.91 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2060 ASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRT--FAqLAAMAAVwHRGAAWL---PLDPQHPDARQIAVlddSGA 2134
Cdd:PLN02246 49 RVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCpeFV-LAFLGAS-RRGAVTTtanPFYTPAEIAKQAKA---SGA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2135 RIVIgwgAAPAWVPaSVRWLDAESVLDVV-----------------SAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVV 2197
Cdd:PLN02246 124 KLII---TQSCYVD-KLKGLAEDDGVTVVtiddppegclhfseltqADENELPEVEISPDDVVALPYSSGTTGLPKGVML 199
|
170
....*....|
gi 1246793773 2198 SQGNLANYVA 2207
Cdd:PLN02246 200 THKGLVTSVA 209
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
588-1041 |
2.70e-07 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 56.42 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAqglAGFAPSVAIAVDELKLDGAGEngs 667
Cdd:PRK09029 56 VALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEELLPSLTLDFALVLE---GENTFSALTSLHLQLVEGAHA--- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 668 gENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAvdttleqILAAW-SRG 740
Cdd:PRK09029 130 -VAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQDSWLlslplfHVSGQG-------IVWRWlYAG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 741 ACVVARPDELLEpqrflaflseRAITVTDLAPAYANELVRAsVADDWRDLALRCLVVGGDVLPVALAQRWFELGLdrRCA 820
Cdd:PRK09029 202 ATLVVRDKQPLE----------QALAGCTHASLVPTQLWRL-LDNRSEPLSLKAVLLGGAAIPVELTEQAEQQGI--RCW 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 821 LinAYGPTEA--TISshyhrVQAIDASRPVplGQLLPGRiaAVldahgrivpRGVCGELALGGIGLAEGYrgdaaaserr 898
Cdd:PRK09029 269 C--GYGLTEMasTVC-----AKRADGLAGV--GSPLPGR--EV---------KLVDGEIWLRGASLALGY---------- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 899 faplrlpsgeslrmYRSGDRVRLLDD--------------GELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAa 964
Cdd:PRK09029 319 --------------WRQGQLVPLVNDegwfatrdrgewqnGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVF- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 965 gVV-------GegaaQRLVAWVECAgedgfgqadlnqTDSDQTESERWhraLCERLPAYMVPTQFVALPRLPRNASGKID 1037
Cdd:PRK09029 384 -VVpvadaefG----QRPVAVVESD------------SEAAVVNLAEW---LQDKLARFQQPVAYYLLPPELKNGGIKIS 443
|
....
gi 1246793773 1038 RRAL 1041
Cdd:PRK09029 444 RQAL 447
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
101-290 |
3.24e-07 |
|
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380458 [Multi-domain] Cd Length: 423 Bit Score: 55.96 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 101 EQFEPGG---HAYhlaalFELRGE-LDAAALERAVHGLLIRHEVLdRCIQGEDS----VAAGGGAAVESADLRGRGQDEI 172
Cdd:cd19535 17 DDQELGGvgcHAY-----LEFDGEdLDPDRLERAWNKLIARHPML-RAVFLDDGtqqiLPEVPWYGITVHDLRGLSEEEA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 173 DALVEGFR--L--RPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSLGLLTQDLSRAYRVECglaaEPAP 248
Cdd:cd19535 91 EAALEELRerLshRVLDVERGPLFDIRLSLLPEG-----RTRLHLSIDLLVADALSLQILLRELAALYEDPG----EPLP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1246793773 249 PLPCQYGDY-ARWQRDTLDRLDASLRH---HVEALSGAPhlhELPL 290
Cdd:cd19535 162 PLELSFRDYlLAEQALRETAYERARAYwqeRLPTLPPAP---QLPL 204
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
3665-3944 |
3.70e-07 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 56.21 E-value: 3.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3665 LIYTSGSTGTPKGVVVTHRNVERLFTAATQTGRFSFD----EHDVWSLFHSHA----FDfavweLWGAWLYGGravlvpe 3736
Cdd:cd05933 155 LIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPAtvgqESVVSYLPLSHIaaqiLD-----IWLPIKVGG------- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3737 AVC-RQPDA----FLDLLAEYGVTVLNQTPSAF---------YALQSQAMRRELALNVRAVVF-------GGEaLEPSRL 3795
Cdd:cd05933 223 QVYfAQPDAlkgtLVKTLREVRPTAFMGVPRVWekiqekmkaVGAKSGTLKRKIASWAKGVGLetnlklmGGE-SPSPLF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3796 QPWRERY----------------------PQAE------------LVNMYGITETTvhvSFHRLSDEDLQSPTSrIGSAL 3841
Cdd:cd05933 302 YRLAKKLvfkkvrkalgldrcqkfftgaaPISRetlefflslnipIMELYGMSETS---GPHTISNPQAYRLLS-CGKAL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3842 P--DLAVHVLDAAGQpvplgvvGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQV 3919
Cdd:cd05933 378 PgcKTKIHNPDADGI-------GEICFWGRHVFMGYLNMEDKTEEAIDEDG---WLHSGDLGKLDEDGFLYITGRIKELI 447
|
330 340
....*....|....*....|....*..
gi 1246793773 3920 KLR-GYRIEPGEIAAKI-ASLPQVSDA 3944
Cdd:cd05933 448 ITAgGENVPPVPIEDAVkKELPIISNA 474
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
679-1043 |
3.92e-07 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 56.34 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 679 ILYTSGSTGIPKG-VEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVV---ARPDeLLEPQ 754
Cdd:cd05968 241 IIYTSGTTGKPKGtVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVlydGAPD-HPKAD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 755 RFLAFLSERAITVTDLAPAyaneLVRASVA--DDWRD----LALRclVVGGDVLPVAL-AQRW-FELGLDRRCALINAYG 826
Cdd:cd05968 320 RLWRMVEDHEITHLGLSPT----LIRALKPrgDAPVNahdlSSLR--VLGSTGEPWNPePWNWlFETVGKGRNPIINYSG 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 827 PTEatISSHYHRVQAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRGVcGELALGG--IGLAEGYRGDaaasERRFAPL-- 902
Cdd:cd05968 394 GTE--ISGGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARPEV-GELVLLApwPGMTRGFWRD----EDRYLETyw 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 903 -RLPSgeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQRLVAWVe 980
Cdd:cd05968 467 sRFDN-----VWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLeSAAIGVPHPVKGEAIVCFV- 540
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 981 cAGEDGFGQADLNQTDSDQTESERWHRALCerlpaymvPTQFVALPRLPRNASGKIDRRALPA 1043
Cdd:cd05968 541 -VLKPGVTPTEALAEELMERVADELGKPLS--------PERILFVKDLPKTRNAKVMRRVIRA 594
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
2098-2205 |
5.35e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 55.72 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2098 AQLAAMAAvwhrGAAWLPLDPQHP---DARQIAVLDDSGARIVIGWGAA-----------PAWVPASVRWLDAesvLDVV 2163
Cdd:PRK05850 75 AFLGALQA----GLIAVPLSVPQGgahDERVSAVLRDTSPSVVLTTSAVvddvteyvapqPGQSAPPVIEVDL---LDLD 147
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1246793773 2164 SAYEEPPRVDvDADTPAYLIYTSGSTGTPKGVVVSQGNL-ANY 2205
Cdd:PRK05850 148 SPRGSDARPR-DLPSTAYLQYTSGSTRTPAGVMVSHRNViANF 189
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
1142-1371 |
5.98e-07 |
|
Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380460 [Multi-domain] Cd Length: 395 Bit Score: 55.27 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1142 LSPIQRWFFdsapaqpdryHQY------------VALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAap 1209
Cdd:cd19537 4 LSPIEREWW----------HKYqlstgtssfnvsFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYS-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1210 gpAPAIQAQdWRGAADLDSRVDAAFARMQEaTPLagpLVALTHAHcddgerLLICAHHLIVDAVSWRLLLGElfdgLAAL 1289
Cdd:cd19537 72 --SSPPRVQ-RVDTLDVWKEINRPFDLERE-DPI---RVFISPDT------LLVVMSHIICDLTTLQLLLRE----VSAA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1290 ARGEAWTPSARgaSYADYVEALREADDAQRFdagFWRE-LAAQPMQALPqdRPVALADARQSnvgRIVQTLDAGLTADLL 1368
Cdd:cd19537 135 YNGKLLPPVRR--EYLDSTAWSRPASPEDLD---FWSEyLSGLPLLNLP--RRTSSKSYRGT---SRVFQLPGSLYRSLL 204
|
...
gi 1246793773 1369 ERA 1371
Cdd:cd19537 205 QFS 207
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
3533-4005 |
6.77e-07 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 55.57 E-value: 6.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3533 PARIAVSaEDG---ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDP----HAPA 3605
Cdd:PRK03584 101 PAIIFRG-EDGprrELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPdfgvQGVL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3606 ARRG------FILED----SGVCLSVSQ--RALAVELPG-TALC----LDDPFTRAQL-------DAVEPGELPE----- 3656
Cdd:PRK03584 180 DRFGqiepkvLIAVDgyryGGKAFDRRAkvAELRAALPSlEHVVvvpyLGPAAAAAALpgallweDFLAPAEAAElefep 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3657 VPTEAPAYLIYTSGSTGTPK-------GVVVTH----------RNVERLFTAATqTGrfsfdehdvwslfhshafdfavW 3719
Cdd:PRK03584 260 VPFDHPLWILYSSGTTGLPKcivhghgGILLEHlkelglhcdlGPGDRFFWYTT-CG----------------------W 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3720 ELWGaWLYGGRAV---LV--------PeavcrQPDAFLDLLAEYGVTVLNqTPSAFYALQSQA---MRRELAL-NVRAVV 3784
Cdd:PRK03584 317 MMWN-WLVSGLLVgatLVlydgspfyP-----DPNVLWDLAAEEGVTVFG-TSAKYLDACEKAglvPGETHDLsALRTIG 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3785 FGGEALEPSrLQPW--RERYPQAELVNMYGITettvhvsfhrlsdeDLQS------PTS-----RIGSALPDLAVHVLDA 3851
Cdd:PRK03584 390 STGSPLPPE-GFDWvyEHVKADVWLASISGGT--------------DICScfvggnPLLpvyrgEIQCRGLGMAVEAWDE 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3852 AGQPVpLGVVGELVVegdgvAQ-------GYWQRPeltaerfverGGQRfYRS------------GDLGRYRADGSLEYR 3912
Cdd:PRK03584 455 DGRPV-VGEVGELVC-----TKpfpsmplGFWNDP----------DGSR-YRDayfdtfpgvwrhGDWIEITEHGGVVIY 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3913 GRGDDQVKLRGYRIEPGEIAAKIASLPQVSDA-AVTVEGQGEGAWLMAYAVAADGAEPDP---QSLREALRALLPDYMLP 3988
Cdd:PRK03584 518 GRSDATLNRGGVRIGTAEIYRQVEALPEVLDSlVIGQEWPDGDVRMPLFVVLAEGVTLDDalrARIRTTIRTNLSPRHVP 597
|
570
....*....|....*..
gi 1246793773 3989 RLIQLLPALPLTANGKL 4005
Cdd:PRK03584 598 DKIIAVPDIPRTLSGKK 614
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
549-1036 |
6.81e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 55.40 E-value: 6.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 549 PERAALETAQG--RLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAE 626
Cdd:PRK13390 11 PDRPAVIVAETgeQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 627 VVAASGCDAVLTDAqGLAGFAPSVAiAVDELKL------DGAGENGSGENAAPNQL------AYILYTSGSTGIPKGVEv 694
Cdd:PRK13390 91 IVGDSGARVLVASA-ALDGLAAKVG-ADLPLRLsfggeiDGFGSFEAALAGAGPRLteqpcgAVMLYSSGTTGFPKGIQ- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 695 ghaalaahiDAAAEALALSADDRVLHVAGLAVDTTLEQIL--------AAWSR---------GACVVARPdelLEPQRFL 757
Cdd:PRK13390 168 ---------PDLPGRDVDAPGDPIVAIARAFYDISESDIYyssapiyhAAPLRwcsmvhalgGTVVLAKR---FDAQATL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 758 AFLSERAITVTDLAPAYANELVR--ASVADDWRDLALRCLVVGGDVLPValaqrwfelglDRRCALINAYGPT--EATIS 833
Cdd:PRK13390 236 GHVERYRITVTQMVPTMFVRLLKldADVRTRYDVSSLRAVIHAAAPCPV-----------DVKHAMIDWLGPIvyEYYSS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 834 SHYHRVQAIDA----SRPVPLGQLLPGRIaAVLDAHGRIVPRGVCGELALGGIGLAEGYRGD---AAASERRFAPLrlps 906
Cdd:PRK13390 305 TEAHGMTFIDSpdwlAHPGSVGRSVLGDL-HICDDDGNELPAGRIGTVYFERDRLPFRYLNDpekTAAAQHPAHPF---- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 907 geslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQRLVAWVE-CAGE 984
Cdd:PRK13390 380 -----WTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHdVAVIGVPDPEMGEQVKAVIQlVEGI 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 985 DgfGQADLNQTDSDQTESerwhralceRLPAYMVPTQFVALPRLPRNASGKI 1036
Cdd:PRK13390 455 R--GSDELARELIDYTRS---------RIAHYKAPRSVEFVDELPRTPTGKL 495
|
|
| TubC_N |
pfam18563 |
TubC N-terminal docking domain; This is the N-terminal docking domain found in TubC proteins ... |
21-68 |
7.60e-07 |
|
TubC N-terminal docking domain; This is the N-terminal docking domain found in TubC proteins from the tubulysin polyketide synthase and nonribosomal polypeptide synthetase (PKS-NRPS) system, which binds to C-terminal docking domain of TubB.
Pssm-ID: 436580 [Multi-domain] Cd Length: 52 Bit Score: 48.67 E-value: 7.60e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1246793773 21 LERARAAGVALHVEDGRLGYKATRAPLDAQLRADIVAQREALITLLSQ 68
Cdd:pfam18563 5 LAELYALGIKLWLEGGRLRFRAPKGVLTPELREKLKERKAEIIAFLQQ 52
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
740-1041 |
9.49e-07 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 55.00 E-value: 9.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 740 GACVVARPDEllEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRD-LA-LRCLVVGGDVLPVALAQRW-FELGld 816
Cdd:PRK10946 250 GGTVVLAPDP--SATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAqLAsLKLLQVGGARLSETLARRIpAELG-- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 817 rrCALINAYGPTEATISshYHRVQAID------ASRPVPlgqllPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRG 890
Cdd:PRK10946 326 --CQLQQVFGMAEGLVN--YTRLDDSDerifttQGRPMS-----PDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYK 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 891 DAAASERRFaplrlpsgESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagvvgeg 970
Cdd:PRK10946 397 SPQHNASAF--------DANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAA------- 461
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 971 aaqrLVAWVECA-GEDGFgqADLNQTDSDQTESERwhRALCERLPA-YMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK10946 462 ----LVSMEDELmGEKSC--AFLVVKEPLKAVQLR--RFLREQGIAeFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
2063-2207 |
9.62e-07 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 54.95 E-value: 9.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2063 TYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAwlpldpqH--------PDARQIAVLDdSGA 2134
Cdd:TIGR02188 90 TYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAI-------HsvvfggfsAEALADRIND-AGA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2135 RIVI----GW---------------------------------GAAPAWVPASVRWLdaESVLDVVSAYEEPPrvDVDAD 2177
Cdd:TIGR02188 162 KLVItadeGLrggkviplkaivdealekcpvsvehvlvvrrtgNPVVPWVEGRDVWW--HDLMAKASAYCEPE--PMDSE 237
|
170 180 190
....*....|....*....|....*....|
gi 1246793773 2178 TPAYLIYTSGSTGTPKGVVVSQGNLANYVA 2207
Cdd:TIGR02188 238 DPLFILYTSGSTGKPKGVLHTTGGYLLYAA 267
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
3162-3663 |
9.85e-07 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 55.26 E-value: 9.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3162 DWSGLEPAQARSRLS--------ELQAQQCEAGFDLAAPPLMRLALLRRSADEH--WLVWTRHHLIVDGWSSALLLDEVW 3231
Cdd:COG3321 848 DWSALYPGRGRRRVPlptypfqrEDAAAALLAAALAAALAAAAALGALLLAALAaaLAAALLALAAAAAAALALAAAALA 927
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3232 RLYAALRESRTPQLPAAPPFRDYLHWLRGQDEAAARAFWREQLTGLEPAALPEATEPAEGYASSTRRFDLAAASAWAQSH 3311
Cdd:COG3321 928 ALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAA 1007
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3312 GLTASSLLQGALALVLQRYYGRDDFALGITIAGRPPELAGVERMLGVFINSVPLRVTPAGEATPAPWLQALQQRNLDLRT 3391
Cdd:COG3321 1008 AALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALA 1087
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3392 HGYLPLAQIQRAGAADAVSPFDVLLVFENLPTESREERSGMRIEELDHRAHSNYPLMLTAIPDAGGLRIEAALDRSKLDG 3471
Cdd:COG3321 1088 AALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAAL 1167
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3472 WLVEQMLDDLDFVLQQVPALQRFDALPLLPSQTRSAAWTSRERYACTGNLVSRFAEIARRYPARIAVSAEDGELDYATLD 3551
Cdd:COG3321 1168 LAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAA 1247
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3552 RRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVCLSVSQRALAVELP 3631
Cdd:COG3321 1248 LAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLA 1327
|
490 500 510
....*....|....*....|....*....|..
gi 1246793773 3632 GTALCLDDPFTRAQLDAVEPGELPEVPTEAPA 3663
Cdd:COG3321 1328 AALAALAAAVAAALALAAAAAAAAAAAAAAAA 1359
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
3825-4085 |
1.18e-06 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 53.60 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3825 LSDEDLQSPTSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE-----RGGQRFYRSGD 3899
Cdd:COG3433 4 ATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARApfipvPYPAQPGRQAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3900 LGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEGAW---LMAYAVAADGAEPDPQSLRE 3976
Cdd:COG3433 84 DLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGvglLLIVGAVAALDGLAAAAALA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3977 ALRALLPDYMLPRLIQLLPALPLTANGKLDRKALPKPETQDRDEG------VLESASERRLAELWRQLLGGEL--PGRGA 4048
Cdd:COG3433 164 ALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAaspapaLETALTEEELRADVAELLGVDPeeIDPDD 243
|
250 260 270
....*....|....*....|....*....|....*..
gi 1246793773 4049 HFFARGGHSLLVVRLAEAIRAEFaIAVPLKSLFEQPR 4085
Cdd:COG3433 244 NLFDLGLDSIRLMQLVERWRKAG-LDVSFADLAEHPT 279
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
526-970 |
1.30e-06 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 54.72 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 526 KREPAPRTVGNVVDAIARAADEFPERAALETAQG----RLSYRELLTaadaraaalrrrlgaQARSVAlclpRGL----- 596
Cdd:COG1022 2 SEFSDVPPADTLPDLLRRRAARFPDRVALREKEDgiwqSLTWAEFAE---------------RVRALA----AGLlalgv 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 597 --------------DWYCLLLGAWRAGLSVIPLDtewPQARRAEV---VAASGCDAVLTDAQ------------------ 641
Cdd:COG1022 63 kpgdrvailsdnrpEWVIADLAILAAGAVTVPIY---PTSSAEEVayiLNDSGAKVLFVEDQeqldkllevrdelpslrh 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 642 -----GLAGFAPSVAIAVDELKLDGAGENGSGE------NAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEAL 710
Cdd:COG1022 140 ivvldPRGLRDDPRLLSLDELLALGREVADPAElearraAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 711 ALSADDRVL------HVAglavdttlEQIL--AAWSRGACV--VARPDELLE------PQRFLA---------------- 758
Cdd:COG1022 220 PLGPGDRTLsflplaHVF--------ERTVsyYALAAGATVafAESPDTLAEdlrevkPTFMLAvprvwekvyagiqaka 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 759 --------FLSERAItvtDLAPAYANEL-----------VRASVADD-----WRDL---ALRCLVVGGDVLPVALAqRWF 811
Cdd:COG1022 292 eeagglkrKLFRWAL---AVGRRYARARlagkspslllrLKHALADKlvfskLREAlggRLRFAVSGGAALGPELA-RFF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 812 E-LGLDrrcaLINAYGPTEAT--ISshyhrVQAIDASRPVPLGQLLPG---RIAAvldahgrivprgvCGELALGGIGLA 885
Cdd:COG1022 368 RaLGIP----VLEGYGLTETSpvIT-----VNRPGDNRIGTVGPPLPGvevKIAE-------------DGEILVRGPNVM 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 886 EGYRGDAAASERRFAP---LrlpsgeslrmyRSGDRVRLLDDGELQFLGRADFQVKLR-GYRIELEEIEHCLGQLPQVRA 961
Cdd:COG1022 426 KGYYKNPEATAEAFDAdgwL-----------HTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQ 494
|
....*....
gi 1246793773 962 AAagVVGEG 970
Cdd:COG1022 495 AV--VVGDG 501
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
2150-2466 |
1.34e-06 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 54.52 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2150 SVRWLDAESVL--DVVSAYEEPPRVD-VDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAgvlPVLDLGEDASLATLST 2226
Cdd:PLN02654 245 DTKWQEGRDVWwqDVVPNYPTKCEVEwVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTA---TTFKYAFDYKPTDVYW 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2227 VAADLGFTA-----LFGALLSGRRVrllpaeLAFDaqalAAHLQAHPVDCLKIVPSHlaglLAAAGGTA-VLPRECLVTG 2300
Cdd:PLN02654 322 CTADCGWITghsyvTYGPMLNGATV------LVFE----GAPNYPDSGRCWDIVDKY----KVTIFYTApTLVRSLMRDG 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2301 GEALTGALVQQVRALAPTLRIVNhygPTE-----TTVGILTCTVPEE-WPVEQGVPVGHPLAGneAW-------VLDRFG 2367
Cdd:PLN02654 388 DEYVTRHSRKSLRVLGSVGEPIN---PSAwrwffNVVGDSRCPISDTwWQTETGGFMITPLPG--AWpqkpgsaTFPFFG 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2368 L-PAPVGVAGELYLG--GGNLSL-GYWQRAEQTA----ERFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIR 2439
Cdd:PLN02654 463 VqPVIVDEKGKEIEGecSGYLCVkKSWPGAFRTLygdhERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVS 542
|
330 340
....*....|....*....|....*..
gi 1246793773 2440 GYRVELGEVEQVLAQLPGVEVAAVLAL 2466
Cdd:PLN02654 543 GHRIGTAEVESALVSHPQCAEAAVVGI 569
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
2176-2465 |
1.58e-06 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 54.03 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2176 ADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFTAL-FGALLSGRRVRLLPAELA 2254
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFhLAPLIAGMNQYLMPTRLF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2255 FdaqalaahlqAHPVDCLKIVPSHLAGLLAAA--GGTAVLPR--------------ECLVTGGEALTGALVQQ-VRALAP 2317
Cdd:cd05908 185 I----------RRPILWLKKASEHKATIVSSPnfGYKYFLKTlkpekandwdlssiRMILNGAEPIDYELCHEfLDHMSK 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2318 -TLR---IVNHYGPTETTVGI------------------LTCTVPEEWPVEQG------VPVGHPLAGNEAWVLDRFGLP 2369
Cdd:cd05908 255 yGLKrnaILPVYGLAEASVGAslpkaqspfktitlgrrhVTHGEPEPEVDKKDsecltfVEVGKPIDETDIRICDEDNKI 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2370 APVGVAGELYLGGGNLSLGYWQRAEQTAERFvahplAPDRLLyRSGDLArLDGEGRIVYLGRGDHQVKIRGYRVELGEVE 2449
Cdd:cd05908 335 LPDGYIGHIQIRGKNVTPGYYNNPEATAKVF-----TDDGWL-KTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIE 407
|
330
....*....|....*.
gi 1246793773 2450 QVLAQLPGVEVAAVLA 2465
Cdd:cd05908 408 RIAEELEGVELGRVVA 423
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
533-980 |
2.71e-06 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 53.36 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 533 TVGNVVDAIARAADEFPERAALETAQGR-----LSYRELLTAADARAAALRRRLGAQA------RSVALCLPrGLDWYCL 601
Cdd:PRK09274 4 SMANIARHLPRAAQERPDQLAVAVPGGRgadgkLAYDELSFAELDARSDAIAHGLNAAgigrgmRAVLMVTP-SLEFFAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 602 LLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTD-----AQGLAGFA-PSVAIAV-------------DELKLDGA 662
Cdd:PRK09274 83 TFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIGIpkahlARRLFGWGkPSVRRLVtvggrllwggttlATLLRDGA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 663 GENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDR--------VLHVAGLAVDTTLEQIL 734
Cdd:PRK09274 163 AAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIdlptfplfALFGPALGMTSVIPDMD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 735 AawSRGACVvarpdellEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFELg 814
Cdd:PRK09274 243 P--TRPATV--------DPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAM- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 815 LDRRCALINAYGPTEA----TISSHYH---RVQAIDASRPVPLGQLLPG---RIAAVLDA------HGRIVPRGVCGELA 878
Cdd:PRK09274 312 LPPDAEILTPYGATEAlpisSIESREIlfaTRAATDNGAGICVGRPVDGvevRIIAISDApipewdDALRLATGEIGEIV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 879 LGGIGLAEGYRGDAAASerRFAplRLPSGESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQ 958
Cdd:PRK09274 392 VAGPMVTRSYYNRPEAT--RLA--KIPDGQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPG 467
|
490 500
....*....|....*....|..
gi 1246793773 959 VRAAAAGVVGEGAAQRLVAWVE 980
Cdd:PRK09274 468 VKRSALVGVGVPGAQRPVLCVE 489
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
2636-2812 |
2.96e-06 |
|
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380454 [Multi-domain] Cd Length: 427 Bit Score: 53.13 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2636 WFFEQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARF--------QR-DAAGQWQQTLGDWQADRFAHR 2706
Cdd:cd19531 12 WFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFvevdgepvQViLPPLPLPLPVVDLSGLPEAER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2707 EADAgqrEDLLAQwQAGLSFD---GALLRVLALpdpQDGDTR--VLFAAHHLLVDAVSWGIIVDDLQHAYAERRAGRSPA 2781
Cdd:cd19531 92 EAEA---QRLARE-EARRPFDlarGPLLRATLL---RLGEDEhvLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRPSP 164
|
170 180 190
....*....|....*....|....*....|....
gi 1246793773 2782 LAAEACGFG---AWQAalRQLSAATLDGWRSYWR 2812
Cdd:cd19531 165 LPPLPIQYAdyaVWQR--EWLQGEVLERQLAYWR 196
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
2167-2420 |
3.32e-06 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 53.20 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2167 EEPPRVDVDA-------DTPAYLIYTSGSTGTPKGVVVSQGNLAN---YVAGVLPVLDlGEDASLATLSTVAADLGFTAL 2236
Cdd:cd05921 148 ATPPTAAVDAafaavgpDTVAKFLFTSGSTGLPKAVINTQRMLCAnqaMLEQTYPFFG-EEPPVLVDWLPWNHTFGGNHN 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2237 FGALLSGrrvrllPAELAFDAQALAAHLQAHPVDCLK--------IVPSHLAGLLAAAGGTAVLPR------ECLVTGGE 2302
Cdd:cd05921 227 FNLVLYN------GGTLYIDDGKPMPGGFEETLRNLReisptvyfNVPAGWEMLVAALEKDEALRRrffkrlKLMFYAGA 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2303 ALTGALVQQVRALA-----PTLRIVNHYGPTETTVGILTCTvpeeWPVEQGVPVGHPLAGNEAWVldrfglpAPVGVAGE 2377
Cdd:cd05921 301 GLSQDVWDRLQALAvatvgERIPMMAGLGATETAPTATFTH----WPTERSGLIGLPAPGTELKL-------VPSGGKYE 369
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1246793773 2378 LYLGGGNLSLGYWQRAEQTAERFvahplaPDRLLYRSGDLARL 2420
Cdd:cd05921 370 VRVKGPNVTPGYWRQPELTAQAF------DEEGFYCLGDAAKL 406
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
924-1043 |
3.88e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 52.73 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 924 DGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA-----GVVGEGAAQRLVAwvecagEDGFGQADLNQtdsd 998
Cdd:PRK08308 304 RGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVyrgkdPVAGERVKAKVIS------HEEIDPVQLRE---- 373
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1246793773 999 qteserWHRalcERLPAYMVPTQFVALPRLPRNASGKIDRRALPA 1043
Cdd:PRK08308 374 ------WCI---QHLAPYQVPHEIESVTEIPKNANGKVSRKLLEL 409
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
673-1038 |
4.04e-06 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 52.88 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 673 PNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLeqilaAWSRGACVVARPDELLE 752
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGL-----IAFHLAPLIAGMNQYLM 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 753 PQR--------FLAFLSERAITVTDlAPAYANELV----RASVADDWRDLALRCLVVGGDVLPVALAQRWFE----LGLd 816
Cdd:cd05908 180 PTRlfirrpilWLKKASEHKATIVS-SPNFGYKYFlktlKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDhmskYGL- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 817 RRCALINAYGPTEATIS-------------SHYHR-------VQAIDASRP-----VPLGQLLPGRIAAVLDAHGRIVPR 871
Cdd:cd05908 258 KRNAILPVYGLAEASVGaslpkaqspfktiTLGRRhvthgepEPEVDKKDSecltfVEVGKPIDETDIRICDEDNKILPD 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 872 GVCGELALGGIGLAEGYRGDAAASERRFAplrlPSGeslrMYRSGDrVRLLDDGELQFLGRADFQVKLRGYRIELEEIEH 951
Cdd:cd05908 338 GYIGHIQIRGKNVTPGYYNNPEATAKVFT----DDG----WLKTGD-LGFIRNGRLVITGREKDIIFVNGQNVYPHDIER 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 952 CLGQLPQV---RAAAAGVVGEGAAQ-RLVAWVECA-GEDGFgqADLNQ-TDSDQTESERWHraLCERLPaymvptqfvaL 1025
Cdd:cd05908 409 IAEELEGVelgRVVACGVNNSNTRNeEIFCFIEHRkSEDDF--YPLGKkIKKHLNKRGGWQ--INEVLP----------I 474
|
410
....*....|...
gi 1246793773 1026 PRLPRNASGKIDR 1038
Cdd:cd05908 475 RRIPKTTSGKVKR 487
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
2362-2518 |
4.37e-06 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 51.92 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2362 VLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHplapdrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGY 2441
Cdd:cd17636 176 ILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRGG-------WHHTNDLGRREPDGSLSFVGPKTRMIKSGAE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2442 RVELGEVEQVLAQLPGVEVAAVLALPG--------ANGVLQLGACIqgSLEGVAEALAQRLPEYLCPSRWRAVESMPRLG 2513
Cdd:cd17636 249 NIYPAEVERCLRQHPAVADAAVIGVPDprwaqsvkAIVVLKPGASV--TEAELIEHCRARIASYKKPKSVEFADALPRTA 326
|
....*
gi 1246793773 2514 NGKID 2518
Cdd:cd17636 327 GGADD 331
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
2098-2243 |
4.45e-06 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 52.84 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2098 AQLAAMAAvwHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGWGAAP----------------AWVPASVRWLDAESVLD 2161
Cdd:cd17632 130 AQLAPILA--ETEPRLLAVSAEHLDLAVEAVLEGGTPPRLVVFDHRPevdahraalesarerlAAVGIPVTTLTLIAVRG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2162 VVSAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLAT----LSTVAadlGFTALF 2237
Cdd:cd17632 208 RDLPPAPLFRPEPDDDPLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASITLnfmpMSHIA---GRISLY 284
|
....*.
gi 1246793773 2238 GALLSG 2243
Cdd:cd17632 285 GTLARG 290
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
2609-3082 |
4.84e-06 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 52.94 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2609 QASSPAPATIKPATEAEQSFGLTPIQHWFFEQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARFQRDAA 2688
Cdd:COG1020 1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2689 GQWQQTLGDWQA-------DRFAHREADAGQREDLLAQWQAGLSFDGALLRVLALPDPQDGDTRVLFAAHHLLVDAVSWG 2761
Cdd:COG1020 81 RPVQVIQPVVAAplpvvvlLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2762 IIVDDLQHAYAERRAGRSPALAAEACGFGAWQAALRQ-LSAATLDGWRSYWRAqAADAEAIALPWQDSDNRYADTVHLHD 2840
Cdd:COG1020 161 LLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREwLQGEELARQLAYWRQ-QLAGLPPLLELPTDRPRPAVQSYRGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2841 RFERDWTERL---LTQTARAYGnepqevlltalalalrdggdaATLWVEMEG---------HGRDDLGAGL--------D 2900
Cdd:COG1020 240 RVSFRLPAELtaaLRALARRHG---------------------VTLFMVLLAafalllarySGQDDVVVGTpvagrprpE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2901 LSRTVGWFTARYPLALHLPAGEDLGAALRSTKDRMR-AVPDRGLGFGVLR---YLHGELAELPVPQVCFNYLGQ-LRAGE 2975
Cdd:COG1020 299 LEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLaAYAHQDLPFERLVeelQPERDLSRNPLFQVMFVLQNApADELE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2976 RDGWALCEEPdgggrAGGNRRRHLLDVNAMLVDGELRLDWAWPQDAASREAMQALSRRYLAVLRELIacvqtAEPRPTLA 3055
Cdd:COG1020 379 LPGLTLEPLE-----LDSGTAKFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALA-----ADPDQPLG 448
|
490 500
....*....|....*....|....*..
gi 1246793773 3056 DLPLagLDNAPLDALLSQHPQTQDVYP 3082
Cdd:COG1020 449 DLPL--LTAAERQQLLAEWNATAAPYP 473
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
588-1041 |
5.36e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 52.21 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQGLAGFAPSVA---IAVDELKLDGAGE 664
Cdd:PRK08276 39 VAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVSAALADTAAELAAelpAGVPLLLVVAGPV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 665 NG--SGENAAPNQLAY----------ILYTSGSTGIPKGVEV------GHAALAAHIDAAAEALALSADDRVLHVAGLAV 726
Cdd:PRK08276 119 PGfrSYEEALAAQPDTpiadetagadMLYSSGTTGRPKGIKRplpgldPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYH 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 727 DTTLEQILAAWSRGACVVArpDELLEPQRFLAFLSERAITVTDLAPAYANEL------VRASVaddwrDLA-LRCLVVGG 799
Cdd:PRK08276 199 TAPLRFGMSALALGGTVVV--MEKFDAEEALALIERYRVTHSQLVPTMFVRMlklpeeVRARY-----DVSsLRVAIHAA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 800 DVLPVALAQrwfelgldrrcALINAYGPT--EATISSHYHRVQAIDA----SRPVPLGQLLPGRIaAVLDAHGRIVPRGV 873
Cdd:PRK08276 272 APCPVEVKR-----------AMIDWWGPIihEYYASSEGGGVTVITSedwlAHPGSVGKAVLGEV-RILDEDGNELPPGE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 874 CGELALGGIGLAEGYRGDAAASERrfapLRLPSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCL 953
Cdd:PRK08276 340 IGTVYFEMDGYPFEYHNDPEKTAA----ARNPHG----WVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 954 GQLPQVR-AAAAGVVGEGAAQRLVAWVECAgeDGFgqadlnqTDSDQTESE--RWHRalcERLPAYMVPTQFVALPRLPR 1030
Cdd:PRK08276 412 VTHPKVAdVAVFGVPDEEMGERVKAVVQPA--DGA-------DAGDALAAEliAWLR---GRLAHYKCPRSIDFEDELPR 479
|
490
....*....|.
gi 1246793773 1031 NASGKIDRRAL 1041
Cdd:PRK08276 480 TPTGKLYKRRL 490
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
526-1023 |
5.58e-06 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 52.57 E-value: 5.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 526 KREPAPRTVGnvvDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGA 605
Cdd:PRK08279 31 ITPDSKRSLG---DVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 606 WRAGLSVIPLDTewpQARRA------------EVVAASGCDAVLTDAQGLAGFAPSVAIAVDELK--------LDGAGEN 665
Cdd:PRK08279 108 AKLGAVVALLNT---QQRGAvlahslnlvdakHLIVGEELVEAFEEARADLARPPRLWVAGGDTLddpegyedLAAAAAG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 666 GSGENAA------PNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVdtTLEQI 733
Cdd:PRK08279 185 APTTNPAsrsgvtAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYcclplyHNTGGTV--AWSSV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 734 LAAwsrGACVVARPdellepqRFLA--FLSE-RAITVTdlAPAYANELVR----ASVADDWRDLALRClVVG----GDVL 802
Cdd:PRK08279 263 LAA---GATLALRR-------KFSAsrFWDDvRRYRAT--AFQYIGELCRyllnQPPKPTDRDHRLRL-MIGnglrPDIW 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 803 PvALAQRWfelGLDRRCALinaYGPTEATIS--SHYHRVQAIdasrpvplgqllpGRIAAVLDAHGRIV----------- 869
Cdd:PRK08279 330 D-EFQQRF---GIPRILEF---YAASEGNVGfiNVFNFDGTV-------------GRVPLWLAHPYAIVkydvdtgepvr 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 870 -PRGVCGELALGGIGLA----------EGYRgDAAASERR-----FAPlrlpsGEslRMYRSGDRVRLLDDGELQFLGRA 933
Cdd:PRK08279 390 dADGRCIKVKPGEVGLLigritdrgpfDGYT-DPEASEKKilrdvFKK-----GD--AWFNTGDLMRDDGFGHAQFVDRL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 934 dfqvklrG--YRIELE-----EIEHCLGQLPQVraAAAGVVGegaaqrlvawVECAGEDG-FGQADLNQTDSDQTESERW 1005
Cdd:PRK08279 462 -------GdtFRWKGEnvattEVENALSGFPGV--EEAVVYG----------VEVPGTDGrAGMAAIVLADGAEFDLAAL 522
|
570
....*....|....*...
gi 1246793773 1006 HRALCERLPAYMVPtQFV 1023
Cdd:PRK08279 523 AAHLYERLPAYAVP-LFV 539
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
1138-1371 |
6.19e-06 |
|
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.
Pssm-ID: 380468 [Multi-domain] Cd Length: 440 Bit Score: 52.10 E-value: 6.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1138 GEVGLSPIQR--WFFDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQV----AAPGP 1211
Cdd:cd19546 3 DEVPATAGQLrtWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRIldadAARPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1212 APAIQAQDWRGAADLDSRVDAAFARMQEaTPLAGPLVALThahcDDGERLLICAHHLIVDAVSWRLLLGELFDGLAALAR 1291
Cdd:cd19546 83 LPVVPATEEELPALLADRAAHLFDLTRE-TPWRCTLFALS----DTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARRE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1292 GEAWTPSARGASYADYV----EALREADDAQRF---DAGFWRELAA--QPMQALPQDRPVALADARQSnvGRIVQTLDAG 1362
Cdd:cd19546 158 GRAPERAPLPLQFADYAlwerELLAGEDDRDSLigdQIAYWRDALAgaPDELELPTDRPRPVLPSRRA--GAVPLRLDAE 235
|
....*....
gi 1246793773 1363 LTADLLERA 1371
Cdd:cd19546 236 VHARLMEAA 244
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
2062-2516 |
6.59e-06 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 51.97 E-value: 6.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2062 WTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWhrgaawlpldpqhpdarqiavlddsgaRIvigwG 2141
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLV---------------------------KI----G 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2142 AAPAWVPASVRWLDAESVLDVVSAYEepprVDVDadtPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPV-LDLGEDAS 2220
Cdd:cd05940 53 AVAALINYNLRGESLAHCLNVSSAKH----LVVD---AALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSgGALPSDVL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2221 LATLSTVAADLGFTALFGALLSGRRVRLLPaelafdaqalaahlqahpvdclKIVPSHLAGLLAAAGGTavlpreCLVTG 2300
Cdd:cd05940 126 YTCLPLYHSTALIVGWSACLASGATLVIRK----------------------KFSASNFWDDIRKYQAT------IFQYI 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2301 GEALTGALVQ---------QVRA-----LAPTL-----------RIVNHYGPTE------------TTVGILTCTVPEEW 2343
Cdd:cd05940 178 GELCRYLLNQppkpterkhKVRMifgngLRPDIweefkerfgvpRIAEFYAATEgnsgfinffgkpGAIGRNPSLLRKVA 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2344 P---VEQGVPVGHPLAGNEAwvldrFGLPAPVGVAGEL--YLGGGNLSLGYWQRAEQTaERFVAHPLAPDRLLYRSGDLA 2418
Cdd:cd05940 258 PlalVKYDLESGEPIRDAEG-----RCIKVPRGEPGLLisRINPLEPFDGYTDPAATE-KKILRDVFKKGDAWFNTGDLM 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2419 RLDGEGRIVYLGR-GDhQVKIRGYRVELGEVEQVLAQLPGVEVAAV--LALPGANG-------VLQLGACIQGSleGVAE 2488
Cdd:cd05940 332 RLDGEGFWYFVDRlGD-TFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPGTDGragmaaiVLQPNEEFDLS--ALAA 408
|
490 500
....*....|....*....|....*...
gi 1246793773 2489 ALAQRLPEYLCPSRWRAVESMPRLGNGK 2516
Cdd:cd05940 409 HLEKNLPGYARPLFLRLQPEMEITGTFK 436
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2300-2522 |
6.81e-06 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 51.71 E-value: 6.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2300 GGEALTGALVQQVRAlAPTLRIVNHYGPTETTVGIlTCTVPE--EWPVEQGVPVghPLAGNEAWVLD---RFGLPAPVGV 2374
Cdd:cd05944 129 GAAPLPVELRARFED-ATGLPVVEGYGLTEATCLV-AVNPPDgpKRPGSVGLRL--PYARVRIKVLDgvgRLLRDCAPDE 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2375 AGELYLGGGNLSLGYWQrAEQTAERFVahplapDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQ 2454
Cdd:cd05944 205 VGEICVAGPGVFGGYLY-TEGNKNAFV------ADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLR 277
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 2455 LPGVEVAAVLALPGAN------GVLQLGACIQGSLEGVAEALAQRLPEYLC-PSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:cd05944 278 HPAVAFAGAVGQPDAHagelpvAYVQLKPGAVVEEEELLAWARDHVPERAAvPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
2063-2200 |
7.54e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 52.07 E-value: 7.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2063 TYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAwlpldpqH--------PDA---RqiavLDD 2131
Cdd:PRK00174 100 TYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAV-------HsvvfggfsAEAladR----IID 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVI----GW-------------------------------GAAPAWVPASVRWLDaeSVLDVVSAYEEPprVDVDA 2176
Cdd:PRK00174 169 AGAKLVItadeGVrggkpiplkanvdealancpsvekvivvrrtGGDVDWVEGRDLWWH--ELVAGASDECEP--EPMDA 244
|
170 180
....*....|....*....|....
gi 1246793773 2177 DTPAYLIYTSGSTGTPKGVVVSQG 2200
Cdd:PRK00174 245 EDPLFILYTSGSTGKPKGVLHTTG 268
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
88-442 |
7.97e-06 |
|
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.
Pssm-ID: 380466 [Multi-domain] Cd Length: 413 Bit Score: 51.67 E-value: 7.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 88 APLslgQERLWFLEQFEPGGHAYHLAALFEL--RGELDA--AALERAVHglliRHEVLDRCIQGEdsvaaGGGAAVE--- 160
Cdd:cd19544 5 APL---QEGILFHHLLAEEGDPYLLRSLLAFdsRARLDAflAALQQVID----RHDILRTAILWE-----GLSEPVQvvw 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 161 -SADLR------GRGQDEIDALVEGFRLRPFELQRQRP--LRMQLLRLDGQGdgpvRHWLQVVVHHIACDGVSLGLLTQD 231
Cdd:cd19544 73 rQAELPveeltlDPGDDALAQLRARFDPRRYRLDLRQAplLRAHVAEDPANG----RWLLLLLFHHLISDHTSLELLLEE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 232 LsRAYrvECGLAAEPAPPLPcqYGDY---ARWQRDTldrlDASLRHHVEALSG-----APH-LHELPLDherpavlGQSG 302
Cdd:cd19544 149 I-QAI--LAGRAAALPPPVP--YRNFvaqARLGASQ----AEHEAFFREMLGDvdeptAPFgLLDVQGD-------GSDI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 303 AKLRLAFPPGLSERVAAYAQA---SRATAFH-----VLQaafaallaRCGAGDDLLIGTPVAGRVR--PELDSLVGLFVN 372
Cdd:cd19544 213 TEARLALDAELAQRLRAQARRlgvSPASLFHlawalVLA--------RCSGRDDVVFGTVLSGRMQggAGADRALGMFIN 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 373 TVVLRTQLhDDPDFASLVARCRdHQLAAL---EHQALPLervietlqVERSSR---HAPLFQLMFALRHDADLALD 442
Cdd:cd19544 285 TLPLRVRL-GGRSVREAVRQTH-ARLAELlrhEHASLAL--------AQRCSGvpaPTPLFSALLNYRHSAAAAAA 350
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
844-1041 |
9.64e-06 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 51.79 E-value: 9.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 844 ASRPvplgqlLPGRIAAVLDAHGRIVPRGVCGELAlggI-----GLAEGYRGDaaasERRFAPLRLP--SGeslrMYRSG 916
Cdd:cd05966 412 ATRP------FFGIEPAILDEEGNEVEGEVEGYLV---IkrpwpGMARTIYGD----HERYEDTYFSkfPG----YYFTG 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 917 DRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVraAAAGVVG---EGAAQRLVAWVecAGEDGFgqadln 993
Cdd:cd05966 475 DGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAV--AEAAVVGrphDIKGEAIYAFV--TLKDGE------ 544
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1246793773 994 qTDSDQTESE--RWHRalcERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05966 545 -EPSDELRKElrKHVR---KEIGPIATPDKIQFVPGLPKTRSGKIMRRIL 590
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
2174-2224 |
9.75e-06 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 51.66 E-value: 9.75e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 2174 VDADTP-----AYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVL-DLG-EDASLATL 2224
Cdd:PLN02387 242 VDPDLPspndiAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVpKLGkNDVYLAYL 299
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
3660-3975 |
1.01e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 51.64 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3660 EAPAYLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEHDVW-----------------SLFHSHAFDFAVWELW 3722
Cdd:PLN02736 221 EDVATICYTSGTTGTPKGVVLTHGNL--IANVAGSSLSTKFYPSDVHisylplahiyervnqivMLHYGVAVGFYQGDNL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3723 GawLYGGRAVLVPEAVCRQP-------DAFLDLLAEYGVtVLNQTPSAFYALQSQAM------------------RRELA 3777
Cdd:PLN02736 299 K--LMDDLAALRPTIFCSVPrlynriyDGITNAVKESGG-LKERLFNAAYNAKKQALengknpspmwdrlvfnkiKAKLG 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3778 LNVRAVVFGGEALEPSRLQPWRERYpQAELVNMYGITETTVHVSFHRLSDedlqSPTSRIGSALPDLAVHVLD------- 3850
Cdd:PLN02736 376 GRVRFMSSGASPLSPDVMEFLRICF-GGRVLEGYGMTETSCVISGMDEGD----NLSGHVGSPNPACEVKLVDvpemnyt 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3851 AAGQPVPLgvvGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKL-RGYRIEPG 3929
Cdd:PLN02736 451 SEDQPYPR---GEICVRGPIIFKGYYKDEVQTREVIDEDG---WLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPE 524
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1246793773 3930 EIAAKIASLPQVSDAAVtvegqgEGAWLMAYAVAAdgAEPDPQSLR 3975
Cdd:PLN02736 525 KIENVYAKCKFVAQCFV------YGDSLNSSLVAV--VVVDPEVLK 562
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
2145-2207 |
1.11e-05 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 51.41 E-value: 1.11e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 2145 AWVPASVRWLDaeSVLDVVSAYEEPprVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVA 2207
Cdd:cd05966 203 PMTEGRDLWWH--DLMAKQSPECEP--EWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAA 261
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
821-1041 |
1.14e-05 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 51.38 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 821 LINAYGPTEATiSSHYHRVQAIDASRPVPLGQLLPGRIAAVLD-AHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRF 899
Cdd:PLN02574 348 FIQGYGMTEST-AVGTRGFNTEKLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 900 aplrlpsgESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQ-VRAAAAGVVGEGAAQRLVAW 978
Cdd:PLN02574 427 --------DKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEiIDAAVTAVPDKECGEIPVAF 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 979 VECAGEDGFGQADLNQTDSDQTESERWHRalcerlpaymvptQFVALPRLPRNASGKIDRRAL 1041
Cdd:PLN02574 499 VVRRQGSTLSQEAVINYVAKQVAPYKKVR-------------KVVFVQSIPKSPAGKILRREL 548
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
602-1043 |
1.22e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 51.18 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 602 LLGAWRAGLSVIPLDTewpqARRAEVVAA----SGCDAVLTDAQGLA-----GFAPSVAIAVDEL----KLDGAGENGSG 668
Cdd:PRK13388 69 LAAAALGGYVLVGLNT----TRRGAALAAdirrADCQLLVTDAEHRPlldglDLPGVRVLDVDTPayaeLVAAAGALTPH 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 669 ENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDrVLHVA-----GLAVdttleqiLAAWS----R 739
Cdd:PRK13388 145 REVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDD-VCYVSmplfhSNAV-------MAGWApavaS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 740 GACVVARPDelLEPQRFLAFLSE-RAITVTDLAPAYANELVRASVADDwRDLALRcLVVGGDVLPVALAQrwFElgldRR 818
Cdd:PRK13388 217 GAAVALPAK--FSASGFLDDVRRyGATYFNYVGKPLAYILATPERPDD-ADNPLR-VAFGNEASPRDIAE--FS----RR 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 819 --CALINAYGPTEATISshyhrVQAIDASRPVPLGQLLPGRI-----------AAVLDAHGRIV-PRGVCGELA-LGGIG 883
Cdd:PRK13388 287 fgCQVEDGYGSSEGAVI-----VVREPGTPPGSIGRGAPGVAiynpetltecaVARFDAHGALLnADEAIGELVnTAGAG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 884 LAEGYRGDAAASERRFAplrlpSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAA 963
Cdd:PRK13388 362 FFEGYYNNPEATAERMR-----HG----MYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVA 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 964 A-GVVGEGAAQRLVAWVECAGEDGFGQADLNQTDSDQTEserwhralcerLPAYMVPTQFVALPRLPRNASGKIDRRALP 1042
Cdd:PRK13388 433 VyAVPDERVGDQVMAALVLRDGATFDPDAFAAFLAAQPD-----------LGTKAWPRYVRIAADLPSTATNKVLKRELI 501
|
.
gi 1246793773 1043 A 1043
Cdd:PRK13388 502 A 502
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
4029-4084 |
1.41e-05 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 45.25 E-value: 1.41e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 4029 RRLAELWRQLLGGELPGRGAH--FFARGGHSLLVVRLAEAIRAEFAIAVPLKSLFEQP 4084
Cdd:pfam00550 1 ERLRELLAEVLGVPAEEIDPDtdLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHP 58
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
2051-2218 |
1.45e-05 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 51.03 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGA--AWL-------PL----- 2116
Cdd:PRK08279 52 DRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAvvALLntqqrgaVLahsln 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2117 --DPQH--PDARQIAVLDDSGARIVIG---WGAAPAWVPASVRWLDAESVLDVVSAYEEPPRVDVDADTPAYLIYTSGST 2189
Cdd:PRK08279 132 lvDAKHliVGEELVEAFEEARADLARPprlWVAGGDTLDDPEGYEDLAAAAAGAPTTNPASRSGVTAKDTAFYIYTSGTT 211
|
170 180
....*....|....*....|....*....
gi 1246793773 2190 GTPKGVVVSQGNLANYVAGVLPVLDLGED 2218
Cdd:PRK08279 212 GLPKAAVMSHMRWLKAMGGFGGLLRLTPD 240
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
2297-2498 |
1.47e-05 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 50.92 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2297 LVTGGEALTGALVQQVRALAPtLRIVNHYGPTETTVGILTctvpeEWPVEQGVPVghplagNEAWVL-----DRFGLPAP 2371
Cdd:COG1541 208 GIFGGEPWSEEMRKEIEERWG-IKAYDIYGLTEVGPGVAY-----ECEAQDGLHI------WEDHFLveiidPETGEPVP 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2372 VGVAGELYLgggnlslgywqraeqTAERFVAHPLapdrLLYRSGDLARLDGEG--------RIVY-LGRGDHQVKIRGYR 2442
Cdd:COG1541 276 EGEEGELVV---------------TTLTKEAMPL----IRYRTGDLTRLLPEPcpcgrthpRIGRiLGRADDMLIIRGVN 336
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2443 VELGEVEQVLAQLPGVEVAAVLALPGANG----VLQLGACIQGSLEGVAEALAQRLPEYL 2498
Cdd:COG1541 337 VFPSQIEEVLLRIPEVGPEYQIVVDREGGldelTVRVELAPGASLEALAEAIAAALKAVL 396
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
2041-2203 |
1.71e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 50.80 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2041 AQSLLWQMPAQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGA-HVALCLPRTFAQLAAMAAVW-----------H 2108
Cdd:PRK13388 6 AQLLRDRAGDDTIAVRYGDRTWTWREVLAEAAARAAALIALADPDRPlHVGVLLGNTPEMLFWLAAAAlggyvlvglntT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2109 RGAAWLPLDPQHPDArQIAVLDDSGARIVIGWG--AAPAWVPASVRWLDAesvldVVSAYEEPPRVDVDADTPAYLIYTS 2186
Cdd:PRK13388 86 RRGAALAADIRRADC-QLLVTDAEHRPLLDGLDlpGVRVLDVDTPAYAEL-----VAAAGALTPHREVDAMDPFMLIFTS 159
|
170
....*....|....*..
gi 1246793773 2187 GSTGTPKGVVVSQGNLA 2203
Cdd:PRK13388 160 GTTGAPKAVRCSHGRLA 176
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
672-1041 |
1.98e-05 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 50.65 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 672 APNQLAYILYTSGSTGIPKGVEVGHA-----ALAAHIDAAAEALALSADDRVL------HVAGLAVDTtleqiLAAWSRG 740
Cdd:PRK08751 206 EPDDIAFLQYTGGTTGVAKGAMLTHRnlvanMQQAHQWLAGTGKLEEGCEVVItalplyHIFALTANG-----LVFMKIG 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 741 AC--VVARPDEL------LEPQRFLAFLSERAITvtdlapayaNELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFE 812
Cdd:PRK08751 281 GCnhLISNPRDMpgfvkeLKKTRFTAFTGVNTLF---------NGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQ 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 813 L-GLdrrcALINAYGPTEATISSHYHRVQAIDASRPVplGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGY--R 889
Cdd:PRK08751 352 VtGL----TLVEAYGLTETSPAACINPLTLKEYNGSI--GLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYwkR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 890 GDAAASerrfaplrlpSGESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQV-RAAAAGVVG 968
Cdd:PRK08751 426 PEETAK----------VMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVlEVAAVGVPD 495
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 969 EGAAQRLVAWVEcagedgfgQADLNQTDSDQTESERwhralcERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK08751 496 EKSGEIVKVVIV--------KKDPALTAEDVKAHAR------ANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
2676-2812 |
2.29e-05 |
|
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380467 [Multi-domain] Cd Length: 395 Bit Score: 49.99 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2676 HPMLRARF-QRDAAGQWQQTLGDWQadrFAHREADagQREDLLA-QWQAGLSFDGALLRvLALPDPQDGDTRVLFAAHHL 2753
Cdd:cd19545 50 NPILRTRIvQSDSGGLLQVVVKESP---ISWTEST--SLDEYLEeDRAAPMGLGGPLVR-LALVEDPDTERYFVWTIHHA 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 2754 LVDAVSWGIIVDDLQHAYAERRAGRSPAlaaeacgFGAWQAALRQLSaatLDGWRSYWR 2812
Cdd:cd19545 124 LYDGWSLPLILRQVLAAYQGEPVPQPPP-------FSRFVKYLRQLD---DEAAAEFWR 172
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
1142-1340 |
2.42e-05 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.
Pssm-ID: 380469 [Multi-domain] Cd Length: 422 Bit Score: 50.00 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1142 LSPIQRWFFDSAPAQPDR--YHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPAIQAQD 1219
Cdd:cd19547 4 LAPMQEGMLFRGLFWPDSdaYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDLAPPWALLD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1220 WRGAaDLDSRVDAaFARMQEATPLAG------PLVALTHAHCDDGERLLICAHH-LIVDAVSWRLLLGELFDGLAALARG 1292
Cdd:cd19547 84 WSGE-DPDRRAEL-LERLLADDRAAGlsladcPLYRLTLVRLGGGRHYLLWSHHhILLDGWCLSLIWGDVFRVYEELAHG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 1293 -EAWTPSARgaSYADYVEALR----EADDAQRFDAGFWRELAAQPMQALPQDR 1340
Cdd:cd19547 162 rEPQLSPCR--PYRDYVRWIRartaQSEESERFWREYLRDLTPSPFSTAPADR 212
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
1139-1341 |
2.42e-05 |
|
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380461 [Multi-domain] Cd Length: 432 Bit Score: 49.96 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1139 EVGLSPIQR--WFFDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPA-PAI 1215
Cdd:cd19538 1 EIPLSFAQRrlWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEAtPKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1216 QAQDwRGAADLDSRVDAA----FARMQEAtPLAGPLVALthahcDDGER-LLICAHHLIVDAVSWRLLLGELFDGLAALA 1290
Cdd:cd19538 81 EIKE-VDEEELESEINEAvrypFDLSEEP-PFRATLFEL-----GENEHvLLLLLHHIAADGWSLAPLTRDLSKAYRARC 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 1291 RGEA--WTPSArgASYADYV----EALREADDAQRFDA---GFWRE-LAAQPMQ-ALPQDRP 1341
Cdd:cd19538 154 KGEApeLAPLP--VQYADYAlwqqELLGDESDPDSLIArqlAYWKKqLAGLPDEiELPTDYP 213
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
2168-2209 |
2.99e-05 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 49.91 E-value: 2.99e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1246793773 2168 EPPrvdvDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGV 2209
Cdd:cd05927 109 PPP----KPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGV 146
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
679-1038 |
3.18e-05 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 49.19 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 679 ILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVDTTLEQilaawSRGACVVArpdELLE 752
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLnmlplfHIAGLNLALATFH-----AGGANVVM---EKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 753 PQRFLAFLSERAITV-TDLAPAYANELvrASVADDWRDLA-LRcLVVGGDVlPvALAQRWFELGLDRRCALinaYGPTEA 830
Cdd:cd17637 77 PAEALELIEEEKVTLmGSFPPILSNLL--DAAEKSGVDLSsLR-HVLGLDA-P-ETIQRFEETTGATFWSL---YGQTET 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 831 TISSHYHRVQAIDAS--RPVPLGQLlpgriaAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFaplrlpsge 908
Cdd:cd17637 149 SGLVTLSPYRERPGSagRPGPLVRV------RIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF--------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 909 slR--MYRSGDRVRLLDDGELQFLGRADFQ--VKLRGYRIELEEIEHCLGQLPQVraAAAGVVGEGAAQrlvawvecage 984
Cdd:cd17637 214 --RngWHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAI--AEVCVIGVPDPK----------- 278
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 985 dgFGQADlnqtdsdqteserwhRALCERLPAYMVPTQ----FVA-------LPR-------LPRNASGKIDR 1038
Cdd:cd17637 279 --WGEGI---------------KAVCVLKPGATLTADelieFVGsriarykKPRyvvfveaLPKTADGSIDR 333
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
719-1253 |
3.23e-05 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 50.26 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 719 LHVAGLAVDTTLeqiLAAWSRGACVV------ARPDELLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLAL 792
Cdd:COG3321 840 LWVAGVPVDWSA---LYPGRGRRRVPlptypfQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAA 916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 793 RCLVVGGDVLPVALAQRWFELGLDRRCALINAYGPTEATISSHYHRVQAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRG 872
Cdd:COG3321 917 AALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAAL 996
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 873 VCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHC 952
Cdd:COG3321 997 AAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAE 1076
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 953 LGQLPQVRAAAAGVVGEGAAQRLVAWVECAGEDGFGQADLNQTDSDQTESERWHRALCERLPAYMVPTQFVALPRLPRNA 1032
Cdd:COG3321 1077 LALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAA 1156
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1033 SGKIDRRALPAPPVLAQAERTPPRTAEESALCEVWAEVLQCEVGIHDSFFRLGGDSIRSLQVVARLRERGYAVTPKLMYQ 1112
Cdd:COG3321 1157 AALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALL 1236
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1113 YQSAAELAPQLIALQAAPAEAAPLVGEVGLSPIQRWFFDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLR 1192
Cdd:COG3321 1237 ALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAA 1316
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 1193 ASFERADGQWRQQVAAPGPAPAIQAQDWRGAADLDSRVDAAFARMQEATPLAGPLVALTHA 1253
Cdd:COG3321 1317 AAAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALA 1377
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
2061-2522 |
3.29e-05 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 49.95 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2061 SWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRT----FAQLAAMAAvwhrGAA----WLpLDPQHpdarqIA-VLDD 2131
Cdd:PRK07529 58 TWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLpethFALWGGEAA----GIAnpinPL-LEPEQ-----IAeLLRA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVI-------------------------------GWGAAPAWVPASVRWLDAESVLDVVSAYEEPPRVDVD----- 2175
Cdd:PRK07529 128 AGAKVLVtlgpfpgtdiwqkvaevlaalpelrtvvevdLARYLPGPKRLAVPLIRRKAHARILDFDAELARQPGDrlfsg 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2176 ----ADTPAYLIYTSGSTGTPKGVVVSQGNLAnYVAGVLP-VLDLGEDASLAT---LSTVAADLgfTALFGALLSGRRVr 2247
Cdd:PRK07529 208 rpigPDDVAAYFHTGGTTGMPKLAQHTHGNEV-ANAWLGAlLLGLGPGDTVFCglpLFHVNALL--VTGLAPLARGAHV- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2248 LLPAELAFDAQALAAH----LQAHPVDCLKIVPShlagllaAAGGTAVLPRE-----CL---VTGGEALTGALVQQVRAl 2315
Cdd:PRK07529 284 VLATPQGYRGPGVIANfwkiVERYRINFLSGVPT-------VYAALLQVPVDghdisSLryaLCGAAPLPVEVFRRFEA- 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2316 APTLRIVNHYGPTETTVgiLTCTVPEEWPVEQGvPVGHPLAGNEAWVL-----DRFGLPAPVGVAGELYLGGGNLSLGYw 2390
Cdd:PRK07529 356 ATGVRIVEGYGLTEATC--VSSVNPPDGERRIG-SVGLRLPYQRVRVVilddaGRYLRDCAVDEVGVLCIAGPNVFSGY- 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2391 QRAEQTAERFVAhplapDRLLyRSGDLARLDGEGRIVYLGRGDHQVkIR-GYRVELGEVEQVLAQLPGVEVAAVLALPGA 2469
Cdd:PRK07529 432 LEAAHNKGLWLE-----DGWL-NTGDLGRIDADGYFWLTGRAKDLI-IRgGHNIDPAAIEEALLRHPAVALAAAVGRPDA 504
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2470 N------GVLQLGACIQGSLEGVAEALAQRLPEYLC-PSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:PRK07529 505 HagelpvAYVQLKPGASATEAELLAFARDHIAERAAvPKHVRILDALPKTAVGKIFKPAL 564
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1148-1348 |
3.64e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 50.04 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1148 WFFDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPAIQAQDWRGAADld 1227
Cdd:PRK10252 18 WMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFPLPEIIDLRTQPD-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1228 sRVDAAFARMQeaTPLAGPLvALTHAHCDDGERLLICA----------HHLIVDAVSWRLLLGELFDGLAALARGEAWTP 1297
Cdd:PRK10252 96 -PHAAAQALMQ--ADLQQDL-RVDSGKPLVFHQLIQLGdnrwywyqryHHLLVDGFSFPAITRRIAAIYCAWLRGEPTPA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 1298 SARG------ASYADYvealrEADDAQRFDAGFWRELAAQpmqaLPQdrPVALADAR 1348
Cdd:PRK10252 172 SPFTpfadvvEEYQRY-----RASEAWQRDAAFWAEQRRQ----LPP--PASLSPAP 217
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
2058-2216 |
3.99e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 49.71 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2058 GAASW-TYAQLRAAAGRIAGALDAVGVQPGAHVALclprTFAQLAAMAAVWHRGAAW----LPL-DPQHPDARQIAV--- 2128
Cdd:PLN02736 74 GEYKWmTYGEAGTARTAIGSGLVQHGIPKGACVGL----YFINRPEWLIVDHACSAYsyvsVPLyDTLGPDAVKFIVnha 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2129 -------------------LDDSGARIVIGWGAAPAWVP-----ASVRWLDAESVLDVVSAYEEPPRVDVDADTpAYLIY 2184
Cdd:PLN02736 150 evaaifcvpqtlntllsclSEIPSVRLIVVVGGADEPLPslpsgTGVEIVTYSKLLAQGRSSPQPFRPPKPEDV-ATICY 228
|
170 180 190
....*....|....*....|....*....|..
gi 1246793773 2185 TSGSTGTPKGVVVSQGNLANYVAGVLPVLDLG 2216
Cdd:PLN02736 229 TSGTTGTPKGVVLTHGNLIANVAGSSLSTKFY 260
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
675-1053 |
5.42e-05 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 49.31 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 675 QLAYILYTSGSTGIPKGVEvghaalaahIDAAAEALALSADDRVLHVAGLAVDTTLEQI------------LAAWSRGAC 742
Cdd:PRK12406 153 QPQSMIYTSGTTGHPKGVR---------RAAPTPEQAAAAEQMRALIYGLKPGIRALLTgplyhsapnaygLRAGRLGGV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 743 VVARPDelLEPQRFLAFLSERAITVTDLAPAYANELVR--ASVADDWRDLALRCLVVGGDVLPVALAQrwfelgldrrcA 820
Cdd:PRK12406 224 LVLQPR--FDPEELLQLIERHRITHMHMVPTMFIRLLKlpEEVRAKYDVSSLRHVIHAAAPCPADVKR-----------A 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 821 LINAYGP--------TEATISSHYHRVQAIdaSRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAE-GYRGD 891
Cdd:PRK12406 291 MIEWWGPviyeyygsTESGAVTFATSEDAL--SHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNK 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 892 aaaserrfaPLRLPSGESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA-GVVGEG 970
Cdd:PRK12406 369 ---------PEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVfGIPDAE 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 971 AAQRLVAWVECAGEDGFGQADLNQTdsdqteserwhraLCERLPAYMVPTQFVALPRLPRNASGKIDRRALpAPPVLAQA 1050
Cdd:PRK12406 440 FGEALMAVVEPQPGATLDEADIRAQ-------------LKARLAGYKVPKHIEIMAELPREDSGKIFKRRL-RDPYWANA 505
|
...
gi 1246793773 1051 ERT 1053
Cdd:PRK12406 506 GRK 508
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
673-1037 |
5.89e-05 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 49.32 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 673 PNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDR------VLHVAGLAVDttleqILAAWSRGACVVAR 746
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRfmsalpLFHSFGLTVG-----LFTPLLTGAEVFLY 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 747 PDEL---LEPQrflaFLSERAITVTDLAPAYANELVR-ASVADDWRdlaLRCLVVGGDVLPVALAQRWFE-LGLdrrcAL 821
Cdd:PRK08043 439 PSPLhyrIVPE----LVYDRNCTVLFGTSTFLGNYARfANPYDFAR---LRYVVAGAEKLQESTKQLWQDkFGL----RI 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 822 INAYGPTEATisshyhRVQAID---ASRPVPLGQLLPGRIAAVLDAHGriVPRGvcGELALGGIGLAEGYRgdaaaseRR 898
Cdd:PRK08043 508 LEGYGVTECA------PVVSINvpmAAKPGTVGRILPGMDARLLSVPG--IEQG--GRLQLKGPNIMNGYL-------RV 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 899 FAP--LRLPSGESLR------MYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEH-CLGQLPQVRAAAAGVVGE 969
Cdd:PRK08043 571 EKPgvLEVPTAENARgemergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAIKSDA 650
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 970 GAAQRLVawvecagedgfgqadLNQTDSDQTESERWHRALCERLPAYMVPTQFVALPRLPRNASGKID 1037
Cdd:PRK08043 651 SKGEALV---------------LFTTDSELTREKLQQYAREHGVPELAVPRDIRYLKQLPLLGSGKPD 703
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
3526-4048 |
6.76e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 49.33 E-value: 6.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3526 AEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPA 3605
Cdd:PRK07868 454 AEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLMPPDTDL 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3606 ARRGFILEDSGVCLSVSQRALAVELPGTALCL----------DDPFTRAQLDAVEPG--ELPEVPTEAP------AYLIY 3667
Cdd:PRK07868 534 AAAVRLGGVTEIITDPTNLEAARQLPGRVLVLgggesrdldlPDDADVIDMEKIDPDavELPGWYRPNPglardlAFIAF 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3668 -TSGSTGTPKGVVvTHRNVERLFTAATQTGrfsFDEHD-VWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAvcrQPDAF 3745
Cdd:PRK07868 614 sTAGGELVAKQIT-NYRWALSAFGTASAAA---LDRRDtVYCLTPLHHESGLLVSLGGAVVGGSRIALSRGL---DPDRF 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3746 LDLLAEYGVTVLNQTpsafyalqsQAMRRELalnVRAVVFGGEALEPSRL-----QP---WR---ERYPQAELVNMYGIT 3814
Cdd:PRK07868 687 VQEVRQYGVTVVSYT---------WAMLREV---VDDPAFVLHGNHPVRLfigsgMPtglWErvvEAFAPAHVVEFFATT 754
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3815 ETTV---HVSFHRLSDEDLQSPTS---RIGSALPDLAVHVLDAAG--QPVPLGVVGELVVEGDGVAQgywqrPELTAERF 3886
Cdd:PRK07868 755 DGQAvlaNVSGAKIGSKGRPLPGAgrvELAAYDPEHDLILEDDRGfvRRAEVNEVGVLLARARGPID-----PTASVKRG 829
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3887 VERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVK-LRG-YRIEPgeIAAKIASLPQVsDAAVTVeGQGEGAWLMAYAVAA 3964
Cdd:PRK07868 830 VFAPADTWISTEYLFRRDDDGDYWLVDRRGSVIRtARGpVYTEP--VTDALGRIGGV-DLAVTY-GVEVGGRQLAVAAVT 905
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3965 --DGAEPDPQSLREALRALLPDYMlPRLIQLLPALPLTAN-----GKLDRKALPKPETQD--RDEgvlESASERRLAELW 4035
Cdd:PRK07868 906 lrPGAAITAADLTEALASLPVGLG-PDIVHVVPEIPLSATyrptvSALRAAGIPKPGRQAwyFDP---ETNRYRRLTPAV 981
|
570
....*....|...
gi 1246793773 4036 RQLLGGELPGRGA 4048
Cdd:PRK07868 982 RAELTGGHRRGAA 994
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
588-932 |
7.17e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 48.96 E-value: 7.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 588 VALCLPRGLDWYCLLLGAWRAGLSVIPL-DTEWP--QARRAEVVAASGCDAVLTDAQGLAG----FAPSVA------IAV 654
Cdd:PRK07769 82 VAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAILTTTDSAEGvrkfFRARPAkerprvIAV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 655 DELKlDGAGENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDR------VLHVAGLavdt 728
Cdd:PRK07769 162 DAVP-DEVGATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRgvswlpFFHDMGL---- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 729 tLEQILAAWSRG-------ACVVARPDELLepqRFLAFLSERAITVTDLAPAYANEL--VRASVADDWRDLAL---RCLV 796
Cdd:PRK07769 237 -ITVLLPALLGHyitfmspAAFVRRPGRWI---RELARKPGGTGGTFSAAPNFAFEHaaARGLPKDGEPPLDLsnvKGLL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 797 VGGDVLPVALAQRWFE----LGLdRRCALINAYGPTEAT--ISS-----------------HYHRVQAIDASRPVPLGQL 853
Cdd:PRK07769 313 NGSEPVSPASMRKFNEafapYGL-PPTAIKPSYGMAEATlfVSTtpmdeeptviyvdrdelNAGRFVEVPADAPNAVAQV 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 854 LPGRI-----AAVLDAH-GRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPL---RLP------SGESLRMYRSGDR 918
Cdd:PRK07769 392 SAGKVgvsewAVIVDPEtASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFQNIlksRLSeshaegAPDDALWVRTGDY 471
|
410
....*....|....
gi 1246793773 919 VRLLdDGELQFLGR 932
Cdd:PRK07769 472 GVYF-DGELYITGR 484
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
824-968 |
7.23e-05 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 48.07 E-value: 7.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 824 AYGPTEAT---ISSHYHRVQAIDASRPVPLGQLlpgriaAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFA 900
Cdd:cd17636 142 GYGQTEVMglaTFAALGGGAIGGAGRPSPLVQV------RILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR 215
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 901 plrlpSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVG 968
Cdd:cd17636 216 -----GG----WHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAA--VIG 272
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
1187-1371 |
8.50e-05 |
|
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.
Pssm-ID: 380466 [Multi-domain] Cd Length: 413 Bit Score: 48.20 E-value: 8.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1187 RHDLLRASFeRADG-----Q--WRQ------QVAAPGPAPAiqaqdwrgAADLDSRVDAAFARM--QEAtplagPLVALT 1251
Cdd:cd19544 51 RHDILRTAI-LWEGlsepvQvvWRQaelpveELTLDPGDDA--------LAQLRARFDPRRYRLdlRQA-----PLLRAH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1252 HAHCDDGER--LLICAHHLIVDAVSWRLLLGElfdgLAALARGEAWT-PSArgASYADYVEALREADDAQRFDAgFWREL 1328
Cdd:cd19544 117 VAEDPANGRwlLLLLFHHLISDHTSLELLLEE----IQAILAGRAAAlPPP--VPYRNFVAQARLGASQAEHEA-FFREM 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1246793773 1329 AAQpmqalpQDRPVA---LADARQ--SNVGRIVQTLDAGLTADLLERA 1371
Cdd:cd19544 190 LGD------VDEPTApfgLLDVQGdgSDITEARLALDAELAQRLRAQA 231
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
2123-2213 |
9.08e-05 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 48.72 E-value: 9.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2123 ARQIAVLDDSGARIVIGWGAAPAwvPASVRW---LDAESVLDVVSAYEEpprvdVDADTPAYLIYTSGSTGTPKGVVVSQ 2199
Cdd:PRK08180 159 ARALAAVVPADVEVVAVRGAVPG--RAATPFaalLATPPTAAVDAAHAA-----VGPDTIAKFLFTSGSTGLPKAVINTH 231
|
90
....*....|....*..
gi 1246793773 2200 GNL-AN--YVAGVLPVL 2213
Cdd:PRK08180 232 RMLcANqqMLAQTFPFL 248
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
2056-2202 |
9.63e-05 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 48.63 E-value: 9.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2056 EEGAASWTYAQLRAAAGRIAGAL-DAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQ-----------HPDA 2123
Cdd:PRK05620 33 GAEQEQTTFAAIGARAAALAHALhDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQlmndqivhiinHAED 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2124 RQIaVLDDSGA-------------RIVIGWGAAPA-----WVPASVRWLDAESVLDVVSA-YEEPprvDVDADTPAYLIY 2184
Cdd:PRK05620 113 EVI-VADPRLAeqlgeilkecpcvRAVVFIGPSDAdsaaaHMPEGIKVYSYEALLDGRSTvYDWP---ELDETTAAAICY 188
|
170
....*....|....*...
gi 1246793773 2185 TSGSTGTPKGVVVSQGNL 2202
Cdd:PRK05620 189 STGTTGAPKGVVYSHRSL 206
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
791-1041 |
9.67e-05 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 48.51 E-value: 9.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 791 ALRCLVVGGDVLPVALAQRWFELgldRRCALINAYGPTEAT--ISSHYHRVQAIDASRPVPLgqllPGRIAAVLDAHGRI 868
Cdd:PRK08974 326 SLKLSVGGGMAVQQAVAERWVKL---TGQYLLEGYGLTECSplVSVNPYDLDYYSGSIGLPV----PSTEIKLVDDDGNE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 869 VPRGVCGELALGGIGLAEGY--RGDAAAserrfaplrlpsgESLR--MYRSGDRVRLLDDGELQFLGRADFQVKLRGYRI 944
Cdd:PRK08974 399 VPPGEPGELWVKGPQVMLGYwqRPEATD-------------EVIKdgWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNV 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 945 ELEEIEHCLGQLPQV-RAAAAGVVGEGAAQRLVAWVEcagedgfgqadlnQTDSDQTESERwhRALCER-LPAYMVPTQF 1022
Cdd:PRK08974 466 YPNEIEDVVMLHPKVlEVAAVGVPSEVSGEAVKIFVV-------------KKDPSLTEEEL--ITHCRRhLTGYKVPKLV 530
|
250
....*....|....*....
gi 1246793773 1023 VALPRLPRNASGKIDRRAL 1041
Cdd:PRK08974 531 EFRDELPKSNVGKILRREL 549
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
901-1041 |
1.03e-04 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 48.27 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 901 PLRLPSGESLRmyRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQ--VRAAAAGVVGEGAAQRLVAW 978
Cdd:PLN03051 349 PMYGSKGMPLR--RHGDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACDRAVAgiAETAAVGVAPPDGGPELLVI 426
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 979 VECAG--EDGFGQADLNQTdsdqteSERWHRALCERL-PAYMVptQFVAL-PRLPRNASGKIDRRAL 1041
Cdd:PLN03051 427 FLVLGeeKKGFDQARPEAL------QKKFQEAIQTNLnPLFKV--SRVKIvPELPRNASNKLLRRVL 485
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
2676-2812 |
1.18e-04 |
|
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380458 [Multi-domain] Cd Length: 423 Bit Score: 47.87 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2676 HPMLRARFQRDAAGQWQQTLGDWQADRFAHREADAGQREDLLAQWQAGLS---FD---GALLRVLA--LPdpqDGDTRVL 2747
Cdd:cd19535 53 HPMLRAVFLDDGTQQILPEVPWYGITVHDLRGLSEEEAEAALEELRERLShrvLDverGPLFDIRLslLP---EGRTRLH 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 2748 FAAHHLLVDAVSWGIIVDDLQHAYAERRAgrspALAAEACGFGAWQAALRQLSAATLDGWRSYWR 2812
Cdd:cd19535 130 LSIDLLVADALSLQILLRELAALYEDPGE----PLPPLELSFRDYLLAEQALRETAYERARAYWQ 190
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
3663-3914 |
1.30e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 48.05 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3663 AYLIYTSGSTGTPKGVVVTHRNVERLFTAATQ-----TGRFSFDEHDVWSLFHSHAFDFAVWELW---GAWL-YGgravl 3733
Cdd:PTZ00216 267 ALIMYTSGTTGDPKGVMHTHGSLTAGILALEDrlndlIGPPEEDETYCSYLPLAHIMEFGVTNIFlarGALIgFG----- 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3734 vpeavcrQPDAFLDL-------LAEYGVTVLNQTPSAF-----------------------YALQSQ------------- 3770
Cdd:PTZ00216 342 -------SPRTLTDTfarphgdLTEFRPVFLIGVPRIFdtikkaveaklppvgslkrrvfdHAYQSRlralkegkdtpyw 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3771 ------AMRRELALNVRAVVFGGEALEPsrlqpwreryPQAELVNM--------YGITETTVHVSFHRLSDEDlqspTSR 3836
Cdd:PTZ00216 415 nekvfsAPRAVLGGRVRAMLSGGGPLSA----------ATQEFVNVvfgmviqgWGLTETVCCGGIQRTGDLE----PNA 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3837 IGSALPDLAVHVLDAAG-----QPVPLGvvgELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEY 3911
Cdd:PTZ00216 481 VGQLLKGVEMKLLDTEEykhtdTPEPRG---EILLRGPFLFKGYYKQEELTREVLDEDG---WFHTGDVGSIAANGTLRI 554
|
...
gi 1246793773 3912 RGR 3914
Cdd:PTZ00216 555 IGR 557
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
2064-2207 |
1.35e-04 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 48.08 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2064 YAQLRAAAGRIAGALDAVGVQPGAHVALcLPRTFAQLAAM------AAVWhrgAAWLPLdpqhPDA--------RQIAV- 2128
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVAL-IAETDGDFVEAffacqyAGLV---PVPLPL----PMGfggresyiAQLRGm 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2129 LDDSGARIVIGWGAAPAWVPASVRWLDAESVLDVVSAYEEP-PRVD---VDADTPAYLIYTSGSTGTPKGVVVSQGNL-A 2203
Cdd:PRK09192 124 LASAQPAAIITPDELLPWVNEATHGNPLLHVLSHAWFKALPeADVAlprPTPDDIAYLQYSSGSTRFPRGVIITHRALmA 203
|
....
gi 1246793773 2204 NYVA 2207
Cdd:PRK09192 204 NLRA 207
|
|
| PRK09294 |
PRK09294 |
phthiocerol/phthiodiolone dimycocerosyl transferase; |
3108-3329 |
1.51e-04 |
|
phthiocerol/phthiodiolone dimycocerosyl transferase;
Pssm-ID: 181765 [Multi-domain] Cd Length: 416 Bit Score: 47.40 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3108 TVALHGALDREAFAAAWQQALERHPILRSGFAVQGLPSPRQLPHRQVSLPLAEQDWSGLEPaqarsrLSELQAQQCEAgf 3187
Cdd:PRK09294 27 TAHLRGVLDIDALSDAFDALLRAHPVLAAHLEQDSDGGWELVADDLLHPGIVVVDGDAARP------LPELQLDQGVS-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3188 dlaappLMRLALLRRSADEHWLVWTrHHLIVDGWSSALLLDEVWRLYAALRESRTPQLPAAPPFRDYLHWLrgqdeAAAR 3267
Cdd:PRK09294 99 ------LLALDVVPDDGGARVTLYI-HHSIADAHHSASLLDELWSRYTDVVTTGDPGPIRPQPAPQSLEAV-----LAQR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3268 AFWREQLTGLE---------------PAALPEATEPAEGYASSTRRFDLAAASAWAQS---HGLTASSLLQGALALVLQR 3329
Cdd:PRK09294 167 GIRRQALSGAErfmpamyayelpptpTAAVLAKPGLPQAVPVTRCRLSKAQTSSLAAFgrrHRLTVNALVSAAILLAEWQ 246
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
674-1041 |
1.52e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 47.72 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 674 NQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAE--ALALSADDRVL------HVAGLAVDTTLEQIlaawsRGACVVA 745
Cdd:PRK06710 206 NDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQwlYNCKEGEEVVLgvlpffHVYGMTAVMNLSIM-----QGYKMVL 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 746 RPDelLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFELGLDRrcaLINAY 825
Cdd:PRK06710 281 IPK--FDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFETVTGGK---LVEGY 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 826 GPTEATISSHYHRVQaiDASRPVPLGQLLPGRIAAVLDAH-GRIVPRGVCGELALGGIGLAEGYRGDaaaSERRFAPLRl 904
Cdd:PRK06710 356 GLTESSPVTHSNFLW--EKRVPGSIGVPWPDTEAMIMSLEtGEALPPGEIGEIVVKGPQIMKGYWNK---PEETAAVLQ- 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 905 pSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA-GVVGEGAAQRLVAWVeCAG 983
Cdd:PRK06710 430 -DG----WLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTiGVPDPYRGETVKAFV-VLK 503
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 984 EDgfgqadlnqTDSDQTESERWHRalcERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK06710 504 EG---------TECSEEELNQFAR---KYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
2545-2610 |
1.77e-04 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 43.01 E-value: 1.77e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2545 EVLRELWQKLLGR---EHIGAHDNFFALGGDSILSLQLVARARQA-GLALMPRQLYDHPTLAGLSAQVQA 2610
Cdd:smart00823 15 DLVREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAAtGLRLPATLVFDHPTPAALAEHLAA 84
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
1019-1558 |
2.21e-04 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 47.56 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1019 PTQFVALPRLPRNASGKIDRRALPAPPVLAQAERTPPRTAEESALCEVWAEVLQCEVGIHDSFFRLGGDSIRSLQVVARL 1098
Cdd:COG3321 857 GRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALA 936
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1099 RERGYAVTPKLMYQYQSAAELAPQLIALQAAPAEAAPLVGEVGLSPIQRWFFDSAPAQPDRYHQYVALRLKQPLDAQHLA 1178
Cdd:COG3321 937 AAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAA 1016
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1179 QVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPAIQAQDWRGAADLDSRVDAAFARMQEATPLAGPLVALTHAHCDDG 1258
Cdd:COG3321 1017 AAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALA 1096
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1259 ERLLICAHHLIVDAVSWRLLLGELFDGLAALARGEAWTPSARGASYADYVEALREADDAQRFDAGFWRELAAQPMQALPQ 1338
Cdd:COG3321 1097 LALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLA 1176
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1339 DRPVALADARQSNVGRIVQTLDAGLTADLLERAgeayrcrtdevllialarALATRTG----RNRLWLDRERHGRDVLDG 1414
Cdd:COG3321 1177 LALALAAALAAALAGLAALLLAALLAALLAALL------------------ALALAALaaaaAALLAAAAAAAALALLAL 1238
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1415 RDWSSVLGWYTAVHPLPLDLGVADGPAQIGALKEQIRALARRGLDYMPLVASARIPALPAGQLLFNYHGVVDAGAHPAFE 1494
Cdd:COG3321 1239 AAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAA 1318
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 1495 VEPRTLASGNGADNPPGALVEINARVQAGRLGLVWNYAGEAYDAATIEAWSQAFAAELAALVAH 1558
Cdd:COG3321 1319 AALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALA 1382
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
3190-3778 |
2.31e-04 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 47.56 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3190 AAPPLMRLALLRRSADEHWLVWTrhhLIVDGWSSALLLDevWRLYAALRESRTPQLPAAPpfrdylhWLRgQDEAAARAF 3269
Cdd:COG3321 813 AAGDAVVLPSLRRGEDELAQLLT---ALAQLWVAGVPVD--WSALYPGRGRRRVPLPTYP-------FQR-EDAAAALLA 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3270 WREQLTGLEPAALPEATEPAEGYASSTRRFDLAAASAWAQSHGLTASSLLQGALALVLQRyygrdDFALGITIAGRPPEL 3349
Cdd:COG3321 880 AALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAA-----AALLALAAAAAAAAA 954
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3350 AGVERMLGVFINSVPLRVTPAGEATPAPWLQALQQRNLDLRTHGYLPLAQIQRAGAADAVSPFDVLLVFENLPTESREER 3429
Cdd:COG3321 955 ALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAA 1034
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3430 SGMRIEELDHRAHSNYPLMLTAIPDAGGLRIEAALDRSKLDGWLVEQMLDDLDFVLQQVPALQRFDALPLLPSQTRSAAW 3509
Cdd:COG3321 1035 LAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAA 1114
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3510 TSRERYACTGNLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAI 3589
Cdd:COG3321 1115 LALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAA 1194
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3590 LKTGAAYVPVDPHAPAARRGFILEDSGVCLSVSQRALAVELPGTALCLDDPFTRAQLDAVEPGELPEVPTEAPAYLIYTS 3669
Cdd:COG3321 1195 LLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAAL 1274
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3670 GSTGTPKGVVVTHRNVERLFTAATQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLL 3749
Cdd:COG3321 1275 AAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAAAAAAA 1354
|
570 580
....*....|....*....|....*....
gi 1246793773 3750 AEYGVTVLNQTPSAFYALQSQAMRRELAL 3778
Cdd:COG3321 1355 AAAAAAAALAAAAGAAAAAAALALAALAA 1383
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
2630-2810 |
2.40e-04 |
|
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380459 [Multi-domain] Cd Length: 419 Bit Score: 47.06 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2630 LTPIQHWFFEQALDQPahwNMSLYL-----KLPGALDTAAFAAALADVAAAHPMLRARFQRDAAG---QWQ--QTLGDWQ 2699
Cdd:cd19536 4 LSSLQEGMLFHSLLNP---GGSVYLhnytyTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGqpvQVVhrQAQVPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2700 ADRFAHREADAGQREDLLAQWQA-GLSFDGA-LLRVLALPDPQDGDTRVLFAAHHLLVDAVSWGIIVDDLQHAYAERRAG 2777
Cdd:cd19536 81 ELDLTPLEEQLDPLRAYKEETKIrRFDLGRApLVRAALVRKDERERFLLVISDHHSILDGWSLYLLVKEILAVYNQLLEY 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1246793773 2778 RSPALaAEACGFG---AWQAALRQlSAATLDGWRSY 2810
Cdd:cd19536 161 KPLSL-PPAQPYRdfvAHERASIQ-QAASERYWREY 194
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
948-1035 |
3.41e-04 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 41.76 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 948 EIEHCLGQLPQVR-AAAAGVVGEGAAQRLVAWVECAGEDGFGQADLNQtdsdqteserwhrALCERLPAYMVPTQFVALP 1026
Cdd:pfam13193 1 EVESALVSHPAVAeAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVA-------------HVREELGPYAVPKEVVFVD 67
|
....*....
gi 1246793773 1027 RLPRNASGK 1035
Cdd:pfam13193 68 ELPKTRSGK 76
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
2041-2200 |
4.08e-04 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 46.33 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2041 AQSLLWQMPAQAVAV----EEGA-ASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWlp 2115
Cdd:PRK03584 89 AENLLRHRRDDRPAIifrgEDGPrRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIW-- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2116 lDPQHPDARQIAVLD------------------------------------DSGARIVI----GWGAAPAWVPASVRWLD 2155
Cdd:PRK03584 167 -SSCSPDFGVQGVLDrfgqiepkvliavdgyryggkafdrrakvaelraalPSLEHVVVvpylGPAAAAAALPGALLWED 245
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1246793773 2156 AesvldVVSAYEEPPR-VDVDADTPAYLIYTSGSTGTPKGVVVSQG 2200
Cdd:PRK03584 246 F-----LAPAEAAELEfEPVPFDHPLWILYSSGTTGLPKCIVHGHG 286
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
2078-2426 |
4.18e-04 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 46.27 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2078 LDAVG------VQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLD----PQHPDaRQIAVLDDSGARIVIGWGAAPAWV 2147
Cdd:PRK12476 78 LRAVGarlqqvAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFapelPGHAE-RLDTALRDAEPTVVLTTTAAAEAV 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2148 PASVRWLDAES-----VLDVV--SAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNL-ANYVAGVLPVLDLGEDA 2219
Cdd:PRK12476 157 EGFLRNLPRLRrprviAIDAIpdSAGESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVgTNLVQMILSIDLLDRNT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2220 SLATLSTVAADLG-----FTALFGA---LLS--------GRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLL 2283
Cdd:PRK12476 237 HGVSWLPLYHDMGlsmigFPAVYGGhstLMSptafvrrpQRWIKALSEGSRTGRVVTAAPNFAYEWAAQRGLPAEGDDID 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2284 aaaggtavLPRECLVTGGEALTGALVQQVRA------LAPTLrIVNHYGPTETTVGILTC------TV----PEEWPVEQ 2347
Cdd:PRK12476 317 --------LSNVVLIIGSEPVSIDAVTTFNKafapygLPRTA-FKPSYGIAEATLFVATIapdaepSVvyldREQLGAGR 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2348 GVPV--GHPLA------GNEA---W---VLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFV------------ 2401
Cdd:PRK12476 388 AVRVaaDAPNAvahvscGQVArsqWaviVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFGaklqsrlaegsh 467
|
410 420 430
....*....|....*....|....*....|
gi 1246793773 2402 AHPLAPDRLLYRSGDLA-RLDGE----GRI 2426
Cdd:PRK12476 468 ADGAADDGTWLRTGDLGvYLDGElyitGRI 497
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
4028-4082 |
4.51e-04 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 41.76 E-value: 4.51e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 4028 ERRLAELWRQLLG--GELPGRGAHFFAR-GGHSLLVVRLAEAIRAEFAIAVPLKSLFE 4082
Cdd:COG0236 7 EERLAEIIAEVLGvdPEEITPDDSFFEDlGLDSLDAVELIAALEEEFGIELPDTELFE 64
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
676-1019 |
5.09e-04 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 45.81 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 676 LAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVdtTLEQILAAwsrGACVVARpde 749
Cdd:cd05940 83 AALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYtclplyHSTALIV--GWSACLAS---GATLVIR--- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 750 llepQRFLA--FLSE-RAITVTdlAPAYANELVR----ASVADDWRDLALRCLVVGG---DVlpvalaqrWFEL----GL 815
Cdd:cd05940 155 ----KKFSAsnFWDDiRKYQAT--IFQYIGELCRyllnQPPKPTERKHKVRMIFGNGlrpDI--------WEEFkerfGV 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 816 DRRCALinaYGPTEATISS--HYHRVQAIDASRPVplgQLLPGRIAAV----------LDAHGRI--VPRGVCGEL--AL 879
Cdd:cd05940 221 PRIAEF---YAATEGNSGFinFFGKPGAIGRNPSL---LRKVAPLALVkydlesgepiRDAEGRCikVPRGEPGLLisRI 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 880 GGIGLAEGYrGDAAASERRFAPLRLPSGEslRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQV 959
Cdd:cd05940 295 NPLEPFDGY-TDPAATEKKILRDVFKKGD--AWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGV 371
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 960 RAAAagVVGegaaqrlvawVECAGEDG-FGQADLNQTDSDQTESERWHRALCERLPAYMVP 1019
Cdd:cd05940 372 EEAN--VYG----------VQVPGTDGrAGMAAIVLQPNEEFDLSALAAHLEKNLPGYARP 420
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
2631-2859 |
8.12e-04 |
|
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380464 [Multi-domain] Cd Length: 401 Bit Score: 44.99 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2631 TPIQHWFFEQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARF-QRDAAGQWQQ-TLGDWQADRFAHREA 2708
Cdd:cd19542 5 TPMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFvESSAEGTFLQvVLKSLDPPIEEVETD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2709 D---AGQREDLLaQWQAGlsfDGALLRVLALPDPQDGDTRVLFAAHHLLVDAVSWGIIVDDLQHAYAERRAGRSPALAae 2785
Cdd:cd19542 85 EdslDALTRDLL-DDPTL---FGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPPAPPFS-- 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 2786 acgfgawqAALRQLSAATLDGWRSYWRAQAADAEAIALPWQDSDNRYADTVHLHDRferdwTERLLTQTARAYG 2859
Cdd:cd19542 159 --------DYISYLQSQSQEESLQYWRKYLQGASPCAFPSLSPKRPAERSLSSTRR-----SLAKLEAFCASLG 219
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
2174-2493 |
8.16e-04 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 45.53 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2174 VDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLA-TLSTVAADLGFTALFGALLSGRRVRLLPAE 2252
Cdd:PRK05851 149 PDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDVGcSWLPLYHDMGLAFLLTAALAGAPLWLAPTT 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2253 lAFdaqalaahlQAHPVDCLK-IVPSHLAGLLAAAGGTAVLPR-------------ECLVTGGEALTGALVQQ-VRALAP 2317
Cdd:PRK05851 229 -AF---------SASPFRWLSwLSDSRATLTAAPNFAYNLIGKyarrvsdvdlgalRVALNGGEPVDCDGFERfATAMAP 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2318 ----TLRIVNHYGPTETT---------VGILT--CTVPEEWPVEQGVPVGHPLAGNEAWVLDRFGlPAPVGV--AGELYL 2380
Cdd:PRK05851 299 fgfdAGAAAPSYGLAESTcavtvpvpgIGLRVdeVTTDDGSGARRHAVLGNPIPGMEVRISPGDG-AAGVAGreIGEIEI 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2381 GGGNLSLGYWQRAeqtaerfvahPLAPDRLlYRSGDLARLdGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEV 2460
Cdd:PRK05851 378 RGASMMSGYLGQA----------PIDPDDW-FPTGDLGYL-VDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVRE 445
|
330 340 350
....*....|....*....|....*....|...
gi 1246793773 2461 AAVLALPGANGVLQLGACIQGSLEGVAEALAQR 2493
Cdd:PRK05851 446 GAVVAVGTGEGSARPGLVIAAEFRGPDEAGARS 478
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
844-1062 |
8.39e-04 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 45.38 E-value: 8.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 844 ASRPVPLGQL---LPGRIAAVLDAHGRIVPRGVCGELALGGiGLAEGYRGDAAASERRFAPLRLpsGESLRMYRSGDRVR 920
Cdd:cd05967 404 EPLPIKAGSPgkpVPGYQVQVLDEDGEPVGPNELGNIVIKL-PLPPGCLLTLWKNDERFKKLYL--SKFPGYYDTGDAGY 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 921 LLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVraAAAGVVGegaaqrlvawVECA--GEDGFGQADLNQTDS- 997
Cdd:cd05967 481 KDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAV--AECAVVG----------VRDElkGQVPLGLVVLKEGVKi 548
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 998 DQTESERWHRALC-ERLPAYMVPTQFVALPRLPRNASGKIDRRALPAppvLAQAER-TPPRTAEESA 1062
Cdd:cd05967 549 TAEELEKELVALVrEQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRK---IADGEDyTIPSTIEDPS 612
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
665-967 |
8.92e-04 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 45.19 E-value: 8.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 665 NGSGENaaPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVdTTLEQILAaws 738
Cdd:PRK06334 176 GVSDKD--PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMsflppfHAYGFNS-CTLFPLLS--- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 739 rGACVVARPDElLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRwfELGLDRR 818
Cdd:PRK06334 250 -GVPVVFAYNP-LYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQE--ALKTFPH 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 819 CALINAYGPTEATISSHYHRVQAIDASRPVplGQLLPGRIAAVLDAHGRI-VPRGVCGELALGGIGLAEGYRGdaAASER 897
Cdd:PRK06334 326 IQLRQGYGTTECSPVITINTVNSPKHESCV--GMPIRGMDVLIVSEETKVpVSSGETGLVLTRGTSLFSGYLG--EDFGQ 401
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 898 RFAPLrlpSGESlrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQ---LPQVRAAAAGVV 967
Cdd:PRK06334 402 GFVEL---GGET--WYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEgfgQNAADHAGPLVV 469
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
1726-1910 |
9.19e-04 |
|
Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380460 [Multi-domain] Cd Length: 395 Bit Score: 44.87 E-value: 9.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1726 LVWSIHHLIVDGWSTPLLVGEMLQRYtagaQGATLRLPPAPgfqaYLDWR--ERQDLARQRGWWRERLSGYAGTAALPAP 1803
Cdd:cd19537 110 LLVVMSHIICDLTTLQLLLREVSAAY----NGKLLPPVRRE----YLDSTawSRPASPEDLDFWSEYLSGLPLLNLPRRT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1804 VAAAHHPVQREeceRRLSAHDSERLRAFCRERGCTLSDL-IAMVwGLANARYGNHDDVVLGATRSGRPPElaGVESMVGV 1882
Cdd:cd19537 182 SSKSYRGTSRV---FQLPGSLYRSLLQFSTSSGITLHQLaLAAV-ALALQDLSDRTDIVLGAPYLNRTSE--EDMETVGL 255
|
170 180 190
....*....|....*....|....*....|..
gi 1246793773 1883 FINTLPLRLR--IDAGQPALDLLSALR--SQS 1910
Cdd:cd19537 256 FLEPLPIRIRfpSSSDASAADFLRAVRrsSQA 287
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
2049-2200 |
9.41e-04 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 45.34 E-value: 9.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2049 PAQAVAVEEGAAS-WTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWL------------- 2114
Cdd:cd05943 85 PAAIYAAEDGERTeVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSscspdfgvpgvld 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2115 ---PLDP--------------QH-------------PDARQIAVLDDSGARIVIGWGAAPAWVpasvrWLDaesvlDVVS 2164
Cdd:cd05943 165 rfgQIEPkvlfavdaytyngkRHdvrekvaelvkglPSLLAVVVVPYTVAAGQPDLSKIAKAL-----TLE-----DFLA 234
|
170 180 190
....*....|....*....|....*....|....*...
gi 1246793773 2165 AYEEPPR--VDVDADTPAYLIYTSGSTGTPKGVVVSQG 2200
Cdd:cd05943 235 TGAAGELefEPLPFDHPLYILYSSGTTGLPKCIVHGAG 272
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
3811-3927 |
1.04e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 45.09 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3811 YGITETTVHVSFHRLSDEDLQSptsrIGSAL-PDLAVHVL-----DAAGQPvPLGvvgELVVEGDGVAQGYWQRPELTAE 3884
Cdd:PTZ00342 493 YGLTETTGPIFVQHADDNNTES----IGGPIsPNTKYKVRtwetyKATDTL-PKG---ELLIKSDSIFSGYFLEKEQTKN 564
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1246793773 3885 RFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKL-RGYRIE 3927
Cdd:PTZ00342 565 AFTEDG---YFKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYIE 605
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
2447-2516 |
1.23e-03 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 40.22 E-value: 1.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 2447 EVEQVLAQLPGVEVAAVLALPGANG--------VLQLGAciQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGK 2516
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKgeapvafvVLKPGV--ELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
786-984 |
1.34e-03 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 44.37 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 786 DWRDLALRCLVVGGDVLPVALAQRwfelgLDRR--CALINAYGPTEATIS--------SHYHrvqaidasrpvpLGQLLp 855
Cdd:COG1541 199 DPRDLSLKKGIFGGEPWSEEMRKE-----IEERwgIKAYDIYGLTEVGPGvayeceaqDGLH------------IWEDH- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 856 gRIAAVLD-AHGRIVPRGVCGELALGGIGlAEGYrgdaaaserrfaPLrlpsgesLRmYRSGDRVRLLDDGE-------- 926
Cdd:COG1541 261 -FLVEIIDpETGEPVPEGEEGELVVTTLT-KEAM------------PL-------IR-YRTGDLTRLLPEPCpcgrthpr 318
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 927 -LQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAAGVV-GEGAAQRLVAWVECAGE 984
Cdd:COG1541 319 iGRILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVdREGGLDELTVRVELAPG 378
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
2746-2812 |
1.41e-03 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380455 [Multi-domain] Cd Length: 421 Bit Score: 44.37 E-value: 1.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2746 VLFAAHHLLVDAVSWGIIVDDLQHAYaerragRSPALAAEACGFGAWqaALRQLSAATLDGWRS---YWR 2812
Cdd:cd19532 125 LIFGYHHIAMDGVSFQIFLRDLERAY------NGQPLLPPPLQYLDF--AARQRQDYESGALDEdlaYWK 186
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
2063-2210 |
1.48e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 44.58 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2063 TYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGA------AWLpldpqHPDARQIAVLDDSGARI 2136
Cdd:PTZ00216 123 TYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMvaatvyANL-----GEDALAYALRETECKAI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2137 V------------IGWGAAPAWV-------PASVrwlDAESV-----LDVVS-----AYEEPPRVDVDADTPAYLIYTSG 2187
Cdd:PTZ00216 198 VcngknvpnllrlMKSGGMPNTTiiyldslPASV---DTEGCrlvawTDVVAkghsaGSHHPLNIPENNDDLALIMYTSG 274
|
170 180
....*....|....*....|...
gi 1246793773 2188 STGTPKGVVVSQGNLAnyvAGVL 2210
Cdd:PTZ00216 275 TTGDPKGVMHTHGSLT---AGIL 294
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
671-696 |
1.52e-03 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 44.51 E-value: 1.52e-03
10 20
....*....|....*....|....*.
gi 1246793773 671 AAPNQLAYILYTSGSTGIPKGVEVGH 696
Cdd:cd05927 111 PKPEDLATICYTSGTTGNPKGVMLTH 136
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
861-1036 |
1.69e-03 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 44.21 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 861 VLDAHGRI-VPR-GVC-GELALGGIGLAEGYRGDAAASERRFAplrlpSGeslrMYRSGDRVRLLDDGELQFLGRADFQV 937
Cdd:cd12118 323 VLDPETMKpVPRdGKTiGEIVFRGNIVMKGYLKNPEATAEAFR-----GG----WFHSGDLAVIHPDGYIEIKDRSKDII 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 938 KLRGYRIELEEIEHCLGQLPQVRAAAagVVG---EGAAQRLVAWVECagEDGfgqadlnqtdSDQTESE--RWHRalcER 1012
Cdd:cd12118 394 ISGGENISSVEVEGVLYKHPAVLEAA--VVArpdEKWGEVPCAFVEL--KEG----------AKVTEEEiiAFCR---EH 456
|
170 180
....*....|....*....|....
gi 1246793773 1013 LPAYMVPTQFVALPrLPRNASGKI 1036
Cdd:cd12118 457 LAGFMVPKTVVFGE-LPKTSTGKI 479
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
2629-2785 |
1.83e-03 |
|
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380456 [Multi-domain] Cd Length: 419 Bit Score: 43.90 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2629 GLTPIQH--WFFEQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARFQRDAAGQWQQTLG---------D 2697
Cdd:cd19533 3 PLTSAQRgvWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPytpvpirhiD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2698 WQADRFAHREADAGQREDL---LAQWQAGLsFDGALLRVlalpdpqdGDTRVLFAA--HHLLVDAVSWGIIVDDLQHAYA 2772
Cdd:cd19533 83 LSGDPDPEGAAQQWMQEDLrkpLPLDNDPL-FRHALFTL--------GDNRHFWYQrvHHIVMDGFSFALFGQRVAEIYT 153
|
170
....*....|...
gi 1246793773 2773 ERRAGRSPALAAE 2785
Cdd:cd19533 154 ALLKGRPAPPAPF 166
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
661-1041 |
2.19e-03 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 43.86 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 661 GAGENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDR-------------VLHVAGLAVD 727
Cdd:PRK07059 191 GARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAFEKKprpdqlnfvcalpLYHIFALTVC 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 728 TtleqiLAAWSRGACVVARPDellePQRFLAFLSERAITVTDLAPAyANELVRASV-ADDWRDLALRCLVV---GGDVLP 803
Cdd:PRK07059 271 G-----LLGMRTGGRNILIPN----PRDIPGFIKELKKYQVHIFPA-VNTLYNALLnNPDFDKLDFSKLIVangGGMAVQ 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 804 VALAQRWFELgldRRCALINAYGPTEATISSHYHRVQAIDASRPVplGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIG 883
Cdd:PRK07059 341 RPVAERWLEM---TGCPITEGYGLSETSPVATCNPVDATEFSGTI--GLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQ 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 884 LAEGY--RGDAAASerrfapLRLPSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQV-R 960
Cdd:PRK07059 416 VMAGYwnRPDETAK------VMTADG----FFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVlE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 961 AAAAGVVGEGAAQRLVAWVEcagedgfgQADLNQTDSDQteserwhRALC-ERLPAYMVPTQFVALPRLPRNASGKIDRR 1039
Cdd:PRK07059 486 VAAVGVPDEHSGEAVKLFVV--------KKDPALTEEDV-------KAFCkERLTNYKRPKFVEFRTELPKTNVGKILRR 550
|
..
gi 1246793773 1040 AL 1041
Cdd:PRK07059 551 EL 552
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
2062-2219 |
2.37e-03 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 43.95 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2062 WTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIG-- 2139
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAed 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2140 ----------WGAAPA------WVPASVRWLDAESVLDVVSAYE--------EPPRVD--VDADTP---AYLIYTSGSTG 2190
Cdd:cd17641 92 eeqvdklleiADRIPSvryviyCDPRGMRKYDDPRLISFEDVVAlgraldrrDPGLYEreVAAGKGedvAVLCTTSGTTG 171
|
170 180
....*....|....*....|....*....
gi 1246793773 2191 TPKGVVVSQGNLANYVAGVLPVLDLGEDA 2219
Cdd:cd17641 172 KPKLAMLSHGNFLGHCAAYLAADPLGPGD 200
|
|
| PRK09294 |
PRK09294 |
phthiocerol/phthiodiolone dimycocerosyl transferase; |
1719-1853 |
3.26e-03 |
|
phthiocerol/phthiodiolone dimycocerosyl transferase;
Pssm-ID: 181765 [Multi-domain] Cd Length: 416 Bit Score: 43.16 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1719 RGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGA-QGATLRLPPAPGFQAYldwrerQDLARQRGWWRERLSG---- 1793
Cdd:PRK09294 106 PDDGGARVTLYIHHSIADAHHSASLLDELWSRYTDVVtTGDPGPIRPQPAPQSL------EAVLAQRGIRRQALSGaerf 179
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 1794 ----YAGTAALPAPVAAAHHPVQREEC---ERRLSAHDSERLRAFCRERGCTLSDLIAMVWGLANAR 1853
Cdd:PRK09294 180 mpamYAYELPPTPTAAVLAKPGLPQAVpvtRCRLSKAQTSSLAAFGRRHRLTVNALVSAAILLAEWQ 246
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
875-1043 |
3.68e-03 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 43.29 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 875 GELALGGIGLAEGYRGDAAASERRFAplrlpSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLG 954
Cdd:PLN02479 403 GEIVMRGNMVMKGYLKNPKANEEAFA-----NG----WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVY 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 955 QLPQVRAAAagVVGEGAAQrlvaWVE--CAG---EDGFGQADLNQTDSDQTESERwhralcERLPAYMVPTQFVALPrLP 1029
Cdd:PLN02479 474 THPAVLEAS--VVARPDER----WGEspCAFvtlKPGVDKSDEAALAEDIMKFCR------ERLPAYWVPKSVVFGP-LP 540
|
170
....*....|....
gi 1246793773 1030 RNASGKIDRRALPA 1043
Cdd:PLN02479 541 KTATGKIQKHVLRA 554
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
672-696 |
4.14e-03 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 43.18 E-value: 4.14e-03
10 20
....*....|....*....|....*
gi 1246793773 672 APNQLAYILYTSGSTGIPKGVEVGH 696
Cdd:PLN02387 248 SPNDIAVIMYTSGSTGLPKGVMMTH 272
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
2321-2531 |
4.27e-03 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 43.01 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2321 IVNHYGPTETTVGILT-CTVPEEWPVEQGVPvGHPLAGNEAWVLDRF-GLPAPVGVAGELYLGGgNLSLGYWQRAEQTAE 2398
Cdd:PRK10524 383 VIDNYWQTETGWPILAiARGVEDRPTRLGSP-GVPMYGYNVKLLNEVtGEPCGPNEKGVLVIEG-PLPPGCMQTVWGDDD 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2399 RFV-AHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGV-EVAAV---LALPG----A 2469
Cdd:PRK10524 461 RFVkTYWSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVaEVAVVgvkDALKGqvavA 540
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 2470 NGVLQLGACIQG-----SLEG-VAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLLQQDDA 2531
Cdd:PRK10524 541 FVVPKDSDSLADrearlALEKeIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAEGRDP 608
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
529-1041 |
4.62e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 43.11 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 529 PAPRTVGNVVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRA 608
Cdd:PRK07470 1 PMSRRVMNLAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 609 GLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQ---------------------GLAGFAPSVAIAVDElKLDGAGENGS 667
Cdd:PRK07470 81 GAVWVPTNFRQTPDEVAYLAEASGARAMICHADfpehaaavraaspdlthvvaiGGARAGLDYEALVAR-HLGARVANAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 668 GENAAPnqlAYILYTSGSTGIPKGVEVGHAALA--AHIDAAAEALALSADDRVLHVAGLAVDTTLEQiLAAWSRGACVVA 745
Cdd:PRK07470 160 VDHDDP---CWFFFTSGTTGRPKAAVLTHGQMAfvITNHLADLMPGTTEQDASLVVAPLSHGAGIHQ-LCQVARGAATVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 746 RPDELLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFE-LGLdrrcALINA 824
Cdd:PRK07470 236 LPSERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAkLGK----VLVQY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 825 YGPTEAT-----ISSHYHRVQAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRF 899
Cdd:PRK07470 312 FGLGEVTgnitvLPPALHDAEDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 900 aplrlpsgeslR--MYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA-----GVVGEgaa 972
Cdd:PRK07470 392 -----------RdgWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVlgvpdPVWGE--- 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 973 qrlVAWVECAGEDGfgqadlnqTDSDQTESERWhraLCERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK07470 458 ---VGVAVCVARDG--------APVDEAELLAW---LDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
604-1041 |
4.92e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 42.76 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 604 GAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTD------AQGLAGFAPSVAIavdELKLDGAGENGSGENAAPNQLA 677
Cdd:PRK13391 68 AAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSaakldvARALLKQCPGVRH---RLVLDGDGELEGFVGYAEAVAG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 678 Y-------------ILYTSGSTGIPKGV-----EVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSR 739
Cdd:PRK13391 145 LpatpiadeslgtdMLYSSGTTGRPKGIkrplpEQPPDTPLPLTAFLQRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 740 GACVVARpdELLEPQRFLAFLSERAITVTDLAPAYANELVR--ASVADDWRDLALRCLVVGGDVLPVALAQrwfelgldr 817
Cdd:PRK13391 225 GGTVIVM--EHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKlpEEVRDKYDLSSLEVAIHAAAPCPPQVKE--------- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 818 rcALINAYGPT--EATISSHYHRVQAIDA----SRPVPLGQLLPGRIaAVLDAHGRIVPRGVCGELALGGiGLAEGYRGD 891
Cdd:PRK13391 294 --QMIDWWGPIihEYYAATEGLGFTACDSeewlAHPGTVGRAMFGDL-HILDDDGAELPPGEPGTIWFEG-GRPFEYLND 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 892 AAaserRFAPLRLPSGEslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA-GVVGEG 970
Cdd:PRK13391 370 PA----KTAEARHPDGT---WSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVfGVPNED 442
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 971 AAQRLVAWVECAgEDGFGQADLNQtdsdqtESERWHRalcERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK13391 443 LGEEVKAVVQPV-DGVDPGPALAA------ELIAFCR---QRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
2062-2198 |
5.29e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 42.77 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2062 WTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQ-HPDarQIA-VLDDSGARIVI- 2138
Cdd:PRK07008 40 YTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRlFPE--QIAyIVNHAEDRYVLf 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2139 -------------------GWGAA--PAWVPASV-------RWLDAESvldvvSAYEEPPrvdVDADTPAYLIYTSGSTG 2190
Cdd:PRK07008 118 dltflplvdalapqcpnvkGWVAMtdAAHLPAGStpllcyeTLVGAQD-----GDYDWPR---FDENQASSLCYTSGTTG 189
|
....*...
gi 1246793773 2191 TPKGVVVS 2198
Cdd:PRK07008 190 NPKGALYS 197
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
672-1024 |
6.50e-03 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 42.46 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 672 APNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARPDEL- 750
Cdd:cd05932 135 FPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLd 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 751 -----LEPQRFLAFLS-ERAIT-----VTDLAPA----------YANELVRASVADDWRDLALRCLVVGGDVLPVALAQR 809
Cdd:cd05932 215 tfvedVQRARPTLFFSvPRLWTkfqqgVQDKIPQqklnlllkipVVNSLVKRKVLKGLGLDQCRLAGCGSAPVPPALLEW 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 810 WFELGLDrrcaLINAYGPTEATISSHYHRVqaiDASRPVPLGQLLPGriaavldAHGRIVPRgvcGELALGGIGLAEGYR 889
Cdd:cd05932 295 YRSLGLN----ILEAYGMTENFAYSHLNYP---GRDKIGTVGNAGPG-------VEVRISED---GEILVRSPALMMGYY 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 890 GDAAASERRFAplrlPSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKL-RGYRIELEEIEHCLGQLPQVRAAAagVVG 968
Cdd:cd05932 358 KDPEATAEAFT----ADG----FLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVC--VIG 427
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 969 EGAAQRLVAWVecAGEDGFGQADlnqtDSDQTESERWHRALCERLPAYMVPTQFVA 1024
Cdd:cd05932 428 SGLPAPLALVV--LSEEARLRAD----AFARAELEASLRAHLARVNSTLDSHEQLA 477
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
2666-3180 |
6.90e-03 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 42.55 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2666 AAALADVAAAHPMLRARFQRDAAGQWQQTLGDWQADRFAHREADAGQREDLLAQWQAGLSFDGALLRVLALPDPQDGDTR 2745
Cdd:COG3321 869 QREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAA 948
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2746 VLFAAHHLLVDAVSWGIIVDDLQHAYAERRAGRSPALAAEACGFGAWQAALRQLSAATLDGWRSywRAQAADAEAIALPW 2825
Cdd:COG3321 949 AAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLL--AAAAAAAALLALAA 1026
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2826 QDSDNRYADTVHLHDRFERDWTERLLTQTARAYGNEPQEVLLTALALALRDGGDAATLWVEMEGHGRDDLGAGLDLSRTV 2905
Cdd:COG3321 1027 LLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAAL 1106
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2906 GWFTARYPLALHLPAGEDLGAALRSTKDRMRAVPDRGLGFGVLRYLHGELAELPVPQVCFNYLGQLRAGERDGWALCEEP 2985
Cdd:COG3321 1107 LLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALA 1186
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2986 DGGGRAGGNRRRHLLDVNAMLVDGELRLDWAWPQDAASREAMQALSRRYLAVLRELIACVQTAEPRPTLADLPLAGLDNA 3065
Cdd:COG3321 1187 AALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLA 1266
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3066 PLDALLSQHPQTQDVYPLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFAVQGLPS 3145
Cdd:COG3321 1267 AAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAA 1346
|
490 500 510
....*....|....*....|....*....|....*
gi 1246793773 3146 PRQLPHRQVSLPLAEQDWSGLEPAQARSRLSELQA 3180
Cdd:COG3321 1347 AAAAAAAAAAAAAAAALAAAAGAAAAAAALALAAL 1381
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
670-696 |
7.94e-03 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 42.20 E-value: 7.94e-03
10 20
....*....|....*....|....*..
gi 1246793773 670 NAAPNQLAYILYTSGSTGIPKGVEVGH 696
Cdd:cd17639 84 DGKPDDLACIMYTSGSTGNPKGVMLTH 110
|
|
|