|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
12-1595 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 818.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 12 LPAEKKEKLLRQLAQSGVSPSRIPIIK-ADPAQAIPLSFNQERLWFLQKYDSTATNYNLYVVYRLHGVVDMPMLTEALRH 90
Cdd:PRK12467 16 LPLEKRRLYLEKMQEEGVSFANLPIPQvRSAFERIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 91 VQARHAILRTRIIVRNDRPCQVIDDASSLVLDTVTLAAQAPTSA---LDAVIQQVINTRFDLARGPLWGVTQIIQPDQGC 167
Cdd:PRK12467 96 LVARHESLRTRFVQDEEGFRQVIDASLSLTIPLDDLANEQGRAResqIEAYINEEVARPFDLANGPLLRVRLLRLADDEH 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 168 HLVFCAHHIIIDGISLRLLFDELQQQYARLHAGNETSLPPPPLQYADYAFWQREWFQDTLLANELAYWRARLQDAPLLST 247
Cdd:PRK12467 176 VLVVTLHHIISDGWSMRVLVEELVQLYSAYSQGREPSLPALPIQYADYAIWQRSWLEAGERERQLAYWQEQLGGEHTVLE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 248 FPSLHPRPAQPSTHGSRFSITLDETLSLALKHVARTQETTPFVLMLTAFQLVLMRYAQQQRLVIGMPVSGRIRPELQSSI 327
Cdd:PRK12467 256 LPTDRPRPAVPSYRGARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLI 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 328 GYYASTAVIYTDFNGVEVGREALQRVKASVKETQGRQQLPFENLVNMLDLPRSLSHSPLFQILYIYHNHVT----PRAFT 403
Cdd:PRK12467 336 GFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQNTATggrdREGAQ 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 404 LAGAYWEQVTYHNQTVKYDMTVEVFQNDATFDVSFEYDLGLYDADVVKQIAEALRQHCLSLTSSLETPIGAIPLHapeTA 483
Cdd:PRK12467 416 LPGLTVEELSWARHTAQFDLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLL---DA 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 484 TPRRDPLNATNVP--WLGPQDVLRIIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRH 561
Cdd:PRK12467 493 EERARELVRWNAPatEYAPDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERS 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 562 RDVIATMLATWFVGACYVPFDIHQPAARLQrLMQRARLVCLVVRQPGEWGE------IVQLSLPELMQDMSNAIRYSTPC 635
Cdd:PRK12467 573 IEMVVGLLAVLKAGGAYVPLDPEYPQDRLA-YMLDDSGVRLLLTQSHLLAQlpvpagLRSLCLDEPADLLCGYSGHNPEV 651
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 636 ALLPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLTEAE 715
Cdd:PRK12467 652 ALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPD 731
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 716 RAADSFRMIPLIADYRPTLMQATPSFWHGLLMAGWRGD--PELCVLAGGEALPTKVAEEL--LRCCGSLWNLYGPTETTI 791
Cdd:PRK12467 732 CARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALprPQRALVCGGEALQVDLLARVraLGPGARLINHYGPTETTV 811
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 792 WSLKSQITQAE----NITLGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEP-GVPGGRM 866
Cdd:PRK12467 812 GVSTYELSDEErdfgNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPfGADGGRL 891
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 867 FRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPlHKALAAFIITSEPPS----- 941
Cdd:PRK12467 892 YRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDA-GLQLVAYLVPAAVADgaehq 970
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 942 -LFEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAEnFVA---DSSLVSPQTqalsDTEQMLLALWMRYLPI 1017
Cdd:PRK12467 971 aTRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPK-PDAsavQATFVAPQT----ELEKRLAAIWADVLKV 1045
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1018 KNVDPECDFFRLGGHSLLAVTLVAEINRTFHCALTLKDIFHYSTLRALSARIAQQSITDAAASQddwvivhdPEHRHQPF 1097
Cdd:PRK12467 1046 ERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALP--------DVDRDQPL 1117
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1098 PLTDVQRAYWLGRQTGATSIATHI------YHEFDVEHFNvtrftHAVNALIARHEMLRAR-VLPDG-TQQILAQVPAYQ 1169
Cdd:PRK12467 1118 PLSYAQERQWFLWQLEPGSAAYHIpqalrlKGPLDIEALE-----RSFDALVARHESLRTTfVQEDGrTRQVIHPVGSLT 1192
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1170 LEQRDLsaLSPNARNDALMAIRDRLSHHVHPADRWPLFDFSYSACTAQHGRLHFSLDLLIADALSMRTLQQELMMLYRE- 1248
Cdd:PRK12467 1193 LEEPLL--LAADKDEAQLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAy 1270
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1249 ---PHVSLPLLPFSFRDYvqALLVEQASEAYARDQ--AYWQRalpQLYGP-PTLPVQGDLAQLSAIRFVRRRHR--LSAH 1320
Cdd:PRK12467 1271 sqgQSLQLPALPIQYADY--AVWQRQWMDAGERARqlAYWKA---QLGGEqPVLELPTDRPRPAVQSHRGARLAfeLPPA 1345
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1321 NWGVLSALAQRTRITKTALLLTVFSQVLARWSLSPTFTLNLTLFNRPQGypNAEAVIGDFTAVSLLNVCYDSQHSYAHNA 1400
Cdd:PRK12467 1346 LAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRA--ETEGLIGFFVNTQVLRAEVDGQASFQQLL 1423
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1401 QRIQVQLWEDLEHRRFSGIRASEALIHSGRF-HAPMpvvFTSMLD---IDGETTAQDP----------RDTTRFTLcpDA 1466
Cdd:PRK12467 1424 QQVKQAALEAQAHQDLPFEQLVEALQPERSLsHSPL---FQVMFNhqrDDHQAQAQLPglsveslsweSQTAQFDL--TL 1498
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1467 NITQTPQvwldhqviELAGELHFNWDaveqLFDTTLLDQMFGAYCHALQALVAMPQSWWG-------VNSSLALPTVSAP 1539
Cdd:PRK12467 1499 DTYESSE--------GLQASLTYATD----LFEASTIERLAGHWLNLLQGLVADPERRLGeldlldeAERRQILEGWNAT 1566
|
1610 1620 1630 1640 1650
....*....|....*....|....*....|....*....|....*....|....*..
gi 1288439980 1540 VTQAPAptALLHHGLL-RQAALTPQETALISPIRELTYRQLSTAADHVARALLALGV 1595
Cdd:PRK12467 1567 HTGYPL--ARLVHQLIeDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGV 1621
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
31-1350 |
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: 785.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 31 PSRIPIIKADPAQAIPLSFNQERLWFLQKYDSTATNYNLYVVYRLHGVVDMPMLTEALRHVQARHAILRTRIIVRNDRPC 110
Cdd:COG1020 4 AAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 111 QVIDDASSLVLDTVTLAAQAPTSALDAVIQQVIN---TRFDLARGPLWGVTQIIQPDQGCHLVFCAHHIIIDGISLRLLF 187
Cdd:COG1020 84 QVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAealAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 188 DELQQQYARLHAGNETSLPPPPLQYADYAFWQREWFQDTLLANELAYWRARLQDAPLLSTFPSLHPRPAQPSTHGSRFSI 267
Cdd:COG1020 164 AELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 268 TLDETLSLALKHVARTQETTPFVLMLTAFQLVLMRYAQQQRLVIGMPVSGRIRPELQSSIGYYASTAVIYTDFNGVEVGR 347
Cdd:COG1020 244 RLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 348 EALQRVKASVKETQGRQQLPFENLVNMLDLPRSLSHSPLFQILYIYHNHVTPrAFTLAGAYWEQVTYHNQTVKYDMTVEV 427
Cdd:COG1020 324 ELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPAD-ELELPGLTLEPLELDSGTAKFDLTLTV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 428 FQNDATFDVSFEYDLGLYDADVVKQIAEALRQHCLSLTSSLETPIGAIPLHAPETATPRRDPLNATNVPWLGPQDVLRII 507
Cdd:COG1020 403 VETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELF 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 508 EQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPA 587
Cdd:COG1020 483 EAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPA 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 588 ARLQRLMQRARLVCLVVrQPGEWGEIVQLSLPELMQDMSNAIRYST---PCALLPDMQAYLLFTSGSTGEPKGVCVVHRG 664
Cdd:COG1020 563 ERLAYMLEDAGARLVLT-QSALAARLPELGVPVLALDALALAAEPAtnpPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRA 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 665 LLNLLLDMQRTFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLTEAERAADSFRMIPLIADYRPTLMQATPSFWHG 744
Cdd:COG1020 642 LVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRA 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 745 LLMAGWRGDPEL-CVLAGGEALPTKVAEELLRCCGS--LWNLYGPTETTIWSLKSQITQAE----NITLGAPIANTRIYI 817
Cdd:COG1020 722 LLDAAPEALPSLrLVLVGGEALPPELVRRWRARLPGarLVNLYGPTETTVDSTYYEVTPPDadggSVPIGRPIANTRVYV 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 818 LDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEP-GVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGY 896
Cdd:COG1020 802 LDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPfGFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGF 881
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 897 RIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIIT-SEPPSLFEQLKNELRQQLPDYMVPTLWQRVADFPNTDNG 975
Cdd:COG1020 882 RIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPeAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNG 961
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 976 KIDRKRLAENFVADSSLVSPQTQALSDTEQMLLALWmryLPIKNVDPECDFFRLGGHSLLAVTLVAEINRTFHCALTLKD 1055
Cdd:COG1020 962 KLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLL---LLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLL 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1056 IFHYSTLRALSARIAQQSITDAAASQDDWVIVHDPEHRHQPFPLTDVQRAYWLGRQTGATSIATHIYHEFDVEHfnvtrf 1135
Cdd:COG1020 1039 LFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALL------ 1112
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1136 tHAVNALIARHEMLRARVLPDGTQQILAQVPAYQLEQRDLSALSPNARNDALMAIRDRLSHHVHPADRWPLFDFSYSACT 1215
Cdd:COG1020 1113 -LLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLL 1191
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1216 AQHGRLHFSLDLLIADALSMRTLQQELMMLYREPHVSLPLLPFSFRDYVQALLVEQASEAYARDQAYW-QRALPQLYGPP 1294
Cdd:COG1020 1192 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALlALALALLALAL 1271
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*.
gi 1288439980 1295 TLPVQGDLAQLSAIRFVRRRHRLSAHNWGVLSALAQRTRITKTALLLTVFSQVLAR 1350
Cdd:COG1020 1272 LLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLA 1327
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
12-1519 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 707.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 12 LPAEKKEKLLRQLAQSGVSPSRIPII-KADPAQAIPLSFNQERLWFLQKYDSTATNYNLYVVYRLHGVVDMPMLTEALRH 90
Cdd:PRK12316 16 LPLEKRRVFLATLRGEGVDFSLFPIPaGVSSAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFAS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 91 VQARHAILRTRIIVRNDRPCQVIDDASSLVLDTVTLAAQAPTS---ALDAVIQQVINTRFDLARGPLWGVTQIIQPDQGC 167
Cdd:PRK12316 96 LVQRHETLRTVFPRGADDSLAQVPLDRPLEVEFEDCSGLPEAEqeaRLRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEH 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 168 HLVFCAHHIIIDGISLRLLFDELQQQYARLHAGNETSLPPPPLQYADYAFWQREWFQDTLLANELAYWRARLQDAPLLST 247
Cdd:PRK12316 176 VLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRAQLGEEHPVLE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 248 FPSLHPRPAQPSTHGSRFSITLDETLSLALKHVARTQETTPFVLMLTAFQLVLMRYAQQQRLVIGMPVSGRIRPELQSSI 327
Cdd:PRK12316 256 LPTDHPRPAVPSYRGSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLI 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 328 GYYASTAVIYTDFNGVEVGREALQRVKASVKETQGRQQLPFENLVNMLDLPRSLSHSPLFQILYIYHNHVT--PRAFTLA 405
Cdd:PRK12316 336 GFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYNHQPLVAdiEALDTVA 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 406 GAYWEQVTYHNQTVKYDMTVEVFQNDATFDVSFEYDLGLYDADVVKQIAEALRQHCLSLTSSLETPIGAIPLHAPETATP 485
Cdd:PRK12316 416 GLEFGQLEWKSRTTQFDLTLDTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQ 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 486 RRDPLNATNVPWLGPQDVLRIIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVI 565
Cdd:PRK12316 496 LVEGWNATAAEYPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMV 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 566 ATMLATWFVGACYVPFDIHQPAARLQRLMQRARLVCLVVRQpgewGEIVQLSLPELMQDM---------SNAIRYSTPCA 636
Cdd:PRK12316 576 VALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQS----HLGRKLPLAAGVQVLdldrpaawlEGYSEENPGTE 651
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 637 LLPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLTEAER 716
Cdd:PRK12316 652 LNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGD 731
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 717 AADSFRMIPLIADYRPTLMQATPSFWHGLLMAgwrGDPELC-----VLAGGEALPTKVAEEL--LRCCGSLWNLYGPTET 789
Cdd:PRK12316 732 HRDPAKLVELINREGVDTLHFVPSMLQAFLQD---EDVASCtslrrIVCSGEALPADAQEQVfaKLPQAGLYNLYGPTEA 808
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 790 TI----WSLKSQItqAENITLGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEPGVPGGR 865
Cdd:PRK12316 809 AIdvthWTCVEEG--GDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGER 886
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 866 MFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLhkaLAAFIITSEPPSLFEQ 945
Cdd:PRK12316 887 MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKQL---VGYVVLESEGGDWREA 963
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 946 LKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRL--AENFVADSSLVSPQTqalsDTEQMLLALWMRYLPIKNVDPE 1023
Cdd:PRK12316 964 LKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALpaPEASVAQQGYVAPRN----ALERTLAAIWQDVLGVERVGLD 1039
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1024 CDFFRLGGHSLLAVTLVAEInRTFHCALTLKDIFHYSTLR--ALSARIAQQSITDAAASQDDwvivhdpehrhqpFPLTD 1101
Cdd:PRK12316 1040 DNFFELGGDSIVSIQVVSRA-RQAGIQLSPRDLFQHQTIRslALVAKAGQATAADQGPASGE-------------VALAP 1105
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1102 VQRAYWL----GRQTGATSIATHIYHEFDVEhfnvtRFTHAVNALIARHEMLRAR-VLPDGT--QQILAQVPAYQLEQRD 1174
Cdd:PRK12316 1106 VQRWFFEqaipQRQHWNQSLLLQARQPLDPD-----RLGRALERLVAHHDALRLRfREEDGGwqQAYAAPQAGEVLWQRQ 1180
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1175 LsalspnARNDALMAIRDR----LSHHVHPADRWPLFDFSYSActaqhGRLHFSLDLLIADALSMRTLQQELMMLYREPH 1250
Cdd:PRK12316 1181 A------ASEEELLALCEEaqrsLDLEQGPLLRALLVDMADGS-----QRLLLVIHHLVVDGVSWRILLEDLQRAYADLD 1249
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1251 VSLPLLPFSFRDYVQaLLVEQASeAYARDQAYWQRALPQlyGPPTLPV---QGDLAQlsaiRFVRRRH-RLSAHNWGVL- 1325
Cdd:PRK12316 1250 ADLPARTSSYQAWAR-RLHEHAG-ARAEELDYWQAQLED--APHELPCenpDGALEN----RHERKLElRLDAERTRQLl 1321
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1326 --SALAQRTRITKtaLLLTVFSQVLARWSLSPTFTLNLTLFNRPQGYPNAE--AVIGDFTAVSLLNVCYDSQHSYAHNAQ 1401
Cdd:PRK12316 1322 qeAPAAYRTQVND--LLLTALARVTCRWSGQASVLVQLEGHGREDLFEDIDlsRTVGWFTSLFPVRLTPAADLGESIKAI 1399
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1402 RIQVQLWED-------LEHRRFSGIRASEALIHSGRfhapmpVVFTSMLDIDGE--------------TTAQDPRdttrf 1460
Cdd:PRK12316 1400 KEQLRAVPDkgigyglLRYLAGEEAAARLAALPQPR------ITFNYLGQFDRQfdeaalfvpatesaGAAQDPC----- 1468
|
1530 1540 1550 1560 1570 1580
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1288439980 1461 tlCPDANitqtpqvWL--DHQVieLAGELHFNWDAVEQLFDTTLLDQMFGAYCHALQALVA 1519
Cdd:PRK12316 1469 --APLAN-------WLsiEGQV--YGGELSLHWSFSREMFAEATVQRLADDYARELQALIE 1518
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
35-1518 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 686.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 35 PIIKADPAQAIPLSFNQERLWFLQKYDSTATNYNLYVVYRLHGVVDMPMLTEALRHVQARHAILRTRIIVRNDRPCQVID 114
Cdd:PRK12467 1107 ALPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIH 1186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 115 DASSLVLDTVTL-AAQAPTSALDAVIQQVINTRFDLARGPLWGVTQIIQPDQGCHLVFCAHHIIIDGISLRLLFDELQQQ 193
Cdd:PRK12467 1187 PVGSLTLEEPLLlAADKDEAQLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVAL 1266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 194 YARLHAGNETSLPPPPLQYADYAFWQREWFQDTLLANELAYWRARL-QDAPLLStFPSLHPRPAQPSTHGSRFSITLDET 272
Cdd:PRK12467 1267 YAAYSQGQSLQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLgGEQPVLE-LPTDRPRPAVQSHRGARLAFELPPA 1345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 273 LSLALKHVARTQETTPFVLMLTAFQLVLMRYAQQQRLVIGMPVSGRIRPELQSSIGYYASTAVIYTDFNGVEVGREALQR 352
Cdd:PRK12467 1346 LAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQ 1425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 353 VKASVKETQGRQQLPFENLVNMLDLPRSLSHSPLFQILYIYHNHVTPRAFTLAGAYWEQVTYHNQTVKYDMTVEVFQNDA 432
Cdd:PRK12467 1426 VKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQAQLPGLSVESLSWESQTAQFDLTLDTYESSE 1505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 433 TFDVSFEYDLGLYDADVVKQIAEALRQHCLSLTSSLETPIGAIPLHAPETATPRRDPLNATNVPWLGPQDVLRIIEQRCV 512
Cdd:PRK12467 1506 GLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLIEDQAA 1585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 513 QHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQR 592
Cdd:PRK12467 1586 ATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAY 1665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 593 LMQ--RARLV-----------------CLVVRQPGEWGEivqlslpelMQDMSNAIrystpCALLPDMQAYLLFTSGSTG 653
Cdd:PRK12467 1666 MIEdsGIELLltqshlqarlplpdglrSLVLDQEDDWLE---------GYSDSNPA-----VNLAPQNLAYVIYTSGSTG 1731
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 654 EPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLTEAERAADSFRMIPLIADYRPT 733
Cdd:PRK12467 1732 RPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVT 1811
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 734 LMQATPSFWHGLL-MAGWRGDPELC--VLAGGEALPTKVAEELLRCCG--SLWNLYGPTETTI----WSLK-SQITQAEN 803
Cdd:PRK12467 1812 TLHFVPSMLQQLLqMDEQVEHPLSLrrVVCGGEALEVEALRPWLERLPdtGLFNLYGPTETAVdvthWTCRrKDLEGRDS 1891
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 804 ITLGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEP-GVPGGRMFRTGDLVRSDAQGQLF 882
Cdd:PRK12467 1892 VPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPfGTVGSRLYRTGDLARYRADGVIE 1971
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 883 FVGRKDSQIKLRGYRIELGEIERTLARHPHV-DAAVVACieRAPLHKALAAFIITSEPP---------SLFEQLKNELRQ 952
Cdd:PRK12467 1972 YLGRIDHQVKIRGFRIELGEIEARLREQGGVrEAVVIAQ--DGANGKQLVAYVVPTDPGlvdddeaqvALRAILKNHLKA 2049
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 953 QLPDYMVPTLWQRVADFPNTDNGKIDRKRL--AENFVADSSLVSPQTQAlsdtEQMLLALWMRYLPIKNVDPECDFFRLG 1030
Cdd:PRK12467 2050 SLPEYMVPAHLVFLARMPLTPNGKLDRKALpaPDASELQQAYVAPQSEL----EQRLAAIWQDVLGLEQVGLHDNFFELG 2125
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1031 GHSLLAVTLVAEiNRTFHCALTLKDIFHYSTLRALSArIAQQsiTDAAASQDDWVIVHDpehrhqpFPLTDVQRAYWLG- 1109
Cdd:PRK12467 2126 GDSIISIQVVSR-ARQAGIRFTPKDLFQHQTVQSLAA-VAQE--GDGTVSIDQGPVTGD-------LPLLPIQQMFFADd 2194
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1110 ---RQTGATSIATHIYHEFDVEHFNvtrftHAVNALIARHEMLRARVLPDGTQQILAQVPAYQLEQRDL--SALSPNARN 1184
Cdd:PRK12467 2195 ipeRHHWNQSVLLEPREALDAELLE-----AALQALLVHHDALRLGFVQEDGGWSAMHRAPEQERRPLLwqVVVADKEEL 2269
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1185 DALMAIRDR---LSHHvhpadrwPLFDFSYSACTAQHGRLHFSLDLLIADALSMRTLQQELMMLYREPH----VSLPLLP 1257
Cdd:PRK12467 2270 EALCEQAQRsldLEEG-------PLLRAVLATLPDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQggqpVKLPAKT 2342
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1258 FSFRDYVQALLVEQASEAYARDQAYWQRalpQLYGPPT-LPvqGDLAQLSairfVRRRHRLSAHNWgvLSA--------- 1327
Cdd:PRK12467 2343 SAFKAWAERLQTYAASAALADELGYWQA---QLQGASTeLP--CDHPQGG----LQRRHAASVTTH--LDSewtrrllqe 2411
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1328 --LAQRTRITKtaLLLTVFSQVLARWSLSPTFTLNLTLFNRPQGYPNAE--AVIGDFTavSLLNVCYDSQHSYAHNAQRI 1403
Cdd:PRK12467 2412 apAAYRTQVND--LLLTALARVIARWTGQASTLIQLEGHGREDLFDEIDltRTVGWFT--SLYPVKLSPTASLATSIKTI 2487
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1404 QVQLwEDLEHR--RFSGIR--ASEALIHSGRfHAPMP-VVFTSMLDIDGETTAQ---------DPRDTTRFTLCPDANit 1469
Cdd:PRK12467 2488 KEQL-RAVPNKglGFGVLRylGSEAARQTLQ-ALPVPrITFNYLGQFDGSFDAEkqalfvpsgEFSGAEQSEEAPLGN-- 2563
|
1530 1540 1550 1560 1570
....*....|....*....|....*....|....*....|....*....|.
gi 1288439980 1470 qtpqvWL--DHQVieLAGELHFNWDAVEQLFDTTLLDQMFGAYCHALQALV 1518
Cdd:PRK12467 2564 -----WLsiNGQV--YGGELNLGWTFSQEMFDEATIQRLADAYAEELRALI 2607
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
25-1519 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 663.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 25 AQSGVSPSRIPIIKADPAQAIPLSFNQERLWFLQKYDSTATNYNLYVVYRLHGVVDMPMLTEALRHVQARHAILRTRIIV 104
Cdd:PRK12316 2583 LESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVE 2662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 105 RNDRPCQVIDDASSLVlDTVTLAAQAPTSALDAVIQQVINTRFDLARGPLWGVTQIIQPDQGCHLVFCAHHIIIDGISLR 184
Cdd:PRK12316 2663 VGEQTRQVILPNMSLR-IVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQ 2741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 185 LLFDELQQQYARLHAGNETSLPPPPLQYADYAFWQREWFQDTLLANELAYWRARLQDAPLLSTFPSLHPRPAQPSTHGSR 264
Cdd:PRK12316 2742 VMVDELVQAYAGARRGEQPTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHRGAR 2821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 265 FSITLDETLSLALKHVARTQETTPFVLMLTAFQLVLMRYAQQQRLVIGMPVSGRIRPELQSSIGYYASTAVIYTDFNGVE 344
Cdd:PRK12316 2822 LDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQL 2901
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 345 VGREALQRVKASVKETQGRQQLPFENLVNMLDLPRSLSHSPLFQILYIYHNHVTPRAfTLAGAYWEQVTYHNQTVKYDMT 424
Cdd:PRK12316 2902 AFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERAAA-QLPGLHIESFAWDGAATQFDLA 2980
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 425 VEVFQNDATFDVSFEYDLGLYDADVVKQIAEALRQHCLSLTSSLETPIGAIPLHAPETATPRRDPLNATNVPWLGPQDVL 504
Cdd:PRK12316 2981 LDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAAEYPLERGVH 3060
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 505 RIIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIH 584
Cdd:PRK12316 3061 RLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPE 3140
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 585 QPAARLQRLMQRARLVCLVVRQPGEWGEIVQLSLPELMQDMSNAIRYSTPCALLPDMQAYLLFTSGSTGEPKGVCVVHRG 664
Cdd:PRK12316 3141 YPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSA 3220
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 665 LLNLLLDMQRTFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLTEAERAADSFRMIPLIADYRPTLMQATPSFWHG 744
Cdd:PRK12316 3221 LSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQA 3300
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 745 LL--MAGWRGDPELCVLAGGEALPTKVAEELLrCCGSLWNLYGPTETTIWSLKSQITQAENITL--GAPIANTRIYILDN 820
Cdd:PRK12316 3301 FLeeEDAHRCTSLKRIVCGGEALPADLQQQVF-AGLPLYNLYGPTEATITVTHWQCVEEGKDAVpiGRPIANRACYILDG 3379
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 821 EGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEPGVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIEL 900
Cdd:PRK12316 3380 SLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIEL 3459
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 901 GEIERTLARHPHVDAAVVACIERAPLhkaLAAFIITSEPPSLFEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRK 980
Cdd:PRK12316 3460 GEIEARLLEHPWVREAVVLAVDGRQL---VAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRK 3536
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 981 RLAENFVADS--SLVSPQTQAlsdtEQMLLALWMRYLPIKNVDPECDFFRLGGHSLLAVTLVAEInRTFHCALTLKDIFH 1058
Cdd:PRK12316 3537 ALPRPDAALLqqDYVAPVNEL----ERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRA-RQAGIRFTPKDLFQ 3611
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1059 YSTLRALS--ARIAQQSITDAAASQDDWVIVHDpehRHQPFPLTDVQRAYWLGRQTGATSiathiyhefdvEHFNVTRFT 1136
Cdd:PRK12316 3612 HQTIQGLArvARVGGGVAVDQGPVSGETLLLPI---QQQFFEEPVPERHHWNQSLLLKPR-----------EALDAAALE 3677
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1137 HAVNALIARHEMLRARVLPDGtqqilAQVPAYQLEQRDLSALSPNARNDALMAIRDRLSHHVHPAD--RWPLFDFSYSAC 1214
Cdd:PRK12316 3678 AALQALVEHHDALRLRFVEDA-----GGWTAEHLPVELGGALLWRAELDDAEELERLGEEAQRSLDlaDGPLLRALLATL 3752
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1215 TAQHGRLHFSLDLLIADALSMRTLQQELMMLYRE----PHVSLPLLPFSFRDYVQALLVEQASEAYARDQAYWQRALPQL 1290
Cdd:PRK12316 3753 ADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQllqgEAPRLPAKTSSFKAWAERLQEHARGEALKAELAYWQEQLQGV 3832
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1291 YGP-PTLPVQGDLAQLSAIRFVRRRHRLSAHNWGVLSALAQRTRITKtaLLLTVFSQVLARWSLSPTFTLNLTLFNRPQG 1369
Cdd:PRK12316 3833 SSElPCDHPQGALQNRHAASVQTRLDRELTRRLLQQAPAAYRTQVND--LLLTALARVVCRWTGEASALVQLEGHGREDL 3910
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1370 YPNAE--AVIGDFTAVSLLNVCydSQHSYAHNAQRIQVQLWEDLEHRRFSGIRASEALIHSGRFHAPMPV---VFTSMLD 1444
Cdd:PRK12316 3911 FADIDlsRTVGWFTSLFPVRLS--PVEDLGASIKAIKEQLRAIPNKGIGFGLLRYLGDEESRRTLAGLPVpriTFNYLGQ 3988
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1445 IDGETTAQ----DP-RDTTRFTLCPDANITQtpqvWLDHQVIELAGELHFNWDAVEQLFDTTLLDQMFGAYCHALQALVA 1519
Cdd:PRK12316 3989 FDGSFDEEmalfVPaGESAGAEQSPDAPLDN----WLSLNGRVYGGELSLDWTFSREMFEEATIQRLADDYAAELTALVE 4064
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
22-1595 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 620.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 22 RQLAQSGVSPSRIPIIKADpaQAIPLSFNQERLWFLQKYDSTATNYNLYVVYRLHGVVDMPMLTEALRHVQARHAILRTR 101
Cdd:PRK05691 655 RQLAGGGAAQAAIARLPRG--QALPQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTR 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 102 IIVRNDRPCQVIDDASSLVLDTVTLAAqAPTSALDAVIQQV----INTRFDLARGPLWGVTQIIQPDQGCHLVFCAHHII 177
Cdd:PRK05691 733 FYERDGVALQRIDAQGEFALQRIDLSD-LPEAEREARAAQIreeeARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIV 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 178 IDGISLRLLFDELQQQYARLHAGNETSLPPPPLQYADYAFWQREWFQDTLLANELAYWRARLQDAPLLSTFPSLHPRPAQ 257
Cdd:PRK05691 812 ADGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPVLELATDHPRSAR 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 258 PSTHGSRFSITLDETLSLALKHVARTQETTPFVLMLTAFQLVLMRYAQQQRLVIGMPVSGRIRPELQSSIGYYASTAVIY 337
Cdd:PRK05691 892 QAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLR 971
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 338 TDFNGVEVGREALQRVKASVKETQGRQQLPFENLVNMldLPRSLSHSpLFQILYIYHNHVTPRAFTLAGAYWEQVTYHNQ 417
Cdd:PRK05691 972 AQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEA--LPQAREQG-LFQVMFNHQQRDLSALRRLPGLLAEELPWHSR 1048
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 418 TVKYDMTVEVFQ-NDATFDVSFEYDLGLYDADVVKQIAEALRQHCLSLTSSLETPIGAIPLHapeTATPRRDPLNATNVP 496
Cdd:PRK05691 1049 EAKFDLQLHSEEdRNGRLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLL---DAAERAQLAQWGQAP 1125
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 497 WLGPQDVL-RIIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVG 575
Cdd:PRK05691 1126 CAPAQAWLpELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAG 1205
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 576 ACYVPFDIHQPAARLQRLMQRARLVCLVV------RQPGEWGEIVqLSLPELmqDMSNAIRYSTPCALLPDMQAYLLFTS 649
Cdd:PRK05691 1206 GAYVPLDPDYPAERLAYMLADSGVELLLTqshlleRLPQAEGVSA-IALDSL--HLDSWPSQAPGLHLHGDNLAYVIYTS 1282
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 650 GSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLTEAERAADSFRMIPLIAD 729
Cdd:PRK05691 1283 GSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQ 1362
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 730 YRPTLMQATPSfwhglLMAGWRGDPEL--C-----VLAGGEALPTKVAEELLRCCG--SLWNLYGPTETTI----WslKS 796
Cdd:PRK05691 1363 YGVTTLHFVPP-----LLQLFIDEPLAaaCtslrrLFSGGEALPAELRNRVLQRLPqvQLHNRYGPTETAInvthW--QC 1435
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 797 QITQAENITLGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEP-GVPGGRMFRTGDLVRS 875
Cdd:PRK05691 1436 QAEDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPlGEDGARLYRTGDRARW 1515
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 876 DAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEPPSLFEQLKNELRQQLP 955
Cdd:PRK05691 1516 NADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEAGQEAEAERLKAALAAELP 1595
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 956 DYMVPTLWQRVADFPNTDNGKIDRKRLAENFVADSSLVSPQTqalsDTEQMLLALWMRYLPIKNVDPECDFFRLGGHSLL 1035
Cdd:PRK05691 1596 EYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQREHVEPRT----ELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLL 1671
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1036 AVTLVAEINRTFHCALTLKDIFHYSTLRALSARIAQQSITDAAASQDDWVIVhdpeHRHQPFPLTDVQRAYWLGRQTGAT 1115
Cdd:PRK05691 1672 ATQIVSRTRQACDVELPLRALFEASELGAFAEQVARIQAAGERNSQGAIARV----DRSQPVPLSYSQQRMWFLWQMEPD 1747
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1116 SIAthiYHEFDVEHFN----VTRFTHAVNALIARHEMLRArVLP--DGT--QQILAQvPAYQLEQRDLSALSPNARNDAL 1187
Cdd:PRK05691 1748 SPA---YNVGGMARLSgvldVDRFEAALQALILRHETLRT-TFPsvDGVpvQQVAED-SGLRMDWQDFSALPADARQQRL 1822
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1188 MAIRDRLSHHVHPADRWPLFdfsySACTAQHG-RLHF---SLDLLIADALSMRTLQQELMMLYR----EPHVSLPLLPFS 1259
Cdd:PRK05691 1823 QQLADSEAHQPFDLERGPLL----RACLVKAAeREHYfvlTLHHIVTEGWAMDIFARELGALYEafldDRESPLEPLPVQ 1898
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1260 FRDYVQALLVEQASEAYARDQAYWQRAL----PQLYGP---PTLPVQGdlaqlsairfvrrrHRLSAHNWGVLSALAQRT 1332
Cdd:PRK05691 1899 YLDYSVWQRQWLESGERQRQLDYWKAQLgnehPLLELPadrPRPPVQS--------------HRGELYRFDLSPELAARV 1964
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1333 RITKTALLLTVF-------SQVLARWSLSPTFTLNLTLFNRPQgyPNAEAVIGDFTAVSLLNVCYDSQHSYAHNAQRIQV 1405
Cdd:PRK05691 1965 RAFNAQRGLTLFmtmtatlAALLYRYSGQRDLRIGAPVANRIR--PESEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQ 2042
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1406 QLWEDLEHRRFSGIRASEALiHSGRFHAPMPvVFTSMLDIDgETTAQDPRDTTRFTLCPDANITQTPQVWLDHQVIELAG 1485
Cdd:PRK05691 2043 TVIEGQSHQDLPFDHLVEAL-QPPRSAAYNP-LFQVMCNVQ-RWEFQQSRQLAGMTVEYLVNDARATKFDLNLEVTDLDG 2119
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1486 ELHFNWDAVEQLFDTTLLDQMFGAYCHALQALVAMPQswwgvnSSLA-LPTVSAPVTQA-----------PAPTALLHHG 1553
Cdd:PRK05691 2120 RLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQ------QRLAeLPLLAAAEQQQlldslageageARLDQTLHGL 2193
|
1610 1620 1630 1640
....*....|....*....|....*....|....*....|..
gi 1288439980 1554 LLRQAALTPQETALISPIRELTYRQLSTAADHVARALLALGV 1595
Cdd:PRK05691 2194 FAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGV 2235
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
515-982 |
4.79e-165 |
|
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: 507.21 E-value: 4.79e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 515 PKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLM 594
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 595 QRARLVCLVVRQPGEWGEIVQLSLPELMQDMSNAIRYSTPCALLPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQR 674
Cdd:cd12116 81 EDAEPALVLTDDALPDRLPAGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 675 TFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLTEAERAADSFRMIPLIADYRPTLMQATPSFWHGLLMAGWRGDP 754
Cdd:cd12116 161 RLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLDAGWQGRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 755 ELCVLAGGEALPTKVAEELLRCCGSLWNLYGPTETTIWSLKSQITQA-ENITLGAPIANTRIYILDNEGHPVPQGVDGEL 833
Cdd:cd12116 241 GLTALCGGEALPPDLAARLLSRVGSLWNLYGPTETTIWSTAARVTAAaGPIPIGRPLANTQVYVLDAALRPVPPGVPGEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 834 YIAGDGVAQGYDGQPELNAQFFLSEP-GVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPH 912
Cdd:cd12116 321 YIGGDGVAQGYLGRPALTAERFVPDPfAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPG 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1288439980 913 V-DAAVVACIERAPLHkaLAAFIITSEPPSL-FEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRL 982
Cdd:cd12116 401 VaQAAVVVREDGGDRR--LVAYVVLKAGAAPdAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1096-1519 |
4.39e-164 |
|
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: 502.79 E-value: 4.39e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1096 PFPLTDVQRAYWLGRQTGAT--SIATHIYHEFDVEHFNVTRFTHAVNALIARHEMLRARVLPDGTQQILAQVPAYQLEQR 1173
Cdd:cd19535 1 PFPLTDVQYAYWIGRQDDQElgGVGCHAYLEFDGEDLDPDRLERAWNKLIARHPMLRAVFLDDGTQQILPEVPWYGITVH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1174 DLSALSPNARNDALMAIRDRLSHHVHPADRWPLFDFSYSACTAQHGRLHFSLDLLIADALSMRTLQQELMMLYREPHVSL 1253
Cdd:cd19535 81 DLRGLSEEEAEAALEELRERLSHRVLDVERGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYEDPGEPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1254 PLLPFSFRDYVQALLVEQASeAYARDQAYWQRALPQLYGPPTLPVQGDLAQLSAIRFVRRRHRLSAHNWGVLSALAQRTR 1333
Cdd:cd19535 161 PPLELSFRDYLLAEQALRET-AYERARAYWQERLPTLPPAPQLPLAKDPEEIKEPRFTRREHRLSAEQWQRLKERARQHG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1334 ITKTALLLTVFSQVLARWSLSPTFTLNLTLFNRPQGYPNAEAVIGDFTAVSLLNVCYDSQHSYAHNAQRIQVQLWEDLEH 1413
Cdd:cd19535 240 VTPSMVLLTAYAEVLARWSGQPRFLLNLTLFNRLPLHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQLWEDLDH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1414 RRFSGIR-ASEALIHSGRFHAPMPVVFTSMLDIDGETtaqdprDTTRFTL-CPDANITQTPQVWLDHQVIELAGELHFNW 1491
Cdd:cd19535 320 SSYSGVVvVRRLLRRRGGQPVLAPVVFTSNLGLPLLD------EEVREVLgELVYMISQTPQVWLDHQVYEEDGGLLLNW 393
|
410 420
....*....|....*....|....*...
gi 1288439980 1492 DAVEQLFDTTLLDQMFGAYCHALQALVA 1519
Cdd:cd19535 394 DAVDELFPEGMLDDMFDAYVRLLERLAD 421
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
21-1361 |
1.35e-162 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 549.00 E-value: 1.35e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 21 LRQLAQSGVSPSRIPIIKADPAQAIPLSFNQERLWFLQKYDSTATNYNLYVVYRLHGVVDMPMLTEALRHVQARHAILRT 100
Cdd:PRK05691 1705 VARIQAAGERNSQGAIARVDRSQPVPLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRT 1784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 101 RIIVRNDRPCQVIDDASSLVL---DTVTLAAQAPTSALDAVIQQVINTRFDLARGPLWGVTQIIQPDQGCHLVFCAHHII 177
Cdd:PRK05691 1785 TFPSVDGVPVQQVAEDSGLRMdwqDFSALPADARQQRLQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIV 1864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 178 IDGISLRLLFDELQQQYARLHAGNETSLPPPPLQYADYAFWQREWFQDTLLANELAYWRARLQDAPLLSTFPSLHPRPAQ 257
Cdd:PRK05691 1865 TEGWAMDIFARELGALYEAFLDDRESPLEPLPVQYLDYSVWQRQWLESGERQRQLDYWKAQLGNEHPLLELPADRPRPPV 1944
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 258 PSTHGSRFSITLDETLSLALKHVARTQETTPFVLMLTAFQLVLMRYAQQQRLVIGMPVSGRIRPELQSSIGYYASTAVIY 337
Cdd:PRK05691 1945 QSHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLR 2024
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 338 TDFNGVEVGREALQRVKASVKETQGRQQLPFENLVNMLDLPRSLSHSPLFQILYIYHNHVTPRAFTLAGAYWEQVTYHNQ 417
Cdd:PRK05691 2025 CQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEFQQSRQLAGMTVEYLVNDAR 2104
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 418 TVKYDMTVEVFQNDATFDVSFEYDLGLYDADVVKQIAEALRQHCLSLTSSLETPIGAIPLHAPETATPRRDPLNATNVPW 497
Cdd:PRK05691 2105 ATKFDLNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEAGEA 2184
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 498 LGPQDVLRIIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGAC 577
Cdd:PRK05691 2185 RLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGA 2264
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 578 YVPFDIHQPAARLQRLMQRARLVCLVVRQP-----GEW-GEIVQLSLPELMQDMSNAIRYSTPCALLPDMQAYLLFTSGS 651
Cdd:PRK05691 2265 YVPLDPEYPLERLHYMIEDSGIGLLLSDRAlfealGELpAGVARWCLEDDAAALAAYSDAPLPFLSLPQHQAYLIYTSGS 2344
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 652 TGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLtEAERAADSFRMIPLIADYR 731
Cdd:PRK05691 2345 TGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVL-RAQGQWGAEEICQLIREQQ 2423
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 732 PTLMQATPSFwhGLLMAGW---RGD--PELCVLAGGEALptkVAEELLRCCG-----SLWNLYGPTETTIWSLKSQITQ- 800
Cdd:PRK05691 2424 VSILGFTPSY--GSQLAQWlagQGEqlPVRMCITGGEAL---TGEHLQRIRQafapqLFFNAYGPTETVVMPLACLAPEq 2498
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 801 ----AENITLGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEPGVP-GGRMFRTGDLVRS 875
Cdd:PRK05691 2499 leegAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdGGRLYRTGDLVRL 2578
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 876 DAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIErAPLHKALAAFIITS-------EPPSLFEQLKN 948
Cdd:PRK05691 2579 RADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALD-TPSGKQLAGYLVSAvagqddeAQAALREALKA 2657
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 949 ELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAenfVADSSLVSPQTQA-LSDTEQMLLALWMRYLPIKNVDPECDFF 1027
Cdd:PRK05691 2658 HLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALP---APDPELNRQAYQApRSELEQQLAQIWREVLNVERVGLGDNFF 2734
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1028 RLGGHSLLAVTLVAEInRTFHCALTLKDIFHYSTLRALsARIAQQSITdAAASQDdwvivhdpeHRHQPFPLTDVQraYW 1107
Cdd:PRK05691 2735 ELGGDSILSIQVVSRA-RQLGIHFSPRDLFQHQTVQTL-AAVATHSEA-AQAEQG---------PLQGASGLTPIQ--HW 2800
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1108 LgrqtgatsIATHIYHEfdvEHFNVT------------RFTHAVNALIARHEMLR-----------ARVLPDGTQQILAQ 1164
Cdd:PRK05691 2801 F--------FDSPVPQP---QHWNQAllleprqaldpaLLEQALQALVEHHDALRlrfsqadgrwqAEYRAVTAQELLWQ 2869
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1165 VPAYQLEQRdlsalspnarnDALMAIRDR-LSHHVHPADRWPLFDfsySACTAQhgRLHFSLDLLIADALSMRTLQQELM 1243
Cdd:PRK05691 2870 VTVADFAEC-----------AALFADAQRsLDLQQGPLLRALLVD---GPQGQQ--RLLLAIHHLVVDGVSWRVLLEDLQ 2933
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1244 MLYREPH----VSLPLLPFSFRDYVQALLVEQASEAYARDQAYWQRalpQLYGPPT-LPV---QGD----LAQLSAIRFV 1311
Cdd:PRK05691 2934 ALYRQLSagaePALPAKTSAFRDWAARLQAYAGSESLREELGWWQA---QLGGPRAeLPCdrpQGGnlnrHAQTVSVRLD 3010
|
1370 1380 1390 1400 1410
....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1312 RRRHRLSAHNwgvlSALAQRTRITKtaLLLTVFSQVLARWSLSPTFTLNL 1361
Cdd:PRK05691 3011 AERTRQLLQQ----APAAYRTQVND--LLLTALARVLCRWSGQPSVLVQL 3054
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
515-982 |
1.74e-160 |
|
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: 493.97 E-value: 1.74e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 515 PKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLM 594
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 595 QRARLVCLVVrqpgewgeivqlslpelmqDMSNAirystpcallpdmqAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQR 674
Cdd:cd05930 81 EDSGAKLVLT-------------------DPDDL--------------AYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 675 TFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLTEAERAADSFRMIPLIADYRPTLMQATPSFWHGLLMAGWRGDP 754
Cdd:cd05930 128 AYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAAL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 755 EL--CVLAGGEALPTKVAEELLRCCGS--LWNLYGPTETTIWS----LKSQITQAENITLGAPIANTRIYILDNEGHPVP 826
Cdd:cd05930 208 PSlrLVLVGGEALPPDLVRRWRELLPGarLVNLYGPTEATVDAtyyrVPPDDEEDGRVPIGRPIPNTRVYVLDENLRPVP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 827 QGVDGELYIAGDGVAQGYDGQPELNAQFFLSEPGVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERT 906
Cdd:cd05930 288 PGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAA 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1288439980 907 LARHPHVDAAVVACIERAPLHKALAAFIITSEPPSL-FEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRL 982
Cdd:cd05930 368 LLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELdEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
23-1595 |
2.03e-155 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 527.60 E-value: 2.03e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 23 QLAQSGVSPSRIPIIKAD---------PAQAI----PLSFNQERLWFLQKYDSTATNYNLYVVYRLHGVvDMPMLTEALR 89
Cdd:PRK12316 1522 DERNRGVTPSDFPLAGLSqaqldalplPAGEIadiyPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQGL-DPDRFRAAWQ 1600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 90 HVQARHAILRTRIIVRND--RPCQVIDDASSLVLDTVTLAAQAP-TSALDAVIQQVINTRFDLARGPLWGVTQIIQPDQG 166
Cdd:PRK12316 1601 ATVDRHEILRSGFLWQDGleQPLQVIHKQVELPFAELDWRGREDlGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGR 1680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 167 CHLVFCAHHIIIDGISLRLLFDELQQQYArlhaGNEtsLPPPPLQYADYAFW-QRewfQDTLLANelAYWRARLqdAPLL 245
Cdd:PRK12316 1681 HHLIYTNHHILMDGWSNAQLLGEVLQRYA----GQP--VAAPGGRYRDYIAWlQR---QDAAASE--AFWKEQL--AALE 1747
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 246 StfPSLHPR----PAQPSTHGSRFSiTLDETLSLALKHVARTQETTPFVLMLTAFQLVLMRYAQQQRLVIGMPVSGRIR- 320
Cdd:PRK12316 1748 E--PTRLAQaartEDGQVGYGDHQQ-LLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAe 1824
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 321 -PELQSSIGYYAST-AVIYTDFNGVEVGrEALQRVKAsvketqgrQQLPFenlvnmldlpRSLSHSPLFQI--------- 389
Cdd:PRK12316 1825 lPGIEQQIGLFINTlPVIAAPRPDQSVA-DWLQEVQA--------LNLAL----------REHEHTPLYDIqrwagqgge 1885
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 390 -----LYIYHNHVTPRAF---TLAGAYWEQVTYHNQTvKYDMTVEVFQNDaTFDVSFEYDLGLYDADVVKQIAEALRQHC 461
Cdd:PRK12316 1886 alfdsLLVFENYPVAEALkqgAPAGLVFGRVSNHEQT-NYPLTLAVTLGE-TLSLQYSYDRGHFDAAAIERLDRHLLHLL 1963
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 462 LSLTSSLETPIGAIPLHAPETATPRRDPLNATNVPWLGPQDVLRIIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAM 541
Cdd:PRK12316 1964 EQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAH 2043
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 542 RFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLMQRAR-------------------LVCL 602
Cdd:PRK12316 2044 RLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGaallltqrhllerlplpagVARL 2123
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 603 VVRQPGEWGEIVQLSlPELmqdmsnairystpcALLPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQD 682
Cdd:PRK12316 2124 PLDRDAEWADYPDTA-PAV--------------QLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPAD 2188
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 683 RLLSVTTPTFDISFLEYLLPLISGASLYLTEAERAaDSFRMIPLIADYRPTLMQATPSFWHGLL----MAGWRGDPELCV 758
Cdd:PRK12316 2189 CELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELW-DPEQLYDEMERHGVTILDFPPVYLQQLAehaeRDGRPPAVRVYC 2267
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 759 LaGGEALPTKVAEELLRCCGS--LWNLYGPTETTI----WSLKSQITQ-AENITLGAPIANTRIYILDNEGHPVPQGVDG 831
Cdd:PRK12316 2268 F-GGEAVPAASLRLAWEALRPvyLFNGYGPTEAVVtpllWKCRPQDPCgAAYVPIGRALGNRRAYILDADLNLLAPGMAG 2346
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 832 ELYIAGDGVAQGYDGQPELNAQFFLSEP-GVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARH 910
Cdd:PRK12316 2347 ELYLGGEGLARGYLNRPGLTAERFVPDPfSASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAH 2426
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 911 PHVDAAVVACIErAPLHKALAAFIITSEPPSLF-EQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAENFVA- 988
Cdd:PRK12316 2427 PAVREAVVVAQD-GASGKQLVAYVVPDDAAEDLlAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSq 2505
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 989 -DSSLVSPQTQalsdTEQMLLALWMRYLPIKNVDPECDFFRLGGHSLLAVTLVAEINRTFHCALTLKDIFHYSTLRALSA 1067
Cdd:PRK12316 2506 lRQAYVAPQEG----LEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAA 2581
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1068 RIAQQSITDAAASQddwvivhdPEHRHQPFPLTDVQRAYWLGRQTGATSIATHIYHEFDVEH-FNVTRFTHAVNALIARH 1146
Cdd:PRK12316 2582 SLESGQTSRAPVLQ--------KVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGvLDQAALEQAFDALVLRH 2653
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1147 EMLRARVLPDGTQQIlaQVPAYQLEQRDLSALSPNARNDALMAIRDRLSHHVHPADRWPLFDFSYSACTAQHGRLHFSLD 1226
Cdd:PRK12316 2654 ETLRTRFVEVGEQTR--QVILPNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQH 2731
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1227 LLIADALSMRTLQQELMMLYRE----PHVSLPLLPFSFRDYVQALLVEQASEAYARDQAYWQRALPQLYGPPTLPVQGDL 1302
Cdd:PRK12316 2732 HIVSDGWSMQVMVDELVQAYAGarrgEQPTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPLDRPR 2811
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1303 AQLSAIRFVRRRHRLSAHNWGVLSALAQRTRITKTALLLTVFSQVLARWSLSPTFTLNLTLFNRPQgyPNAEAVIGDFTA 1382
Cdd:PRK12316 2812 PALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNR--AETERLIGFFVN 2889
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1383 VSLLNVCYDSQHSYAHNAQRIQVQLWEDLEHRRFSGIRASEALI-HSGRFHAPMPVVFTSMLDIDGETTAQDPRDTTRFT 1461
Cdd:PRK12316 2890 TQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQpERSLSHSPLFQVMYNHQSGERAAAQLPGLHIESFA 2969
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1462 lcPDANITQTPqvwLDHQVIELAGELHFNWDAVEQLFDTTLLDQMFGAYCHALQALVAMPQSWWGVNSSLALPTVSAPV- 1540
Cdd:PRK12316 2970 --WDGAATQFD---LALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLe 3044
|
1610 1620 1630 1640 1650 1660
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1541 ----TQAPAPTALLHHGLLR-QAALTPQETALISPIRELTYRQLSTAADHVARALLALGV 1595
Cdd:PRK12316 3045 awnaTAAEYPLERGVHRLFEeQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGV 3104
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
28-1077 |
2.81e-148 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 506.42 E-value: 2.81e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 28 GVSPSRIPIIKADPAQ-------------AIPLSFNQERLWFLQKYDSTATNYNLYVVYRLHGVvDMPMLTEALRHVQAR 94
Cdd:PRK12316 4073 GVTPSDFPLAGLDQARldalplplgeiedIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQGL-DVERFRAAWQAALDR 4151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 95 HAILRTRIIVRND--RPCQVIDDASSLVLDTVTLAAQAP-TSALDAVIQQVINTRFDLARGPLWGVTQIIQPDQGCHLVF 171
Cdd:PRK12316 4152 HDVLRSGFVWQGElgRPLQVVHKQVSLPFAELDWRGRADlQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIY 4231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 172 CAHHIIIDGISLRLLFDELQQQYArlhagnETSLPPPPLQYADYAFW-QRewfQDTLLANelAYWRARLQ--DAPLLSTF 248
Cdd:PRK12316 4232 TNHHILMDGWSNSQLLGEVLERYS------GRPPAQPGGRYRDYIAWlQR---QDAAASE--AFWREQLAalDEPTRLAQ 4300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 249 PSLHPRPAQPSTHGSrFSITLDETLSLALKHVARTQETTPFVLMLTAFQLVLMRYAQQQRLVIGMPVSGRI--RPELQSS 326
Cdd:PRK12316 4301 AIARADLRSANGYGE-HVRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPaeLPGIEGQ 4379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 327 IGYYASTAVIYTDFNGVEVGREALQRVKASVKETQGRQQLPFENLVNMldlpRSLSHSPLFQILYIYHNHVTPRAF---T 403
Cdd:PRK12316 4380 IGLFINTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEIQRW----AGQGGEALFDSLLVFENYPVSEALqqgA 4455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 404 LAGAYWEQVTYHNQTVkYDMTVEVFQNDaTFDVSFEYDLGLYDADVVKQIAEALRQHCLSLTSSLETPIGAIPLHAPETA 483
Cdd:PRK12316 4456 PGGLRFGEVTNHEQTN-YPLTLAVGLGE-TLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQ 4533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 484 TPRRDPLNATNVPWLGPQDVLRIIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRD 563
Cdd:PRK12316 4534 QRIVALWNRTDAGYPATRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAE 4613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 564 VIATMLATWFVGACYVPFDIHQPAARLQRLMQ--RARLV-----------------CLVVRQPGEWgeivqlslpelmQD 624
Cdd:PRK12316 4614 MMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEdsGAALLltqshllqrlpipdglaSLALDRDEDW------------EG 4681
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 625 MSNAirySTPCALLPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSVTTPTFDISFLEYLLPLI 704
Cdd:PRK12316 4682 FPAH---DPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLI 4758
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 705 SGASLYLTEAErAADSFRMIPLIADYRPTLMQATPSFWHGLLM-AGWRGDPELC--VLAGGEALPTKVAEELLRCCG--S 779
Cdd:PRK12316 4759 NGASVVIRDDS-LWDPERLYAEIHEHRVTVLVFPPVYLQQLAEhAERDGEPPSLrvYCFGGEAVAQASYDLAWRALKpvY 4837
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 780 LWNLYGPTETTIWSL-----KSQITQAENITLGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQF 854
Cdd:PRK12316 4838 LFNGYGPTETTVTVLlwkarDGDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAER 4917
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 855 FLSEP-GVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIErAPLHKALAAF 933
Cdd:PRK12316 4918 FVPDPfGAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQE-GAVGKQLVGY 4996
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 934 IITSEP---------PSLFEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAEnfvADSSL-----VSPQTQA 999
Cdd:PRK12316 4997 VVPQDPaladadeaqAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQ---PDASLlqqayVAPRSEL 5073
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1288439980 1000 lsdtEQMLLALWMRYLPIKNVDPECDFFRLGGHSLLAVTLVAEINRTFHCALTLKDIFHYSTLRALSARIAQQSITDA 1077
Cdd:PRK12316 5074 ----EQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPTLAAFVELAAAAGSGDD 5147
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
39-1079 |
3.05e-134 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 449.88 E-value: 3.05e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 39 ADPAQAIPLSFNQERLWFLQKYDSTATNYNLYVVYRLHGVVDMPMLTEALRHVQARHAILRTRIIVRNDRPCQVIDDASS 118
Cdd:PRK10252 2 EPMSQHLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 119 L-VLDTVTLAAQA-PTSALDAVIQQVINTRFDLARGPLWGVTQIIQPDQGCHLVFCA-HHIIIDGISLRLLFDELQQQYA 195
Cdd:PRK10252 82 FpLPEIIDLRTQPdPHAAAQALMQADLQQDLRVDSGKPLVFHQLIQLGDNRWYWYQRyHHLLVDGFSFPAITRRIAAIYC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 196 RLHAGNETSLPP-PPLQ--YADYAFWQrewfQDTLLANELAYWRARLQDAPLLStfpSLHPRPA---QPSTHGSRFSITL 269
Cdd:PRK10252 162 AWLRGEPTPASPfTPFAdvVEEYQRYR----ASEAWQRDAAFWAEQRRQLPPPA---SLSPAPLpgrSASADILRLKLEF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 270 DETLSLALKHVARTQETTPFVLMLTAfqLVLMRYAQQQRLVIGMPVSGRI-RPELQSSiGYYASTAVIYTDFNGVEVGRE 348
Cdd:PRK10252 235 TDGAFRQLAAQASGVQRPDLALALVA--LWLGRLCGRMDYAAGFIFMRRLgSAALTAT-GPVLNVLPLRVHIAAQETLPE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 349 ALQRVKASVKETQGRQQLPFENLVNMLDL---PRSLsHSPLFQILYIYHNHvtprafTLAGAyweQVTYHNQT---VKyD 422
Cdd:PRK10252 312 LATRLAAQLKKMRRHQRYDAEQIVRDSGRaagDEPL-FGPVLNIKVFDYQL------DFPGV---QAQTHTLAtgpVN-D 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 423 MTVEVFQN-DATFDVSFEYDLGLYDADVVKQIAEALrQHCLSLTSSLET-PIGAIPLHAPETATpRRDPLNATNVPwLGP 500
Cdd:PRK10252 381 LELALFPDeHGGLSIEILANPQRYDEATLIAHAERL-KALIAQFAADPAlLCGDVDILLPGEYA-QLAQVNATAVE-IPE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 501 QDVLRIIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVP 580
Cdd:PRK10252 458 TTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 581 FDIHQPAARLQRLMQRARLVCLVVRQpGEWGEIVQLSLPELMQ-DMSNAIRYSTPCAL-LPDMQAYLLFTSGSTGEPKGV 658
Cdd:PRK10252 538 LDTGYPDDRLKMMLEDARPSLLITTA-DQLPRFADVPDLTSLCyNAPLAPQGAAPLQLsQPHHTAYIIFTSGSTGRPKGV 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 659 CVVHRGLLNLLLDMQRTFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLTEAERAADSFRMIPLIADYRPTLMQAT 738
Cdd:PRK10252 617 MVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFV 696
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 739 PSFWHGLLMAGwrgDPELC---------VLAGGEALPTKVAEELLRCCGS-LWNLYGPTETTI-------WSLKSQITQA 801
Cdd:PRK10252 697 PSMLAAFVASL---TPEGArqscaslrqVFCSGEALPADLCREWQQLTGApLHNLYGPTEAAVdvswypaFGEELAAVRG 773
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 802 ENITLGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEPGVPGGRMFRTGDLVRSDAQGQL 881
Cdd:PRK10252 774 SSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAV 853
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 882 FFVGRKDSQIKLRGYRIELGEIERTLARHPHVD-AAVVACIER-APLH----KALAAFIITSEPPSL-FEQLKNELRQQL 954
Cdd:PRK10252 854 EYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEqAVTHACVINqAAATggdaRQLVGYLVSQSGLPLdTSALQAQLRERL 933
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 955 PDYMVPTLWQRVADFPNTDNGKIDRKRL-AENFVADSSLVSPQTQalsdTEQMLLALWMRYLPIKNVDPECDFFRLGGHS 1033
Cdd:PRK10252 934 PPHMVPVVLLQLDQLPLSANGKLDRKALpLPELKAQVPGRAPKTG----TETIIAAAFSSLLGCDVVDADADFFALGGHS 1009
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*.
gi 1288439980 1034 LLAVTLVAEINRTFHCALTLKDIFHYSTLRALSARIAQQSITDAAA 1079
Cdd:PRK10252 1010 LLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAEEDESRRL 1055
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
505-982 |
9.92e-131 |
|
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: 415.45 E-value: 9.92e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 505 RIIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIH 584
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 585 QPAARLQRLMQRARLVCLVVRQ--PGEWGEIVQLSLPELMQDMSNAIRYSTPCAllPDMQAYLLFTSGSTGEPKGVCVVH 662
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRslAGRAGGLEVAVVIDEALDAGPAGNPAVPVS--PDDLAYVMYTSGSTGRPKGVAVTH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 663 RGLLNLLLDmQRTFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLTEAERAADSFRMIPLIADYRPTLMQATPSFW 742
Cdd:cd12117 159 RGVVRLVKN-TNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 743 HGL------LMAGWRgdpelCVLAGGEALPTK-VAEELLRCCG-SLWNLYGPTETTIWSLKSQITQ----AENITLGAPI 810
Cdd:cd12117 238 NQLadedpeCFAGLR-----ELLTGGEVVSPPhVRRVLAACPGlRLVNGYGPTENTTFTTSHVVTEldevAGSIPIGRPI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 811 ANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEPGVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQ 890
Cdd:cd12117 313 ANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 891 IKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEPPSLfEQLKNELRQQLPDYMVPTLWQRVADFP 970
Cdd:cd12117 393 VKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDA-AELRAFLRERLPAYMVPAAFVVLDELP 471
|
490
....*....|..
gi 1288439980 971 NTDNGKIDRKRL 982
Cdd:cd12117 472 LTANGKVDRRAL 483
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
26-1070 |
2.88e-130 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 451.54 E-value: 2.88e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 26 QSGVSPSRIPIIKADPAQ-------------AIPLSFNQERLWFLQKYDSTATNYNLYVVYRLHGVvDMPMLTEALRHVQ 92
Cdd:PRK12467 2615 QRGVTPSDFPLAGLSQEQldrlpvavgdiedIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEGL-DVERFRTAWQAVI 2693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 93 ARHAILRTRIIVRN--DRPCQVIDDASSLVLDTVTLAAQAPTS-ALDAVIQQVINTRFDLARGPLWGVTQIIQPDQGCHL 169
Cdd:PRK12467 2694 DRHEILRSGFLWDGelEEPLQVVYKQARLPFSRLDWRDRADLEqALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHL 2773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 170 VFCAHHIIIDGISLRLLFDELQQQYArlhagnETSLPPPPLQYADYAFW-QRewfQDTllANELAYWRAR---LQDAPLL 245
Cdd:PRK12467 2774 IYTNHHILMDGWSGSQLLGEVLQRYF------GQPPPAREGRYRDYIAWlQA---QDA--EASEAFWKEQlaaLEEPTRL 2842
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 246 StfPSLHPRPAQP-STHGSRFsITLDETLSLALKHVARTQETTPFVLMLTAFQLVLMRYAQQQRLVIGMPVSGRiRPELQ 324
Cdd:PRK12467 2843 A--RALYPAPAEAvAGHGAHY-LHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGR-PAQLR 2918
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 325 ---SSIGYYAST-AVIYTDfngvevgrEALQRVkasvkeTQGRQQLPFENLVnmldlPRSLSHSPLFQI----------- 389
Cdd:PRK12467 2919 gaeQQLGLFINTlPVIASP--------RAEQTV------SDWLQQVQAQNLA-----LREFEHTPLADIqrwagqggeal 2979
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 390 ---LYIYHNHVTPRAFTLAGA---YWEQVTYHNQTvKYDMTVEVFQNDaTFDVSFEYDLGLYDADVVKQIAEALRQHCLS 463
Cdd:PRK12467 2980 fdsILVFENYPISEALKQGAPsglRFGAVSSREQT-NYPLTLAVGLGD-TLELEFSYDRQHFDAAAIERLAESFDRLLQA 3057
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 464 LTSSLETPIGAIPLHAPETATPRRDPLNATNVPWLGPQDVLRIIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRF 543
Cdd:PRK12467 3058 MLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRL 3137
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 544 RAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLMQRARLVCLVVRQpgewGEIVQLSLPE--- 620
Cdd:PRK12467 3138 IAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQA----HLLEQLPAPAgdt 3213
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 621 -LMQDMSNAIRYSTPC---ALLPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSVTTPTFDISF 696
Cdd:PRK12467 3214 aLTLDRLDLNGYSENNpstRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQ 3293
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 697 LEYLLPLISGASLYLtEAERAADSFRMIPLIADYRPTLMQATPSFWHGLLMAGWRGD--PELCVLAGGEALPTKVAEELL 774
Cdd:PRK12467 3294 ERFLWTLICGGCLVV-RDNDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGADcaSLDIYVFGGEAVPPAAFEQVK 3372
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 775 RCCG--SLWNLYGPTETTIWSL-----KSQITQAENITLGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQ 847
Cdd:PRK12467 3373 RKLKprGLTNGYGPTEAVVTVTlwkcgGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQR 3452
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 848 PELNAQFFLSEP-GVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPl 926
Cdd:PRK12467 3453 PSLTAERFVADPfSGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAG- 3531
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 927 HKALAAFIITSEP-PSLFEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAE-NFVADSSLVSPQtqalSDTE 1004
Cdd:PRK12467 3532 GKQLVAYVVPADPqGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDpDAKGSREYVAPR----SEVE 3607
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1288439980 1005 QMLLALWMRYLPIKNVDPECDFFRLGGHSLLAVTLVAEINRTFHCALTLKDIFHYSTLRALSARIA 1070
Cdd:PRK12467 3608 QQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYSP 3673
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
44-459 |
1.18e-125 |
|
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: 399.42 E-value: 1.18e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 44 AIPLSFNQERLWFLQKYDSTATNYNLYVVYRLHGVVDMPMLTEALRHVQARHAILRTRIIVRNDRPCQVIDDASSLVLDT 123
Cdd:cd19531 1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 124 VTLAAQAPT---SALDAVIQQVINTRFDLARGPLWGVTqIIQPDQGCH-LVFCAHHIIIDGISLRLLFDELQQQYARLHA 199
Cdd:cd19531 81 VDLSGLPEAereAEAQRLAREEARRPFDLARGPLLRAT-LLRLGEDEHvLLLTMHHIVSDGWSMGVLLRELAALYAAFLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 200 GNETSLPPPPLQYADYAFWQREWFQDTLLANELAYWRARLQDAPLLSTFPSLHPRPAQPSTHGSRFSITLDETLSLALKH 279
Cdd:cd19531 160 GRPSPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALRA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 280 VARTQETTPFVLMLTAFQLVLMRYAQQQRLVIGMPVSGRIRPELQSSIGYYASTAVIYTDFNGVEVGREALQRVKASVKE 359
Cdd:cd19531 240 LARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 360 TQGRQQLPFENLVNMLDLPRSLSHSPLFQILYIYHNhVTPRAFTLAGAYWEQVTYHNQTVKYDMTVEVFQNDATFDVSFE 439
Cdd:cd19531 320 AYAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQN-APAAALELPGLTVEPLEVDSGTAKFDLTLSLTETDGGLRGSLE 398
|
410 420
....*....|....*....|
gi 1288439980 440 YDLGLYDADVVKQIAEALRQ 459
Cdd:cd19531 399 YNTDLFDAATIERMAGHFQT 418
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
528-918 |
1.00e-121 |
|
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: 387.78 E-value: 1.00e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 528 TYAELWARVQFIAMRFRA-HGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLMQRARLVCLVV-- 604
Cdd:TIGR01733 1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTds 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 605 ----RQPGEWGEIVQLSLPELMQDMSNAIRYSTPCALLPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGS 680
Cdd:TIGR01733 81 alasRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 681 QDRLLSVTTPTFDISFLEYLLPLISGASLYL-TEAERAADSFRMIPLIADYRPTLMQATPSFWHGLLMAGWRGDPEL-CV 758
Cdd:TIGR01733 161 DDRVLQFASLSFDASVEEIFGALLAGATLVVpPEDEERDDAALLAALIAEHPVTVLNLTPSLLALLAAALPPALASLrLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 759 LAGGEALPTKVAEELLRCCGS--LWNLYGPTETTIWSLKSQI-----TQAENITLGAPIANTRIYILDNEGHPVPQGVDG 831
Cdd:TIGR01733 241 ILGGEALTPALVDRWRARGPGarLINLYGPTETTVWSTATLVdpddaPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 832 ELYIAGDGVAQGYDGQPELNAQFFLSEP--GVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLAR 909
Cdd:TIGR01733 321 ELYIGGPGVARGYLNRPELTAERFVPDPfaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400
|
....*....
gi 1288439980 910 HPHVDAAVV 918
Cdd:TIGR01733 401 HPGVREAVV 409
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
507-982 |
3.95e-121 |
|
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: 389.33 E-value: 3.95e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 507 IEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQP 586
Cdd:cd17646 4 VAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 587 AARLQRLMQRARlVCLVVRQPGEWGEIVQLSLPELMQDMSNAIRYSTP--CALLPDMQAYLLFTSGSTGEPKGVCVVHRG 664
Cdd:cd17646 84 ADRLAYMLADAG-PAVVLTTADLAARLPAGGDVALLGDEALAAPPATPplVPPRPDNLAYVIYTSGSTGRPKGVMVTHAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 665 LLNLLLDMQRTFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLTEAERAADSFRMIPLIADYRPTLMQATPSFWHG 744
Cdd:cd17646 163 IVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSMLRV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 745 LLmaGWRgDPELC-----VLAGGEALPTKVAEELLRCCG-SLWNLYGPTETTIWSLKSQITQAEN---ITLGAPIANTRI 815
Cdd:cd17646 243 FL--AEP-AAGSCaslrrVFCSGEALPPELAARFLALPGaELHNLYGPTEAAIDVTHWPVRGPAEtpsVPIGRPVPNTRL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 816 YILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEPGVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRG 895
Cdd:cd17646 320 YVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 896 YRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITS--EPPSLFEQLKNELRQQLPDYMVPTLWQRVADFPNTD 973
Cdd:cd17646 400 FRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAagAAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTA 479
|
....*....
gi 1288439980 974 NGKIDRKRL 982
Cdd:cd17646 480 NGKLDRAAL 488
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
507-982 |
4.02e-115 |
|
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: 372.83 E-value: 4.02e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 507 IEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQP 586
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 587 AARLQRLMQRARLVClVVRQPGEWGEIVQLSLPELMQDMS---NAIRYSTPCALLPDMQAYLLFTSGSTGEPKGVCVVHR 663
Cdd:cd17651 81 AERLAFMLADAGPVL-VLTHPALAGELAVELVAVTLLDQPgaaAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 664 GLLNLLLDMQRTFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLTEAERAADSFRMIPLIADYRPTLMQATPSFWH 743
Cdd:cd17651 160 SLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 744 GLLMAGWRGDPEL----CVLAGGEALPtkVAEELLRCCGS-----LWNLYGPTETTI---WSLKSQITQA-ENITLGAPI 810
Cdd:cd17651 240 ALAEHGRPLGVRLaalrYLLTGGEQLV--LTEDLREFCAGlpglrLHNHYGPTETHVvtaLSLPGDPAAWpAPPPIGRPI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 811 ANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEPGVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQ 890
Cdd:cd17651 318 DNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 891 IKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEPPSLF-EQLKNELRQQLPDYMVPTLWQRVADF 969
Cdd:cd17651 398 VKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDaAELRAALATHLPEYMVPSAFVLLDAL 477
|
490
....*....|...
gi 1288439980 970 PNTDNGKIDRKRL 982
Cdd:cd17651 478 PLTPNGKLDRRAL 490
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
515-982 |
3.93e-114 |
|
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: 368.12 E-value: 3.93e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 515 PKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLM 594
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 595 QRARLVCLVVrqpgewgeivqlslpelmqdmsnairystpcalLPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQR 674
Cdd:cd17652 81 ADARPALLLT---------------------------------TPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 675 TFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLTEAERAADSFRMIPLIADYRPTLMQATPSfwhGLLMAGWRGDP 754
Cdd:cd17652 128 AFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPA---ALAALPPDDLP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 755 EL-CVLAGGEALPTKVAEELLRCCgSLWNLYGPTETTIWSLKSQITQAEN-ITLGAPIANTRIYILDNEGHPVPQGVDGE 832
Cdd:cd17652 205 DLrTLVVAGEACPAELVDRWAPGR-RMINAYGPTETTVCATMAGPLPGGGvPPIGRPVPGTRVYVLDARLRPVPPGVPGE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 833 LYIAGDGVAQGYDGQPELNAQFFLSEP-GVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHP 911
Cdd:cd17652 284 LYIAGAGLARGYLNRPGLTAERFVADPfGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHP 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1288439980 912 HVDAAVVACIERAPLHKALAAFIITSEPPSL-FEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRL 982
Cdd:cd17652 364 GVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPtAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
515-982 |
3.33e-111 |
|
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: 361.59 E-value: 3.33e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 515 PKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLM 594
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 595 QRARLVCLVVRQPGEWGEIVQLSLPELMQDMSNAIRYSTPCALLPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQR 674
Cdd:cd12114 81 ADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 675 TFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLTEAERAADSFRMIPLIADYRPTLMQATPSfWHGLLMAGWRGDP 754
Cdd:cd12114 161 RFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPA-LLEMLLDVLEAAQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 755 EL-----CVLAGGE----ALPTKVAEELLRCcgSLWNLYGPTETTIWSLKSQITQAE----NITLGAPIANTRIYILDNE 821
Cdd:cd12114 240 ALlpslrLVLLSGDwiplDLPARLRALAPDA--RLISLGGATEASIWSIYHPIDEVPpdwrSIPYGRPLANQRYRVLDPR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 822 GHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEPgvPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELG 901
Cdd:cd12114 318 GRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 902 EIERTLARHPHVDAAVVACIERaPLHKALAAFIITSEPPSLFEQ--LKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDR 979
Cdd:cd12114 396 EIEAALQAHPGVARAVVVVLGD-PGGKRLAAFVVPDNDGTPIAPdaLRAFLAQTLPAYMIPSRVIALEALPLTANGKVDR 474
|
...
gi 1288439980 980 KRL 982
Cdd:cd12114 475 AAL 477
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
515-982 |
1.20e-110 |
|
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: 358.99 E-value: 1.20e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 515 PKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLM 594
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 595 QRARLVCLvvrqpgewgeivqlslpeLMQDmsnairystpcallPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQR 674
Cdd:cd17649 81 EDSGAGLL------------------LTHH--------------PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 675 TFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLTEAERAADSFRMIPLIADYRPTLMQATPSFWHGLLM----AGW 750
Cdd:cd17649 129 RYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEeadrTGD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 751 RGDPELCVLA-GGEALPTKVAEELLRCCGSLWNLYGPTETTI----WSLKSQIT-QAENITLGAPIANTRIYILDNEGHP 824
Cdd:cd17649 209 GRPPSLRLYIfGGEALSPELLRRWLKAPVRLFNAYGPTEATVtplvWKCEAGAArAGASMPIGRPLGGRSAYILDADLNP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 825 VPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEP-GVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEI 903
Cdd:cd17649 289 VPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPfGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 904 ERTLARHPHV-DAAVVAciERAPLHKALAAFIITSEP---PSLFEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDR 979
Cdd:cd17649 369 EAALLEHPGVrEAAVVA--LDGAGGKQLVAYVVLRAAaaqPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDR 446
|
...
gi 1288439980 980 KRL 982
Cdd:cd17649 447 KAL 449
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
513-982 |
1.93e-108 |
|
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: 352.70 E-value: 1.93e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 513 QHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQR 592
Cdd:cd05945 3 ANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 593 LMqrarlvclvvrqpgewgEIVQLSLpeLMQDmsnairystpcallPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDM 672
Cdd:cd05945 83 IL-----------------DAAKPAL--LIAD--------------GDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWM 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 673 QRTFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLTEAERAADSFRMIPLIADYRPTLMQATPSFWHGLLMagwrg 752
Cdd:cd05945 130 LSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLL----- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 753 DPELC---------VLAGGEALPTKVAEELLRCC--GSLWNLYGPTETTIWSLKSQIT-----QAENITLGAPIANTRIY 816
Cdd:cd05945 205 SPTFTpeslpslrhFLFCGEVLPHKTARALQQRFpdARIYNTYGPTEATVAVTYIEVTpevldGYDRLPIGYAKPGAKLV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 817 ILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEPGVPGgrmFRTGDLVRSDAQGQLFFVGRKDSQIKLRGY 896
Cdd:cd05945 285 ILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQRA---YRTGDLVRLEADGLLFYRGRLDFQVKLNGY 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 897 RIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEPPSLF--EQLKNELRQQLPDYMVPTLWQRVADFPNTDN 974
Cdd:cd05945 362 RIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGltKAIKAELAERLPPYMIPRRFVYLDELPLNAN 441
|
....*...
gi 1288439980 975 GKIDRKRL 982
Cdd:cd05945 442 GKIDRKAL 449
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
507-982 |
2.06e-108 |
|
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: 352.39 E-value: 2.06e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 507 IEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQP 586
Cdd:cd12115 5 VEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 587 AARLQRLMQRARlvCLVVrqpgewgeIVQlslpelmqdmsnairystpcallPDMQAYLLFTSGSTGEPKGVCVVHRGLL 666
Cdd:cd12115 85 PERLRFILEDAQ--ARLV--------LTD-----------------------PDDLAYVIYTSGSTGRPKGVAIEHRNAA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 667 NLLLDMQRTFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLTEaeraaDSFRMIPLIADYRPTLMQATPSFWHGLL 746
Cdd:cd12115 132 AFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLAD-----NVLALPDLPAAAEVTLINTVPSAAAELL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 747 MAGwrGDPE--LCVLAGGEALPTKVAEELLRCCGS--LWNLYGPTETTIWSLKSQITQA--ENITLGAPIANTRIYILDN 820
Cdd:cd12115 207 RHD--ALPAsvRVVNLAGEPLPRDLVQRLYARLQVerVVNLYGPSEDTTYSTVAPVPPGasGEVSIGRPLANTQAYVLDR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 821 EGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEPGVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIEL 900
Cdd:cd12115 285 ALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIEL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 901 GEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEP-PSLFEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDR 979
Cdd:cd12115 365 GEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGaAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDR 444
|
...
gi 1288439980 980 KRL 982
Cdd:cd12115 445 SAL 447
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
506-984 |
1.62e-107 |
|
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: 351.46 E-value: 1.62e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 506 IIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQ 585
Cdd:cd05918 4 LIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 586 PAARLQRLMQR--ARLVcLVvrqpgewgeivqlslpelmqdmsnairySTPCALlpdmqAYLLFTSGSTGEPKGVCVVHR 663
Cdd:cd05918 84 PLQRLQEILQDtgAKVV-LT----------------------------SSPSDA-----AYVIFTSGSTGKPKGVVIEHR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 664 GLLNLLLDMQRTFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLT-EAERAADSFRMIpliADYRPTLMQATPSFW 742
Cdd:cd05918 130 ALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPsEEDRLNDLAGFI---NRLRVTWAFLTPSVA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 743 HGLlmaGWRGDPELCVLA-GGEALPTKVAEELLRCCgSLWNLYGPTETTIWSLKSQITQAENI-TLGAPIAnTRIYILDN 820
Cdd:cd05918 207 RLL---DPEDVPSLRTLVlGGEALTQSDVDTWADRV-RLINAYGPAECTIAATVSPVVPSTDPrNIGRPLG-ATCWVVDP 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 821 EGH--PVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEP-------GVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQI 891
Cdd:cd05918 282 DNHdrLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 892 KLRGYRIELGEIERTLARHPHVDAAVVACI---ERAPLHKALAAFI------------------ITSEPPSLFEQLKNEL 950
Cdd:cd05918 362 KIRGQRVELGEIEHHLRQSLPGAKEVVVEVvkpKDGSSSPQLVAFVvldgsssgsgdgdslflePSDEFRALVAELRSKL 441
|
490 500 510
....*....|....*....|....*....|....
gi 1288439980 951 RQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAE 984
Cdd:cd05918 442 RQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRE 475
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
505-984 |
2.96e-107 |
|
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: 350.86 E-value: 2.96e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 505 RIIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIH 584
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 585 QPAARLQRLMQRARLVCLVVRQPGEWGEI-VQLSLPELMQDMSNAIRYSTPCALLPDMQAYLLFTSGSTGEPKGVCVVHR 663
Cdd:cd17655 81 YPEERIQYILEDSGADILLTQSHLQPPIAfIGLIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 664 GLLNLLLDMQRTFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLTEAERAADSFRMIPLIADYRPTLMQATPSfwH 743
Cdd:cd17655 161 GVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPA--H 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 744 GLLMAGWRGDPELCV---LAGGEALPTKVAEELLRCCGS---LWNLYGPTETT----IWSLKSQITQAENITLGAPIANT 813
Cdd:cd17655 239 LKLLDAADDSEGLSLkhlIVGGEALSTELAKKIIELFGTnptITNAYGPTETTvdasIYQYEPETDQQVSVPIGKPLGNT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 814 RIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEPGVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKL 893
Cdd:cd17655 319 RIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 894 RGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFiITSEPPSLFEQLKNELRQQLPDYMVPTLWQRVADFPNTD 973
Cdd:cd17655 399 RGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAY-IVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTP 477
|
490
....*....|.
gi 1288439980 974 NGKIDRKRLAE 984
Cdd:cd17655 478 NGKVDRKALPE 488
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
505-984 |
3.37e-102 |
|
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: 334.66 E-value: 3.37e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 505 RIIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIH 584
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 585 QPAARLQRLMQRARlVCLVVrqpgewgeivqlslpelmqdmsnairystpCALLPDMQAYLLFTSGSTGEPKGVCVVHRG 664
Cdd:cd17653 81 LPSARIQAILRTSG-ATLLL------------------------------TTDSPDDLAYIIFTSGSTGIPKGVMVPHRG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 665 LLNLLLDMQRTFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLteaeraADSfrMIPLIADYRP-TLMQATPSFwh 743
Cdd:cd17653 130 VLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVL------ADP--SDPFAHVARTvDALMSTPSI-- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 744 gLLMAGWRGDPEL-CVLAGGEALPTKVAEELL--RCcgsLWNLYGPTETTIWSLKSQITQAENITLGAPIANTRIYILDN 820
Cdd:cd17653 200 -LSTLSPQDFPNLkTIFLGGEAVPPSLLDRWSpgRR---LYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTCYILDA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 821 EGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEPGVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIEL 900
Cdd:cd17653 276 DLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINL 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 901 GEIERTLAR-HPHVDAAVVACIEraplhKALAAFIItsePPSL-FEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKID 978
Cdd:cd17653 356 EEIEEVVLQsQPEVTQAAAIVVN-----GRLVAFVT---PETVdVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVD 427
|
....*.
gi 1288439980 979 RKRLAE 984
Cdd:cd17653 428 RKALRE 433
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
506-990 |
7.99e-102 |
|
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: 334.09 E-value: 7.99e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 506 IIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQ 585
Cdd:COG0318 4 LLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 586 PAARLQRLMQRARLVCLVVrqpgewgeivqlslpelmqdmsnairystpcallpdmqAYLLFTSGSTGEPKGVCVVHRGL 665
Cdd:COG0318 84 TAEELAYILEDSGARALVT--------------------------------------ALILYTSGTTGRPKGVMLTHRNL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 666 LNLLLDMQRTFAVGSQDRLLSVTTPTFDISFLEYLL-PLISGASLYLTEAERAAdsfRMIPLIADYRPTLMQATPSFWHG 744
Cdd:COG0318 126 LANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLaPLLAGATLVLLPRFDPE---RVLELIERERVTVLFGVPTMLAR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 745 LLMAGWRGDPEL----CVLAGGEALPTKVAEELLRCCGS-LWNLYGPTETT--IWSLKSQITQAENITLGAPIANTRIYI 817
Cdd:COG0318 203 LLRHPEFARYDLsslrLVVSGGAPLPPELLERFEERFGVrIVEGYGLTETSpvVTVNPEDPGERRPGSVGRPLPGVEVRI 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 818 LDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFlsepgvpGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYR 897
Cdd:COG0318 283 VDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-------RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGEN 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 898 IELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEPPSL-FEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGK 976
Cdd:COG0318 356 VYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELdAEELRAFLRERLARYKVPRRVEFVDELPRTASGK 435
|
490
....*....|....
gi 1288439980 977 IDRKRLAENFVADS 990
Cdd:COG0318 436 IDRRALRERYAAGA 449
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
515-982 |
1.22e-100 |
|
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: 330.81 E-value: 1.22e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 515 PKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLM 594
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 595 QRARLVCLVVRqpgewgeivqlslpelmqdmsnairystpcallPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQR 674
Cdd:cd17643 81 ADSGPSLLLTD---------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 675 TFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLTEAE--RAADSFRMipLIADYRPTLMQATPSFWHGLLMAGWRG 752
Cdd:cd17643 128 WFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEvaRSPEDFAR--LLRDEGVTVLNQTPSAFYQLVEAADRD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 753 DPELCVLA----GGEALPTKV----AEELLRCCGSLWNLYGPTETTIWS-----LKSQITQAENITLGAPIANTRIYILD 819
Cdd:cd17643 206 GRDPLALRyvifGGEALEAAMlrpwAGRFGLDRPQLVNMYGITETTVHVtfrplDAADLPAAAASPIGRPLPGLRVYVLD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 820 NEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEP-GVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRI 898
Cdd:cd17643 286 ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPfGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRI 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 899 ELGEIERTLARHPHVDAAVVACIERAPLHKALAA-FIITSEPPSLFEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKI 977
Cdd:cd17643 366 ELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAyVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKL 445
|
....*
gi 1288439980 978 DRKRL 982
Cdd:cd17643 446 DRAAL 450
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
28-1069 |
4.97e-100 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 357.94 E-value: 4.97e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 28 GVSPSRIPIIKAD---------PAQAI----PLSFNQERLWFLQKYDSTATNYNLYVVYRLHGVVDMPMLTEALRHVQAR 94
Cdd:PRK05691 3228 GLTPSDFPLAQLTqaqldalpvPAAEIedvyPLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVAR 3307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 95 HAILRTRIIVR-NDRPCQVIDDASSL---VLDTVTLAAQAPTSALDAVIQQVINTRFDLARGPLWGVTQIIQPDQGCHLV 170
Cdd:PRK05691 3308 HEALRASFSWNaGETMLQVIHKPGRTpidYLDWRGLPEDGQEQRLQALHKQEREAGFDLLNQPPFHLRLIRVDEARYWFM 3387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 171 FCAHHIIIDGISLRLLFDELQQQYARLHAGNETSLPPPPlQYADYAFW-QRewfQDtlLANELAYWRARLQ----DAPLL 245
Cdd:PRK05691 3388 MSNHHILIDAWCRSLLMNDFFEIYTALGEGREAQLPVPP-RYRDYIGWlQR---QD--LAQARQWWQDNLRgferPTPIP 3461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 246 STFPSLHPRPAQPSTH--GSRFSiTLDETLSLALKHVARTQETTPFVLMLTAFQLVLMRYAQQQRLVIGMPVSGRI--RP 321
Cdd:PRK05691 3462 SDRPFLREHAGDSGGMvvGDCYT-RLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPvsMP 3540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 322 ELQSSIGYYASTAVIYTDFNGVEVG---REALQRVKASVKETQGRQQLPFENLVNMLDLPRSlshSPLFQILYIYHN--- 395
Cdd:PRK05691 3541 QMQRTVGLFINSIALRVQLPAAGQRcsvRQWLQGLLDSNMELREYEYLPLVAIQECSELPKG---QPLFDSLFVFENapv 3617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 396 --HVTPRAFTLAGAYWEQVTYHNqtvkYDMTVEVFQNDaTFDVSFEYDLGLYDADVVKQIAEALRQHCLSLTSSLETPIG 473
Cdd:PRK05691 3618 evSVLDRAQSLNASSDSGRTHTN----FPLTAVCYPGD-DLGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLS 3692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 474 AIPLHAPETATPRRDPLNATNVPWLGPQDVLRIIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDR 553
Cdd:PRK05691 3693 ELPLLGEQERDFLLDGCNRSERDYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQP 3772
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 554 IGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLMQRAR---LVC----------LVVRQPGE-------WGEI 613
Cdd:PRK05691 3773 VALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRtpvLVCsaacreqaraLLDELGCAnrprllvWEEV 3852
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 614 VQLSLPElmqdmSNAIRYSTPcallpDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSVTTPTFD 693
Cdd:PRK05691 3853 QAGEVAS-----HNPGIYSGP-----DNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFD 3922
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 694 ISFLEYLLPLISGASLYLTEAERAADSFRMIPLIADYRPTLMQATPSFWHGLL------MAGWRgdpelCVLAGGEALPT 767
Cdd:PRK05691 3923 ISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITVLESVPSLIQGMLaedrqaLDGLR-----WMLPTGEAMPP 3997
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 768 KVAEE-LLRCCG-SLWNLYGPTETT----IWSLKSQITQAENITLGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVA 841
Cdd:PRK05691 3998 ELARQwLQRYPQiGLVNAYGPAECSddvaFFRVDLASTRGSYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVG 4077
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 842 QGYDGQPELNAQFFLSEP-GVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVAC 920
Cdd:PRK05691 4078 RGYVGDPLRTALAFVPHPfGAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAV 4157
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 921 IERaPLHKALAAFIITSE----PPSLFEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAENFVADS---SLV 993
Cdd:PRK05691 4158 QEG-VNGKHLVGYLVPHQtvlaQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLqsqAYL 4236
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1288439980 994 SPQTqalsDTEQMLLALWMRYLPIKNVDPECDFFRLGGHSLLAVTLVAEINRTFHCALTLKDIFHYSTLRALSARI 1069
Cdd:PRK05691 4237 APRN----ELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYI 4308
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
508-982 |
2.55e-91 |
|
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: 305.13 E-value: 2.55e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 508 EQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPA 587
Cdd:cd17644 7 EEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 588 ARLQRLMQRARLVCLVVRqpgewgeivqlslpelmqdmsnairystpcallPDMQAYLLFTSGSTGEPKGVCVVHRGLLN 667
Cdd:cd17644 87 ERLTYILEDAQISVLLTQ---------------------------------PENLAYVIYTSGSTGKPKGVMIEHQSLVN 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 668 LLLDMQRTFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLTEAERAADSFRMIPLIADYRPTLMQATPSFWHGLLM 747
Cdd:cd17644 134 LSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 748 AgwrGDPELC--------VLAGGEA-LPTKVA--EELLRCCGSLWNLYGPTETTIWSLKSQIT-----QAENITLGAPIA 811
Cdd:cd17644 214 E---LLLSTIdlpsslrlVIVGGEAvQPELVRqwQKNVGNFIQLINVYGPTEATIAATVCRLTqlterNITSVPIGRPIA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 812 NTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEP--GVPGGRMFRTGDLVRSDAQGQLFFVGRKDS 889
Cdd:cd17644 291 NTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPfnSSESERLYKTGDLARYLPDGNIEYLGRIDN 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 890 QIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIItsePPSLFEQLKNELRQ----QLPDYMVPTLWQR 965
Cdd:cd17644 371 QVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIV---PHYEESPSTVELRQflkaKLPDYMIPSAFVV 447
|
490
....*....|....*..
gi 1288439980 966 VADFPNTDNGKIDRKRL 982
Cdd:cd17644 448 LEELPLTPNGKIDRRAL 464
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
515-982 |
4.11e-91 |
|
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: 303.62 E-value: 4.11e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 515 PKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLM 594
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 595 QRARlVCLVVRQPGEwgeivqlslpelmqdmsnairystpcallpdmQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQR 674
Cdd:cd17650 81 EDSG-AKLLLTQPED--------------------------------LAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 675 TFAVGSQD-RLLSVTTPTFDISFLEYLLPLISGASLYLTEAERAADSFRMIPLIADYRPTLMQATPS---------FWHG 744
Cdd:cd17650 128 EYELDSFPvRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPAlirpvmayvYRNG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 745 LLMAGWRgdpelCVLAGGEALPTKVAEELLRCCGS---LWNLYGPTETTIWSLKSQITQAE-----NITLGAPIANTRIY 816
Cdd:cd17650 208 LDLSAMR-----LLIVGSDGCKAQDFKTLAARFGQgmrIINSYGVTEATIDSTYYEEGRDPlgdsaNVPIGRPLPNTAMY 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 817 ILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEPGVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGY 896
Cdd:cd17650 283 VLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGF 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 897 RIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEPPSLFEqLKNELRQQLPDYMVPTLWQRVADFPNTDNGK 976
Cdd:cd17650 363 RIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAE-LRAFLAKELPSYMIPSYYVQLDALPLTPNGK 441
|
....*.
gi 1288439980 977 IDRKRL 982
Cdd:cd17650 442 VDRRAL 447
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
515-982 |
1.08e-86 |
|
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: 291.23 E-value: 1.08e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 515 PKQLAIQQHDGTLTYAELWARVQFIAMRFRAHG-IQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRL 593
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 594 MQ--RARLVCLVVRQpgewgeivqlslpelmqdmsnairystpcallpdmQAYLLFTSGSTGEPKGVCVVHRGLLNLLLD 671
Cdd:cd17648 81 LEdtGARVVITNSTD-----------------------------------LAYAIYTSGTTGKPKGVLVEHGSVVNLRTS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 672 MQRTFAVGSQD--RLLSVTTPTFDISFLEYLLPLISGASLYLTEAERAADSFRMIPLIADYRPTLMQATPSFwhgLLMAG 749
Cdd:cd17648 126 LSERYFGRDNGdeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSV---LQQYD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 750 WRGDPEL-CVLAGGEALPTKVAEELL-RCCGSLWNLYGPTETTIWSLKSQI--TQAENITLGAPIANTRIYILDNEGHPV 825
Cdd:cd17648 203 LARLPHLkRVDAAGEEFTAPVFEKLRsRFAGLIINAYGPTETTVTNHKRFFpgDQRFDKSLGRPVRNTKCYVLNDAMKRV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 826 PQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEP---------GVPGgRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGY 896
Cdd:cd17648 283 PVGAVGELYLGGDGVARGYLNRPELTAERFLPNPfqteqerarGRNA-RLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQ 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 897 RIELGEIERTLARHPHVDAAVVACIERA-----PLHKALAAFiITSEPPSLFEQ-LKNELRQQLPDYMVPTLWQRVADFP 970
Cdd:cd17648 362 RIEPGEVEAALASYPGVRECAVVAKEDAsqaqsRIQKYLVGY-YLPEPGHVPESdLLSFLRAKLPRYMVPARLVRLEGIP 440
|
490
....*....|..
gi 1288439980 971 NTDNGKIDRKRL 982
Cdd:cd17648 441 VTINGKLDVRAL 452
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
505-982 |
1.80e-86 |
|
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: 290.22 E-value: 1.80e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 505 RIIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIH 584
Cdd:cd17645 2 QLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 585 QPAARLQRLMQRARlVCLVVRQPGEWgeivqlslpelmqdmsnairystpcallpdmqAYLLFTSGSTGEPKGVCVVHRG 664
Cdd:cd17645 82 YPGERIAYMLADSS-AKILLTNPDDL--------------------------------AYVIYTSGSTGLPKGVMIEHHN 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 665 LLNLLLDMQRTFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLTEAERAADSFRMIPLIAD------YRPTlmQAT 738
Cdd:cd17645 129 LVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQegitisFLPT--GAA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 739 PSFWHgLLMAGWRgdpelCVLAGGEALptKVAEellRCCGSLWNLYGPTETTIWSLKSQITQAE-NITLGAPIANTRIYI 817
Cdd:cd17645 207 EQFMQ-LDNQSLR-----VLLTGGDKL--KKIE---RKGYKLVNNYGPTENTVVATSFEIDKPYaNIPIGKPIDNTRVYI 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 818 LDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEPGVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYR 897
Cdd:cd17645 276 LDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYR 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 898 IELGEIERTLARHPHVDAAVVACIERAPLHKALAAFiITSEPPSLFEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKI 977
Cdd:cd17645 356 IEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAY-VTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKV 434
|
....*
gi 1288439980 978 DRKRL 982
Cdd:cd17645 435 DRKAL 439
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
507-894 |
6.91e-86 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 287.67 E-value: 6.91e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 507 IEQRCVQHPKQLAIQQHDG-TLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQ 585
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGrRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 586 PAARLQRLMQRARLVCLVVRQPG------EWGEIVQLSLPELMQDMSNAIRYST--------------PCALLPDMQAYL 645
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALkleellEALGKLEVVKLVLVLDRDPVLKEEPlpeeakpadvppppPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 646 LFTSGSTGEPKGVCVVHRGLLNLLLDM----QRTFAVGSQDRLLSVTTPTFDISF-LEYLLPLISGASLYLTEAERAADS 720
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 721 FRMIPLIADYRPTLMQATPSFWHGLLMAGWRGDPEL----CVLAGGEALPTKVAEELLRC-CGSLWNLYGPTETTIWSLK 795
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLsslrLVLSGGAPLPPELARRFRELfGGALVNGYGLTETTGVVTT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 796 SQITQAENITL---GAPIANTRIYILD-NEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEpgvpggRMFRTGD 871
Cdd:pfam00501 321 PLPLDEDLRSLgsvGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED------GWYRTGD 394
|
410 420
....*....|....*....|...
gi 1288439980 872 LVRSDAQGQLFFVGRKDSQIKLR 894
Cdd:pfam00501 395 LGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
515-982 |
1.13e-82 |
|
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: 280.51 E-value: 1.13e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 515 PKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLM 594
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 595 QRARlVCLVVRQ------PGEWGEIVQLSLPELMQDMSNAIRYSTPcallPDMQAYLLFTSGSTGEPKGVCVVHRGLLNL 668
Cdd:cd17656 82 LDSG-VRVVLTQrhlkskLSFNKSTILLEDPSISQEDTSNIDYINN----SDDLLYIIYTSGTTGKPKGVQLEHKNMVNL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 669 LLDMQRTFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLTEAERAADSFRMIPLIADYRPTLMQATPSFWHglLMA 748
Cdd:cd17656 157 LHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLK--FIF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 749 GWRG---DPELCV---LAGGEALP-TKVAEELLRCCG-SLWNLYGPTET---TIWSLKSQITQAENITLGAPIANTRIYI 817
Cdd:cd17656 235 SEREfinRFPTCVkhiITAGEQLViTNEFKEMLHEHNvHLHNHYGPSEThvvTTYTINPEAEIPELPPIGKPISNTWIYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 818 LDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEPGVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYR 897
Cdd:cd17656 315 LDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 898 IELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIItSEPPSLFEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKI 977
Cdd:cd17656 395 IELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV-MEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKV 473
|
....*
gi 1288439980 978 DRKRL 982
Cdd:cd17656 474 DRKAL 478
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
45-458 |
3.71e-79 |
|
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: 268.91 E-value: 3.71e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 45 IPLSFNQERLWFLQKYDSTATNYNLYVVYRLHGVVDMPMLTEALRHVQARHAILRTRIIVRNDRPCQVI--DDASSLVLD 122
Cdd:cd19540 2 IPLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVlpAAEARPDLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 123 TVTLAAqaptSALDAVIQQVINTRFDLARG-PLWGVTQIIQPDQgcH-LVFCAHHIIIDGISLRLLFDELQQQY-ARLhA 199
Cdd:cd19540 82 VVDVTE----DELAARLAEAARRGFDLTAElPLRARLFRLGPDE--HvLVLVVHHIAADGWSMAPLARDLATAYaARR-A 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 200 GNETSLPPPPLQYADYAFWQREWF-----QDTLLANELAYWRARLQDAPLLSTFPSLHPRPAQPSTHGSRFSITLDETLS 274
Cdd:cd19540 155 GRAPDWAPLPVQYADYALWQRELLgdeddPDSLAARQLAYWRETLAGLPEELELPTDRPRPAVASYRGGTVEFTIDAELH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 275 LALKHVARTQETTPFVLMLTAFQLVLMRYAQQQRLVIGMPVSGRIRPELQSSIGYYASTAVIYTDFNGVEVGREALQRVK 354
Cdd:cd19540 235 ARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 355 ASVKETQGRQQLPFENLVNMLDLPRSLSHSPLFQILYIYHNHVTPRaFTLAGAYWEQVTYHNQTVKYDMTVEVFQN---- 430
Cdd:cd19540 315 ETDLAAFAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAAT-LELPGLTVEPVPVDTGVAKFDLSFTLTERrdad 393
|
410 420 430
....*....|....*....|....*....|
gi 1288439980 431 --DATFDVSFEYDLGLYDADVVKQIAEALR 458
Cdd:cd19540 394 gaPAGLTGELEYATDLFDRSTAERLADRFV 423
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
45-473 |
9.97e-78 |
|
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: 265.35 E-value: 9.97e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 45 IPLSFNQERLWFLQKYDSTATNYNLYVVYRLHGVVDMPMLTEALRHVQARHAILRTRIIV-RNDRPCQVIDDASSL---V 120
Cdd:pfam00668 5 YPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRqENGEPVQVILEERPFeleI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 121 LDTVTLAAQAPTSALDAVIQQVINTRFDLARGPLWGVTQIIQPDQGCHLVFCAHHIIIDGISLRLLFDELQQQYARLHAG 200
Cdd:pfam00668 85 IDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLLKG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 201 NETSLPPPPlQYADYAFWQREWFQDTLLANELAYWRARLQDAPLLSTFPSLHPRPAQPSTHGSRFSITLDETLSLALKHV 280
Cdd:pfam00668 165 EPLPLPPKT-PYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLRKL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 281 ARTQETTPFVLMLTAFQLVLMRYAQQQRLVIGMPVSGRIRPELQSSIGYYASTAVIYTDFNGVEVGREALQRVKASVKET 360
Cdd:pfam00668 244 AKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLSA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 361 QGRQQLPFENLVNMLDLPRSLSHSPLFQILYIYHNH----VTPRAFTLAGAYWEQVTYHNQTVKYDMTVEVFQNDATFDV 436
Cdd:pfam00668 324 EPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYlgqdSQEEEFQLSELDLSVSSVIEEEAKYDLSLTASERGGGLTI 403
|
410 420 430
....*....|....*....|....*....|....*..
gi 1288439980 437 SFEYDLGLYDADVVKQIAEALRQHCLSLTSSLETPIG 473
Cdd:pfam00668 404 KIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLS 440
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
45-471 |
1.15e-77 |
|
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: 264.51 E-value: 1.15e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 45 IPLSFNQERLWFLQKYDSTATNYNLYVVYRLHGVVDMPMLTEALRHVQARHAILRTRIIVRNDRPCQVI--DDASSLVLD 122
Cdd:cd19538 2 IPLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLIleEDEATPKLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 123 TVtlaaQAPTSALDAVIQQVINTRFDLARGPLWGVTqIIQPDQGCH-LVFCAHHIIIDGISLRLLFDELQQQYARLHAGN 201
Cdd:cd19538 82 IK----EVDEEELESEINEAVRYPFDLSEEPPFRAT-LFELGENEHvLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 202 ETSLPPPPLQYADYAFWQREWFQD-----TLLANELAYWRARLQDAPLLSTFPSLHPRPAQPSTHGSRFSITLDETLSLA 276
Cdd:cd19538 157 APELAPLPVQYADYALWQQELLGDesdpdSLIARQLAYWKKQLAGLPDEIELPTDYPRPAESSYEGGTLTFEIDSELHQQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 277 LKHVARTQETTPFVLMLTAFQLVLMRYAQQQRLVIGMPVSGRIRPELQSSIGYYASTAVIYTDFNGVEVGREALQRVKAS 356
Cdd:cd19538 237 LLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKET 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 357 VKETQGRQQLPFENLVNMLDLPRSLSHSPLFQILYIYHNHVTPRaFTLAGAYWEQVTYHNQTVKYDMTVEVFQ-----ND 431
Cdd:cd19538 317 NLEAYEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPS-LDLPGLEAKLELRTVGSAKFDLTFELREqyndgTP 395
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1288439980 432 ATFDVSFEYDLGLYDADVVKQIAEALrqhCLSLTSSLETP 471
Cdd:cd19538 396 NGIEGFIEYRTDLFDHETIEALAQRY---LLLLESAVENP 432
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
501-984 |
2.46e-72 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 251.35 E-value: 2.46e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 501 QDVLRIIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAmrfraHGIQ---PGDRIGVLLPRHR--DVIATMLATWFVG 575
Cdd:PRK04813 2 MDIIETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALA-----AFIDslkLPDKSPIIVFGHMspEMLATFLGAVKAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 576 ACYVPFDIHQPAARLQRLMQ--RARLVCLVVRQPGEWGEIVQLSLPELMQDMSNAIRYSTPCALLPDMQAYLLFTSGSTG 653
Cdd:PRK04813 77 HAYIPVDVSSPAERIEMIIEvaKPSLIIATEELPLEILGIPVITLDELKDIFATGNPYDFDHAVKGDDNYYIIFTSGTTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 654 EPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSVTTPTFDISFLeYLLP-LISGASLYL---TEAERAADSFRMIPliaD 729
Cdd:PRK04813 157 KPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVM-DLYPtLASGGTLVAlpkDMTANFKQLFETLP---Q 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 730 YRPTLMQATPSFWHGLLMagwrgDPELC---------VLAGGEALPTKVAEELLRCCGS--LWNLYGPTETTIWSLKSQI 798
Cdd:PRK04813 233 LPINVWVSTPSFADMCLL-----DPSFNeehlpnlthFLFCGEELPHKTAKKLLERFPSatIYNTYGPTEATVAVTSIEI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 799 TQ---AENITL--GAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEPGVPGgrmFRTGDLV 873
Cdd:PRK04813 308 TDemlDQYKRLpiGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTFDGQPA---YHTGDAG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 874 RSDaQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAplHK--ALAAFIITSEppSLFE------- 944
Cdd:PRK04813 385 YLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKD--HKvqYLIAYVVPKE--EDFErefeltk 459
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1288439980 945 QLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAE 984
Cdd:PRK04813 460 AIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKALIE 499
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
45-450 |
5.21e-69 |
|
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: 239.20 E-value: 5.21e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 45 IPLSFNQERLWFLQKYDSTATNYNLYVVYRLHGVVDMPMLTEALRHVQARHAILRTRIIV-RNDRPCQVIDDASSLVLDT 123
Cdd:cd19539 2 IPLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRdDGGVPRQEILPPGPAPLEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 124 VTL--AAQAPTSALDAVIQQVINTRFDLARGPLWgVTQIIQPDQGCH-LVFCAHHIIIDGISLRLLFDELQQQYARLHAG 200
Cdd:cd19539 82 RDLsdPDSDRERRLEELLRERESRGFDLDEEPPI-RAVLGRFDPDDHvLVLVAHHTAFDAWSLDVFARDLAALYAARRKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 201 NETSLPPPPLQYADYAFWQREWFQDTLLANELAYWRARLQDAPLLsTFPSLHPRPAQPSTHGSRFSITLDETLSLALKHV 280
Cdd:cd19539 161 PAAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRGAEPT-ALPTDRPRPAGFPYPGADLRFELDAELVAALREL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 281 ARTQETTPFVLMLTAFQLVLMRYAQQQRLVIGMPVSGRIRPELQSSIGYYASTAVIYTDFNGVEVGREALQRVKASVKET 360
Cdd:cd19539 240 AKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 361 QGRQQLPFENLVNMLDLPRSLSHSPLFQILYIYHNHVTPRAFTLAGAYWEQVTYHNQTVKYDMTVEVFQNDATFDVSFEY 440
Cdd:cd19539 320 QRHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGELELAGGLSYTEGSDIPDGAKFDLNLTVTEEGTGLRGSLGY 399
|
410
....*....|
gi 1288439980 441 DLGLYDADVV 450
Cdd:cd19539 400 ATSLFDEETI 409
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
45-465 |
8.40e-69 |
|
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: 238.46 E-value: 8.40e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 45 IPLSFNQERLWFLQKYDSTATNYNLYVVYRLHGVVDMPMLTEALRHVQARHAILRTRIIVRNDRPCQVIDDASS----LV 120
Cdd:cd19066 2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVrfriEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 121 LDTVTLAAqaPTSALDAVIQQVINTRFDLARGPLWGVTQIIQPDQGCHLVFCAHHIIIDGISLRLLFDELQQQYARLHAG 200
Cdd:cd19066 82 IDLRNLAD--PEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 201 NETSlPPPPLQYADYAFWQREWFQDTLLANELAYWRARLQDAPLLSTFPSLHPRPAQPSTHGSRFSITLDETLSLALKHV 280
Cdd:cd19066 160 KPTL-PPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 281 ARTQETTPFVLMLTAFQLVLMRYAQQQRLVIGMPVSGRIRPELQSSIGYYASTAVIYTDFNGVEVGREALQRVKASVKET 360
Cdd:cd19066 239 ARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 361 QGRQQLPFENLVNMLDLPRSLSHSPLFQILYIYHNHVTPRAFTLAGAYWEQVTYHNQTVKYDMTVEVFQN-DATFDVSFE 439
Cdd:cd19066 319 IEHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIFTTPVYTSSEGTVFDLDLEASEDpDGDLLLRLE 398
|
410 420
....*....|....*....|....*.
gi 1288439980 440 YDLGLYDADVVKQIAEALRQHCLSLT 465
Cdd:cd19066 399 YSRGVYDERTIDRFAERYMTALRQLI 424
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
47-289 |
9.80e-67 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 225.69 E-value: 9.80e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 47 LSFNQERLWFLqkyDSTATNYNLYVVYRLHGVVDMPMLTEALRHVQARHAILRTRIIVRNDRPCQVIDDASSL---VLDT 123
Cdd:COG4908 1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLpleVVDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 124 VTLAAQAPTSALDAVIQQVINTRFDLARGPLWGVTQIIQPDQGCHLVFCAHHIIIDGISLRLLFDELQQQYARLHAGNET 203
Cdd:COG4908 78 SALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 204 SLPPPPLQYADYAFWQREWFQDTLLANELAYWRARLQDAPLLSTFPSLHPRPAQPSTHGSRFSITLDETLSLALKHVART 283
Cdd:COG4908 158 PLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAKA 237
|
....*.
gi 1288439980 284 QETTPF 289
Cdd:COG4908 238 HGATVN 243
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
45-455 |
1.53e-66 |
|
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: 232.15 E-value: 1.53e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 45 IPLSFNQERLWFLQKYDSTATNYNLYVVYRLHGVVDMPMLTEALRHVQARHAILRTRIIVRNDRPCQVIDDASSLVLDTV 124
Cdd:cd20483 2 RPMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 125 TLAAQA-PTSALDAVIQQVINTRFDLARGPLWGVTQIIQPDQGCHLVFCAHHIIIDGISLRLLFDELQQQYARLHAG-NE 202
Cdd:cd20483 82 DLSEAAdPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGrDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 203 TSLPPPPLQYADYAFWQREWFQDTLLANELAYWRARLQDAPLLStfpSLHP-----RPAQPSTHGSRFSITLDETLSLAL 277
Cdd:cd20483 162 ATVPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEGIPDAS---KLLPfakaeRPPVKDYERSTVEATLDKELLARM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 278 KHVARTQETTPFVLMLTAFQLVLMRYAQQQRLVIGMPVSGRIRPELQSSIGYYASTAVIYTDFNGVEVGREALQRVKASV 357
Cdd:cd20483 239 KRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 358 KETQGRQQLPFENLVNMLDLPRSLSHSPLFQILYIYHNHVTPRAFTLAGAYWEQVTYHNQTVKYDMTVEVFQN-DATFDV 436
Cdd:cd20483 319 LEAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQVHGKFPEYDTGDFKFTDYDHYDIPTACDIALEAEEDpDGGLDL 398
|
410
....*....|....*....
gi 1288439980 437 SFEYDLGLYDADVVKQIAE 455
Cdd:cd20483 399 RLEFSTTLYDSADMERFLD 417
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
46-432 |
1.06e-65 |
|
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: 229.27 E-value: 1.06e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 46 PLSFNQERLWFLQKY--DSTAtnYNLYVVYRLHGVVDMPMLTEALRHVQARHAILRTRIIVR--NDRPCQVIDDASSLVL 121
Cdd:cd19532 3 PMSFGQSRFWFLQQYleDPTT--FNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDpeDGEPMQGVLASSPLRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 122 DTVTLAAQAptsALDAVIQQVINTRFDLARGPLWGVTQIIQPDQGCHLVFCAHHIIIDGISLRLLFDELQQQYARLhagn 201
Cdd:cd19532 81 EHVQISDEA---EVEEEFERLKNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQ---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 202 etSLPPPPLQYADYAFWQREWFQDTLLANELAYWRARLQDA----PLLStFPSLHPRPAQPSTHGSRFSITLDETLSLAL 277
Cdd:cd19532 154 --PLLPPPLQYLDFAARQRQDYESGALDEDLAYWKSEFSTLpeplPLLP-FAKVKSRPPLTRYDTHTAERRLDAALAARI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 278 KHVARTQETTPFVLMLTAFQLVLMRYAQQQRLVIGMPVSGRIRPELQSSIGYYASTAVIYTDFNGVEVGREALQRVKASV 357
Cdd:cd19532 231 KEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDKA 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1288439980 358 KETQGRQQLPFENLVNMLDLPRSLSHSPLFQILYIYHNHVTpRAFTLAGAYWEQVTYHNQTVKYDMTVEVFQNDA 432
Cdd:cd19532 311 YAALAHSRVPFDVLLDELGVPRSATHSPLFQVFINYRQGVA-ESRPFGDCELEGEEFEDARTPYDLSLDIIDNPD 384
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
643-978 |
4.41e-65 |
|
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: 224.47 E-value: 4.41e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 643 AYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSvTTPTFDISFL-EYLLPLISGASLYLTEAERAADsf 721
Cdd:cd04433 3 ALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLS-TLPLFHIGGLfGLLGALLAGGTVVLLPKFDPEA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 722 rMIPLIADYRPTLMQATPSFWHGLLMAGWRGDPEL----CVLAGGEALPTKVAEELLRCCGS-LWNLYGPTET----TIW 792
Cdd:cd04433 80 -ALELIEREKVTILLGVPTLLARLLKAPESAGYDLsslrALVSGGAPLPPELLERFEEAPGIkLVNGYGLTETggtvATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 793 SLKSQITQAEniTLGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFlsepgvpGGRMFRTGDL 872
Cdd:cd04433 159 PPDDDARKPG--SVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD-------EDGWYRTGDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 873 VRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEPPSL-FEQLKNELR 951
Cdd:cd04433 230 GRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLdAEELRAHVR 309
|
330 340
....*....|....*....|....*..
gi 1288439980 952 QQLPDYMVPTLWQRVADFPNTDNGKID 978
Cdd:cd04433 310 ERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
235-1071 |
6.07e-60 |
|
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: 227.64 E-value: 6.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 235 WRARLqDAPLLSTFPSLHPRPAQ-PSTHGSrfsitldETLSLALKHVARTQETTPFVLMLTAFQLVLMRYAQQQRLVIGm 313
Cdd:TIGR03443 2 WSERL-DNPTLSVLPHDYLRPANnRLVEAT-------YSLQLPSAEVTAGGGSTPFIILLAAFAALVYRLTGDEDIVLG- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 314 pvsgrirpelqSSIGYYASTAVIYTDFNGVEVGREALQRVKASVKETQGRQQLPFENLVNMLDLPRSL-SHSPLFQILYi 392
Cdd:TIGR03443 73 -----------TSSNKSGRPFVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLeRTPPLFRLAF- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 393 YHNHVTPraftlagayweQVTYhNQTVKYDMTVEVFQNDATFDVSFEYDLGLYDADVVKQIAEALRQHCLSLTSSLETPI 472
Cdd:TIGR03443 141 QDAPDNQ-----------QTTY-STGSTTDLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPI 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 473 GAIPLHAPETATPRRDPlnATNVPWLG----PQDVL-----RIIEQRC-VQHPKQLAIQQHDGTLTYAELWARVQFIAMR 542
Cdd:TIGR03443 209 GKVSLITPSQKSLLPDP--TKDLDWSGfrgaIHDIFadnaeKHPDRTCvVETPSFLDPSSKTRSFTYKQINEASNILAHY 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 543 FRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLMQRARLVCLVV-RQPGEWGEIV------Q 615
Cdd:TIGR03443 287 LLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIViEKAGTLDQLVrdyidkE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 616 LSL----PEL-MQD----------------MSNAIRY-STPCALL--PDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLD 671
Cdd:TIGR03443 367 LELrteiPALaLQDdgslvggsleggetdvLAPYQALkDTPTGVVvgPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPW 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 672 MQRTFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLTEAERAADSFRMIPLIADYRPTLMQATPSFwhGLLMAG-- 749
Cdd:TIGR03443 447 MAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAM--GQLLSAqa 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 750 -----------WRGDpelcVLaggealpTKvaeellRCCGSLW---------NLYGPTET-------TIWSLKSQITQAE 802
Cdd:TIGR03443 525 ttpipslhhafFVGD----IL-------TK------RDCLRLQtlaenvcivNMYGTTETqravsyfEIPSRSSDSTFLK 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 803 N----ITLGAPIANTRIYILDNEGHPVPQGVD--GELYIAGDGVAQGYDGQPELNAQFFLS----EPGV----------- 861
Cdd:TIGR03443 588 NlkdvMPAGKGMKNVQLLVVNRNDRTQTCGVGevGEIYVRAGGLAEGYLGLPELNAEKFVNnwfvDPSHwidldkennkp 667
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 862 -------PGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFI 934
Cdd:TIGR03443 668 erefwlgPRDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYI 747
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 935 ITSEPPSLFEQLKNE---------------------------LRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRL----- 982
Cdd:TIGR03443 748 VPQDKSDELEEFKSEvddeessdpvvkglikyrklikdireyLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALpfpdt 827
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 983 AE-NFVADSSLVSPQTQALSDTEQMLLALWMRYLPIK--NVDPECDFFRLGGHSLLAVTLVAEINRTFHCALTLKDIFHY 1059
Cdd:TIGR03443 828 AQlAAVAKNRSASAADEEFTETEREIRDLWLELLPNRpaTISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKS 907
|
970
....*....|..
gi 1288439980 1060 STLRALSARIAQ 1071
Cdd:TIGR03443 908 PTIKGFAKEVDR 919
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
524-982 |
1.18e-58 |
|
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: 210.02 E-value: 1.18e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 524 DGTLTYAELWARVQFIAMRFRAHGiQPGDRiGVLLPRHRDVIATM--LATWFVGACYVPFDIHQPAARLQRLMQRARLVC 601
Cdd:cd17654 14 DTTVSYADLAEKISNLSNFLRKKF-QTEER-AIGLRCDRGTESPVaiLAILFLGAAYAPIDPASPEQRSLTVMKKCHVSY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 602 LVVRQpgewgeivqlslpelmqDMSNAIRYSTPCALLPDMQ-----AYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTF 676
Cdd:cd17654 92 LLQNK-----------------ELDNAPLSFTPEHRHFNIRtdeclAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 677 AVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLTEAERAADSFRMIPLIA-DYRPTLMQATPSFWHGLLMAGWR---- 751
Cdd:cd17654 155 NITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILFkRHRITVLQATPTLFRRFGSQSIKstvl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 752 -GDPELCVLA-GGEALPTKVAEELLRCCGS---LWNLYGPTETTIWSLKSQITQAEN-ITLGAPIANTRIYILDNEGHPv 825
Cdd:cd17654 235 sATSSLRVLAlGGEPFPSLVILSSWRGKGNrtrIFNIYGITEVSCWALAYKVPEEDSpVQLGSPLLGTVIEVRDQNGSE- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 826 pqgVDGELYIAGdgvaqgydgqpeLNAQFFLSEP-GVPGGRMFRTGDLVRSDaQGQLFFVGRKDSQIKLRGYRIELGEIE 904
Cdd:cd17654 314 ---GTGQVFLGG------------LNRVCILDDEvTVPKGTMRATGDFVTVK-DGELFFLGRKDSQIKRRGKRINLDLIQ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 905 RTLARHPHVDAAVVACIERAPLHkalaAFIITSEPPS-LFEQLKNEL--RQQLPDYMVptlwqRVADFPNTDNGKIDRKR 981
Cdd:cd17654 378 QVIESCLGVESCAVTLSDQQRLI----AFIVGESSSSrIHKELQLTLlsSHAIPDTFV-----QIDKLPLTSHGKVDKSE 448
|
.
gi 1288439980 982 L 982
Cdd:cd17654 449 L 449
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1089-1595 |
1.23e-57 |
|
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: 220.11 E-value: 1.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1089 DPEHRHQPFPLTDVQRAYWLGRQTGATSIATHIYHEFDVEHFNVTRFTHAVNALIARHEMLRARVLPDGTQQILAQVPAY 1168
Cdd:COG1020 17 PLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1169 QLEQRDLSALSPNARNDALMAIRDRLSHHVHPADRWPLFDFSYSACTAQHGRLHFSLDLLIADALSMRTLQQELMMLYRE 1248
Cdd:COG1020 97 VVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYAG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1249 PHVSLPLLPFSFRDYVQALLVEQASEAYARDQAYWQRALPQLYGPPTLPVQGDLAQLSAIRFVRRRHRLSAHNWGVLSAL 1328
Cdd:COG1020 177 APLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAALRAL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1329 AQRTRITKTALLLTVFSQVLARWSLSPTFTLNLTLFNRPQgyPNAEAVIGDFTAVSLLNVCYDSQHSYAHNAQRIQVQLW 1408
Cdd:COG1020 257 ARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPR--PELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1409 EDLEHRRFSGIRASEALiHSGRFHAPMPvVFTSMLDIdgETTAQDPRDTTRFTLCPDANITQTPQVWLDHQVIELAGELH 1488
Cdd:COG1020 335 AAYAHQDLPFERLVEEL-QPERDLSRNP-LFQVMFVL--QNAPADELELPGLTLEPLELDSGTAKFDLTLTVVETGDGLR 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1489 FNWDAVEQLFDTTLLDQMFGAYCHALQALVAMPQSWWGvnsslALPTVSAP----------VTQAPAPT-ALLHHGLLRQ 1557
Cdd:COG1020 411 LTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLG-----DLPLLTAAerqqllaewnATAAPYPAdATLHELFEAQ 485
|
490 500 510
....*....|....*....|....*....|....*...
gi 1288439980 1558 AALTPQETALISPIRELTYRQLSTAADHVARALLALGV 1595
Cdd:COG1020 486 AARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGV 523
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
507-979 |
2.28e-57 |
|
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: 205.54 E-value: 2.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 507 IEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDihqp 586
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLN---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 587 aarlQRLMqrarlvclvvrqPGEWGEIVQLSLPELMQDmsnairystpcallpDMqAYLLFTSGSTGEPKGVCVVHRGLL 666
Cdd:cd17631 77 ----FRLT------------PPEVAYILADSGAKVLFD---------------DL-ALLMYTSGTTGRPKGAMLTHRNLL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 667 NLLLDMQRTFAVGSQDRLLsVTTPTFDISFLE-YLLP-LISGASLYLTEAERAADSFRmipLIADYRPTLMQATPSFWHG 744
Cdd:cd17631 125 WNAVNALAALDLGPDDVLL-VVAPLFHIGGLGvFTLPtLLRGGTVVILRKFDPETVLD---LIERHRVTSFFLVPTMIQA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 745 LLMAGWRGDPEL----CVLAGGEALPTKVAEELLRCCGSLWNLYGPTETT--IWSLKSQITQAENITLGAPIANTRIYIL 818
Cdd:cd17631 201 LLQHPRFATTDLsslrAVIYGGAPMPERLLRALQARGVKFVQGYGMTETSpgVTFLSPEDHRRKLGSAGRPVFFVEVRIV 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 819 DNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFlsepgvpGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRI 898
Cdd:cd17631 281 DPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-------RDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENV 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 899 ELGEIERTLARHPHV-DAAVVAcierAPLHK---ALAAFIITSEPPSLFE-QLKNELRQQLPDYMVPTLWQRVADFPNTD 973
Cdd:cd17631 354 YPAEVEDVLYEHPAVaEVAVIG----VPDEKwgeAVVAVVVPRPGAELDEdELIAHCRERLARYKIPKSVEFVDALPRNA 429
|
....*.
gi 1288439980 974 NGKIDR 979
Cdd:cd17631 430 TGKILK 435
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
503-982 |
5.81e-56 |
|
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: 202.41 E-value: 5.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 503 VLRIIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFD 582
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 583 IHQPAARLQRLMQR--ARLVclvvrqpgewgeIVQLSLPELMQDmsnAIRYSTPCALLPDMQAYLLFTSGSTGEPKGVCV 660
Cdd:cd05936 81 PLYTPRELEHILNDsgAKAL------------IVAVSFTDLLAA---GAPLGERVALTPEDVAVLQYTSGTTGVPKGAML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 661 VHRgllNLLLDMQRTFAV-----GSQDRLLsVTTPTFDISFLE--YLLPLISGASLYLTEAERAAdsfRMIPLIADYRPT 733
Cdd:cd05936 146 THR---NLVANALQIKAWledllEGDDVVL-AALPLFHVFGLTvaLLLPLALGATIVLIPRFRPI---GVLKEIRKHRVT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 734 LMQATPSFWHGLLMAGWRGDPEL----CVLAGGEALPTKVA---EELLRCcgslwNL---YGPTETtiwslkSQITQAEN 803
Cdd:cd05936 219 IFPGVPTMYIALLNAPEFKKRDFsslrLCISGGAPLPVEVAerfEELTGV-----PIvegYGLTET------SPVVAVNP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 804 I-------TLGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLsepgvpGGRmFRTGDLVRSD 876
Cdd:cd05936 288 LdgprkpgSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV------DGW-LRTGDIGYMD 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 877 AQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEPPSLFE-QLKNELRQQLP 955
Cdd:cd05936 361 EDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEeEIIAFCREQLA 440
|
490 500
....*....|....*....|....*..
gi 1288439980 956 DYMVPTLWQRVADFPNTDNGKIDRKRL 982
Cdd:cd05936 441 GYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
526-982 |
1.82e-54 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 200.72 E-value: 1.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 526 TLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGAcyvpfdIHQP----------AARLQRLmq 595
Cdd:COG0365 39 TLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGA------VHSPvfpgfgaealADRIEDA-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 596 RARLV-------------------------------CLVVRQPGEWGEIV-QLSLPELMQDMSNAIrysTPCALLPDMQA 643
Cdd:COG0365 111 EAKVLitadgglrggkvidlkekvdealeelpslehVIVVGRTGADVPMEgDLDWDELLAAASAEF---EPEPTDADDPL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 644 YLLFTSGSTGEPKGVCVVHRG-LLNLLLDMQRTFAVGSQDRLLSVTTPTFdISFLEYLL--PLISGASLYLTE-AERAAD 719
Cdd:COG0365 188 FILYTSGTTGKPKGVVHTHGGyLVHAATTAKYVLDLKPGDVFWCTADIGW-ATGHSYIVygPLLNGATVVLYEgRPDFPD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 720 SFRMIPLIADYRPTLMQATPSFWHGLLMAG--WRGDP-----ELCVLAGgEALPTKVAE---ELLRCCgsLWNLYGPTET 789
Cdd:COG0365 267 PGRLWELIEKYGVTVFFTAPTAIRALMKAGdePLKKYdlsslRLLGSAG-EPLNPEVWEwwyEAVGVP--IVDGWGQTET 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 790 TiwslkSQITQAENIT------LGAPIANTRIYILDNEGHPVPQGVDGELYIAGD--GVAQGYDGQPELNAQFFLSE-PG 860
Cdd:COG0365 344 G-----GIFISNLPGLpvkpgsMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPwpGMFRGYWNDPERYRETYFGRfPG 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 861 VpggrmFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHV-DAAVVAcierAPLHK---ALAAFIIT 936
Cdd:COG0365 419 W-----YRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVaEAAVVG----VPDEIrgqVVKAFVVL 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1288439980 937 SEPPSLFEQLKNEL----RQQLPDYMVPTLWQRVADFPNTDNGKIDRKRL 982
Cdd:COG0365 490 KPGVEPSDELAKELqahvREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
44-468 |
2.78e-53 |
|
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: 193.69 E-value: 2.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 44 AIPLSFNQERLWFLQKYDSTATNYNLYVVYRLHGVVDMPMLTEALRHVQARHAILRTRIIVRNDRPCQVIDDASSLVLDT 123
Cdd:cd20484 1 RSPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 124 VTLAAQAPtSALDAVIQQVINTRFDLARGPLWGVTQIIQPDQGCHLVFCAHHIIIDGISLRLLFDELQQQYARLHAGNET 203
Cdd:cd20484 81 EDISSLKE-SEIIAYLREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 204 SLPPPPLQYADYAfwqrEWFQDTLLANE----LAYWRARLQDA-PLLStFPSLHPRPAQPSTHGSRFSITLDETLSLALK 278
Cdd:cd20484 160 TLASSPASYYDFV----AWEQDMLAGAEgeehRAYWKQQLSGTlPILE-LPADRPRSSAPSFEGQTYTRRLPSELSNQIK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 279 HVARTQETTPFVLMLTAFQLVLMRYAQQQRLVIGMPVSGRIRPELQSSIGYYASTAVIYTDFNGVEVGREALQRVKASVK 358
Cdd:cd20484 235 SFARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 359 ETQGRQQLPFENLVNMLDLPRSLSHSPLFQILYIYHNHVTPRAFTLAGAYW------EQVTYHNQTVKYDMTVEVFQNDA 432
Cdd:cd20484 315 DGLDHAAYPFPAMVRDLNIPRSQANSPVFQVAFFYQNFLQSTSLQQFLAEYqdvlsiEFVEGIHQEGEYELVLEVYEQED 394
|
410 420 430
....*....|....*....|....*....|....*.
gi 1288439980 433 TFDVSFEYDLGLYDADVVKQIAEalrqHCLSLTSSL 468
Cdd:cd20484 395 RFTLNIKYNPDLFDASTIERMME----HYVKLAEEL 426
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
500-1595 |
4.32e-51 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 200.01 E-value: 4.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 500 PQDVLRIIEQRCVQHPKQLAI------QQHDGTLTYAELWARVQFIAMRFRAHGiQPGDRIGVLLPRHRDVIATMLATWF 573
Cdd:PRK05691 8 PLTLVQALQRRAAQTPDRLALrfladdPGEGVVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 574 VGACYVPF-------DIHQpaARLQRLMQRAR----LVCLVVRQP-GEWGEIVQLSLPELMQ----DMSNAIRYSTPcAL 637
Cdd:PRK05691 87 AGVIAVPAyppesarRHHQ--ERLLSIIADAEprllLTVADLRDSlLQMEELAAANAPELLCvdtlDPALAEAWQEP-AL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 638 LPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFA--VGSQDRLLSVTTPTFDISFLEYLL-PLISGASLYL-TE 713
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGLIGGLLqPIFSGVPCVLmSP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 714 AERAADSFRMIPLIADYRPTLmQATPSFWH-------------GLLMAGWRgdpelCVLAGGEALPTKVAE---ELLRCC 777
Cdd:PRK05691 244 AYFLERPLRWLEAISEYGGTI-SGGPDFAYrlcservsesaleRLDLSRWR-----VAYSGSEPIRQDSLErfaEKFAAC 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 778 G----SLWNLYGPTETTIWSLKSQITQ------------AEN----------ITLGAPIANTRIYILD-NEGHPVPQGVD 830
Cdd:PRK05691 318 GfdpdSFFASYGLAEATLFVSGGRRGQgipaleldaealARNraepgtgsvlMSCGRSQPGHAVLIVDpQSLEVLGDNRV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 831 GELYIAGDGVAQGYDGQPELNAQFFLSEPGvpgGRMFRTGDL--VRsdaQGQLFFVGRKDSQIKLRGYRIELGEIERTLA 908
Cdd:PRK05691 398 GEIWASGPSIAHGYWRNPEASAKTFVEHDG---RTWLRTGDLgfLR---DGELFVTGRLKDMLIVRGHNLYPQDIEKTVE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 909 RhphvdaavvaciERAPLHKA-LAAFIIT---SEPPSLFEQLKNELRQQL-PDYMVPTLWQRVAD--------------- 968
Cdd:PRK05691 472 R------------EVEVVRKGrVAAFAVNhqgEEGIGIAAEISRSVQKILpPQALIKSIRQAVAEacqeapsvvlllnpg 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 969 -FPNTDNGKIDRK----RLAENFV--------ADSSLVSPQTQALSDTEQMLLALWMRYLPIKNVDPECDFFRLGGHSLL 1035
Cdd:PRK05691 540 aLPKTSSGKLQRSacrlRLADGSLdsyalfpaLQAVEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIA 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1036 AVTLVAEINRTFHCALTLKDIFHYSTLRALSARIAQQSITDAAASQddwVIVHDPehRHQPFPLTDVQRAYWLGRQTGAT 1115
Cdd:PRK05691 620 ATQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVARQLAGGGAAQA---AIARLP--RGQALPQSLAQNRLWLLWQLDPQ 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1116 SIATHIYHEFDVE-HFNVTRFTHAVNALIARHEMLRARVLP-DGT--QQILAQVPaYQLEQRDLSALSPNARNDALMAIR 1191
Cdd:PRK05691 695 SAAYNIPGGLHLRgELDEAALRASFQRLVERHESLRTRFYErDGValQRIDAQGE-FALQRIDLSDLPEAEREARAAQIR 773
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1192 DRLSHHVHPADRWPLFDFSYSACTAQHGRLHFSLDLLIADALSMRTLQQELMMLYREP----HVSLPLLPFSFRDYVQAL 1267
Cdd:PRK05691 774 EEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAAcqgqTAELAPLPLGYADYGAWQ 853
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1268 LVEQASEAYARDQAYWQRALPQLYGPPTLPV---QGDLAQLSAIRFVRrrhRLSAHNWGVLSALAQRTRITKTALLLTVF 1344
Cdd:PRK05691 854 RQWLAQGEAARQLAYWKAQLGDEQPVLELATdhpRSARQAHSAARYSL---RVDASLSEALRGLAQAHQATLFMVLLAAF 930
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1345 SQVLARWSLSPTFTLNLTLFNRPQgyPNAEAVIGDFTAVSLLNVCYDSQHSYAHNAQRIQVQLWEDLEHRRFSGIRASEA 1424
Cdd:PRK05691 931 QALLHRYSGQGDIRIGVPNANRPR--LETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEA 1008
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1425 LiHSGRFHAPMPVVFTsmldidgettaQDPRDTTRFTLCPDANITQTP------------QVWLDHQvielaGELHFNWD 1492
Cdd:PRK05691 1009 L-PQAREQGLFQVMFN-----------HQQRDLSALRRLPGLLAEELPwhsreakfdlqlHSEEDRN-----GRLTLSFD 1071
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1493 AVEQLFDTTLLDQMFGAYCHALQALVAMPQSWWGVNSSLALPTVS--APVTQAPAPTA--LLHHGLLRQAALTPQETALI 1568
Cdd:PRK05691 1072 YAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAqlAQWGQAPCAPAqaWLPELLNEQARQTPERIALV 1151
|
1210 1220
....*....|....*....|....*..
gi 1288439980 1569 SPIRELTYRQLSTAADHVARALLALGV 1595
Cdd:PRK05691 1152 WDGGSLDYAELHAQANRLAHYLRDKGV 1178
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
528-982 |
3.77e-49 |
|
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: 181.34 E-value: 3.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 528 TYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLMQRARlvclvvrqp 607
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSG--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 608 gewgeivqlslpelmqdmsnairystPCALLPDMqAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLsV 687
Cdd:cd05934 76 --------------------------AQLVVVDP-ASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYL-T 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 688 TTPTFDISFLEY--LLPLISGASLYLTEAERAAdsfRMIPLIADYRPTLMQATPSFWHGLLMAGWRGDPE---LCVLAGG 762
Cdd:cd05934 128 VLPLFHINAQAVsvLAALSVGATLVLLPRFSAS---RFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRahrLRAAYGA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 763 EALPTKVAEELLRCCGSLWNLYGPTETT--IWSLKSQITQAENITLGAPIANTRIyiLDNEGHPVPQGVDGELYI---AG 837
Cdd:cd05934 205 PNPPELHEEFEERFGVRLLEGYGMTETIvgVIGPRDEPRRPGSIGRPAPGYEVRI--VDDDGQELPAGEPGELVIrglRG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 838 DGVAQGYDGQPELNAQFFlsepgvPGGrMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAV 917
Cdd:cd05934 283 WGFFKGYYNMPEATAEAM------RNG-WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAA 355
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1288439980 918 VACIERAPLHKALAAFIITSEPPSL-FEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRL 982
Cdd:cd05934 356 VVAVPDEVGEDEVKAVVVLRPGETLdPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQL 421
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
515-984 |
2.14e-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: 180.97 E-value: 2.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 515 PKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLM 594
Cdd:cd05926 3 APALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 595 QRARLVcLVVRQPGEWGEIV------QLSLPELMQDMSNAIRY----------------STPCALLPDMQAYLLFTSGST 652
Cdd:cd05926 83 ADLGSK-LVLTPKGELGPASraasklGLAILELALDVGVLIRApsaeslsnlladkknaKSEGVPLPDDLALILHTSGTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 653 GEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLsVTTPTFDISFL--EYLLPLISGASLYLTEAERAADSFrmiPLIADY 730
Cdd:cd05926 162 GRPKGVPLTHRNLAASATNITNTYKLTPDDRTL-VVMPLFHVHGLvaSLLSTLAAGGSVVLPPRFSASTFW---PDVRDY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 731 RPTLMQATPSFWHGLLM----AGWRGDPEL-CVLAGGEALPTKVAEELLRCCG-SLWNLYGPTETTiwslkSQITqAENI 804
Cdd:cd05926 238 NATWYTAVPTIHQILLNrpepNPESPPPKLrFIRSCSASLPPAVLEALEATFGaPVLEAYGMTEAA-----HQMT-SNPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 805 --------TLGAPiANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLsepgvpGGRMFRTGDLVRSD 876
Cdd:cd05926 312 ppgprkpgSVGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAF------KDGWFRTGDLGYLD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 877 AQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEPPSL-FEQLKNELRQQLP 955
Cdd:cd05926 385 ADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVtEEELRAFCRKHLA 464
|
490 500
....*....|....*....|....*....
gi 1288439980 956 DYMVPTLWQRVADFPNTDNGKIDRKRLAE 984
Cdd:cd05926 465 AFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
517-982 |
7.15e-48 |
|
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: 178.04 E-value: 7.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 517 QLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGAcyVPFDIHqpaarlqrlmqr 596
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGA--IAVVIN------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 597 arlvclvvrqpgewgeivqlslPELM-QDMSNAIRYSTPCALL--PDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQ 673
Cdd:cd05919 67 ----------------------PLLHpDDYAYIARDCEARLVVtsADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 674 R-TFAVGSQDRLLSVTTPTFDISFLEYLL-PLISGASLYLTEAERAADsfRMIPLIADYRPTLMQATPSFWHGLLMAGwR 751
Cdd:cd05919 125 ReALGLTPGDRVFSSAKMFFGYGLGNSLWfPLAVGASAVLNPGWPTAE--RVLATLARFRPTVLYGVPTFYANLLDSC-A 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 752 GDPEL-----CVLAGGEALPTKVAEELLRCCG-SLWNLYGPTETTIWSLKSQITQAENITLGAPIANTRIYILDNEGHPV 825
Cdd:cd05919 202 GSPDAlrslrLCVSAGEALPRGLGERWMEHFGgPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEGHTI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 826 PQGVDGELYIAGDGVAQGYDGQPELNAQFFLsepgvpgGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIER 905
Cdd:cd05919 282 PPGEEGDLLVRGPSAAVGYWNNPEKSRATFN-------GGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVES 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 906 TLARHPHV-DAAVVACIERAPLHKaLAAFIITSEP----PSLFEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRK 980
Cdd:cd05919 355 LIIQHPAVaEAAVVAVPESTGLSR-LTAFVVLKSPaapqESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRF 433
|
..
gi 1288439980 981 RL 982
Cdd:cd05919 434 KL 435
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
543-983 |
1.70e-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: 174.55 E-value: 1.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 543 FRAHGIQPGDRIGVLLPRHRDVIATM---------LATWFV--GACYVPFDIHQPAARLQR--------LMQRARLVCLV 603
Cdd:cd05922 10 LLEAGGVRGERVVLILPNRFTYIELSfavayaggrLGLVFVplNPTLKESVLRYLVADAGGrivladagAADRLRDALPA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 604 VRQPGEWgeivqLSLPELMQDMSNAIRYStpcaLLPDMQAYLLFTSGSTGEPKGVCVVHRGLL------NLLLDMQRTfa 677
Cdd:cd05922 90 SPDPGTV-----LDADGIRAARASAPAHE----VSHEDLALLLYTSGSTGSPKLVRLSHQNLLanarsiAEYLGITAD-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 678 vgsqDRLLSVTTPTFDISFLEYLLPLISGASLYLTEAERAADSFrmIPLIADYRPTLMQATPSFWHGLLMAGWR--GDPE 755
Cdd:cd05922 159 ----DRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAF--WEDLREHGATGLAGVPSTYAMLTRLGFDpaKLPS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 756 LCVL--AGGEALPTKVAEelLRCCGSLWNL---YGPTETTiwsLKSQITQAENI-----TLGAPIANTRIYILDNEGHPV 825
Cdd:cd05922 233 LRYLtqAGGRLPQETIAR--LRELLPGAQVyvmYGQTEAT---RRMTYLPPERIlekpgSIGLAIPGGEFEILDDDGTPT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 826 PQGVDGELYIAGDGVAQGYdgqpeLNAQFFLSEPGVPGGRMfRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIER 905
Cdd:cd05922 308 PPGEPGEIVHRGPNVMKGY-----WNDPPYRRKEGRGGGVL-HTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEA 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1288439980 906 TLARHPHVDAAVVACIErAPLHKALAAFIITSEPPSLFEQLKnELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLA 983
Cdd:cd05922 382 AARSIGLIIEAAAVGLP-DPLGEKLALFVTAPDKIDPKDVLR-SLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
526-984 |
2.66e-46 |
|
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: 173.34 E-value: 2.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 526 TLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFdihQPAARLQRL---MQRARLVCL 602
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPI---LPFFREHELafiLRRAKAKVF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 603 VVrqPGEWGeivqlslpelmqdmsnairySTPCALLPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQD 682
Cdd:cd05903 78 VV--PERFR--------------------QFDPAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 683 RLLsVTTPTFDISFLEY--LLPLISGASLYLTEAERAADSFRmipLIADYRPTLMQATPSFWHGLLMAGWRGDPELC--- 757
Cdd:cd05903 136 VFL-VASPMAHQTGFVYgfTLPLLLGAPVVLQDIWDPDKALA---LMREHGVTFMMGATPFLTDLLNAVEEAGEPLSrlr 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 758 -VLAGGEALPTKVAEELLRCCGS-LWNLYGPTE--TTIWSLKSQITQAENITLGAPIANTRIYILDNEGHPVPQGVDGEL 833
Cdd:cd05903 212 tFVCGGATVPRSLARRAAELLGAkVCSAYGSTEcpGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGEL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 834 YIAGDGVAQGYDGQPELNAQFFlsepgvPGGrMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHV 913
Cdd:cd05903 292 LSRGPSVFLGYLDRPDLTADAA------PEG-WFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGV 364
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1288439980 914 -DAAVVACI-ERapLHKALAAFIITSEPPSL-FEQLKNEL-RQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAE 984
Cdd:cd05903 365 iEAAVVALPdER--LGERACAVVVTKSGALLtFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
528-982 |
2.72e-46 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 173.40 E-value: 2.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 528 TYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLMQRARLVCLVVRQP 607
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 608 GEWGEIVQLSLPELMQDMSNAIRYSTPCALlpDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSV 687
Cdd:TIGR01923 81 LEEKDFQADSLDRIEAAGRYETSLSASFNM--DQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWLLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 688 TtPTFDISFLEYLLP-LISGASLYLteAERAADSFRMIpliADYRPTLMQATPSFWHGLLMAGWRGDPELCVLAGGEALP 766
Cdd:TIGR01923 159 L-PLYHISGLSILFRwLIEGATLRI--VDKFNQLLEMI---ANERVTHISLVPTQLNRLLDEGGHNENLRKILLGGSAIP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 767 TKVAEELLRCCGSLWNLYGPTETTiwslkSQITQAENITL------GAPIAN--TRIYILDNEGHpvpqgvdGELYIAGD 838
Cdd:TIGR01923 233 APLIEEAQQYGLPIYLSYGMTETC-----SQVTTATPEMLharpdvGRPLAGreIKIKVDNKEGH-------GEIMVKGA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 839 GVAQGYDGQPELNAQFFlsEPGvpggrMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVV 918
Cdd:TIGR01923 301 NLMKGYLYQGELTPAFE--QQG-----WFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVV 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1288439980 919 ACIERAPLHKALAAFIITSEPPSLfEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRL 982
Cdd:TIGR01923 374 VPKPDAEWGQVPVAYIVSESDISQ-AKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
527-982 |
3.12e-46 |
|
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: 172.91 E-value: 3.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 527 LTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVP-FDIHQPAARLQRlMQRARLVCLVVR 605
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPlTTLLGPKDIEYR-LEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 606 QpgewgeivqlslpelmQDMsnairystpcallpdmqAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLL 685
Cdd:cd05972 80 A----------------EDP-----------------ALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHW 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 686 SVTTPTFdISFLEY--LLPLISGASLYLTEAERaADSFRMIPLIADYRPTLMQATPSFWHGL----LMAGWRGDPELCVl 759
Cdd:cd05972 127 NIADPGW-AKGAWSsfFGPWLLGATVFVYEGPR-FDAERILELLERYGVTSFCGPPTAYRMLikqdLSSYKFSHLRLVV- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 760 AGGEALPTKVAEELLRCCG-SLWNLYGPTETTIWSLKSQITQAENITLGAPIANTRIYILDNEGHPVPQGVDGELYI--A 836
Cdd:cd05972 204 SAGEPLNPEVIEWWRAATGlPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIklP 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 837 GDGVAQGYDGQPELNAQFFlsepgvpGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHV-DA 915
Cdd:cd05972 284 PPGLFLGYVGDPEKTEASI-------RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVaEA 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 916 AVVACI--ERAPLHKALAAFIITSEPP-SLFEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRL 982
Cdd:cd05972 357 AVVGSPdpVRGEVVKAFVVLTSGYEPSeELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
525-982 |
8.76e-46 |
|
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: 173.71 E-value: 8.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 525 GTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLMQ--RARLVCL 602
Cdd:cd05959 28 GSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEdsRARVVVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 603 ---------------------VVRQPGEWGEIVQLSLPELMQDMSNAIrysTPCALLPDMQAYLLFTSGSTGEPKGVCVV 661
Cdd:cd05959 108 sgelapvlaaaltksehtlvvLIVSGGAGPEAGALLLAELVAAEAEQL---KPAATHADDPAFWLYSSGSTGRPKGVVHL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 662 HRGLLNLL-LDMQRTFAVGSQDRLLSVTTPTFDISFLEYLL-PLISGASLYLtEAERAADSfRMIPLIADYRPTLMQATP 739
Cdd:cd05959 185 HADIYWTAeLYARNVLGIREDDVCFSAAKLFFAYGLGNSLTfPLSVGATTVL-MPERPTPA-AVFKRIRRYRPTVFFGVP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 740 SFWHGLLMA-GWRGDPE----LCVLAGgEALPTKVAEELLRCCG-SLWNLYGPTETTIWSLKSQITQAENITLGAPIANT 813
Cdd:cd05959 263 TLYAAMLAApNLPSRDLsslrLCVSAG-EALPAEVGERWKARFGlDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGY 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 814 RIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLsepgvpgGRMFRTGDLVRSDAQGQLFFVGRKDSQIKL 893
Cdd:cd05959 342 EVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ-------GEWTRTGDKYVRDDDGFYTYAGRADDMLKV 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 894 RGYRIELGEIERTLARHPHV-DAAVVACIERAPLHKaLAAFII----TSEPPSLFEQLKNELRQQLPDYMVPTLWQRVAD 968
Cdd:cd05959 415 SGIWVSPFEVESALVQHPAVlEAAVVGVEDEDGLTK-PKAFVVlrpgYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDE 493
|
490
....*....|....
gi 1288439980 969 FPNTDNGKIDRKRL 982
Cdd:cd05959 494 LPKTATGKIQRFKL 507
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
526-957 |
7.03e-44 |
|
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: 167.39 E-value: 7.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 526 TLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLMQ--RARLVC-- 601
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKisKPKVIFtd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 602 --------------------LVVRQPGEW-GEIVQLSLPELMQDMSNairYSTPCALLPDMQAYLLFTSGSTGEPKGVCV 660
Cdd:cd05911 90 pdglekvkeaakelgpkdkiIVLDDKPDGvLSIEDLLSPTLGEEDED---LPPPLKDGKDDTAAILYSSGTTGLPKGVCL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 661 VHRGLLNLLLDMQRTF--AVGSQDRLLSVTtPTFDIS-FLEYLLPLISGASLYLTeaeRAADSFRMIPLIADYRPTLMQA 737
Cdd:cd05911 167 SHRNLIANLSQVQTFLygNDGSNDVILGFL-PLYHIYgLFTTLASLLNGATVIIM---PKFDSELFLDLIEKYKITFLYL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 738 TPsfWHGLLMAGwrgDPEL---------CVLAGGEALpTKVAEELLRCCGSLWNL---YGPTETTIWSLKSQITQAENIT 805
Cdd:cd05911 243 VP--PIAAALAK---SPLLdkydlsslrVILSGGAPL-SKELQELLAKRFPNATIkqgYGMTETGGILTVNPDGDDKPGS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 806 LGAPIANTRIYILDNEGHPVpQGVD--GELYIAGDGVAQGYDGQPELNAQFFLSEpgvpggRMFRTGDLVRSDAQGQLFF 883
Cdd:cd05911 317 VGRLLPNVEAKIVDDDGKDS-LGPNepGEICVRGPQVMKGYYNNPEATKETFDED------GWLHTGDIGYFDEDGYLYI 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1288439980 884 VGRKDSQIKLRGYRIELGEIERTLARHPHV-DAAVVAcIERAPLHKALAAFIITSEPPSLFEQ-LKNELRQQLPDY 957
Cdd:cd05911 390 VDRKKELIKYKGFQVAPAELEAVLLEHPGVaDAAVIG-IPDEVSGELPRAYVVRKPGEKLTEKeVKDYVAKKVASY 464
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
46-459 |
7.30e-44 |
|
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: 165.84 E-value: 7.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 46 PLSFNQERLWFLQKYDSTATNYNLYVVYRLHGVVDMPMLTEALRHVQARHAILRTRIIVRN-DRPCQVIDDASSL---VL 121
Cdd:cd19543 3 PLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGlGEPLQVVLKDRKLpwrEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 122 DTVTLAAQAPTSALDAVIQQVINTRFDLARGPLWGVTQIIQPDQGCHLVFCAHHIIIDGISLRLLFDELQQQYARLHAGN 201
Cdd:cd19543 83 DLSHLSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGEGQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 202 ETSLPPPPlQYADY-AFWQRewfQDtlLANELAYWRARLQDAPLLSTFPSLHPRPAQPSTHGSRFSITLDETLSLALKHV 280
Cdd:cd19543 163 PPSLPPVR-PYRDYiAWLQR---QD--KEAAEAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 281 ARTQETTPFVLMLTAFQLVLMRYAQQQRLVIGMPVSGR---IrPELQSSIGYYASTAVIYTDFNGVEVGREALQRVKASV 357
Cdd:cd19543 237 ARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRpaeL-PGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 358 KETQGRQQLPfenlvnmldLPR----SLSHSPLFQILYIYHNHvtPRAFTLAGAYWE------QVTYHNQTvKYDMTVEV 427
Cdd:cd19543 316 LELREHEYVP---------LYEiqawSEGKQALFDHLLVFENY--PVDESLEEEQDEdglritDVSAEEQT-NYPLTVVA 383
|
410 420 430
....*....|....*....|....*....|..
gi 1288439980 428 fQNDATFDVSFEYDLGLYDADVVKQIAEALRQ 459
Cdd:cd19543 384 -IPGEELTIKLSYDAEVFDEATIERLLGHLRR 414
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
518-984 |
9.31e-44 |
|
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: 165.93 E-value: 9.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 518 LAIQQHDGTLTYAELWARVQFIAMRFRAHG-IQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLmqr 596
Cdd:cd05941 3 IAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYV--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 597 arlvclvvrqpgewgeivqlslpelmqdmsnaIRYSTPCALLPDmqAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTF 676
Cdd:cd05941 80 --------------------------------ITDSEPSLVLDP--ALILYTSGTTGRPKGVVLTHANLAANVRALVDAW 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 677 AVGSQDRLLSVtTPTFDIS--FLEYLLPLISGASLYLTeaeRAADSFRMIPLIADYRPTLMQATPSFWHGLL-------- 746
Cdd:cd05941 126 RWTEDDVLLHV-LPLHHVHglVNALLCPLFAGASVEFL---PKFDPKEVAISRLMPSITVFMGVPTIYTRLLqyyeahft 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 747 -MAGWRGDPE----LCVlAGGEALPTKVAEELLRCCG-SLWNLYGPTETTIwsLKSQITQAENI--TLGAPIANTRIYIL 818
Cdd:cd05941 202 dPQFARAAAAerlrLMV-SGSAALPVPTLEEWEAITGhTLLERYGMTEIGM--ALSNPLDGERRpgTVGMPLPGVQARIV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 819 DNE-GHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFlsepgvPGGRMFRTGDLVRSDAQGQLFFVGR-KDSQIKLRGY 896
Cdd:cd05941 279 DEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEF------TDDGWFKTGDLGVVDEDGYYWILGRsSVDIIKSGGY 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 897 RIELGEIERTLARHPHV-DAAVVAcierAP---LHKALAAFIITSE--PPSLFEQLKNELRQQLPDYMVPTLWQRVADFP 970
Cdd:cd05941 353 KVSALEIERVLLAHPGVsECAVIG----VPdpdWGERVVAVVVLRAgaAALSLEELKEWAKQRLAPYKRPRRLILVDELP 428
|
490
....*....|....
gi 1288439980 971 NTDNGKIDRKRLAE 984
Cdd:cd05941 429 RNAMGKVNKKELRK 442
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
1096-1521 |
3.13e-43 |
|
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: 164.12 E-value: 3.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1096 PFPLTDVQRAYWLGRQTGATSIATHIYHEFDVE-HFNVTRFTHAVNALIARHEMLRARVLPDGT---QQILAQVPAYQLE 1171
Cdd:cd19066 1 KIPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTgSLDLARLKQALDAVMERHDVLRTRFCEEAGryeQVVLDKTVRFRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1172 QRDLSALspNARNDALMAIRDRLSHHVHPADRWPLFDFSYSACTAQHGRLHFSLDLLIADALSMRTLQQELMMLY---RE 1248
Cdd:cd19066 81 IIDLRNL--ADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYdaaER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1249 PHVSLPLLPFSFRDYVQALLVEQASEAYARDQAYWQRALPQLYGPPTLPVQGDLAQLSAIRFVRRRHRLSAHNWGVLSAL 1328
Cdd:cd19066 159 QKPTLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1329 AQRTRITKTALLLTVFSQVLARWSLSPTFTLNLTLFNRPQgyPNAEAVIGDFTAVSLLNVCYDSQHSYAHNAQRIQVQLW 1408
Cdd:cd19066 239 ARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPD--EAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1409 EDLEHRRFSGIrasEALIHSGR-----FHAPMPVVFTSMLDIDGETTAQDPRDTTrftlcPDANITQTPQVWLDHQVIEL 1483
Cdd:cd19066 317 EAIEHQRVPFI---ELVRHLGVvpeapKHPLFEPVFTFKNNQQQLGKTGGFIFTT-----PVYTSSEGTVFDLDLEASED 388
|
410 420 430
....*....|....*....|....*....|....*....
gi 1288439980 1484 A-GELHFNWDAVEQLFDTTLLDQMFGAYCHALQALVAMP 1521
Cdd:cd19066 389 PdGDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
509-954 |
2.55e-40 |
|
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: 158.17 E-value: 2.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 509 QRCVQHPKQLAI------QQHDGTLTYAELWARVQFIAMRFRAHGiQPGDRIGVLLPRHRDVIATMLATWFVGACYVPfd 582
Cdd:cd05931 1 RRAAARPDRPAYtflddeGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVP-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 583 IHQP-----AARLQRLMQ--RARLVC-------LVVRQPGEWGEIVQLSLPELMQDMSNAIRYSTPCALLPDMQAYLLFT 648
Cdd:cd05931 78 LPPPtpgrhAERLAAILAdaGPRVVLttaaalaAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 649 SGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSVTTPTFD---ISFLeyLLPLISGASLYLTEAER-AADSFRMI 724
Cdd:cd05931 158 SGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDmglIGGL--LTPLYSGGPSVLMSPAAfLRRPLRWL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 725 PLIADYRPTLMQAtPSFWHGLL--------MAG-----WRGdpelcVLAGGE-----AL--------PTKVAEELLRCCg 778
Cdd:cd05931 236 RLISRYRATISAA-PNFAYDLCvrrvrdedLEGldlssWRV-----ALNGAEpvrpaTLrrfaeafaPFGFRPEAFRPS- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 779 slwnlYGPTETT-------------------------IWSLKSQITQAENIT-LGAPIANTRIYILDNEGH-PVPQGVDG 831
Cdd:cd05931 309 -----YGLAEATlfvsggppgtgpvvlrvdrdalagrAVAVAADDPAARELVsCGRPLPDQEVRIVDPETGrELPDGEVG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 832 ELYIAGDGVAQGYDGQPELNAQFFLSEPGVPGGRMFRTGDL-VRSDaqGQLFFVGRKDSQIKLRGYRIELGEIERTLAR- 909
Cdd:cd05931 384 EIWVRGPSVASGYWGRPEATAETFGALAATDEGGWLRTGDLgFLHD--GELYITGRLKDLIIVRGRNHYPQDIEATAEEa 461
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1288439980 910 HPHVDAAVVACI---ERAPLHKALAAFIITSEPPSLFEQLKNELRQQL 954
Cdd:cd05931 462 HPALRPGCVAAFsvpDDGEERLVVVAEVERGADPADLAAIAAAIRAAV 509
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
45-390 |
8.26e-40 |
|
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: 154.56 E-value: 8.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 45 IPLSFNQERLWFLQKYDSTATNYNLYVVYRLHGVVDMPMLTEALRHVQARHAILRTRIIV-RNDRPCQVIDDASSLVLDT 123
Cdd:cd19546 5 VPATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGdGGDVHQRILDADAARPELP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 124 VTLAAQAptsALDAVIQQVINTRFDLARGPLWGVTQIIQPDQGCHLVFCAHHIIIDGISLRLLFDELQQQYARLHAGNET 203
Cdd:cd19546 85 VVPATEE---ELPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARREGRAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 204 SLPPPPLQYADYAFWQREWF-----QDTLLANELAYWRARLQDAPLLSTFPSLHPRPAQPSTHGSRFSITLDETLSLALK 278
Cdd:cd19546 162 ERAPLPLQFADYALWERELLageddRDSLIGDQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEVHARLM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 279 HVARTQETTPFVLMLTAFQLVLMRYAQQQRLVIGMPVSGRI-RPELQSSIGYYASTAVIYTDFNGVEVGREALQRVKASV 357
Cdd:cd19546 242 EAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDeEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAV 321
|
330 340 350
....*....|....*....|....*....|...
gi 1288439980 358 KETQGRQQLPFENLVNMLDLPRSLSHSPLFQIL 390
Cdd:cd19546 322 REARRHQDVPFERLAELLALPPSADRHPVFQVA 354
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
526-977 |
3.77e-39 |
|
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: 155.43 E-value: 3.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 526 TLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVP-FDIHQPAARLQRL----------- 593
Cdd:cd17634 84 TISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSViFGGFAPEAVAGRIidsssrllita 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 594 ---MQRARLV-------------------CLVVRQPG---EWGEIVQLSLPELMQDMSNAirySTPCALLPDMQAYLLFT 648
Cdd:cd17634 164 dggVRAGRSVplkknvddalnpnvtsvehVIVLKRTGsdiDWQEGRDLWWRDLIAKASPE---HQPEAMNAEDPLFILYT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 649 SGSTGEPKGVCVVHRG-LLNLLLDMQRTFAVGSQDRLLSVTtptfDISFL---EYLL--PLISGASLYLTE-AERAADSF 721
Cdd:cd17634 241 SGTTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTA----DVGWVtghSYLLygPLACGATTLLYEgVPNWPTPA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 722 RMIPLIADYRPTLMQATPSFWHGLLMAG--W--RGD-PELCVLAG-GEALPTKVAEELLRCCGS----LWNLYGPTETTi 791
Cdd:cd17634 317 RMWQVVDKHGVNILYTAPTAIRALMAAGddAieGTDrSSLRILGSvGEPINPEAYEWYWKKIGKekcpVVDTWWQTETG- 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 792 WSLKSQITQAENITLGA---PIANTRIYILDNEGHPVPQGVDGELYIAGD--GVAQGYDGQPELNAQFFLSEpgvpGGRM 866
Cdd:cd17634 396 GFMITPLPGAIELKAGSatrPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHERFEQTYFST----FKGM 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 867 FRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFII----TSEPPSL 942
Cdd:cd17634 472 YFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVlnhgVEPSPEL 551
|
490 500 510
....*....|....*....|....*....|....*
gi 1288439980 943 FEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKI 977
Cdd:cd17634 552 YAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
505-989 |
5.52e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 153.80 E-value: 5.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 505 RIIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLL---PRHrdvIATMLATWFVGACYVPF 581
Cdd:PRK06187 10 RILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDwnsHEY---LEAYFAVPKIGAVLHPI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 582 DIHQPAARLQRLMQRARLVCLVVRqpGEWGEIVQLSLPEL--------------MQDMSNAIRYST----------PCAL 637
Cdd:PRK06187 87 NIRLKPEEIAYILNDAEDRVVLVD--SEFVPLLAAILPQLptvrtvivegdgpaAPLAPEVGEYEEllaaasdtfdFPDI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 638 LPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLsVTTPTFDI--SFLEYlLPLISGASLYLteae 715
Cdd:PRK06187 165 DENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYL-VIVPMFHVhaWGLPY-LALMAGAKQVI---- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 716 raADSF---RMIPLIADYRPTLMQATPSFWHGLLMA---------GWRGdpelcVLAGGEALPtkvaEELLRCCGSLWN- 782
Cdd:PRK06187 239 --PRRFdpeNLLDLIETERVTFFFAVPTIWQMLLKAprayfvdfsSLRL-----VIYGGAALP----PALLREFKEKFGi 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 783 ----LYGPTET----TIWSLKSQITQAEN--ITLGAPIANTRIYILDNEGHPVP--QGVDGELYIAGDGVAQGYDGQPEL 850
Cdd:PRK06187 308 dlvqGYGMTETspvvSVLPPEDQLPGQWTkrRSAGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPEA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 851 NAQFFlsepgvPGGRMfRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHV-DAAVV----------- 918
Cdd:PRK06187 388 TAETI------DGGWL-HTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVaEVAVIgvpdekwgerp 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1288439980 919 -ACIERAPLHKALAafiitseppslfEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAENFVAD 989
Cdd:PRK06187 461 vAVVVLKPGATLDA------------KELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQYAEG 520
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
62-468 |
7.55e-39 |
|
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: 150.53 E-value: 7.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 62 STATNYNLYVVY---RLHGVVDMPMLTEALRHVQARHAILRTRIIVRNDRP--CQVIDDASSLVLDTVTLAAQaptsALD 136
Cdd:cd19542 14 SQLRSPGLYFNHfvfDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGtfLQVVLKSLDPPIEEVETDED----SLD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 137 AVIQQVINTRFDLARgPLWGVTQIIQPDQGCHLVFCAHHIIIDGISLRLLFDELQQQYarlhagnETSLPPPPLQYADYA 216
Cdd:cd19542 90 ALTRDLLDDPTLFGQ-PPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAY-------NGQLLPPAPPFSDYI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 217 FWQREWFQDtllaNELAYWRARLQDAPlLSTFPSLHPRPAQPSTHGS--RFSITLDEtlslalkhVARTQETTPFVLMLT 294
Cdd:cd19542 162 SYLQSQSQE----ESLQYWRKYLQGAS-PCAFPSLSPKRPAERSLSStrRSLAKLEA--------FCASLGVTLASLFQA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 295 AFQLVLMRYAQQQRLVIGMPVSGR--IRPELQSSIGYYASTAVIYTDFNGVEVGREALQRVKASVKETQGRQQLPFENLV 372
Cdd:cd19542 229 AWALVLARYTGSRDVVFGYVVSGRdlPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 373 NMLDLPRSlshSPLFQILYIYHNHVTPRAFTLAG-AYWEQVTYHNQTVkYDMTVEVFQNDATFDVSFEYDLGLYDADVVK 451
Cdd:cd19542 309 RALGLWPS---GTLFNTLVSYQNFEASPESELSGsSVFELSAAEDPTE-YPVAVEVEPSGDSLKVSLAYSTSVLSEEQAE 384
|
410
....*....|....*..
gi 1288439980 452 QIAEALRQHCLSLTSSL 468
Cdd:cd19542 385 ELLEQFDDILEALLANP 401
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
527-979 |
1.81e-38 |
|
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: 150.36 E-value: 1.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 527 LTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVP-FDIHQPAARLQRL-MQRARLVclvv 604
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPlFTAFGPKAIEHRLrTSGARLV---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 605 rqpgewgeivqlslpelMQDMSNAIRYSTPCALLpdmqaylLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRL 684
Cdd:cd05973 77 -----------------VTDAANRHKLDSDPFVM-------MFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSF 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 685 LSVTTPTFDISFLEYLL-PLISGASLYLTEAERAADSFRMIplIADYRPTLMQATPSFWHGLLMAGWRGDPEL-----CV 758
Cdd:cd05973 133 WNAADPGWAYGLYYAITgPLALGHPTILLEGGFSVESTWRV--IERLGVTNLAGSPTAYRLLMAAGAEVPARPkgrlrRV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 759 LAGGEALPTKVAEELLRCCGSL-WNLYGPTETTI-----WSLKSQITQAeniTLGAPIANTRIYILDNEGHPVPQGVDGE 832
Cdd:cd05973 211 SSAGEPLTPEVIRWFDAALGVPiHDHYGQTELGMvlanhHALEHPVHAG---SAGRAMPGWRVAVLDDDGDELGPGEPGR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 833 LYIAGDGVA----QGYDGQPElnaqfflsepGVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLA 908
Cdd:cd05973 288 LAIDIANSPlmwfRGYQLPDT----------PAIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALI 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1288439980 909 RHPHV-DAAVVAcierAPLH---KALAAFIITSE----PPSLFEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDR 979
Cdd:cd05973 358 EHPAVaEAAVIG----VPDPertEVVKAFVVLRGghegTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQR 432
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
527-982 |
7.67e-38 |
|
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: 148.80 E-value: 7.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 527 LTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVP-FDIHQPAARLQRlMQRARLVCLVVR 605
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPlFSAFGPEAIRDR-LENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 606 qpgewgeivqlslPELMQDMSnairystpcallPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLL 685
Cdd:cd05969 80 -------------EELYERTD------------PEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYW 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 686 SVTTPTFdISFLEYLL--PLISGASLYLTEAERAADSFRMIplIADYRPTLMQATPSFWHgLLMagwRGDPELC------ 757
Cdd:cd05969 135 CTADPGW-VTGTVYGIwaPWLNGVTNVVYEGRFDAESWYGI--IERVKVTVWYTAPTAIR-MLM---KEGDELArkydls 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 758 ----VLAGGEAL-PTKVA--EELLRCcgSLWNLYGPTETTIWSLKSQITQAENI-TLGAPIANTRIYILDNEGHPVPQGV 829
Cdd:cd05969 208 slrfIHSVGEPLnPEAIRwgMEVFGV--PIHDTWWQTETGSIMIANYPCMPIKPgSMGKPLPGVKAAVVDENGNELPPGT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 830 DGELYIAGD--GVAQGYDGQPELNAQFFlsepgvPGGrMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTL 907
Cdd:cd05969 286 KGILALKPGwpSMFRGIWNDEERYKNSF------IDG-WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESAL 358
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1288439980 908 ARHPHVDAAVVACIERAPLHKALAAFIITSEPPSLFEQLKNEL----RQQLPDYMVPTLWQRVADFPNTDNGKIDRKRL 982
Cdd:cd05969 359 MEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIinfvRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVL 437
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
500-984 |
1.36e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 149.28 E-value: 1.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 500 PQDVLRIIEQrcvqHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYV 579
Cdd:PRK07656 8 PELLARAARR----FGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 580 PFD-----------IHQPAARL-----------QRLMQRARLVCLVVRQPGEWGEIVQLSLPELMQDMSNAIRYSTPCAL 637
Cdd:PRK07656 84 PLNtrytadeaayiLARGDAKAlfvlglflgvdYSATTRLPALEHVVICETEEDDPHTEKMKTFTDFLAAGDPAERAPEV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 638 LPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSVTtPTFDISFLE--YLLPLISGASLYLTEAE 715
Cdd:PRK07656 164 DPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAAN-PFFHVFGYKagVNAPLMRGATILPLPVF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 716 RAADSFRmipLIADYRPTLMQATPSFWHGLLMAGwRGDPE------LCVlAGGEALPtkVA-----EELLRCcGSLWNLY 784
Cdd:PRK07656 243 DPDEVFR---LIETERITVLPGPPTMYNSLLQHP-DRSAEdlsslrLAV-TGAASMP--VAllerfESELGV-DIVLTGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 785 GPTE----TTIWSL-KSQITQAEniTLGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQfFLSEP 859
Cdd:PRK07656 315 GLSEasgvTTFNRLdDDRKTVAG--TIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAA-AIDAD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 860 GvpggrMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHV-DAAVVAcIERAPLHKALAAFIITSE 938
Cdd:PRK07656 392 G-----WLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVaEAAVIG-VPDERLGEVGKAYVVLKP 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1288439980 939 PPSLFEQlknEL----RQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAE 984
Cdd:PRK07656 466 GAELTEE---ELiaycREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
497-982 |
1.72e-36 |
|
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: 145.55 E-value: 1.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 497 WLGpQDVLRIIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGA 576
Cdd:cd05920 12 WQD-EPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 577 CYVpfdIHQPAAR---LQRLMQRARLVCLVVrqPGEWGEIVQLslpELMQDMSNAIrystpcallPDMqAYLLFTSGSTG 653
Cdd:cd05920 91 VPV---LALPSHRrseLSAFCAHAEAVAYIV--PDRHAGFDHR---ALARELAESI---------PEV-ALFLLSGGTTG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 654 EPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSV--TTPTFDISFLEYLLPLISGASLYLTEAERAADSFrmiPLIADYR 731
Cdd:cd05920 153 TPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVlpAAHNFPLACPGVLGTLLAGGRVVLAPDPSPDAAF---PLIEREG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 732 PTLMQATPSF---WhgLLMAGWRGDP--ELCVL-AGGEALPTKVA---EELLRCcgSLWNLYGPTETTIwslksQITQ-- 800
Cdd:cd05920 230 VTVTALVPALvslW--LDAAASRRADlsSLRLLqVGGARLSPALArrvPPVLGC--TLQQVFGMAEGLL-----NYTRld 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 801 --AENI--TLGAPI-ANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFlSEPGvpggrMFRTGDLVRS 875
Cdd:cd05920 301 dpDEVIihTQGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAF-TPDG-----FYRTGDLVRR 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 876 DAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEPPSLFEQLKNELRQQ-L 954
Cdd:cd05920 375 TPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPSAAQLRRFLRERgL 454
|
490 500
....*....|....*....|....*...
gi 1288439980 955 PDYMVPTLWQRVADFPNTDNGKIDRKRL 982
Cdd:cd05920 455 AAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
509-984 |
2.29e-36 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 145.11 E-value: 2.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 509 QRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAA 588
Cdd:PRK03640 10 QRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 589 RLQRLMQRARLVCLVVRQP--GEWGEIVQLSLPELMQDMSNAIRYSTPCALlpDMQAYLLFTSGSTGEPKGVcvvhrgll 666
Cdd:PRK03640 90 ELLWQLDDAEVKCLITDDDfeAKLIPGISVKFAELMNGPKEEAEIQEEFDL--DEVATIMYTSGTTGKPKGV-------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 667 nllldMQrTF------AVGS--------QDRLLSVtTPTFDISFLEYLL-PLISGASLYLteaERAADSFRMIPLIADYR 731
Cdd:PRK03640 160 -----IQ-TYgnhwwsAVGSalnlglteDDCWLAA-VPIFHISGLSILMrSVIYGMRVVL---VEKFDAEKINKLLQTGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 732 PTLMQATPSFWHGLLMA-GWRGDPE--LCVLAGGEALPTKVAEEllrCcgSLWNL-----YGPTETTiwslkSQItqaen 803
Cdd:PRK03640 230 VTIISVVSTMLQRLLERlGEGTYPSsfRCMLLGGGPAPKPLLEQ---C--KEKGIpvyqsYGMTETA-----SQI----- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 804 ITL------------GAPIANTRIYILDNeGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEpgvpggrMFRTGD 871
Cdd:PRK03640 295 VTLspedaltklgsaGKPLFPCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDG-------WFKTGD 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 872 LVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEPPSLfEQLKNELR 951
Cdd:PRK03640 367 IGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTE-EELRHFCE 445
|
490 500 510
....*....|....*....|....*....|...
gi 1288439980 952 QQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAE 984
Cdd:PRK03640 446 EKLAKYKVPKRFYFVEELPRNASGKLLRHELKQ 478
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
527-982 |
1.66e-35 |
|
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: 141.46 E-value: 1.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 527 LTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLMQRARLVCLVVrq 606
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 607 pgewgeivqlsLPELmQDMsnairystpcALLPdmqayllFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLS 686
Cdd:cd05935 80 -----------GSEL-DDL----------ALIP-------YTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 687 vTTPTFDISFLEYLL--PLISGASLYLT---EAERAADsfrmipLIADYRPTLMQATPSFWHGLLmagwrGDPE------ 755
Cdd:cd05935 131 -CLPLFHVTGFVGSLntAVYVGGTYVLMarwDRETALE------LIEKYKVTFWTNIPTMLVDLL-----ATPEfktrdl 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 756 --LCVLAGGEA-LPTKVAEELLRCCGSLWN-LYGPTETTIWSLKSQITQAENITLGAPIANTRIYILDNE-GHPVPQGVD 830
Cdd:cd05935 199 ssLKVLTGGGApMPPAVAEKLLKLTGLRFVeGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIEtGRELPPNEV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 831 GELYIAGDGVAQGYDGQPELNAQFFLSepgVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARH 910
Cdd:cd05935 279 GEIVVRGPQIFKGYWNRPEETEESFIE---IKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKH 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 911 PhvdAAVVACIERAPLHKA---LAAFII--------TSEppslfEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDR 979
Cdd:cd05935 356 P---AI*EVCVISVPDERVgeeVKAFIVlrpeyrgkVTE-----EDIIEWAREQMAAYKYPREVEFVDELPRSASGKILW 427
|
...
gi 1288439980 980 KRL 982
Cdd:cd05935 428 RLL 430
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
522-988 |
6.40e-35 |
|
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: 142.04 E-value: 6.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 522 QHDGT---LTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIAtmlATWfvgACY----------VPFDIHQPAA 588
Cdd:cd05906 32 DADGSeefQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIP---AFW---ACVlagfvpapltVPPTYDEPNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 589 RLQRLMQ------------RARLVCLVVRQPGEWG--EIVQLSLPELMQDMSNAIRYstpcALLPDMQAYLLFTSGSTGE 654
Cdd:cd05906 106 RLRKLRHiwqllgspvvltDAELVAEFAGLETLSGlpGIRVLSIEELLDTAADHDLP----QSRPDDLALLMLTSGSTGF 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 655 PKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLS------VTTptfdISFLeYLLPLISGAS-LYLTEAERAADSFRMIPLI 727
Cdd:cd05906 182 PKAVPLTHRNILARSAGKIQHNGLTPQDVFLNwvpldhVGG----LVEL-HLRAVYLGCQqVHVPTEEILADPLRWLDLI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 728 ADYRPTLMQAtPSFWHGLLM--------AGWRGDPELCVLAGGEALPTKVAEELLR---------------------CCG 778
Cdd:cd05906 257 DRYRVTITWA-PNFAFALLNdlleeiedGTWDLSSLRYLVNAGEAVVAKTIRRLLRllepyglppdairpafgmtetCSG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 779 SLWNLYGPTETTIWSLksqitqaENITLGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSe 858
Cdd:cd05906 336 VIYSRSFPTYDHSQAL-------EFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTE- 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 859 pgvpgGRMFRTGDLVRSDAqGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAA-VVACIERAPLHKA--LAAFII 935
Cdd:cd05906 408 -----DGWFRTGDLGFLDN-GNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSfTAAFAVRDPGAETeeLAIFFV 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1288439980 936 TS--EPPSLFEQLKnELRQQL-------PDYMVPTlwqRVADFPNTDNGKIDRKRLAENFVA 988
Cdd:cd05906 482 PEydLQDALSETLR-AIRSVVsrevgvsPAYLIPL---PKEEIPKTSLGKIQRSKLKAAFEA 539
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
528-982 |
9.07e-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: 341275 [Multi-domain] Cd Length: 439 Bit Score: 139.49 E-value: 9.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 528 TYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVP-FDIHQPAARLQRLmqrarlvclvvrq 606
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPlFALFGPEALEYRL------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 607 pgewgeivqlslpelmqdmSNAirySTPCAL--LPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRL 684
Cdd:cd05971 75 -------------------SNS---GASALVtdGSDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 685 LSVTTPtfDISFLEYLLPLISGASLY----LTEAERAADSFRMIPLIADYRPTLMQATPSfwhGLLMAGWRGDPE----- 755
Cdd:cd05971 133 LYWTPA--DWAWIGGLLDVLLPSLYFgvpvLAHRMTKFDPKAALDLMSRYGVTTAFLPPT---ALKMMRQQGEQLkhaqv 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 756 --LCVLAGGEALptkvAEELLrccgsLW----------NLYGPTETT-IWSLKSQITQAENITLGAPIANTRIYILDNEG 822
Cdd:cd05971 208 klRAIATGGESL----GEELL-----GWareqfgvevnEFYGQTECNlVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 823 HPVPQGVDGELYIA-GDGVAQ-GYDGQPELNAQFFLsepgvpgGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIEL 900
Cdd:cd05971 279 TPLPPGEVGEIAVElPDPVAFlGYWNNPSATEKKMA-------GDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGP 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 901 GEIERTLARHPHV-DAAVVAC--IERAPLHKA---LAAFIITSEppSLFEQLKNELRQQLPDYMVPTLWQRVADFPNTDN 974
Cdd:cd05971 352 AEIEECLLKHPAVlMAAVVGIpdPIRGEIVKAfvvLNPGETPSD--ALAREIQELVKTRLAAHEYPREIEFVNELPRTAT 429
|
....*...
gi 1288439980 975 GKIDRKRL 982
Cdd:cd05971 430 GKIRRREL 437
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
526-982 |
1.34e-34 |
|
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: 138.25 E-value: 1.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 526 TLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHqpaarlqrlmqrarlvclvvr 605
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTR--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 606 qpgewgeivqLSLPELMQDMSNAirystpcALLPDMQAYLLFTSGSTGEPKGVcvvhrgllnllldmQRTF------AVG 679
Cdd:cd05912 60 ----------LTPNELAFQLKDS-------DVKLDDIATIMYTSGTTGKPKGV--------------QQTFgnhwwsAIG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 680 SQ--------DRLLSVTtPTFDISFLEYLL-PLISGASLYLTEAERAADSFRMIpliADYRPTLMQATPSFWHGLLMAGW 750
Cdd:cd05912 109 SAlnlgltedDNWLCAL-PLFHISGLSILMrSVIYGMTVYLVDKFDAEQVLHLI---NSGKVTIISVVPTMLQRLLEILG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 751 RGDPE--LCVLAGGEALPTKVAEELLRCCGSLWNLYGPTETTiwslkSQItqaenITL------------GAPIANTRIY 816
Cdd:cd05912 185 EGYPNnlRCILLGGGPAPKPLLEQCKEKGIPVYQSYGMTETC-----SQI-----VTLspedalnkigsaGKPLFPVELK 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 817 ILDNEGHPvpqGVDGELYIAGDGVAQGYDGQPELNAQFFlsEPGvpggrMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGY 896
Cdd:cd05912 255 IEDDGQPP---YEVGEILLKGPNVTKGYLNRPDATEESF--ENG-----WFKTGDIGYLDEEGFLYVLDRRSDLIISGGE 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 897 RIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEPPSLfEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGK 976
Cdd:cd05912 325 NIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISE-EELIAYCSEKLAKYKVPKKIYFVDELPRTASGK 403
|
....*.
gi 1288439980 977 IDRKRL 982
Cdd:cd05912 404 LLRHEL 409
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
46-457 |
9.74e-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: 135.96 E-value: 9.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 46 PLSFNQERLWFLQKYDSTATNYNLYVVYRLHGVVDMPMLTEALRHVQARHAILRTRIIVRNDRPCQVIDDASSLVLDTVT 125
Cdd:cd19533 3 PLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIRHID 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 126 L-AAQAPTSALDAVIQQVINTRFDLARGPLWGVtQIIQPDQGCHLVF-CAHHIIIDGISLRLLFDELQQQYARLHAGNET 203
Cdd:cd19533 83 LsGDPDPEGAAQQWMQEDLRKPLPLDNDPLFRH-ALFTLGDNRHFWYqRVHHIVMDGFSFALFGQRVAEIYTALLKGRPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 204 SLPP-PPL--------QYADYAFWQRewfqdtllanELAYWRARLQDAPLLStfpSLHPRPAQPSTHGSRFSITLDETLS 274
Cdd:cd19533 162 PPAPfGSFldlveeeqAYRQSERFER----------DRAFWTEQFEDLPEPV---SLARRAPGRSLAFLRRTAELPPELT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 275 LALKHVARTQETTPFVLMLTAFQLVLMRYAQQQRLVIGMPVSGRIRPELQSSIGYYASTAVIYTDFNGVEVGREALQRVK 354
Cdd:cd19533 229 RTLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 355 ASVKETQGRQQLPFENLVNmlDLPRSLSHSPLFQILYIYhnHVTPRAFTLAGAYWEQVTYHNQTVKyDMTVEVF--QNDA 432
Cdd:cd19533 309 RELRSLLRHQRYRYEDLRR--DLGLTGELHPLFGPTVNY--MPFDYGLDFGGVVGLTHNLSSGPTN-DLSIFVYdrDDES 383
|
410 420
....*....|....*....|....*
gi 1288439980 433 TFDVSFEYDLGLYDADVVKQIAEAL 457
Cdd:cd19533 384 GLRIDFDANPALYSGEDLARHQERL 408
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
528-989 |
1.60e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 136.86 E-value: 1.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 528 TYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLMQRARLVCLVVRQP 607
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDDA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 608 GEWGEIVQLSLPELMQDMSNAIRYSTPcALLPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLsV 687
Cdd:PRK09088 104 VAAGRTDVEDLAAFIASADALEPADTP-SIPPERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFL-C 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 688 TTPTFDIsfleyllplisgaslylteaeraadsfrmIPLIADYRPTLMQA-----TPSFWHGLLMaGWRGDPEL------ 756
Cdd:PRK09088 182 DAPMFHI-----------------------------IGLITSVRPVLAVGgsilvSNGFEPKRTL-GRLGDPALgithyf 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 757 CV------------------------LAGGEALPTK-----VAEELLRCCGslwnlYGPTET-TIW--SLKSQITQAENI 804
Cdd:PRK09088 232 CVpqmaqafraqpgfdaaalrhltalFTGGAPHAAEdilgwLDDGIPMVDG-----FGMSEAgTVFgmSVDCDVIRAKAG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 805 TLGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEPgvpggrMFRTGDLVRSDAQGQLFFV 884
Cdd:PRK09088 307 AAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDG------WFRTGDIARRDADGFFWVV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 885 GRKDSQIKLRGYRIELGEIERTLARHPHV-DAAVVACIERAPLHKALAAFIITSEPPSLFEQLKNELRQQLPDYMVPTLW 963
Cdd:PRK09088 381 DRKKDMFISGGENVYPAEIEAVLADHPGIrECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHL 460
|
490 500
....*....|....*....|....*.
gi 1288439980 964 QRVADFPNTDNGKIDRKRLAENFVAD 989
Cdd:PRK09088 461 RLVDALPRTASGKLQKARLRDALAAG 486
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
512-982 |
1.81e-33 |
|
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: 136.87 E-value: 1.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 512 VQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQ 591
Cdd:cd05923 14 APDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 592 RLMQRARLvCLVVRQPGEWG--EIVQLSLPELMQDMSNAIRYST-------PCALLPDMQAYLLFTSGSTGEPKGVCVVH 662
Cdd:cd05923 94 ELIERGEM-TAAVIAVDAQVmdAIFQSGVRVLALSDLVGLGEPEsagplieDPPREPEQPAFVFYTSGTTGLPKGAVIPQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 663 RGLLNLLLDM--QRTFAVGSQDRLLSVTTPTFDISFLEYLL-PLISGASLYLTEAERAADSFRmipLIADYRPTLMQATP 739
Cdd:cd05923 173 RAAESRVLFMstQAGLRHGRHNVVLGLMPLYHVIGFFAVLVaALALDGTYVVVEEFDPADALK---LIEQERVTSLFATP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 740 SFWHGLL----MAGWRGDPELCVLAGGEALPTKVAEELLRCC-GSLWNLYGPTETTIWSLKSQITQAeniTLGAPIANTR 814
Cdd:cd05923 250 THLDALAaaaeFAGLKLSSLRHVTFAGATMPDAVLERVNQHLpGEKVNIYGTTEAMNSLYMRDARTG---TEMRPGFFSE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 815 IY---ILDNEGHPVPQGVDGELYIA--GDGVAQGYDGQPELNAQFfLSEpgvpggRMFRTGDLVRSDAQGQLFFVGRKDS 889
Cdd:cd05923 327 VRivrIGGSPDEALANGEEGELIVAaaADAAFTGYLNQPEATAKK-LQD------GWYRTGDVGYVDPSGDVRILGRVDD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 890 QIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEPPSLFEQLKNELR-QQLPDYMVPTLWQRVAD 968
Cdd:cd05923 400 MIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADELDQFCRaSELADFKRPRRYFFLDE 479
|
490
....*....|....
gi 1288439980 969 FPNTDNGKIDRKRL 982
Cdd:cd05923 480 LPKNAMNKVLRRQL 493
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
505-984 |
5.02e-33 |
|
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: 136.04 E-value: 5.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 505 RIIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGD--------------------RIGVL----LPR 560
Cdd:COG1021 29 DLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDrvvvqlpnvaefvivffalfRAGAIpvfaLPA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 561 HRDVIATMLATwFVGA-CYV------PFDIHQPAARLQRLMQRARLVcLVVRQPGEWgeivqLSLPELMQDMSNAIRYST 633
Cdd:COG1021 109 HRRAEISHFAE-QSEAvAYIipdrhrGFDYRALARELQAEVPSLRHV-LVVGDAGEF-----TSLDALLAAPADLSEPRP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 634 PcallPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLsVTTPT---FDISFLEYLLPLISGASLY 710
Cdd:COG1021 182 D----PDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYL-AALPAahnFPLSSPGVLGVLYAGGTVV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 711 LTEAERAADSFrmiPLIADYRPTLMQATPSFWHGLLMAGWRGDPEL----CVLAGGEALPTKVAEELlrccgslwnlyGP 786
Cdd:COG1021 257 LAPDPSPDTAF---PLIERERVTVTALVPPLALLWLDAAERSRYDLsslrVLQVGGAKLSPELARRV-----------RP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 787 TettiwsLKSQITQ----AE---NIT-LGAP---IANTR---------IYILDNEGHPVPQGVDGELYIAGDGVAQGYDG 846
Cdd:COG1021 323 A------LGCTLQQvfgmAEglvNYTrLDDPeevILTTQgrpispddeVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 847 QPELNAQFFLSEpGvpggrMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHV-DAAVVAC----- 920
Cdd:COG1021 397 APEHNARAFTPD-G-----FYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVhDAAVVAMpdeyl 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1288439980 921 IERAplhkalAAFIITSEPPSLFEQLKNELRQQ-LPDYMVPTLWQRVADFPNTDNGKIDRKRLAE 984
Cdd:COG1021 471 GERS------CAFVVPRGEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRA 529
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
526-918 |
6.50e-33 |
|
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: 134.26 E-value: 6.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 526 TLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLMQRARLVCLVVr 605
Cdd:cd05907 5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 606 qpgEWgeivqlslpelmqdmsnairystpcallPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLL 685
Cdd:cd05907 84 ---ED----------------------------PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 686 svttptfdiSFLE----------YLLPLISGASLYLTEAERaadsfRMIPLIADYRPTLMQATPSFW-------HGLLMA 748
Cdd:cd05907 133 ---------SFLPlahvferragLYVPLLAGARIYFASSAE-----TLLDDLSEVRPTVFLAVPRVWekvyaaiKVKAVP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 749 GWRGDP-ELCVL-------AGGEALPTKVAEELLRCCGSLWNLYGPTET----TIWSLksqitQAENI-TLGAPIANTRI 815
Cdd:cd05907 199 GLKRKLfDLAVGgrlrfaaSGGAPLPAELLHFFRALGIPVYEGYGLTETsavvTLNPP-----GDNRIgTVGKPLPGVEV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 816 YIldneghpvpqGVDGELYIAGDGVAQGYDGQPELNAQFFLSEPgvpggrMFRTGDLVRSDAQGQLFFVGR-KDSQIKLR 894
Cdd:cd05907 274 RI----------ADDGEILVRGPNVMLGYYKNPEATAEALDADG------WLHTGDLGEIDEDGFLHITGRkKDLIITSG 337
|
410 420
....*....|....*....|....
gi 1288439980 895 GYRIELGEIERTLARHPHVDAAVV 918
Cdd:cd05907 338 GKNISPEPIENALKASPLISQAVV 361
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
515-983 |
1.09e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 134.74 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 515 PKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLM 594
Cdd:PRK13383 49 PGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAAL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 595 QRARLVCLV-----VRQPGEWGEIVQLSLPelmqdmsnAIRYSTPCALLPDMQA---YLLFTSGSTGEPKGVCVVHR--- 663
Cdd:PRK13383 129 RAHHISTVVadnefAERIAGADDAVAVIDP--------ATAGAEESGGRPAVAApgrIVLLTSGTTGKPKGVPRAPQlrs 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 664 --GLLNLLLDMQRtFAVGSQdrlLSVTTPTFDISFLEYLLPLISGASLYLT----EAERA--------ADSFRMIPL--- 726
Cdd:PRK13383 201 avGVWVTILDRTR-LRTGSR---ISVAMPMFHGLGLGMLMLTIALGGTVLThrhfDAEAAlaqaslhrADAFTAVPVvla 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 727 -IADYRPTLMQATPSfwhgllmagwrgdPEL-CVLAGGEALPTKVAEELLRCCGS-LWNLYGPTETTIWSLKsqiTQAE- 802
Cdd:PRK13383 277 rILELPPRVRARNPL-------------PQLrVVMSSGDRLDPTLGQRFMDTYGDiLYNGYGSTEVGIGALA---TPADl 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 803 ---NITLGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQpelnaqfflsepgvpGGR-----MFRTGDLVR 874
Cdd:PRK13383 341 rdaPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDG---------------GGKavvdgMTSTGDMGY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 875 SDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHV-DAAVVACIERAPLHKaLAAFIItSEPPSLFE--QLKNELR 951
Cdd:PRK13383 406 LDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVaDNAVIGVPDERFGHR-LAAFVV-LHPGSGVDaaQLRDYLK 483
|
490 500 510
....*....|....*....|....*....|..
gi 1288439980 952 QQLPDYMVPTLWQRVADFPNTDNGKIDRKRLA 983
Cdd:PRK13383 484 DRVSRFEQPRDINIVSSIPRNPTGKVLRKELP 515
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
52-458 |
1.81e-32 |
|
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: 131.54 E-value: 1.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 52 ERLWFlQKY--DSTATNYNLYVVYRLHGVVDMPMLTEALRHVQARHAILRTRIIVRNDRPCQVIDDASSLVLdtvtlaaq 129
Cdd:cd19537 8 EREWW-HKYqlSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYSSSPPRVQ-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 130 aPTSALDavIQQVINTRFDLARGPLWGVtqIIQPDqgcHLVFCAHHIIIDGISLRLLFDELQQQYARLHagnetsLPPPP 209
Cdd:cd19537 79 -RVDTLD--VWKEINRPFDLEREDPIRV--FISPD---TLLVVMSHIICDLTTLQLLLREVSAAYNGKL------LPPVR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 210 LQYADYAFWQRewfqdTLLANELAYWRARLQDAPLlstfPSLHPRPAQPSTHGSRFSITLDETLSLALKHVARTQETTPF 289
Cdd:cd19537 145 REYLDSTAWSR-----PASPEDLDFWSEYLSGLPL----LNLPRRTSSKSYRGTSRVFQLPGSLYRSLLQFSTSSGITLH 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 290 VLMLTAFQLVLMRYAQQQRLVIGMPVSGRIRPELQSSIGYY------------ASTAVIytdfngvevgREALQRVKASV 357
Cdd:cd19537 216 QLALAAVALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLFleplpirirfpsSSDASA----------ADFLRAVRRSS 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 358 ketqgrQQ-----LPFENLVNMLDLPRSLSHSPLFQILYIYHNHVTPR-AFTLAGAyweQVTYHN-QTVKYDMTVE--VF 428
Cdd:cd19537 286 ------QAalahaIPWHQLLEHLGLPPDSPNHPLFDVMVTFHDDRGVSlALPIPGV---EPLYTWaEGAKFPLMFEftAL 356
|
410 420 430
....*....|....*....|....*....|
gi 1288439980 429 QNDATFdVSFEYDLGLYDADVVKQIAEALR 458
Cdd:cd19537 357 SDDSLL-LRLEYDTDCFSEEEIDRIESLIL 385
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
484-918 |
2.56e-32 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 134.84 E-value: 2.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 484 TPRRDPLNATNVPWLgpqdvlriIEQRCVQHPKQLAIQQHDG----TLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLP 559
Cdd:COG1022 2 SEFSDVPPADTLPDL--------LRRRAARFPDRVALREKEDgiwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 560 -RHRDVIAtMLATWFVGACYVPFDIHQPA--------------------ARLQRLMQ-RARLVCL----VVRQPGEWGEI 613
Cdd:COG1022 74 nRPEWVIA-DLAILAAGAVTVPIYPTSSAeevayilndsgakvlfvedqEQLDKLLEvRDELPSLrhivVLDPRGLRDDP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 614 VQLSLPELM---QDMSNAIRYSTPCALL-PDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSvtt 689
Cdd:COG1022 153 RLLSLDELLalgREVADPAELEARRAAVkPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLS--- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 690 ptfdisFL----------EYLLpLISGASLYLTEAERaadsfRMIPLIADYRPTLMQATPSFWHGLLMA----------- 748
Cdd:COG1022 230 ------FLplahvfertvSYYA-LAAGATVAFAESPD-----TLAEDLREVKPTFMLAVPRVWEKVYAGiqakaeeaggl 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 749 -----------GWR-------GDP------------ELCVLA---------------GGEALPTKVAEeLLRCCG-SLWN 782
Cdd:COG1022 298 krklfrwalavGRRyararlaGKSpslllrlkhalaDKLVFSklrealggrlrfavsGGAALGPELAR-FFRALGiPVLE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 783 LYGPTET----TIWSLKsqitqaENI--TLGAPIANTRIYIldneghpvpqGVDGELYIAGDGVAQGYDGQPELNAQFFL 856
Cdd:COG1022 377 GYGLTETspviTVNRPG------DNRigTVGPPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAEAFD 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1288439980 857 SEpgvpGGrmFRTGDLVRSDAQGQLFFVGRKDSQIKLR-GYRIELGEIERTLARHPHVDAAVV 918
Cdd:COG1022 441 AD----GW--LHTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVV 497
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
514-977 |
4.51e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 133.16 E-value: 4.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 514 HPKQLAIQQHDGTLTYAELWARVQFIAMRF-RAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVP-----------F 581
Cdd:PRK08314 23 YPDKTAIVFYGRAISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPvnpmnreeelaH 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 582 DIHQP-----------AARLQRLMQRARLVCLVVRQ------------PGEWGEiVQLSLPELM-------QDMSNAIRY 631
Cdd:PRK08314 103 YVTDSgarvaivgselAPKVAPAVGNLRLRHVIVAQysdylpaepeiaVPAWLR-AEPPLQALApggvvawKEALAAGLA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 632 STPCALLPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSVTtPTFDISFLEYLL--PLISGASL 709
Cdd:PRK08314 182 PPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVL-PLFHVTGMVHSMnaPIYAGATV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 710 YLT---EAERAADsfrmipLIADYRPTLMQATPSFWHGLLMAGWRGDPEL----CVLAGGEALPTKVAEELLRCCGslwn 782
Cdd:PRK08314 261 VLMprwDREAAAR------LIERYRVTHWTNIPTMVVDFLASPGLAERDLsslrYIGGGGAAMPEAVAERLKELTG---- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 783 L-----YGPTETTIWSLKSQITQAENITLGAPIANTRIYILDNE-GHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFL 856
Cdd:PRK08314 331 LdyvegYGLTETMAQTHSNPPDRPKLQCLGIPTFGVDARVIDPEtLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFI 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 857 SepgVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAavvACIERAP------LHKAL 930
Cdd:PRK08314 411 E---IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQE---ACVIATPdprrgeTVKAV 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1288439980 931 ----AAFIITSEPpslfEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKI 977
Cdd:PRK08314 485 vvlrPEARGKTTE----EEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
526-982 |
9.49e-32 |
|
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: 131.87 E-value: 9.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 526 TLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLMQRARLVCLVVR 605
Cdd:cd17647 20 SFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLIVI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 606 QPGewGEIVQlslpelmqdmsnairystpcallPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLL 685
Cdd:cd17647 100 RAA--GVVVG-----------------------PDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 686 SVTTPTFDISFLEYLLPLISGASLYLTEAERAADSFRMIPLIADYRPTLMQATPSFwhGLLMAGWRGDPELCVLAG---G 762
Cdd:cd17647 155 MLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAM--GQLLTAQATTPFPKLHHAffvG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 763 EALpTKvaeellRCCGSLW---------NLYGPTETT-------IWSLKSQITQAEN----ITLGAPIANTRIYILDNEG 822
Cdd:cd17647 233 DIL-TK------RDCLRLQtlaenvrivNMYGTTETQravsyfeVPSRSSDPTFLKNlkdvMPAGRGMLNVQLLVVNRND 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 823 HPVPQGVD--GELYIAGDGVAQGYDGQPELNAQFFLS----EPGV------------------PGGRMFRTGDLVRSDAQ 878
Cdd:cd17647 306 RTQICGIGevGEIYVRAGGLAEGYRGLPELNKEKFVNnwfvEPDHwnyldkdnnepwrqfwlgPRDRLYRTGDLGRYLPN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 879 GQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFII------------TSEPPS----- 941
Cdd:cd17647 386 GDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVprfdkpddesfaQEDVPKevstd 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1288439980 942 -----------LFEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRL 982
Cdd:cd17647 466 pivkgligyrkLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
505-984 |
6.92e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 129.66 E-value: 6.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 505 RIIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIH 584
Cdd:PRK07788 53 GLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 585 QPAARLQRLMQRARLVCLVVRQpgEWGEIVQLSLPEL-------------------MQDMSNAIRYSTPCAL-LPDMQAY 644
Cdd:PRK07788 133 FSGPQLAEVAAREGVKALVYDD--EFTDLLSALPPDLgrlrawggnpdddepsgstDETLDDLIAGSSTAPLpKPPKPGG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 645 L-LFTSGSTGEPKGVcvvhrgllnlLLDMQRTFAVGSQ--DRL-------LSVTTPTF-DISFLEYLLPLISGASLYLte 713
Cdd:PRK07788 211 IvILTSGTTGTPKGA----------PRPEPSPLAPLAGllSRVpfragetTLLPAPMFhATGWAHLTLAMALGSTVVL-- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 714 aERAADSFRMIPLIADYRPTLMQATPSFWHGLLMAG--WRGDPELC----VLAGGEALPTKVAEELLRCCG-SLWNLYGP 786
Cdd:PRK07788 279 -RRRFDPEATLEDIAKHKATALVVVPVMLSRILDLGpeVLAKYDTSslkiIFVSGSALSPELATRALEAFGpVLYNLYGS 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 787 TETTIWSLKSQITQAEN-ITLGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPelnaqfflSEPGVPGgr 865
Cdd:PRK07788 358 TEVAFATIATPEDLAEApGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGR--------DKQIIDG-- 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 866 MFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHV-DAAVVAcIERAPLHKALAAFIITSEPPSLFE 944
Cdd:PRK07788 428 LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVvEAAVIG-VDDEEFGQRLRAFVVKAPGAALDE 506
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1288439980 945 -QLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAE 984
Cdd:PRK07788 507 dAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
526-982 |
1.50e-30 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 128.26 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 526 TLTYAELWARVQFIAMRFRAHGIQPGDRIGVllprHRDVIATMLATWF----VGACYVPFDIHQPAARLQRLMQRARlVC 601
Cdd:PRK08008 37 RYSYLELNEEINRTANLFYSLGIRKGDKVAL----HLDNCPEFIFCWFglakIGAIMVPINARLLREESAWILQNSQ-AS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 602 LVVRQP---GEWGEIVQ---------LSLPELMQDMSNAIRYSTPCALLP-----------DMQAYLLFTSGSTGEPKGV 658
Cdd:PRK08008 112 LLVTSAqfyPMYRQIQQedatplrhiCLTRVALPADDGVSSFTQLKAQQPatlcyapplstDDTAEILFTSGTTSRPKGV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 659 CVVHrglLNLLLDMQRT---FAVGSQDRLLSVTtPTFDISF-LEYLLPLIS-GASLYLTEAERAADSFRMIpliADYRPT 733
Cdd:PRK08008 192 VITH---YNLRFAGYYSawqCALRDDDVYLTVM-PAFHIDCqCTAAMAAFSaGATFVLLEKYSARAFWGQV---CKYRAT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 734 LMQATPSFWHGLLM---AGWrgDPELCVLAGGEALPTKVAEELL---RCCGSLWNLYGPTETTIWSLKSQITQAENI-TL 806
Cdd:PRK08008 265 ITECIPMMIRTLMVqppSAN--DRQHCLREVMFYLNLSDQEKDAfeeRFGVRLLTSYGMTETIVGIIGDRPGDKRRWpSI 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 807 GAPIANTRIYILDNEGHPVPQGVDGELYI---AGDGVAQGYDGQPELNAQFFlsepgVPGGRMfRTGDLVRSDAQGQLFF 883
Cdd:PRK08008 343 GRPGFCYEAEIRDDHNRPLPAGEIGEICIkgvPGKTIFKEYYLDPKATAKVL-----EADGWL-HTGDTGYVDEEGFFYF 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 884 VGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEPPSL-FEQLKNELRQQLPDYMVPTL 962
Cdd:PRK08008 417 VDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLsEEEFFAFCEQNMAKFKVPSY 496
|
490 500
....*....|....*....|
gi 1288439980 963 WQRVADFPNTDNGKIDRKRL 982
Cdd:PRK08008 497 LEIRKDLPRNCSGKIIKKNL 516
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
514-986 |
1.69e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 128.18 E-value: 1.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 514 HPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPfdIHQPAARLQRL 593
Cdd:PRK06188 25 YPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTA--LHPLGSLDDHA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 594 MQ----------------RARLVCLVVRQPGeWGEIVQLSLPELMQDMSNAIRYSTP----CALLPDMQAYLLFTSGSTG 653
Cdd:PRK06188 103 YVledagistlivdpapfVERALALLARVPS-LKHVLTLGPVPDGVDLLAAAAKFGPaplvAAALPPDIAGLAYTGGTTG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 654 EPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLsVTTPTFDISFLEYLLPLISGASLYLTEAERAADSFRMIpliADYRPT 733
Cdd:PRK06188 182 KPKGVMGTHRSIATMAQIQLAEWEWPADPRFL-MCTPLSHAGGAFFLPTLLRGGTVIVLAKFDPAEVLRAI---EEQRIT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 734 LMQATPSFWHGLLMAGWRGDPELC----VLAGGEAL-PTKVAEELLRCCGSLWNLYGPTET--TIwslkSQITQAENI-- 804
Cdd:PRK06188 258 ATFLVPTMIYALLDHPDLRTRDLSsletVYYGASPMsPVRLAEAIERFGPIFAQYYGQTEApmVI----TYLRKRDHDpd 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 805 ------TLGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFlsepgvPGGRMfRTGDLVRSDAQ 878
Cdd:PRK06188 334 dpkrltSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF------RDGWL-HTGDVAREDED 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 879 GQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIIT-SEPPSLFEQLKNELRQQLPDY 957
Cdd:PRK06188 407 GFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLrPGAAVDAAELQAHVKERKGSV 486
|
490 500
....*....|....*....|....*....
gi 1288439980 958 MVPTLWQRVADFPNTDNGKIDRKRLAENF 986
Cdd:PRK06188 487 HAPKQVDFVDSLPLTALGKPDKKALRARY 515
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
509-984 |
1.97e-30 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 128.33 E-value: 1.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 509 QRCVQHPKQLAIQQHDGT-LTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPA 587
Cdd:PRK06087 31 QTARAMPDKIAVVDNHGAsYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWRE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 588 ARLQRLMQRAR-----------------LVCLVVRQPGEWGEIV-------QLSLPELMQDMSNAIRYSTPCALLPDMQA 643
Cdd:PRK06087 111 AELVWVLNKCQakmffaptlfkqtrpvdLILPLQNQLPQLQQIVgvdklapATSSLSLSQIIADYEPLTTAITTHGDELA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 644 YLLFTSGSTGEPKGVCVVHrgllNLLLDMQRTFAVG----SQDRLLSVTTPTFDISFLEYL-LPLISGASLYLTEAERAA 718
Cdd:PRK06087 191 AVLFTSGTEGLPKGVMLTH----NNILASERAYCARlnltWQDVFMMPAPLGHATGFLHGVtAPFLIGARSVLLDIFTPD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 719 DSfrmIPLIADYRPT-LMQATPsFWHGLLMAGWRGDPELCV----LAGGEALPTKVAEELLRCCGSLWNLYGPTETtiwS 793
Cdd:PRK06087 267 AC---LALLEQQRCTcMLGATP-FIYDLLNLLEKQPADLSAlrffLCGGTTIPKKVARECQQRGIKLLSVYGSTES---S 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 794 LKSQITQAENI-----TLGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQfFLSEPGvpggrMFR 868
Cdd:PRK06087 340 PHAVVNLDDPLsrfmhTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTAR-ALDEEG-----WYY 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 869 TGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHV-DAAVVACI-ERapLHKALAAFIITSEP---PSLF 943
Cdd:PRK06087 414 SGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIhDACVVAMPdER--LGERSCAYVVLKAPhhsLTLE 491
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1288439980 944 EQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAE 984
Cdd:PRK06087 492 EVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
526-983 |
2.53e-30 |
|
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: 126.05 E-value: 2.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 526 TLTYAELWARVQFIAMRFRAH-GIQPGDRIGVLLPRHrdviATMLATWFVgacyvpfdihqpaarlqrlMQRARLVCLVV 604
Cdd:cd05958 10 EWTYRDLLALANRIANVLVGElGIVPGNRVLLRGSNS----PELVACWFG-------------------IQKAGAIAVAT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 605 R---QPGEWGEIvqlslpelmqdmsnaIRYSTPCALLPDMQ-------AYLLFTSGSTGEPKGVCVVHRGLLNLLldmqR 674
Cdd:cd05958 67 MpllRPKELAYI---------------LDKARITVALCAHAltasddiCILAFTSGTTGAPKATMHFHRDPLASA----D 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 675 TFAV---GSQDRLLSVTTPTFDISF---LEYLLPLISGASLYLTEaERAADsfRMIPLIADYRPTLMQATPSFWHGLLMA 748
Cdd:cd05958 128 RYAVnvlRLREDDRFVGSPPLAFTFglgGVLLFPFGVGASGVLLE-EATPD--LLLSAIARYKPTVLFTAPTAYRAMLAH 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 749 GWRGDPEL-----CVLAGgEALPTKVAEELLRCCGS-LWNLYGPTETTIWSLKSQITQAENITLGAPIANTRIYILDNEG 822
Cdd:cd05958 205 PDAAGPDLsslrkCVSAG-EALPAALHRAWKEATGIpIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVDDEG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 823 HPVPQGVDGELYIAGDgVAQGYDGQPELNAQFflsepgvpGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGE 902
Cdd:cd05958 284 NPVPDGTIGRLAVRGP-TGCRYLADKRQRTYV--------QGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPE 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 903 IERTLARHPHV-DAAVVACIERAPLHKaLAAFII----TSEPPSLFEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKI 977
Cdd:cd05958 355 VEDVLLQHPAVaECAVVGHPDESRGVV-VKAFVVlrpgVIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKL 433
|
....*.
gi 1288439980 978 DRKRLA 983
Cdd:cd05958 434 QRFALR 439
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
523-984 |
4.56e-30 |
|
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: 126.98 E-value: 4.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 523 HDGTL---TYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLMQRA-- 597
Cdd:cd12119 19 HEGEVhryTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAed 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 598 -------RLVCLVVRQPGEW----GEIVQLS-LPELMQDMSNAIRYST------PCALLPD----MQAYLLFTSGSTGEP 655
Cdd:cd12119 99 rvvfvdrDFLPLLEAIAPRLptveHVVVMTDdAAMPEPAGVGVLAYEEllaaesPEYDWPDfdenTAAAICYTSGTTGNP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 656 KGVCVVHRGLL--NLLLDMQRTFAVGSQDRLLSVtTPTFDISF--LEYLLPLiSGASLYLTEAERAADSfrMIPLIADYR 731
Cdd:cd12119 179 KGVVYSHRSLVlhAMAALLTDGLGLSESDVVLPV-VPMFHVNAwgLPYAAAM-VGAKLVLPGPYLDPAS--LAELIEREG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 732 PTLMQATPSFWHGLLMAGWRGDPELC----VLAGGEALPTKVAEELLRCCGSLWNLYGPTET----TIWSLKSQITQ--- 800
Cdd:cd12119 255 VTFAAGVPTVWQGLLDHLEANGRDLSslrrVVIGGSAVPRSLIEAFEERGVRVIHAWGMTETsplgTVARPPSEHSNlse 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 801 ----AENITLGAPIANTRIYILDNEGHPVPQgvD----GELYIAGDGVAQGYDGQPELNAQFFlsepgvPGGrMFRTGDL 872
Cdd:cd12119 335 deqlALRAKQGRPVPGVELRIVDDDGRELPW--DgkavGELQVRGPWVTKSYYKNDEESEALT------EDG-WLRTGDV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 873 VRSDAQGQLFFVGR-KDSqIKLRGYRIELGEIERTLARHPHV-DAAVVAC-----IERaPLhkalaAFIITSEPPSL-FE 944
Cdd:cd12119 406 ATIDEDGYLTITDRsKDV-IKSGGEWISSVELENAIMAHPAVaEAAVIGVphpkwGER-PL-----AVVVLKEGATVtAE 478
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1288439980 945 QLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAE 984
Cdd:cd12119 479 ELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
498-982 |
2.05e-29 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 125.26 E-value: 2.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 498 LGPQDVLRIIEQRCVQHPkqlAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGAC 577
Cdd:PRK13382 43 MGPTSGFAIAAQRCPDRP---GLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGAD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 578 YVPFDIHQPAARLQRLMQRARLVCLVVRQpgEWGEIVqlslPELMQDMSNAIRY----STPCALL--------------- 638
Cdd:PRK13382 120 ILLLNTSFAGPALAEVVTREGVDTVIYDE--EFSATV----DRALADCPQATRIvawtDEDHDLTvevliaahagqrpep 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 639 -PDMQAYLLFTSGSTGEPKGVcvvHR----GLLNLLLDMQRTFAVGSQDRLLSvtTPTFDISFLEYLLPLISGASLYLTE 713
Cdd:PRK13382 194 tGRKGRVILLTSGTTGTPKGA---RRsgpgGIGTLKAILDRTPWRAEEPTVIV--APMFHAWGFSQLVLAASLACTIVTR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 714 aeRAADSFRMIPLIADYRPTLMQATPSFWHGLL------MAGWRGDPELCVLAGGEALPTKVAEELLRCCGS-LWNLYGP 786
Cdd:PRK13382 269 --RRFDPEATLDLIDRHRATGLAVVPVMFDRIMdlpaevRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDvIYNNYNA 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 787 TETTIWSLKS-QITQAENITLGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYdgQPELNAQFFLSepgvpggr 865
Cdd:PRK13382 347 TEAGMIATATpADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKDFHDG-------- 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 866 MFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEPPSLF-E 944
Cdd:PRK13382 417 FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATpE 496
|
490 500 510
....*....|....*....|....*....|....*...
gi 1288439980 945 QLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRL 982
Cdd:PRK13382 497 TLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRREL 534
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
527-984 |
2.57e-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: 2.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 527 LTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLMQRARLVCLVVRQ 606
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGAVYAAVDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 607 pgewgeivqlslpelmqdmsnAIRYSTPcaLLpdmqayLLFTSGSTGEPKgvcvvhrgllnLLLDMQRTFAVG------- 679
Cdd:cd05974 81 ---------------------NTHADDP--ML------LYFTSGTTSKPK-----------LVEHTHRSYPVGhlstmyw 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 680 ----SQDRLLSVTTPTF-DISFLEYLLPLISGASLYLTEAERAaDSFRMIPLIADYRPTLMQATPSFWHGLL---MAGWR 751
Cdd:cd05974 121 iglkPGDVHWNISSPGWaKHAWSCFFAPWNAGATVFLFNYARF-DAKRVLAALVRYGVTTLCAPPTVWRMLIqqdLASFD 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 752 GDPELcVLAGGEALPTKVAEELLRccgsLWNL-----YGPTETTIWSLKSQITQAENITLGAPIANTRIYILDNEGHPVP 826
Cdd:cd05974 200 VKLRE-VVGAGEPLNPEVIEQVRR----AWGLtirdgYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGAPAT 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 827 QGvdgELYIA-GD----GVAQGYDGQPELNAqfflsepGVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELG 901
Cdd:cd05974 275 EG---EVALDlGDtrpvGLMKGYAGDPDKTA-------HAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPF 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 902 EIERTLARHPHV-DAAVVAC--IERAPLHKALAAFIITSEP-PSLFEQLKNELRQQLPDYmvptlwQRV-----ADFPNT 972
Cdd:cd05974 345 ELESVLIEHPAVaEAAVVPSpdPVRLSVPKAFIVLRAGYEPsPETALEIFRFSRERLAPY------KRIrrlefAELPKT 418
|
490
....*....|..
gi 1288439980 973 DNGKIDRKRLAE 984
Cdd:cd05974 419 ISGKIRRVELRR 430
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
44-395 |
3.18e-29 |
|
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: 122.56 E-value: 3.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 44 AIPLSFNQERLWFLQKYDSTATNYNLYVVYRLHGVVDMPMLTEALRHVQARHAILRTRII-VRNDRPCQVIDDASSLVLD 122
Cdd:cd19536 1 MYPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIeDGLGQPVQVVHRQAQVPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 123 TVTLA-AQAPTSALDAVIQQVINTRFDLARGPLWGVTQIIQPDQG-CHLVFCAHHIIIDGISLRLLFDELQQQYARLHAG 200
Cdd:cd19536 81 ELDLTpLEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERErFLLVISDHHSILDGWSLYLLVKEILAVYNQLLEY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 201 NETSLPPPPlQYADYAFWQREWFQDtllANELAYWRARLQDAPLLSTFPslhPRPAQPSTHGSRFSITLDETLSLALKHV 280
Cdd:cd19536 161 KPLSLPPAQ-PYRDFVAHERASIQQ---AASERYWREYLAGATLATLPA---LSEAVGGGPEQDSELLVSVPLPVRSRSL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 281 ARTQETTPFVLMLTAFQLVLMRYAQQQRLVIGMPVSGRIRP--ELQSSIGYYASTAVIYTDFNGVEVgREALQRVKASVK 358
Cdd:cd19536 234 AKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEEttGAERLLGLFLNTLPLRVTLSEETV-EDLLKRAQEQEL 312
|
330 340 350
....*....|....*....|....*....|....*..
gi 1288439980 359 ETQGRQQLPfenlvnMLDLPRSLSHSPLFQILYIYHN 395
Cdd:cd19536 313 ESLSHEQVP------LADIQRCSEGEPLFDSIVNFRH 343
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
498-986 |
3.41e-29 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 124.23 E-value: 3.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 498 LGPQ--DVLRIIEQRCVQHPKqLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVG 575
Cdd:PRK05852 14 FGPRiaDLVEVAATRLPEAPA-LVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 576 ACYVPFDIHQPAA----RLQRLMQRARLV----------------CLVVRQPGEWGEIVQLSLPELMQDMSNAIRYSTPC 635
Cdd:PRK05852 93 LVVVPLDPALPIAeqrvRSQAAGARVVLIdadgphdraepttrwwPLTVNVGGDSGPSGGTLSVHLDAATEPTPATSTPE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 636 ALLPDmQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLTEAE 715
Cdd:PRK05852 173 GLRPD-DAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPAR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 716 RAADSFRMIPLIADYRPTLMQATPSFwHGLLM------AGWRGDPELCVLAGGEA-LPTKVAEELLRCCGS-LWNLYGPT 787
Cdd:PRK05852 252 GRFSAHTFWDDIKAVGATWYTAVPTI-HQILLeraatePSGRKPAALRFIRSCSApLTAETAQALQTEFAApVVCAFGMT 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 788 ETTIWSLKSQIT---QAEN--ITLGAPIANT--RIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEpg 860
Cdd:PRK05852 331 EATHQVTTTQIEgigQTENpvVSTGLVGRSTgaQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDG-- 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 861 vpggrMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEP- 939
Cdd:PRK05852 409 -----WLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESa 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1288439980 940 PSLFEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAENF 986
Cdd:PRK05852 484 PPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQF 530
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
479-984 |
4.32e-29 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 124.10 E-value: 4.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 479 APETATPRRDPLNATNVPwlGPQDVLRIIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLL 558
Cdd:PRK06155 1 GEPLGAGLAARAVDPLPP--SERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 559 PRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLMQRARLVCLVVRQPG----EWGEIVQLSLPEL-MQDMSNAIRYST 633
Cdd:PRK06155 79 GNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALlaalEAADPGDLPLPAVwLLDAPASVSVPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 634 PCALLP----------------DMQAyLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSvTTPTFDISFL 697
Cdd:PRK06155 159 GWSTAPlppldapapaaavqpgDTAA-ILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYT-TLPLFHTNAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 698 EYLLP-LISGASLYLTE---AERAADSFR-----MIPLIADYRPTLMQATPSfwhgllmAGWRGDPELCVLAGGeaLPTK 768
Cdd:PRK06155 237 NAFFQaLLAGATYVLEPrfsASGFWPAVRrhgatVTYLLGAMVSILLSQPAR-------ESDRAHRVRVALGPG--VPAA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 769 VAEELLRCCG-SLWNLYGPTETtiwslksqitqaeNITLGAPIANTR------------IYILDNEGHPVPQGVDGELYI 835
Cdd:PRK06155 308 LHAAFRERFGvDLLDGYGSTET-------------NFVIAVTHGSQRpgsmgrlapgfeARVVDEHDQELPDGEPGELLL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 836 AGD---GVAQGYDGQPELNAQFFLSepgvpggRMFRTGDLVRSDAQGQLFFVGR-KDSqIKLRGYRIELGEIERTLARHP 911
Cdd:PRK06155 375 RADepfAFATGYFGMPEKTVEAWRN-------LWFHTGDRVVRDADGWFRFVDRiKDA-IRRRGENISSFEVEQVLLSHP 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1288439980 912 HVDAAVVACIERAPLHKALAAFIITSEPPSL-FEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAE 984
Cdd:PRK06155 447 AVAAAAVFPVPSELGEDEVMAAVVLRDGTALePVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLRE 520
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
526-991 |
8.83e-29 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 123.24 E-value: 8.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 526 TLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVP------------------------- 580
Cdd:PRK13295 55 RFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPlmpifrerelsfmlkhaeskvlvvp 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 581 -----FDIHQPAARLQRLMQRARLVcLVVRQPGEWGEIVQLSLPELMQDmSNAIRYSTPCALLPDMQAYLLFTSGSTGEP 655
Cdd:PRK13295 135 ktfrgFDHAAMARRLRPELPALRHV-VVVGGDGADSFEALLITPAWEQE-PDAPAILARLRPGPDDVTQLIYTSGTTGEP 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 656 KGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSVTTPTFDISFLeY--LLPLISGASLYLT---EAERAADsfrmipLIADY 730
Cdd:PRK13295 213 KGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFM-YglMMPVMLGATAVLQdiwDPARAAE------LIRTE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 731 RPTLMQATPSFWHGLLMAGWRGDPELCVL----AGGEALPTKVAEELLRCCG----SLWnlyGPTET---TIWSLKSQIT 799
Cdd:PRK13295 286 GVTFTMASTPFLTDLTRAVKESGRPVSSLrtflCAGAPIPGALVERARAALGakivSAW---GMTENgavTLTKLDDPDE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 800 QAENiTLGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNaqfflsepGVPGGRMFRTGDLVRSDAQG 879
Cdd:PRK13295 363 RAST-TDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLN--------GTDADGWFDTGDLARIDADG 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 880 QLFFVGR-KDSQIKlRGYRIELGEIERTLARHPHV-DAAVVACI-----ERAplhkalAAFIITSEPPSL-FEQLKNELR 951
Cdd:PRK13295 434 YIRISGRsKDVIIR-GGENIPVVEIEALLYRHPAIaQVAIVAYPderlgERA------CAFVVPRPGQSLdFEEMVEFLK 506
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1288439980 952 -QQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAENFVADSS 991
Cdd:PRK13295 507 aQKVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRGEDA 547
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
514-984 |
9.72e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 122.93 E-value: 9.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 514 HPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRL 593
Cdd:PRK06164 23 RPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 594 MQRARLVCLVVrQPGEWG--------EIVQLSLPELMQ-----DMSNAIRYSTPCALL--------------------PD 640
Cdd:PRK06164 103 LGRGRARWLVV-WPGFKGidfaailaAVPPDALPPLRAiavvdDAADATPAPAPGARVqlfalpdpappaaageraadPD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 641 MQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLTEAERAADS 720
Cdd:PRK06164 182 AGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEPVFDAART 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 721 FRmipLIADYRPTLMQATPSFWHGLL-MAGWRGD-PELCVLAGGEALPT--KVAEELLRCCGSLWNLYGPTETTIWSLKS 796
Cdd:PRK06164 262 AR---ALRRHRVTHTFGNDEMLRRILdTAGERADfPSARLFGFASFAPAlgELAALARARGVPLTGLYGSSEVQALVALQ 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 797 QITQAENITL---GAPI-ANTRIYILDNE-GHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEPgvpggrMFRTGD 871
Cdd:PRK06164 339 PATDPVSVRIeggGRPAsPEARVRARDPQdGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDG------YFRTGD 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 872 LVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEPPSLFEQLKNELR 951
Cdd:PRK06164 413 LGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPVAFVIPTDGASPDEAGLMAACR 492
|
490 500 510
....*....|....*....|....*....|....*.
gi 1288439980 952 QQLPDYMVPTLWQRVADFPNTDNG---KIDRKRLAE 984
Cdd:PRK06164 493 EALAGFKVPARVQVVEAFPVTESAngaKIQKHRLRE 528
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
643-986 |
2.19e-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: 117.82 E-value: 2.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 643 AYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLsVTTPTFDISFLEYLLP-LISGASLYLTEAERAADSF 721
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWL-LSLPLYHVGGLAILVRsLLAGAELVLLERNQALAED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 722 RmipliADYRPTLMQATPSFWHGLLMAGWRGDPEL---CVLAGGEALPTKVAEELLRCCGSLWNLYGPTETtiwslksqi 798
Cdd:cd17630 82 L-----APPGVTHVSLVPTQLQRLLDSGQGPAALKslrAVLLGGAPIPPELLERAADRGIPLYTTYGMTET--------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 799 tqAENITLGAPIANTRIYIldneGHPVPqGV------DGELYIAGDGVAQGYdgqpeLNAQfflSEPGVPGGRMFRTGDL 872
Cdd:cd17630 148 --ASQVATKRPDGFGRGGV----GVLLP-GRelriveDGEIWVGGASLAMGY-----LRGQ---LVPEFNEDGWFTTKDL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 873 VRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEPPSLfEQLKNELRQ 952
Cdd:cd17630 213 GELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADP-AELRAWLKD 291
|
330 340 350
....*....|....*....|....*....|....
gi 1288439980 953 QLPDYMVPTLWQRVADFPNTDNGKIDRKRLAENF 986
Cdd:cd17630 292 KLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
526-995 |
2.64e-28 |
|
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: 122.60 E-value: 2.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 526 TLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVP-FDIHQPAARLQRL----------- 593
Cdd:cd05968 91 TLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPiFSGFGKEAAATRLqdaeakalita 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 594 ---MQRARLVCL------------------VVRQPGewgeivQLSLPELMQDMSNAIRYSTPCALLPDMQA----YLLFT 648
Cdd:cd05968 171 dgfTRRGREVNLkeeadkacaqcptvekvvVVRHLG------NDFTPAKGRDLSYDEEKETAGDGAERTESedplMIIYT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 649 SGSTGEPKGVCVVHRGL-LNLLLDMQRTFAVGSQDRLLSVTtptfDISFL--EYLL--PLISGASLYLTE-AERAADSFR 722
Cdd:cd05968 245 SGTTGKPKGTVHVHAGFpLKAAQDMYFQFDLKPGDLLTWFT----DLGWMmgPWLIfgGLILGATMVLYDgAPDHPKADR 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 723 MIPLIADYRPTLMQATPSFWHGLLMAG-----WRGDPELCVLAG-GEALPTKVAEELLRCCGS----LWNLYGPTETTIW 792
Cdd:cd05968 321 LWRMVEDHEITHLGLSPTLIRALKPRGdapvnAHDLSSLRVLGStGEPWNPEPWNWLFETVGKgrnpIINYSGGTEISGG 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 793 SLKSQ-ITQAENITLGAPIANTRIYILDNEGHPVPQGVdGELYIAGD--GVAQGYDGQPE--LNAqFFLSEPGVpggrmF 867
Cdd:cd05968 401 ILGNVlIKPIKPSSFNGPVPGMKADVLDESGKPARPEV-GELVLLAPwpGMTRGFWRDEDryLET-YWSRFDNV-----W 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 868 RTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEPPSLFEQLK 947
Cdd:cd05968 474 VHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEALA 553
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1288439980 948 NELRQQLPDYM----VPTLWQRVADFPNTDNGKIDRKRLAENFVAD-----SSLVSP 995
Cdd:cd05968 554 EELMERVADELgkplSPERILFVKDLPKTRNAKVMRRVIRAAYLGKelgdlSSLENP 610
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
528-985 |
9.43e-28 |
|
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: 119.91 E-value: 9.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 528 TYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPfDIHQPAAR-LQRLMQRARLVCLVVRQ 606
Cdd:cd05970 49 TFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIP-ATHQLTAKdIVYRIESADIKMIVAIA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 607 PGEWGEIVQLSLPE-----------------------LMQDMSNAIRYSTPCALLP-DMQAYLLFTSGSTGEPKGVCVVH 662
Cdd:cd05970 128 EDNIPEEIEKAAPEcpskpklvwvgdpvpegwidfrkLIKNASPDFERPTANSYPCgEDILLVYFSSGTTGMPKMVEHDF 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 663 RGLLNLLLDMQRTFAVGSQDRLLSVTTPTFDISFLEYLL-PLISGASLYLTEAERAaDSFRMIPLIADYRPTLMQATPSF 741
Cdd:cd05970 208 TYPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWGKIYgQWIAGAAVFVYDYDKF-DPKALLEKLSKYGVTTFCAPPTI 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 742 WHGLLMAGW-RGD---PELCVLAGgEALPTKVAEELLRCCG-SLWNLYGPTETTIWSLKSQITQAENITLGAPIANTRIY 816
Cdd:cd05970 287 YRFLIREDLsRYDlssLRYCTTAG-EALNPEVFNTFKEKTGiKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEID 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 817 ILDNEGHPVPQGVDGELYIAGD-----GVAQGYDGQPELNAQFFlsEPGVpggrmFRTGDLVRSDAQGQLFFVGRKDSQI 891
Cdd:cd05970 366 LIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTAEVW--HDGY-----YHTGDAAWMDEDGYLWFVGRTDDLI 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 892 KLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEPPSLFEQLKNELRQQLPD----YMVPTLWQRVA 967
Cdd:cd05970 439 KSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKvtapYKYPRIVEFVD 518
|
490
....*....|....*...
gi 1288439980 968 DFPNTDNGKIDRKRLAEN 985
Cdd:cd05970 519 ELPKTISGKIRRVEIRER 536
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
55-354 |
2.23e-27 |
|
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: 116.97 E-value: 2.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 55 WFLQKYDSTATNYNLYVVYRLHGVVDMPMLTEALRHVQARHAILRTRIIVRNDRPCQVI--DDASSLVLDTVTLAAQAPT 132
Cdd:cd19534 10 WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIrgDVEELFRLEVVDLSSLAQA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 133 SALDAVIQQvINTRFDLARGPLWGVTQIIQPDQGCHLVFCAHHIIIDGISLRLLFDELQQQYARLHAGNETSLPPPPlQY 212
Cdd:cd19534 90 AAIEALAAE-AQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEPIPLPSKT-SF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 213 ADYAFWQREWFQDTLLANELAYWRARLQDApllstFPSLHPRPAQPSTHGSRFSITLD--ETLSLaLKHVARTQETTPFV 290
Cdd:cd19534 168 QTWAELLAEYAQSPALLEELAYWRELPAAD-----YWGLPKDPEQTYGDARTVSFTLDeeETEAL-LQEANAAYRTEIND 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1288439980 291 LMLTAFQLVLMRYAQQQRLVIGMPVSGR--IRPELQSS--IGYYASTAVIYTDFNGVEVGREALQRVK 354
Cdd:cd19534 242 LLLAALALAFQDWTGRAPPAIFLEGHGReeIDPGLDLSrtVGWFTSMYPVVLDLEASEDLGDTLKRVK 309
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
514-988 |
2.98e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 118.95 E-value: 2.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 514 HPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYV-------------P 580
Cdd:PRK05605 45 FGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVehnplytahelehP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 581 FDIHQP---------AARLQRLMQRARLVCLV-VRQPGEWGEIVQ--LSLP----------------------ELMQDMS 626
Cdd:PRK05605 125 FEDHGArvaivwdkvAPTVERLRRTTPLETIVsVNMIAAMPLLQRlaLRLPipalrkaraaltgpapgtvpweTLVDAAI 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 627 NAIRYSTPC-ALLPDMQAYLLFTSGSTGEPKGVCVVHRGLL-NLLldMQRTFAVG---SQDRLLSVtTPTFDISFLEYLL 701
Cdd:PRK05605 205 GGDGSDVSHpRPTPDDVALILYTSGTTGKPKGAQLTHRNLFaNAA--QGKAWVPGlgdGPERVLAA-LPMFHAYGLTLCL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 702 ---PLIsGASLYLTEAERaadsfrmIPLIAD----YRPTLMQATPSFWHGLLMAGWRGDPELC----VLAGGEALPTKVA 770
Cdd:PRK05605 282 tlaVSI-GGELVLLPAPD-------IDLILDamkkHPPTWLPGVPPLYEKIAEAAEERGVDLSgvrnAFSGAMALPVSTV 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 771 EEL-LRCCGSLWNLYGPTETTIWSLKSQITQAENI-TLGAPIANTRIYILD--NEGHPVPQGVDGELYIAGDGVAQGYDG 846
Cdd:PRK05605 354 ELWeKLTGGLLVEGYGLTETSPIIVGNPMSDDRRPgYVGVPFPDTEVRIVDpeDPDETMPDGEEGELLVRGPQVFKGYWN 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 847 QPELNAQFFLSEpgvpggrMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHV-DAAVVAcIERAP 925
Cdd:PRK05605 434 RPEETAKSFLDG-------WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVeDAAVVG-LPRED 505
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1288439980 926 LHKALAAFIITSEPPSLFEQ-LKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAENFVA 988
Cdd:PRK05605 506 GSEEVVAAVVLEPGAALDPEgLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREELLE 569
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
513-983 |
5.45e-27 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 117.69 E-value: 5.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 513 QHPKQLAIQQHDG----------TLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFD 582
Cdd:PRK09274 18 ERPDQLAVAVPGGrgadgklaydELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 583 --------------------IHQPAARLQRLM----QRARLVCLVVRQPGEWGEIvqlSLPELMQDMSNAirySTPCALL 638
Cdd:PRK09274 98 pgmgiknlkqclaeaqpdafIGIPKAHLARRLfgwgKPSVRRLVTVGGRLLWGGT---TLATLLRDGAAA---PFPMADL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 639 -PDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLsvttPTFdisfleyllPLIS--GASLYLT--- 712
Cdd:PRK09274 172 aPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDL----PTF---------PLFAlfGPALGMTsvi 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 713 ---EAER--AADSFRMIPLIADYRPTLMQATPSFWHGLLMAGWRGDPEL----CVLAGGEALPTKVAE---ELLRCCGSL 780
Cdd:PRK09274 239 pdmDPTRpaTVDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLpslrRVISAGAPVPIAVIErfrAMLPPDAEI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 781 WNLYGPTE---------TTIWSLKSQIT-QAENITLGAPIANTRIYILD---------NEGHPVPQGVDGELYIAGDGVA 841
Cdd:PRK09274 319 LTPYGATEalpissiesREILFATRAATdNGAGICVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVAGPMVT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 842 QGYDGQPELNAQFFLSEPGvpGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVD--AAV-- 917
Cdd:PRK09274 399 RSYYNRPEATRLAKIPDGQ--GDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKrsALVgv 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1288439980 918 --------VACIERAPLhkalaafiITSEPPSLFEQLKnELRQQLPDYMVPTLWQRVADFPnTD---NGKIDRKRLA 983
Cdd:PRK09274 477 gvpgaqrpVLCVELEPG--------VACSKSALYQELR-ALAAAHPHTAGIERFLIHPSFP-VDirhNAKIFREKLA 543
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
502-986 |
8.39e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 116.96 E-value: 8.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 502 DVLRIIEQRcvqHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVP- 580
Cdd:PRK08316 15 DILRRSARR---YPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 581 ----------FDIHQPAARL----QRLMQRARLVC-LVVRQPGEWGEIVQLSLPEL----MQDMSNAIRYSTPCALLPD- 640
Cdd:PRK08316 92 nfmltgeelaYILDHSGARAflvdPALAPTAEAALaLLPVDTLILSLVLGGREAPGgwldFADWAEAGSVAEPDVELADd 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 641 MQAYLLFTSGSTGEPKGVCVVHRGLLN------LLLDMqrtfavGSQDRLLSvTTPTFDISFLE-YLLPLIS-GASLYLT 712
Cdd:PRK08316 172 DLAQILYTSGTESLPKGAMLTHRALIAeyvsciVAGDM------SADDIPLH-ALPLYHCAQLDvFLGPYLYvGATNVIL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 713 EAeraADSFRMIPLIADYRPTLMQATPSFWHGLLMAGWRGDPELCVLA----GGEALPTKVAEELLRCCGSL--WNLYGP 786
Cdd:PRK08316 245 DA---PDPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRkgyyGASIMPVEVLKELRERLPGLrfYNCYGQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 787 TE----TTIWSLKSQITQAEniTLGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLsepgvp 862
Cdd:PRK08316 322 TEiaplATVLGPEEHLRRPG--SAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFR------ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 863 GGrMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHV-DAAVVAC-----IEraplhkALAAFIIT 936
Cdd:PRK08316 394 GG-WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVaEVAVIGLpdpkwIE------AVTAVVVP 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1288439980 937 SEPPSLFE-QLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAENF 986
Cdd:PRK08316 467 KAGATVTEdELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERY 517
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
515-986 |
1.19e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 117.06 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 515 PKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDihqPAARLQRLM 594
Cdd:PRK06178 47 PQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVS---PLFREHELS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 595 ------QRARLVCL--------VVRQPGEWGEIVQLSL----------------------PELMQDMSNAIRYSTPCALL 638
Cdd:PRK06178 124 yelndaGAEVLLALdqlapvveQVRAETSLRHVIVTSLadvlpaeptlplpdslraprlaAAGAIDLLPALRACTAPVPL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 639 P----DMQAYLLFTSGSTGEPKGVCVVHRgllnlllDMQRTFA-------VGSQDRLLSVTTPTFDISF--LEYLLPLIS 705
Cdd:PRK06178 204 PppalDALAALNYTGGTTGMPKGCEHTQR-------DMVYTAAaayavavVGGEDSVFLSFLPEFWIAGenFGLLFPLFS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 706 GASLYL-----TEAERAA-------------DSFRMI---PLIADYRPTLMQATP--SFWHGLlmagwrgDPEL----CV 758
Cdd:PRK06178 277 GATLVLlarwdAVAFMAAveryrvtrtvmlvDNAVELmdhPRFAEYDLSSLRQVRvvSFVKKL-------NPDYrqrwRA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 759 LAGgealpTKVAEellrccGSlwnlYGPTET----TI--------WSLKSQitqaeNITLGAPIANTRIYILDNE-GHPV 825
Cdd:PRK06178 350 LTG-----SVLAE------AA----WGMTEThtcdTFtagfqdddFDLLSQ-----PVFVGLPVPGTEFKICDFEtGELL 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 826 PQGVDGELYIAGDGVAQGYDGQPELNAQFFLsepgvpgGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIER 905
Cdd:PRK06178 410 PLGAEGEIVVRTPSLLKGYWNKPEATAEALR-------DGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEA 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 906 TLARHPHV-DAAVVAcieRAPLHKAlaafiitsEPPSLFEQLKNE-----------LRQQLPDYMVPTLwqRVAD-FPNT 972
Cdd:PRK06178 483 LLGQHPAVlGSAVVG---RPDPDKG--------QVPVAFVQLKPGadltaaalqawCRENMAVYKVPEI--RIVDaLPMT 549
|
570
....*....|....
gi 1288439980 973 DNGKIDRKRLAENF 986
Cdd:PRK06178 550 ATGKVRKQDLQALA 563
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
526-953 |
5.95e-26 |
|
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: 113.61 E-value: 5.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 526 TLTYAELWARVQFIAMRFRAHGIQPGDRIGvLLP--RHRDVIATMlATWFVGACYVPFDIHQPAARLQRLMQRARLVCLV 603
Cdd:cd17640 5 RITYKDLYQEILDFAAGLRSLGVKAGEKVA-LFAdnSPRWLIADQ-GIMALGAVDVVRGSDSSVEELLYILNHSESVALV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 604 VrqpgewgeivqlslpelmqdmSNAirystpcallPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDR 683
Cdd:cd17640 83 V---------------------END----------SDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 684 LLSVTTP--TFDISFlEYLLPLISGASLYLTEAERAADsfrmiplIADYRPTLMQATPSFWHGL-------LMAGWRGDP 754
Cdd:cd17640 132 FLSILPIwhSYERSA-EYFIFACGCSQAYTSIRTLKDD-------LKRVKPHYIVSVPRLWESLysgiqkqVSKSSPIKQ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 755 ELC-----------VLAGGEALPTKVaEELLRCCG-SLWNLYGPTETTIWSLKSQITQAENITLGAPIANTRIYILDNEG 822
Cdd:cd17640 204 FLFlfflsggifkfGISGGGALPPHV-DTFFEAIGiEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 823 H-PVPQGVDGELYIAGDGVAQGYDGQPELNAQFfLSEPGvpggrMFRTGDLVRSDAQGQLFFVGR-KDSQIKLRGYRIEL 900
Cdd:cd17640 283 NvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKV-LDSDG-----WFNTGDLGWLTCGGELVLTGRaKDTIVLSNGENVEP 356
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1288439980 901 GEIERTLARHPHVDAAVVACIERaplhKALAAFIItsepPSlFEQLKNELRQQ 953
Cdd:cd17640 357 QPIEEALMRSPFIEQIMVVGQDQ----KRLGALIV----PN-FEELEKWAKES 400
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
526-983 |
6.88e-26 |
|
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: 113.32 E-value: 6.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 526 TLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDihqPAarlqrlMQRARLV-CLVV 604
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLID---PG------MGRKNLKqCLQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 605 RQPGEWGEIvqlslpelmqdmsnairystPCALLPdmqAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRL 684
Cdd:cd05910 73 AEPDAFIGI--------------------PKADEP---AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 685 LsvttPTFdisfleyllPLIS--GASLYLTEAERAADSFR--------MIPLIADYRPTLMQATPSFWHGLLMAGWRGDP 754
Cdd:cd05910 130 L----ATF---------PLFAlfGPALGLTSVIPDMDPTRparadpqkLVGAIRQYGVSIVFGSPALLERVARYCAQHGI 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 755 EL----CVLAGGEALPTKVAEELLRCC---GSLWNLYGPTET-TIWSLKSQITQAEN---------ITLGAPIANTRIYI 817
Cdd:cd05910 197 TLpslrRVLSAGAPVPIALAARLRKMLsdeAEILTPYGATEAlPVSSIGSRELLATTtaatsggagTCVGRPIPGVRVRI 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 818 L--DNEG-------HPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEPGvpGGRMFRTGDLVRSDAQGQLFFVGRKD 888
Cdd:cd05910 277 IeiDDEPiaewddtLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNS--EGFWHRMGDLGYLDDEGRLWFCGRKA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 889 SQIKLRGYRIELGEIERTLARHPHVD--AAV----------VACIERAPLhkalaafiiTSEPPSlfeQLKNELRQQLPD 956
Cdd:cd05910 355 HRVITTGGTLYTEPVERVFNTHPGVRrsALVgvgkpgcqlpVLCVEPLPG---------TITPRA---RLEQELRALAKD 422
|
490 500 510
....*....|....*....|....*....|...
gi 1288439980 957 YMVPTLWQRV---ADFPnTD---NGKIDRKRLA 983
Cdd:cd05910 423 YPHTQRIGRFlihPSFP-VDirhNAKIFREKLA 454
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
1099-1335 |
9.36e-26 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 107.82 E-value: 9.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1099 LTDVQRAYWLGRQtgatsiATHIYH-----EFDvEHFNVTRFTHAVNALIARHEMLRAR-VLPDGT-QQILAQVPAYQLE 1171
Cdd:COG4908 1 LSPAQKRFLFLEP------GSNAYNipavlRLE-GPLDVEALERALRELVRRHPALRTRfVEEDGEpVQRIDPDADLPLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1172 QRDLSALSPNARNDALMAIRDRlsHHVHPAD--RWPLFDFSYSACTAQHGRLHFSLDLLIADALSMRTLQQELMMLYREP 1249
Cdd:COG4908 74 VVDLSALPEPEREAELEELVAE--EASRPFDlaRGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1250 H----VSLPLLPFSFRDYVQALLVEQASEAYARDQAYWQRALPQLYGPPTLPVQGDLAQLSAIRFVRRRHRLSAHNWGVL 1325
Cdd:COG4908 152 LegepPPLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEAL 231
|
250
....*....|
gi 1288439980 1326 SALAQRTRIT 1335
Cdd:COG4908 232 KALAKAHGAT 241
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
515-982 |
9.89e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 113.44 E-value: 9.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 515 PKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLM 594
Cdd:PRK06145 16 PDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 595 QRARLVCLVVRQpgEWGEIVQLSLPELMQD---MSNAIRYSTPCALLPDMQAY-------LLFTSGSTGEPKGVCVVHRG 664
Cdd:PRK06145 96 GDAGAKLLLVDE--EFDAIVALETPKIVIDaaaQADSRRLAQGGLEIPPQAAVaptdlvrLMYTSGTTDRPKGVMHSYGN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 665 LLNLLLDMQRTFAVGSQDRLLsVTTPTFDISFLEylLPLIS----GASLYLteaERAADSFRMIPLIADYRPTLMQATPS 740
Cdd:PRK06145 174 LHWKSIDHVIALGLTASERLL-VVGPLYHVGAFD--LPGIAvlwvGGTLRI---HREFDPEAVLAAIERHRLTCAWMAPV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 741 FWHGLLMAGWRGDPELC----VLAGGEALPtkvaEELLRCCGSLW------NLYGPTETTIW-SLKSQITQAENI-TLGA 808
Cdd:PRK06145 248 MLSRVLTVPDRDRFDLDslawCIGGGEKTP----ESRIRDFTRVFtraryiDAYGLTETCSGdTLMEAGREIEKIgSTGR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 809 PIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLsepgvpgGRMFRTGDLVRSDAQGQLFFVGRKD 888
Cdd:PRK06145 324 ALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFY-------GDWFRSGDVGYLDEEGFLYLTDRKK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 889 SQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEPPSL-FEQLKNELRQQLPDYMVPTLWQRVA 967
Cdd:PRK06145 397 DMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLtLEALDRHCRQRLASFKVPRQLKVRD 476
|
490
....*....|....*
gi 1288439980 968 DFPNTDNGKIDRKRL 982
Cdd:PRK06145 477 ELPRNPSGKVLKRVL 491
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
509-984 |
1.32e-25 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 115.79 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 509 QRCVQHPKQLAIQQHDGT-LTYAELWARVQFIAMRFRaHGIQPGDRIGVLLPrhrdviATM------LATWFVGAcyVPF 581
Cdd:PRK08633 623 DTAKRNWSRLAVADSTGGeLSYGKALTGALALARLLK-RELKDEENVGILLP------PSVagalanLALLLAGK--VPV 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 582 DIHQPAAR--LQRLMQRARLVCLV-----VRQPGEWGEIVQLSLPE---LMQDMSNAIR-----------YSTPCALL-- 638
Cdd:PRK08633 694 NLNYTASEaaLKSAIEQAQIKTVItsrkfLEKLKNKGFDLELPENVkviYLEDLKAKISkvdkltallaaRLLPARLLkr 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 639 -------PDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSVtTPTFDiSF---LEYLLPLISGAS 708
Cdd:PRK08633 774 lygptfkPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSS-LPFFH-SFgltVTLWLPLLEGIK 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 709 LYL----TEAERAADsfrmipLIADYRPTLMQATPSFWhGLLMAGWRGDPEL-----CVLAGGEALPTKVAEELLRCCG- 778
Cdd:PRK08633 852 VVYhpdpTDALGIAK------LVAKHRATILLGTPTFL-RLYLRNKKLHPLMfaslrLVVAGAEKLKPEVADAFEEKFGi 924
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 779 SLWNLYGPTETT--------------IWslkSQITQAENiTLGAPIANTRIYILD-NEGHPVPQGVDGELYIAGDGVAQG 843
Cdd:PRK08633 925 RILEGYGATETSpvasvnlpdvlaadFK---RQTGSKEG-SVGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKG 1000
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 844 YDGQPELNAQfFLSEpgVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACI-- 921
Cdd:PRK08633 1001 YLGDPEKTAE-VIKD--IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEVVFAVTav 1077
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 922 ------ER-APLHKALAAfiitsEPPSLFEQLKNelrQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAE 984
Cdd:PRK08633 1078 pdekkgEKlVVLHTCGAE-----DVEELKRAIKE---SGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKE 1139
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
507-984 |
2.46e-25 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 111.88 E-value: 2.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 507 IEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAH-GIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQ 585
Cdd:PRK06839 8 IEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 586 PAARLQ-RLMQRARLVCLVVRQPGEWGEIVQ----LSLPELMQDMSNAIRYSTPCALLPDMQAYLL--FTSGSTGEPKGV 658
Cdd:PRK06839 88 TENELIfQLKDSGTTVLFVEKTFQNMALSMQkvsyVQRVISITSLKEIEDRKIDNFVEKNESASFIicYTSGTTGKPKGA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 659 CVVHRGLLNLLLDMQRTFAVGSQDRLLsVTTPTFDISFLE-YLLP-LISGASLYLTeaeRAADSFRMIPLIADYRPTLMQ 736
Cdd:PRK06839 168 VLTQENMFWNALNNTFAIDLTMHDRSI-VLLPLFHIGGIGlFAFPtLFAGGVIIVP---RKFEPTKALSMIEKHKVTVVM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 737 ATPSFWHGLLMAGWRGDPELCVL----AGGEALPTKVAEELLRCCGSLWNLYGPTET--TIWSLKSQITQAENITLGAPI 810
Cdd:PRK06839 244 GVPTIHQALINCSKFETTNLQSVrwfyNGGAPCPEELMREFIDRGFLFGQGFGMTETspTVFMLSEEDARRKVGSIGKPV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 811 ANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQfflsepGVPGGrMFRTGDLVRSDAQGQLFFVGRKDSQ 890
Cdd:PRK06839 324 LFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEE------TIQDG-WLCTGDLARVDEDGFVYIVGRKKEM 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 891 IKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEPPSLFEQ-LKNELRQQLPDYMVPTLWQRVADF 969
Cdd:PRK06839 397 IISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKdVIEHCRLFLAKYKIPKEIVFLKEL 476
|
490
....*....|....*
gi 1288439980 970 PNTDNGKIDRKRLAE 984
Cdd:PRK06839 477 PKNATGKIQKAQLVN 491
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
513-985 |
1.38e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 109.48 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 513 QHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPgDRIGVLLPRHRDVIATMLATWFVGACYVPFDIH-QPAARLQ 591
Cdd:PRK07638 13 LQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKN-KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKwKQDELKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 592 RL-MQRARLVC----LVVRQPGEWGEIVQLSlpELMQDMSNAIRYSTPCALLPDMQAYLLFTSGSTGEPKGVCVVHRGLL 666
Cdd:PRK07638 92 RLaISNADMIVteryKLNDLPDEEGRVIEID--EWKRMIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQSWL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 667 NLLLDMQRTFAVGSQDRLLsVTTPTFDISFLeY--LLPLISGASLYLteaERAADSFRMIPLIADYRPTLMQATPSFWHG 744
Cdd:PRK07638 170 HSFDCNVHDFHMKREDSVL-IAGTLVHSLFL-YgaISTLYVGQTVHL---MRKFIPNQVLDKLETENISVMYTVPTMLES 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 745 LLMAGWRGDPELCVLAGGEALPTKVAEEL------LRccgsLWNLYGPTETT-IWSLKSQITQAENITLGAPIANTRIYI 817
Cdd:PRK07638 245 LYKENRVIENKMKIISSGAKWEAEAKEKIknifpyAK----LYEFYGASELSfVTALVDEESERRPNSVGRPFHNVQVRI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 818 LDNEGHPVPQGVDGELYIAGDGVAQGYDG----QPELNAQFFLSepgvpggrmfrTGDLVRSDAQGQLFFVGRKDSQIKL 893
Cdd:PRK07638 321 CNEAGEEVQKGEIGTVYVKSPQFFMGYIIggvlARELNADGWMT-----------VRDVGYEDEEGFIYIVGREKNMILF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 894 RGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEPPslfEQLKNELRQQLPDYMVPTLWQRVADFPNTD 973
Cdd:PRK07638 390 GGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSATK---QQLKSFCLQRLSSFKIPKEWHFVDEIPYTN 466
|
490
....*....|....*
gi 1288439980 974 NGKIDR---KRLAEN 985
Cdd:PRK07638 467 SGKIARmeaKSWIEN 481
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
522-982 |
1.78e-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: 109.34 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 522 QHDGTLTYAELWARVQFIAMRFRAhGIQPGDRIGVLLPRHRDVIATMLATWFVGacYVPFDIHQPAA--------RL--- 590
Cdd:cd05909 3 TLGTSLTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTAGlrelraciKLagi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 591 ------QRLMQRARLVCLV-------------VRQPGEWGEIVQLSLPELMQDMSNAIRYSTPCALlPDMQAYLLFTSGS 651
Cdd:cd05909 80 ktvltsKQFIEKLKLHHLFdveydarivyledLRAKISKADKCKAFLAGKFPPKWLLRIFGVAPVQ-PDDPAVILFTSGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 652 TGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSVtTPTFDiSF---LEYLLPLISGASLYLteAERAADSFRMIPLIA 728
Cdd:cd05909 159 EGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGA-LPFFH-SFgltGCLWLPLLSGIKVVF--HPNPLDYKKIPELIY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 729 DYRPTLMQATPSFWHGLLMAGWRGD-PEL-CVLAGGEALPTKVAEELLRCCG-SLWNLYGPTETT-IWSLKSQITQAENI 804
Cdd:cd05909 235 DKKATILLGTPTFLRGYARAAHPEDfSSLrLVVAGAEKLKDTLRQEFQEKFGiRILEGYGTTECSpVISVNTPQSPNKEG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 805 TLGAPIANTRIYILDNEGH-PVPQGVDGELYIAGDGVAQGYDGQPELNAQfflsepgVPGGRMFRTGDLVRSDAQGQLFF 883
Cdd:cd05909 315 TVGRPLPGMEVKIVSVETHeEVPIGEGGLLLVRGPNVMLGYLNEPELTSF-------AFGDGWYDTGDIGKIDGEGFLTI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 884 VGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACI---ERAPLHKALAAFIITSEPPSLFEQLKNelrQQLPDYMVP 960
Cdd:cd05909 388 TGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAVVSvpdGRKGEKIVLLTTTTDTDPSSLNDILKN---AGISNLAKP 464
|
490 500
....*....|....*....|..
gi 1288439980 961 TLWQRVADFPNTDNGKIDRKRL 982
Cdd:cd05909 465 SYIHQVEEIPLLGTGKPDYVTL 486
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
645-979 |
2.33e-24 |
|
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: 106.20 E-value: 2.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 645 LLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSVTtPTFDISFLEYLLPLI--SGASLYLT--EAERAADs 720
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNML-PLFHIAGLNLALATFhaGGANVVMEkfDPAEALE- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 721 frmipLIADYRPTLMQATPSFWHGLLMAGWRGDPELCVL---AGGEAlPtKVAEELLRCCGS-LWNLYGPTETTIWSLKS 796
Cdd:cd17637 83 -----LIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLrhvLGLDA-P-ETIQRFEETTGAtFWSLYGQTETSGLVTLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 797 QITQAENiTLGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFlsepgvPGGrMFRTGDLVRSD 876
Cdd:cd17637 156 PYRERPG-SAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF------RNG-WHHTGDLGRFD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 877 AQGQLFFVGRKDSQ--IKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEPPSLFEQlknEL---- 950
Cdd:cd17637 228 EDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTAD---ELiefv 304
|
330 340 350
....*....|....*....|....*....|....
gi 1288439980 951 -----RQQLPDYMVptlwqRVADFPNTDNGKIDR 979
Cdd:cd17637 305 gsriaRYKKPRYVV-----FVEALPKTADGSIDR 333
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
625-982 |
2.85e-24 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 109.58 E-value: 2.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 625 MSNAIRYSTPCAL-----LPDMQ------AYLLFTSGSTGEPKGVCVVHRgllNLLLDMQRTFA-VGSQDRLLS----VT 688
Cdd:PRK08751 182 INGAIRFREALALgrkhsMPTLQiepddiAFLQYTGGTTGVAKGAMLTHR---NLVANMQQAHQwLAGTGKLEEgcevVI 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 689 T--PTFDISFLEY--LLPLISGASLYLTEAERAADSFrmIPLIADYRPTLMQATPSFWHGLLMAgwRGDPEL------CV 758
Cdd:PRK08751 259 TalPLYHIFALTAngLVFMKIGGCNHLISNPRDMPGF--VKELKKTRFTAFTGVNTLFNGLLNT--PGFDQIdfsslkMT 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 759 LAGGEALPTKVAEELLRCCG-SLWNLYGPTETTIWSLKSQITQAE-NITLGAPIANTRIYILDNEGHPVPQGVDGELYIA 836
Cdd:PRK08751 335 LGGGMAVQRSVAERWKQVTGlTLVEAYGLTETSPAACINPLTLKEyNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIK 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 837 GDGVAQGYDGQPELNAQFFLSEPgvpggrMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHV--D 914
Cdd:PRK08751 415 GPQVMKGYWKRPEETAKVMDADG------WLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVleV 488
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1288439980 915 AAVVACIERAplHKALAAFIITSEPPSLFEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRL 982
Cdd:PRK08751 489 AAVGVPDEKS--GEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| ArgR-Cyc_NRPS-like |
cd20480 |
Cyc (heterocyclization)-like domain of Vibrio anguillarum AngR and similar proteins; belongs ... |
1098-1517 |
3.94e-24 |
|
Cyc (heterocyclization)-like domain of Vibrio anguillarum AngR and similar proteins; belongs to the Condensation-domain family; Vibrio anguillarum AngR plays a role in regulating the expression of iron transport genes as well as in the production of the siderophore anguibactin. Cyc-domains are a type of Condensation (C) domain. Cyc-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. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have a alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. Members of this subfamily have an SxxxD motif at the active site. 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). In addition to Cyc-domains there are various other 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. 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: 380470 [Multi-domain] Cd Length: 406 Bit Score: 106.82 E-value: 3.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1098 PLTDVQRayWL----GRQTGATSIATHIYHEFDVEHFNVTRFTHAVNALIARHEMLRARVLPDGTQQILAQVPAYQLEQR 1173
Cdd:cd20480 3 PLTSNQN--WQlstqRQRSEQQSIANFIYQEFDYENISVDTLERCLTVLINHHPMLHALLSDDFYLHINSKNQIDAFAVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1174 DLSALSPNARNDALMAIRDRLSHHVHPAdrwpLFDFSYSACTAQHGRLHFSLDLLIADALSMRTLQQELMMLYREphvsl 1253
Cdd:cd20480 81 DLSSASEQEAAEQLARTRATLTKSRSKA----TISVVLSLLPANKIRLHVRFNSVVVDHPSVNLFFEQLCQLLRG----- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1254 plLPFSFRDYVQAL-----LVEQASEAYARDQAYWQRALPQLYGPPTLPVQGDLAQLSAIRFVRRRHRLSAHNWGVLSAL 1328
Cdd:cd20480 152 --SLLSFLAQEQVIlahnqLVISELQSTGLSSAFWNEQILQLPSSANLPTVCEPEKLRETGITRRTLTLSSDKWQQLVTI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1329 AQRTRITKTALLLTVFSQVLARWSLSPTFTLNLTLFNRpqgyPNAEAVIGDFTAVSLLNVCYDSQH--SYAHNAQriqvQ 1406
Cdd:cd20480 230 SKQHNVTPELTLASIFSAVLSLWGNQKDMMLRFDLNKK----NDVAGVIGQFTQPLLVGLSGFGQSflSLVKENQ----K 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1407 LWEDLEHRR----FSGIRASEALIHSGRFhaPMPVVFTSMLdidgettaqdprDTTRFTLCPDANITQTPQVWLD-HQVI 1481
Cdd:cd20480 302 HFEQAYPFRqipiFDLVRQLAKLSESHRY--PANIAFSSQL------------SGNNTLGRSGWGCRQSANTWLSlHAFI 367
|
410 420 430
....*....|....*....|....*....|....*.
gi 1288439980 1482 ElAGELHFNWDAVEQLFDTTLLDQMFGAYCHALQAL 1517
Cdd:cd20480 368 S-QGGLILQWDSQDALFPKDMIQDMLTSYSKLLESL 402
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
79-315 |
7.98e-24 |
|
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: 106.42 E-value: 7.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 79 VDMPMLTEALRHVQARHAILRTRIivrNDRPCQVIDDASSL----VLDTVTLAAQAPTSALDAVIQQVINTRFDLARGPL 154
Cdd:cd19535 37 LDPDRLERAWNKLIARHPMLRAVF---LDDGTQQILPEVPWygitVHDLRGLSEEEAEAALEELRERLSHRVLDVERGPL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 155 WGVTQIIQPDQGCHLVFCAHHIIIDGISLRLLFDELqqqyARLHAGNETSLPPPPLQYADYAFWQREwFQDTLLANELAY 234
Cdd:cd19535 114 FDIRLSLLPEGRTRLHLSIDLLVADALSLQILLREL----AALYEDPGEPLPPLELSFRDYLLAEQA-LRETAYERARAY 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 235 WRARLqdapllstfPSLHPRPA-----QPSTHG----SRFSITLDETLSLALKHVARTQETTPFVLMLTAFQLVLMRYAQ 305
Cdd:cd19535 189 WQERL---------PTLPPAPQlplakDPEEIKeprfTRREHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSG 259
|
250
....*....|
gi 1288439980 306 QQRLVIGMPV 315
Cdd:cd19535 260 QPRFLLNLTL 269
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
644-979 |
8.94e-24 |
|
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: 104.02 E-value: 8.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 644 YLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLteaERAADSFRM 723
Cdd:cd17633 4 YIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIG---QRKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 724 IPLIADYRPTLMQATPSFWHGLLMAGWRGDPELCVLAGGEALPTKVAEELLRCC--GSLWNLYGPTETTIWSLKSQITQA 801
Cdd:cd17633 81 IRKINQYNATVIYLVPTMLQALARTLEPESKIKSIFSSGQKLFESTKKKLKNIFpkANLIEFYGTSELSFITYNFNQESR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 802 ENITLGAPIANTRIYILDNEGhpvpqGVDGELYIAGDGVAQGYDGQPELNAqfflsepgvpgGRMFRTGDLVRSDAQGQL 881
Cdd:cd17633 161 PPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNP-----------DGWMSVGDIGYVDEEGYL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 882 FFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLhKALAAFIITSEPPSlFEQLKNELRQQLPDYMVPT 961
Cdd:cd17633 225 YLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARF-GEIAVALYSGDKLT-YKQLKRFLKQKLSRYEIPK 302
|
330
....*....|....*...
gi 1288439980 962 LWQRVADFPNTDNGKIDR 979
Cdd:cd17633 303 KIIFVDSLPYTSSGKIAR 320
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
526-925 |
9.23e-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: 107.32 E-value: 9.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 526 TLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLMQRARlVCLVVR 605
Cdd:cd05904 32 ALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSG-AKLAFT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 606 QPGEWGEIVQLSLPELM--QDMSNAIRYSTPCALLPDMQ-----------AYLLFTSGSTGEPKGVCVVHRGLLNLLLdm 672
Cdd:cd05904 111 TAELAEKLASLALPVVLldSAEFDSLSFSDLLFEADEAEppvvvikqddvAALLYSSGTTGRSKGVMLTHRNLIAMVA-- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 673 QRTFAVGSQDRLLSVT---TPTFDIsfleYLLPLISGASLYLTEA---ERAADSFRMIPLIADYRPTLMQATPSFWHGLL 746
Cdd:cd05904 189 QFVAGEGSNSDSEDVFlcvLPMFHI----YGLSSFALGLLRLGATvvvMPRFDLEELLAAIERYKVTHLPVVPPIVLALV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 747 MAGWRGDPELC----VLAGGEALPTKVAEELLRCCGS--LWNLYGPTETTIWS---LKSQITQAENITLGAPIANTRIYI 817
Cdd:cd05904 265 KSPIVDKYDLSslrqIMSGAAPLGKELIEAFRAKFPNvdLGQGYGMTESTGVVamcFAPEKDRAKYGSVGRLVPNVEAKI 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 818 LD-NEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEpgvpggRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGY 896
Cdd:cd05904 345 VDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKE------GWLHTGDLCYIDEDGYLFIVDRLKELIKYKGF 418
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1288439980 897 RIELGEIERTLARHPHV-DAAVV------------ACIERAP 925
Cdd:cd05904 419 QVAPAELEALLLSHPEIlDAAVIpypdeeagevpmAFVVRKP 460
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
510-984 |
1.47e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 107.17 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 510 RCVQHPKqLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDihqPAAR 589
Cdd:PRK12583 30 RFPDREA-LVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNIN---PAYR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 590 LQRL---MQRAR---LVCLVVRQPGEWGEIVQLSLPELMQDMSNAIRystpCALLPDMQ--------------AY----- 644
Cdd:PRK12583 106 ASELeyaLGQSGvrwVICADAFKTSDYHAMLQELLPGLAEGQPGALA----CERLPELRgvvslapapppgflAWhelqa 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 645 ------------------------LLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLsVTTPTFDI--SFLE 698
Cdd:PRK12583 182 rgetvsrealaerqasldrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLC-VPVPLYHCfgMVLA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 699 YLLPLISGASLYLteAERAADSFRMIPLIADYRPTLMQATPSFWHGLLMAGWRGDPELCVL-----AGGEALPT---KVA 770
Cdd:PRK12583 261 NLGCMTVGACLVY--PNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLrtgimAGAPCPIEvmrRVM 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 771 EELLrcCGSLWNLYGPTETTIWSLksQITQAENI-----TLGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYD 845
Cdd:PRK12583 339 DEMH--MAEVQIAYGMTETSPVSL--QTTAADDLerrveTVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYW 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 846 GQPELNAQFFLSEpgvpgGRMFrTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAP 925
Cdd:PRK12583 415 NNPEATAESIDED-----GWMH-TGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEK 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1288439980 926 LHKALAAFI------ITSEppslfEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAE 984
Cdd:PRK12583 489 YGEEIVAWVrlhpghAASE-----EELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMRE 548
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
647-983 |
2.57e-23 |
|
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: 103.51 E-value: 2.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 647 FTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLsVTTPTFDI--SFLEYLLPLISGASL-YLTEAERAADSFRM 723
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLC-IPVPLFHCfgSVLGVLACLTHGATMvFPSPSFDPLAVLEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 724 IpliADYRPTLMQATPSFWHGLLMAGWRGDPELCVLAGGEALPTKVAEELLRCCGSLWNL------YGPTETTIWSLKSQ 797
Cdd:cd05917 88 I---EKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMkdvtiaYGMTETSPVSTQTR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 798 ITQAENI---TLGAPIANTRIYILDNEGHPVPQ-GVDGELYIAGDGVAQGYDGQPELNAQfflsepGVPGGRMFRTGDLV 873
Cdd:cd05917 165 TDDSIEKrvnTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKTAE------AIDGDGWLHTGDLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 874 RSDAQGQLFFVGR-KDSQIKlRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEPPSLF-EQLKNELR 951
Cdd:cd05917 239 VMDEDGYCRIVGRiKDMIIR-GGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTeEDIKAYCK 317
|
330 340 350
....*....|....*....|....*....|..
gi 1288439980 952 QQLPDYMVPTLWQRVADFPNTDNGKIDRKRLA 983
Cdd:cd05917 318 GKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
506-982 |
2.58e-23 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 106.26 E-value: 2.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 506 IIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLP---RHRDVIATMLATWF----VGACY 578
Cdd:PRK07059 28 LLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPnvlQYPVAIAAVLRAGYvvvnVNPLY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 579 VPFDI-HQP--------------AARLQRLMQRARLVCLVVRQPGEW----GEIVQL------------SLPelmqdmsN 627
Cdd:PRK07059 108 TPRELeHQLkdsgaeaivvlenfATTVQQVLAKTAVKHVVVASMGDLlgfkGHIVNFvvrrvkkmvpawSLP-------G 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 628 AIRYST-----------PCALLPDMQAYLLFTSGSTGEPKGVCVVHRGLL-NLL---LDMQRTFAVGSQ-DRLLSVTT-P 690
Cdd:PRK07059 181 HVRFNDalaegarqtfkPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVaNVLqmeAWLQPAFEKKPRpDQLNFVCAlP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 691 TFDISFLE--YLLPLISGASLYLTEAERaaDSFRMIPLIADYRPTLMQATPSFWHGLLMAgwrgdPE---------LCVL 759
Cdd:PRK07059 261 LYHIFALTvcGLLGMRTGGRNILIPNPR--DIPGFIKELKKYQVHIFPAVNTLYNALLNN-----PDfdkldfsklIVAN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 760 AGGEALPTKVAEELLRCCG-SLWNLYGPTETTIWSLKSQITQAE-NITLGAPIANTRIYILDNEGHPVPQGVDGELYIAG 837
Cdd:PRK07059 334 GGGMAVQRPVAERWLEMTGcPITEGYGLSETSPVATCNPVDATEfSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 838 DGVAQGYDGQPELNAQfFLSEPGvpggrMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHV-DAA 916
Cdd:PRK07059 414 PQVMAGYWNRPDETAK-VMTADG-----FFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVlEVA 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1288439980 917 VVACIERaplH--KALAAFIITSEPPSLFEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRL 982
Cdd:PRK07059 488 AVGVPDE---HsgEAVKLFVVKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
519-983 |
1.89e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 102.76 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 519 AIQQHDGTLTYAELWARVQFIAMRFRahgiqPGDRIGVLLprhRDVIATMLATwfVGAC-----YVPFDIHQPAARLQRL 593
Cdd:PRK07787 18 AVRIGGRVLSRSDLAGAATAVAERVA-----GARRVAVLA---TPTLATVLAV--VGALiagvpVVPVPPDSGVAERRHI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 594 MQRARLVCLVVRQPGEWGEivqlsLPELMQDMS--NAIRYSTPCallPDMQAYLLFTSGSTGEPKGVcVVHRGLLNLLLD 671
Cdd:PRK07787 88 LADSGAQAWLGPAPDDPAG-----LPHVPVRLHarSWHRYPEPD---PDAPALIVYTSGTTGPPKGV-VLSRRAIAADLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 672 MQRTFAVGSQDRLLSVTTPTFDIS--FLEYLLPLISGASLYLT-----EAERAADSFRmipliadyrPTLMQATPSFWHG 744
Cdd:PRK07787 159 ALAEAWQWTADDVLVHGLPLFHVHglVLGVLGPLRIGNRFVHTgrptpEAYAQALSEG---------GTLYFGVPTVWSR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 745 LLmagwrGDPELC--------VLAGGEALPTKVAEELLRCCG-SLWNLYGPTETTIwslkSQITQAENI----TLGAPIA 811
Cdd:PRK07787 230 IA-----ADPEAAralrgarlLVSGSAALPVPVFDRLAALTGhRPVERYGMTETLI----TLSTRADGErrpgWVGLPLA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 812 NTRIYILDNEGHPVPQGVD--GELYIAGDGVAQGYDGQPELNAQFFlsepgVPGGrMFRTGDLVRSDAQGQLFFVGRKDS 889
Cdd:PRK07787 301 GVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAF-----TADG-WFRTGDVAVVDPDGMHRIVGREST 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 890 Q-IKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEPPSLfEQLKNELRQQLPDYMVPTLWQRVAD 968
Cdd:PRK07787 375 DlIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAA-DELIDFVAQQLSVHKRPREVRFVDA 453
|
490
....*....|....*
gi 1288439980 969 FPNTDNGKIDRKRLA 983
Cdd:PRK07787 454 LPRNAMGKVLKKQLL 468
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
501-984 |
4.35e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 102.80 E-value: 4.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 501 QDVLRIIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYV- 579
Cdd:PRK06710 24 QPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVq 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 580 ----------PFDIHQPAA-----------RLQRLMQRARLVCLVVR-----------------QPGEWGEIVQLSLPEL 621
Cdd:PRK06710 104 tnplyterelEYQLHDSGAkvilcldlvfpRVTNVQSATKIEHVIVTriadflpfpknllypfvQKKQSNLVVKVSESET 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 622 MQdMSNAIR------YSTPCALLPDMqAYLLFTSGSTGEPKGVCVVHRGLL-NLLLDMQRTFAVGSQDRLLSVTTPTFDI 694
Cdd:PRK06710 184 IH-LWNSVEkevntgVEVPCDPENDL-ALLQYTGGTTGFPKGVMLTHKNLVsNTLMGVQWLYNCKEGEEVVLGVLPFFHV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 695 SFLEYL--LPLISGASLYLTEAeraADSFRMIPLIADYRPTLMQATPSFWHGLLMAGWRGDPEL----CVLAGGEALPTK 768
Cdd:PRK06710 262 YGMTAVmnLSIMQGYKMVLIPK---FDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDIssirACISGSAPLPVE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 769 VAEELLRCCG-SLWNLYGPTETtiwslkSQITQAENI-------TLGAPIANTRIYILDNE-GHPVPQGVDGELYIAGDG 839
Cdd:PRK06710 339 VQEKFETVTGgKLVEGYGLTES------SPVTHSNFLwekrvpgSIGVPWPDTEAMIMSLEtGEALPPGEIGEIVVKGPQ 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 840 VAQGYDGQPELNAqfflsepGVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVA 919
Cdd:PRK06710 413 IMKGYWNKPEETA-------AVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTI 485
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1288439980 920 CIERAPLHKALAAFIITSEPPSLFEQLKNEL-RQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAE 984
Cdd:PRK06710 486 GVPDPYRGETVKAFVVLKEGTECSEEELNQFaRKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIE 551
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
645-979 |
5.16e-22 |
|
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: 99.26 E-value: 5.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 645 LLFTSGSTGEPKGVCVVHRGLLNLLLDMQR-TFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLTEAERAADSFrm 723
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKTFFAVPDILQKeGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYKSL-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 724 IPLIADYRPTLMQATPSFWHGL---LMAGWRGDPEL-CVLAGGE-ALPTKVAEELLRCCGSLWNLYGPTETTIWSLKSQI 798
Cdd:cd17635 84 FKILTTNAVTTTCLVPTLLSKLvseLKSANATVPSLrLIGYGGSrAIAADVRFIEATGLTNTAQVYGLSETGTALCLPTD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 799 TQAENI-TLGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEpgvpggrMFRTGDLVRSDA 877
Cdd:cd17635 164 DDSIEInAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDG-------WVNTGDLGERRE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 878 QGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSE--PPSLFEQLKNELRQQLP 955
Cdd:cd17635 237 DGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAelDENAIRALKHTIRRELE 316
|
330 340
....*....|....*....|....
gi 1288439980 956 DYMVPTLWQRVADFPNTDNGKIDR 979
Cdd:cd17635 317 PYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
501-984 |
1.89e-21 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 100.67 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 501 QDVLRIIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAH-GIQPGDRIGVLLPRHRD----VIATMLATWFV- 574
Cdd:PRK12492 24 KSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQypiaVFGALRAGLIVv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 575 --GACYVPFDI-HQpaarLQRLMQRArLVCLVVrqpgeWGEIVQLSLPEL---------MQDMSNAIR------------ 630
Cdd:PRK12492 104 ntNPLYTAREMrHQ----FKDSGARA-LVYLNM-----FGKLVQEVLPDTgieylieakMGDLLPAAKgwlvntvvdkvk 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 631 -----YSTPCAL--------------------LPDMqAYLLFTSGSTGEPKGVCVVHRgllNLLLDMQRTFAVGSQDR-- 683
Cdd:PRK12492 174 kmvpaYHLPQAVpfkqalrqgrglslkpvpvgLDDI-AVLQYTGGTTGLAKGAMLTHG---NLVANMLQVRACLSQLGpd 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 684 ----------LLSVTTPTFDI-SF-LEYLLPLISGASLYLTEAERAADSFrmIPLIADYRPTLMQATPSFWHGLLmagwr 751
Cdd:PRK12492 250 gqplmkegqeVMIAPLPLYHIyAFtANCMCMMVSGNHNVLITNPRDIPGF--IKELGKWRFSALLGLNTLFVALM----- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 752 GDPELCVL---------AGGEALPTKVAEELLRCCG-SLWNLYGPTETT-IWSLKSQITQAENITLGAPIANTRIYILDN 820
Cdd:PRK12492 323 DHPGFKDLdfsalkltnSGGTALVKATAERWEQLTGcTIVEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 821 EGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEPgvpggrMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIEL 900
Cdd:PRK12492 403 DGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEG------WFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYP 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 901 GEIERTLARHPHVdaAVVACI----ERAplHKALAAFIITSEPPSLFEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGK 976
Cdd:PRK12492 477 NEIEDVVMAHPKV--ANCAAIgvpdERS--GEAVKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGK 552
|
....*...
gi 1288439980 977 IDRKRLAE 984
Cdd:PRK12492 553 ILRRELRD 560
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
526-986 |
4.74e-21 |
|
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: 99.56 E-value: 4.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 526 TLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACY-VPFDIHQPAARLQRLMQ-RARLV--- 600
Cdd:cd05966 84 TITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHsVVFAGFSAESLADRINDaQCKLVita 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 601 ----------------------------CLVVRQPG---EWGEIVQLSLPELMQDMSnaiRYSTPCALLPDMQAYLLFTS 649
Cdd:cd05966 164 dggyrggkviplkeivdealekcpsvekVLVVKRTGgevPMTEGRDLWWHDLMAKQS---PECEPEWMDSEDPLFILYTS 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 650 GSTGEPKGVcvVHR--G-LLNLLLDMQRTFAVGSQDRLLSvttpTFDI------SFLEYLlPLISGASLYLTE-AERAAD 719
Cdd:cd05966 241 GSTGKPKGV--VHTtgGyLLYAATTFKYVFDYHPDDIYWC----TADIgwitghSYIVYG-PLANGATTVMFEgTPTYPD 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 720 SFRMIPLIADYR-------PTLMQAtpsfwhglLMAGwrgdpelcvlagGEALPTKVAEELLRCCGS------------L 780
Cdd:cd05966 314 PGRYWDIVEKHKvtifytaPTAIRA--------LMKF------------GDEWVKKHDLSSLRVLGSvgepinpeawmwY 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 781 WNLYG----PTETTIWslksQ-------ITQAENITLGAPIANTR------IYILDNEGHPVPQGVDGELYIAGD--GVA 841
Cdd:cd05966 374 YEVIGkercPIVDTWW----QtetggimITPLPGATPLKPGSATRpffgiePAILDEEGNEVEGEVEGYLVIKRPwpGMA 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 842 QGYDGQPELNAQFFLSEpgVPGgrMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHV-DAAVVAC 920
Cdd:cd05966 450 RTIYGDHERYEDTYFSK--FPG--YYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVaEAAVVGR 525
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1288439980 921 ieraPlHK----ALAAFII--TSEPPS--LFEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDR---KRLAENF 986
Cdd:cd05966 526 ----P-HDikgeAIYAFVTlkDGEEPSdeLRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRrilRKIAAGE 597
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
505-984 |
5.03e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 98.96 E-value: 5.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 505 RIIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVP---- 580
Cdd:PRK07470 11 HFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPtnfr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 581 -----------------------FDIHQPAARLQRLMQRARLVCLVVRQPGEWGEIVQLSLPELMQDMsnAIRYSTPCal 637
Cdd:PRK07470 91 qtpdevaylaeasgaramichadFPEHAAAVRAASPDLTHVVAIGGARAGLDYEALVARHLGARVANA--AVDHDDPC-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 638 lpdmqaYLLFTSGSTGEPKGVCVVHRGL----LNLLLDMqrTFAVGSQDRLLsVTTPTFDISFLEYLLPLISGASLYLTE 713
Cdd:PRK07470 167 ------WFFFTSGTTGRPKAAVLTHGQMafviTNHLADL--MPGTTEQDASL-VVAPLSHGAGIHQLCQVARGAATVLLP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 714 AER--AADSFRmipLIADYRPTLMQATPS-------------FWHGLL----MAG---WRGDPELcvlaggeALpTKVAE 771
Cdd:PRK07470 238 SERfdPAEVWA---LVERHRVTNLFTVPTilkmlvehpavdrYDHSSLryviYAGapmYRADQKR-------AL-AKLGK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 772 ELLRccgslwnLYGPTETT--IWSLKSQITQAENI------TLGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQG 843
Cdd:PRK07470 307 VLVQ-------YFGLGEVTgnITVLPPALHDAEDGpdarigTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 844 YDGQPELNAQFFLsepgvpgGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIER 923
Cdd:PRK07470 380 YYNNPEANAKAFR-------DGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPD 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1288439980 924 APLHKALAAFIITSEPPSLFE-QLKNELRQQLPDYMVPtlwQRV---ADFPNTDNGKIDRKRLAE 984
Cdd:PRK07470 453 PVWGEVGVAVCVARDGAPVDEaELLAWLDGKVARYKLP---KRFffwDALPKSGYGKITKKMVRE 514
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
495-918 |
7.02e-21 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 99.26 E-value: 7.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 495 VPW---LGPQDVLRIIEQRCVQHPKQLAIQ-QHDG-------TLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRD 563
Cdd:PRK07529 16 VPLaarDLPASTYELLSRAAARHPDAPALSfLLDAdpldrpeTWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 564 VIATMLATWFVG-AC-------------------------YVPF---DIHQPAARLQRLMQRARLVCLV---VRQPGEWG 611
Cdd:PRK07529 96 THFALWGGEAAGiANpinpllepeqiaellraagakvlvtLGPFpgtDIWQKVAEVLAALPELRTVVEVdlaRYLPGPKR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 612 EIVQLSLP-----------ELMQDMSNAIRYSTPcaLLPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGS 680
Cdd:PRK07529 176 LAVPLIRRkaharildfdaELARQPGDRLFSGRP--IGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 681 QDRLLSvTTPTFDI--SFLEYLLPLISGASLYL-TEA----ERAADSFRMIplIADYRPTLMQATPSFWhGLLMAGWRGD 753
Cdd:PRK07529 254 GDTVFC-GLPLFHVnaLLVTGLAPLARGAHVVLaTPQgyrgPGVIANFWKI--VERYRINFLSGVPTVY-AALLQVPVDG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 754 PELC----VLAGGEALPTKVAEELLRCCG-SLWNLYGPTETTIWSLKSQITQAE---NITLGAPIANTRIYILDNEGH-P 824
Cdd:PRK07529 330 HDISslryALCGAAPLPVEVFRRFEAATGvRIVEGYGLTEATCVSSVNPPDGERrigSVGLRLPYQRVRVVILDDAGRyL 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 825 VPQGVD--GELYIAGDGVAQGYDgQPELNAQFFLsepgvpGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGE 902
Cdd:PRK07529 410 RDCAVDevGVLCIAGPNVFSGYL-EAAHNKGLWL------EDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAA 482
|
490
....*....|....*..
gi 1288439980 903 IERTLARHPHV-DAAVV 918
Cdd:PRK07529 483 IEEALLRHPAVaLAAAV 499
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
526-979 |
8.41e-21 |
|
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: 97.51 E-value: 8.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 526 TLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPfdihqpaarlqrlmqrarlvclvvr 605
Cdd:cd05914 7 PLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVP------------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 606 qpgewgeIVQLSLPelmQDMSNAIRYSTPCALL---PDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQD 682
Cdd:cd05914 62 -------ILAEFTA---DEVHHILNHSEAKAIFvsdEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 683 RLLSVTtP---TFDISFlEYLLPLISGASLYLTEaeRAADSFRMIPLIADYRPTLMQATP-------------------- 739
Cdd:cd05914 132 KILSIL-PlhhIYPLTF-TLLLPLLNGAHVVFLD--KIPSAKIIALAFAQVTPTLGVPVPlviekifkmdiipkltlkkf 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 740 -----------SFWHGL---LMAGWRGDPELCVLaGGEALPTKVAEELLR-----CCGslwnlYGPTETT-IWSLksqiT 799
Cdd:cd05914 208 kfklakkinnrKIRKLAfkkVHEAFGGNIKEFVI-GGAKINPDVEEFLRTigfpyTIG-----YGMTETApIISY----S 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 800 QAENITL---GAPIANTRIYILDneghPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFlsepgVPGGrMFRTGDLVRSD 876
Cdd:cd05914 278 PPNRIRLgsaGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAF-----DKDG-WFHTGDLGKID 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 877 AQGQLFFVGRKDSQIKL-RGYRIELGEIERTLARHPHVDAAVVACIE-----RAPLHKALA---AFIITSEPPSLFEQLK 947
Cdd:cd05914 348 AEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESLVVVQEkklvaLAYIDPDFLdvkALKQRNIIDAIKWEVR 427
|
490 500 510
....*....|....*....|....*....|....*....
gi 1288439980 948 NELRQQLPDYmvptlwQRVAD-------FPNTDNGKIDR 979
Cdd:cd05914 428 DKVNQKVPNY------KKISKvkivkeeFEKTPKGKIKR 460
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
1098-1521 |
1.29e-20 |
|
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: 97.02 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1098 PLTDVQRAYWLGRQTGATSIATHIYHEFDVE-HFNVTRFTHAVNALIARHEMLRARVLPDGT----QQILAQVPaYQLEQ 1172
Cdd:pfam00668 6 PLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTgELDPERLEKALQELINRHDALRTVFIRQENgepvQVILEERP-FELEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1173 RDLSALSPNARNDALMAIRDRLSHHVHPADRWPLFDFSYSACTAQHGRLHFSLDLLIADALSMRTLQQELMMLYREPHV- 1251
Cdd:pfam00668 85 IDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLLKg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1252 -SLPLLPF-SFRDYVQALLVEQASEAYARDQAYWQRALPQLYGPPTLPvqGDLAQLSAIRFV--RRRHRLSAHNWGVLSA 1327
Cdd:pfam00668 165 ePLPLPPKtPYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLP--KDYARPADRSFKgdRLSFTLDEDTEELLRK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1328 LAQRTRITKTALLLTVFSQVLARWSLSPTFTLNLTLFNRPQgyPNAEAVIGDFTAVSLLNVCYDSQHSYAHNAQRIQVQL 1407
Cdd:pfam00668 243 LAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPS--PDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1408 WEDLEHRR--FSGIRASEALIHSGRFHA---PMpVVFTSMLDIDGETTAQDPrdtTRFTLCPDANITQTPQVWLDHQVIE 1482
Cdd:pfam00668 321 LSAEPHQGypFGDLVNDLRLPRDLSRHPlfdPM-FSFQNYLGQDSQEEEFQL---SELDLSVSSVIEEEAKYDLSLTASE 396
|
410 420 430
....*....|....*....|....*....|....*....
gi 1288439980 1483 LAGELHFNWDAVEQLFDTTLLDQMFGAYCHALQALVAMP 1521
Cdd:pfam00668 397 RGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHP 435
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1138-1595 |
2.40e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 98.88 E-value: 2.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1138 AVNALIARHEMLRArVLPDGTQQILAQVPA---YQLEQRDLSALSPNARNDALMAIRDRLSHHVHPADRWPLFDFSYSAC 1214
Cdd:PRK12316 92 AFASLVQRHETLRT-VFPRGADDSLAQVPLdrpLEVEFEDCSGLPEAEQEARLRDEAQRESLQPFDLCEGPLLRVRLLRL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1215 TAQHGRLHFSLDLLIADALSMRTLQQELMMLY----REPHVSLPLLPFSFRDYvqALLVEQASEA--YARDQAYWQRAL- 1287
Cdd:PRK12316 171 GEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYsayaTGAEPGLPALPIQYADY--ALWQRSWLEAgeQERQLEYWRAQLg 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1288 ---PQLYGP-----PTLP-VQGDLAQLSAIRFVRRRhrlsahnwgvLSALAQRTRITKTALLLTVFSQVLARWSLSPTFT 1358
Cdd:PRK12316 249 eehPVLELPtdhprPAVPsYRGSRYEFSIDPALAEA----------LRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1359 LNLTLFNRPQGypNAEAVIGDFTAVSLLNVCYDSQHSYAHNAQRIQ-----VQLWEDLEHRRF-SGIRASEALIHSGRF- 1431
Cdd:PRK12316 319 VGVPIANRNRA--EVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKdtvlgAQAHQDLPFERLvEALKVERSLSHSPLFq 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1432 ----HAPMPVVFTSMLDIDGETTAQDPRD--TTRFTLCPDanitqtpqvwldhqVIELAGELHFNWDAVEQLFDTTLLDQ 1505
Cdd:PRK12316 397 vmynHQPLVADIEALDTVAGLEFGQLEWKsrTTQFDLTLD--------------TYEKGGRLHAALTYATDLFEARTVER 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1506 MFGAYCHALQALVAMPQSwwgvnSSLALPTVSA--------PVTQAPAPTAL---LHHGLLRQAALTPQETALISPIREL 1574
Cdd:PRK12316 463 MARHWQNLLRGMVENPQA-----RVDELPMLDAeergqlveGWNATAAEYPLqrgVHRLFEEQVERTPEAPALAFGEETL 537
|
490 500
....*....|....*....|.
gi 1288439980 1575 TYRQLSTAADHVARALLALGV 1595
Cdd:PRK12316 538 DYAELNRRANRLAHALIERGV 558
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
803-982 |
3.34e-20 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 96.66 E-value: 3.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 803 NITLGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFflsepgVPGGRMfRTGDLVRSDAQGQLF 882
Cdd:PRK08974 377 SGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEV------IKDGWL-ATGDIAVMDEEGFLR 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 883 FVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEPPSLFEQLKNELRQQLPDYMVPTL 962
Cdd:PRK08974 450 IVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLTEEELITHCRRHLTGYKVPKL 529
|
170 180
....*....|....*....|
gi 1288439980 963 WQRVADFPNTDNGKIDRKRL 982
Cdd:PRK08974 530 VEFRDELPKSNVGKILRREL 549
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
51-455 |
3.83e-20 |
|
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: 94.67 E-value: 3.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 51 QERLwflqkYDSTATNYNLYV---VYRLHGVVDMPMLTEALRHVQARHAILRTRII-VRNDRPCQViddasslVLDTVTL 126
Cdd:cd19545 8 QEGL-----MALTARQPGAYVgqrVFELPPDIDLARLQAAWEQVVQANPILRTRIVqSDSGGLLQV-------VVKESPI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 127 AAQAPTSaLDAVIQQVINTRFDLArGPLWGVTQIIQPDQGCHLVFCAHHIIIDGISLRLLFDELQQQYarlhAGNETSLP 206
Cdd:cd19545 76 SWTESTS-LDEYLEEDRAAPMGLG-GPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAY----QGEPVPQP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 207 PPPLQYADYafwqrewfqdtLLANELA----YWRARLQDA--PLLSTFPSLHPRPAQPSTHgsRFSITLDETLSLAlkhv 280
Cdd:cd19545 150 PPFSRFVKY-----------LRQLDDEaaaeFWRSYLAGLdpAVFPPLPSSRYQPRPDATL--EHSISLPSSASSG---- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 281 artqeTTPFVLMLTAFQLVLMRYAQQQRLVIGMPVSGRIRP--ELQSSIGYYASTAVIYTDFNGVEVGREALQRVKasvk 358
Cdd:cd19545 213 -----VTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPvpGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQ---- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 359 eTQGRQQLPFEN--LVNMLDLPRSLSHSPLFQILYIyhnhVTPRAFTLAGAYWEQVTYHnQTVKYD------MTVEVFQN 430
Cdd:cd19545 284 -KDLLDMIPFEHtgLQNIRRLGPDARAACNFQTLLV----VQPALPSSTSESLELGIEE-ESEDLEdfssygLTLECQLS 357
|
410 420
....*....|....*....|....*
gi 1288439980 431 DATFDVSFEYDLGLYDADVVKQIAE 455
Cdd:cd19545 358 GSGLRVRARYDSSVISEEQVERLLD 382
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
526-983 |
3.88e-20 |
|
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: 96.62 E-value: 3.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 526 TLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGA----------------------------- 576
Cdd:cd05967 82 TYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAihsvvfggfaakelasriddakpklivta 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 577 ----------CYVPF-------DIHQPAARL--QRLMQRARLVclvvrQPG---EWGEIvqlslpelmqdMSNAIRYstP 634
Cdd:cd05967 162 scgiepgkvvPYKPLldkalelSGHKPHHVLvlNRPQVPADLT-----KPGrdlDWSEL-----------LAKAEPV--D 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 635 CA-LLPDMQAYLLFTSGSTGEPKGVCVVHRG-LLNLLLDMQRTFAVGSQDRLLSVTtptfDI------SFLEYLlPLISG 706
Cdd:cd05967 224 CVpVAATDPLYILYTSGTTGKPKGVVRDNGGhAVALNWSMRNIYGIKPGDVWWAAS----DVgwvvghSYIVYG-PLLHG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 707 ASLYLTEAE--RAADSFRMIPLIADYR-------PT----LMQATPSFWHG----------LLMAGWRGDPELCVLAGgE 763
Cdd:cd05967 299 ATTVLYEGKpvGTPDPGAFWRVIEKYQvnalftaPTairaIRKEDPDGKYIkkydlsslrtLFLAGERLDPPTLEWAE-N 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 764 ALPTKVAEELlrccgslWNlygpTETTiWSLKSQITQAENITL-----GAPIANTRIYILDNEGHPVPQGVDGELYIAGD 838
Cdd:cd05967 378 TLGVPVIDHW-------WQ----TETG-WPITANPVGLEPLPIkagspGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLP 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 839 ---GVAQGYDGQPELNAQFFLSE-PGVpggrmFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHV- 913
Cdd:cd05967 446 lppGCLLTLWKNDERFKKLYLSKfPGY-----YDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVa 520
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1288439980 914 DAAVVACIERAPLHKALAAFIITSEPPSLFEQLKNEL----RQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLA 983
Cdd:cd05967 521 ECAVVGVRDELKGQVPLGLVVLKEGVKITAEELEKELvalvREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLR 594
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
526-990 |
4.73e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 95.74 E-value: 4.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 526 TLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLMQRARLVCLVVR 605
Cdd:PRK08276 11 VVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 606 QPG-----EWGEIVQLSLPELMQDMSNAIRYSTPCALLPDMQAY----------LLFTSGSTGEPKGV------CVVHRG 664
Cdd:PRK08276 91 AALadtaaELAAELPAGVPLLLVVAGPVPGFRSYEEALAAQPDTpiadetagadMLYSSGTTGRPKGIkrplpgLDPDEA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 665 LLNLLLDMQRTFAVGSQDRLLSvTTPTFDISFLEYllpliSGASLYLTEAERAADSF---RMIPLIADYRPTLMQATPSF 741
Cdd:PRK08276 171 PGMMLALLGFGMYGGPDSVYLS-PAPLYHTAPLRF-----GMSALALGGTVVVMEKFdaeEALALIERYRVTHSQLVPTM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 742 WHGLL-----------MAGWRGdpelcVLAGGEALPTKVAEELLRCCGS-LWNLYGPTE---TTIwslksqITQAENI-- 804
Cdd:PRK08276 245 FVRMLklpeevrarydVSSLRV-----AIHAAAPCPVEVKRAMIDWWGPiIHEYYASSEgggVTV------ITSEDWLah 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 805 --TLGAPIAnTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLsepgvpGGRMFRTGDLVRSDAQGQLF 882
Cdd:PRK08276 314 pgSVGKAVL-GEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARN------PHGWVTVGDVGYLDEDGYLY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 883 FVGRKDSQIKLRGYRIELGEIERTLARHPHV-DAAV------------VACIERAPLHKAlaafiitsePPSLFEQLKNE 949
Cdd:PRK08276 387 LTDRKSDMIISGGVNIYPQEIENLLVTHPKVaDVAVfgvpdeemgervKAVVQPADGADA---------GDALAAELIAW 457
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1288439980 950 LRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAENFVADS 990
Cdd:PRK08276 458 LRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWEGR 498
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
638-986 |
8.73e-20 |
|
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: 94.86 E-value: 8.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 638 LPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSVTTPTFD---ISFleYLLPLISGASLYLTEA 714
Cdd:cd05908 104 LADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDmglIAF--HLAPLIAGMNQYLMPT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 715 ERaadsFRMIPL-----IADYRPTLMqATPSFWHGLLM--------AGWRGDPELCVLAGGEALPTKVAEELLRCCG--- 778
Cdd:cd05908 182 RL----FIRRPIlwlkkASEHKATIV-SSPNFGYKYFLktlkpekaNDWDLSSIRMILNGAEPIDYELCHEFLDHMSkyg 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 779 ----SLWNLYGPTE--------------TTIWSLKSQITQAENI--------------TLGAPIANTRIYILDNEGHPVP 826
Cdd:cd05908 257 lkrnAILPVYGLAEasvgaslpkaqspfKTITLGRRHVTHGEPEpevdkkdsecltfvEVGKPIDETDIRICDEDNKILP 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 827 QGVDGELYIAGDGVAQGYDGQPELNAQFFlSEPGvpggrMFRTGDL--VRsdaQGQLFFVGRKDSQIKLRGYRIELGEIE 904
Cdd:cd05908 337 DGYIGHIQIRGKNVTPGYYNNPEATAKVF-TDDG-----WLKTGDLgfIR---NGRLVITGREKDIIFVNGQNVYPHDIE 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 905 RTLARHPHVDAA-VVAC--IERAPLHKALAAFIITSEPPSLFEQLKNELRQQLPDYmvpTLWQ-----RVADFPNTDNGK 976
Cdd:cd05908 408 RIAEELEGVELGrVVACgvNNSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHLNKR---GGWQinevlPIRRIPKTTSGK 484
|
410
....*....|
gi 1288439980 977 IDRKRLAENF 986
Cdd:cd05908 485 VKRYELAQRY 494
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
521-982 |
9.46e-20 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 95.87 E-value: 9.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 521 QQHDGTLTYAELwarvqfiamrFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVG--ACYVPFDIHQPAARLQrlmQRAR 598
Cdd:PRK06060 35 QIHDGAARLGEV----------LRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGvmAFLANPELHRDDHALA---ARNT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 599 LVCLVVRQPGEWGEIVQLSLPELMQDMSNAIRySTPCALLP---DMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQR- 674
Cdd:PRK06060 102 EPALVVTSDALRDRFQPSRVAEAAELMSEAAR-VAPGGYEPmggDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRk 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 675 TFAVGSQDRLLSVTTPTFDISFLEYL-LPLISGASLYLTEAERAADSFRMipLIADYRPTLMQATPSFWHGLLMA----G 749
Cdd:PRK06060 181 ALRLTPEDTGLCSARMYFAYGLGNSVwFPLATGGSAVINSAPVTPEAAAI--LSARFGPSVLYGVPNFFARVIDScspdS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 750 WRGdpELCVLAGGEALPTKVAEELLRCCGSLWNL--YGPTETTIWSLKSQITQAENITLGAPIANTRIYILDNEGHPVPQ 827
Cdd:PRK06060 259 FRS--LRCVVSAGEALELGLAERLMEFFGGIPILdgIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAPDGTTAGP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 828 GVDGELYIAGDGVAQGYDGQPElnaqfflsePGVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTL 907
Cdd:PRK06060 337 GVEGDLWVRGPAIAKGYWNRPD---------SPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLI 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1288439980 908 ARHPHVDAAVVACIERAPLHKALAAFIITSEPP----SLFEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRL 982
Cdd:PRK06060 408 IEDEAVAEAAVVAVRESTGASTLQAFLVATSGAtidgSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGAL 486
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
515-993 |
1.45e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 94.46 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 515 PKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLM 594
Cdd:PRK07786 31 PDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 595 Q--RARLV---------CLVVRQPGEWGEIVQL---SLPELMQDMSNAIRYSTPC---ALLP-DMQAYLLFTSGSTGEPK 656
Cdd:PRK07786 111 SdcGAHVVvteaalapvATAVRDIVPLLSTVVVaggSSDDSVLGYEDLLAEAGPAhapVDIPnDSPALIMYTSGTTGRPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 657 GVCVVHRGLLNLLLDMQRTFAVGSQDRLLSVTTPTFDISFLEYLLP-LISGASLYLTEAeRAADSFRMIPLIADYRPTLM 735
Cdd:PRK07786 191 GAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPgLLLGAPTVIYPL-GAFDPGQLLDVLEAEKVTGI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 736 QATPSFWHGLLmAGWRGDP---ELCVLAGGEA-LPTKVAEELLRCCGSLWNL--YGPTE----TTIWSLKSQITQAENIt 805
Cdd:PRK07786 270 FLVPAQWQAVC-AEQQARPrdlALRVLSWGAApASDTLLRQMAATFPEAQILaaFGQTEmspvTCMLLGEDAIRKLGSV- 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 806 lGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFlsepgvpGGRMFRTGDLVRSDAQGQLFFVG 885
Cdd:PRK07786 348 -GKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF-------AGGWFHSGDLVRQDEEGYVWVVD 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 886 RKDSQIKLRGYRIELGEIERTLARHPH-VDAAVVACIERAPLHKALAAFIITSEPPSL-FEQLKNELRQQLPDYMVPTLW 963
Cdd:PRK07786 420 RKKDMIISGGENIYCAEVENVLASHPDiVEVAVIGRADEKWGEVPVAVAAVRNDDAALtLEDLAEFLTDRLARYKHPKAL 499
|
490 500 510
....*....|....*....|....*....|
gi 1288439980 964 QRVADFPNTDNGKIDRKRLAENFVADSSLV 993
Cdd:PRK07786 500 EIVDALPRNPAGKVLKTELRERYGACVNVE 529
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
527-977 |
2.92e-19 |
|
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: 93.87 E-value: 2.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 527 LTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGA----CYVPFDIHQPAARLQRLMQRARLVCL 602
Cdd:cd05943 99 VTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAiwssCSPDFGVPGVLDRFGQIEPKVLFAVD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 603 VVRQPG-------EWGEIVQlSLPELMQ-------------DMSNAIRYSTPCALLPDMQA--------------YLLFT 648
Cdd:cd05943 179 AYTYNGkrhdvreKVAELVK-GLPSLLAvvvvpytvaagqpDLSKIAKALTLEDFLATGAAgelefeplpfdhplYILYS 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 649 SGSTGEPKgvCVVHRG---LLNLLLDMQRTFAVGSQDRLLSVTTPT-----FDISFleyllpLISGASLYL-TEAERAAD 719
Cdd:cd05943 258 SGTTGLPK--CIVHGAggtLLQHLKEHILHCDLRPGDRLFYYTTCGwmmwnWLVSG------LAVGATIVLyDGSPFYPD 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 720 SFRMIPLIADYRPTLMQATPSFWHGLLMAGWRGDPEL------CVLAGGEALPTKVAEELLRCCGS---LWNLYGPTEtt 790
Cdd:cd05943 330 TNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHdlsslrTILSTGSPLKPESFDYVYDHIKPdvlLASISGGTD-- 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 791 IWSLKSQITQAENITLG---APIANTRIYILDNEGHPVPqGVDGELYIagdgvAQGYDGQP----------ELNAQFFLS 857
Cdd:cd05943 408 IISCFVGGNPLLPVYRGeiqCRGLGMAVEAFDEEGKPVW-GEKGELVC-----TKPFPSMPvgfwndpdgsRYRAAYFAK 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 858 EPGVpggrmFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITS 937
Cdd:cd05943 482 YPGV-----WAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLR 556
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1288439980 938 E----PPSLFEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKI 977
Cdd:cd05943 557 EgvelDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKK 600
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
513-984 |
4.74e-19 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 92.24 E-value: 4.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 513 QHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDriGVLL--PRHRDVIATMLATWFVGACYVPFDIHQPAARL 590
Cdd:PRK09029 15 VRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGS--GVALrgKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 591 QRLMQRARLVCLVVRQPGEWgeivqlsLPELMQDMSNAIRYSTPCALLPDMQAYLLFTSGSTGEPKGvcVVH-------- 662
Cdd:PRK09029 93 EELLPSLTLDFALVLEGENT-------FSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKA--AVHtaqahlas 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 663 -RGLLNLlldmqrtFAVGSQDR-LLSVttPTFDISFLEYLLP-LISGASLYLTEAEraadsfrmiPLIADyrptLMQATp 739
Cdd:PRK09029 164 aEGVLSL-------MPFTAQDSwLLSL--PLFHVSGQGIVWRwLYAGATLVVRDKQ---------PLEQA----LAGCT- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 740 sfwHGLLMAG--WR-----GDPELC--VLAGGEALPTKVAEEL----LRC-CGslwnlYGPTEttiwsLKSQIT--QAEN 803
Cdd:PRK09029 221 ---HASLVPTqlWRlldnrSEPLSLkaVLLGGAAIPVELTEQAeqqgIRCwCG-----YGLTE-----MASTVCakRADG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 804 itlgapiantriyiLDNEGHPVPQG----VDGELYIAGDGVAQGY--DGQ--PELNAQFFlsepgvpggrmFRTGDLVRS 875
Cdd:PRK09029 288 --------------LAGVGSPLPGRevklVDGEIWLRGASLALGYwrQGQlvPLVNDEGW-----------FATRDRGEW 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 876 DaQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPL-HKALAafIITSEPPSLFEQLKNELRQQL 954
Cdd:PRK09029 343 Q-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFgQRPVA--VVESDSEAAVVNLAEWLQDKL 419
|
490 500 510
....*....|....*....|....*....|....*
gi 1288439980 955 PDYMVPtlwqrVADFP---NTDNG--KIDRKRLAE 984
Cdd:PRK09029 420 ARFQQP-----VAYYLlppELKNGgiKISRQALKE 449
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
805-982 |
5.62e-19 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 92.75 E-value: 5.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 805 TLGAPIA-NTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEPgvpggrMFRTGDLVRSDAQGQLFF 883
Cdd:PRK10946 354 TQGRPMSpDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANG------FYCSGDLVSIDPDGYITV 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 884 VGRKDSQIKLRGYRIELGEIERTLARHPHV-DAAVVAcIERAPLHKALAAFIITSEPPSLFeQLKNELRQQ-LPDYMVPT 961
Cdd:PRK10946 428 VGREKDQINRGGEKIAAEEIENLLLRHPAViHAALVS-MEDELMGEKSCAFLVVKEPLKAV-QLRRFLREQgIAEFKLPD 505
|
170 180
....*....|....*....|.
gi 1288439980 962 LWQRVADFPNTDNGKIDRKRL 982
Cdd:PRK10946 506 RVECVDSLPLTAVGKVDKKQL 526
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
645-918 |
6.58e-19 |
|
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: 90.05 E-value: 6.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 645 LLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSVTtPTFDISFLEYLLP--LISGASLY-----------L 711
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSG-PLFHIGTLMFTLAtfHAGGTNVFvrrvdaeevleL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 712 TEAERAADSFRMIPLI-------ADYRPTLmqatPSFWHGLLMAGWRG-----DPELCVLAGGealptkvaeellrccgs 779
Cdd:cd17636 84 IEAERCTHAFLLPPTIdqivelnADGLYDL----SSLRSSPAAPEWNDmatvdTSPWGRKPGG----------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 780 lwnlYGPTETT-IWSLKSQITQAENiTLGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSe 858
Cdd:cd17636 143 ----YGQTEVMgLATFAALGGGAIG-GAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG- 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1288439980 859 pgvpGGRmfRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHV-DAAVV 918
Cdd:cd17636 217 ----GWH--HTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVaDAAVI 271
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
547-982 |
8.44e-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: 92.14 E-value: 8.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 547 GIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLMQRARLVCLVV---------------------- 604
Cdd:cd05928 63 GLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTsdelapevdsvasecpslktkl 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 605 -----RQPGeWgeivqLSLPELMQDMS---NAIRYSTpcalLPDMQAYllFTSGSTGEPKGVCVVHRGL-LNLLLDMQRT 675
Cdd:cd05928 143 lvsekSRDG-W-----LNFKELLNEAStehHCVETGS----QEPMAIY--FTSGTTGSPKMAEHSHSSLgLGLKVNGRYW 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 676 FAVGSQDRLLSVTTPTFDISFLEYLL-PLISGASLYLTEAERAaDSFRMIPLIADYRPTLMQATPSFWHGLL---MAGWR 751
Cdd:cd05928 211 LDLTASDIMWNTSDTGWIKSAWSSLFePWIQGACVFVHHLPRF-DPLVILKTLSSYPITTFCGAPTVYRMLVqqdLSSYK 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 752 GDPELCVLAGGEALPTKVAEELLRCCG-SLWNLYGPTETTIWSLKSQITQAENITLGAPIANTRIYILDNEGHPVPQGVD 830
Cdd:cd05928 290 FPSLQHCVTGGEPLNPEVLEKWKAQTGlDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 831 GELYIAGD-----GVAQGYDGQPELNAQFFLsepgvpgGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIER 905
Cdd:cd05928 370 GDIGIRVKpirpfGLFSGYVDNPEKTAATIR-------GDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVES 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 906 TLARHPHV-DAAVVACIE--RAPLHKA---LAAFIITSEPpslfEQLKNELRQQLPDYMVPTLWQR----VADFPNTDNG 975
Cdd:cd05928 443 ALIEHPAVvESAVVSSPDpiRGEVVKAfvvLAPQFLSHDP----EQLTKELQQHVKSVTAPYKYPRkvefVQELPKTVTG 518
|
....*..
gi 1288439980 976 KIDRKRL 982
Cdd:cd05928 519 KIQRNEL 525
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
645-977 |
1.41e-18 |
|
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: 88.71 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 645 LLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLsVTTPTFDiSF---LEYLLPLISGASLYlteAERAADSF 721
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYL-IINPFFH-TFgykAGIVACLLTGATVV---PVAVFDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 722 RMIPLIADYRPTLMQATPSFWHGLLMAGWRGDPELCVL----AGGEALPTKVAEELLRCCG--SLWNLYGPTETTIWSLK 795
Cdd:cd17638 80 AILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLraavTGAATVPVELVRRMRSELGfeTVLTAYGLTEAGVATMC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 796 SQITQAENI--TLGAPIANTRIYILDneghpvpqgvDGELYIAGDGVAQGYDGQPELNAQfflsepGVPGGRMFRTGDLV 873
Cdd:cd17638 160 RPGDDAETVatTCGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEATAE------AIDADGWLHTGDVG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 874 RSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHV-DAAVVACI-ERapLHKALAAFIITSEPPSLFEQ-LKNEL 950
Cdd:cd17638 224 ELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVaQVAVIGVPdER--MGEVGKAFVVARPGVTLTEEdVIAWC 301
|
330 340
....*....|....*....|....*..
gi 1288439980 951 RQQLPDYMVPTLWQRVADFPNTDNGKI 977
Cdd:cd17638 302 RERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
501-982 |
1.44e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 91.36 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 501 QDVLRIIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAH-GIQPGDRIGVLLPRHRD----VIATMLATWFV- 574
Cdd:PRK05677 24 PNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQypvaVFGAMRAGLIVv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 575 --GACYVPFDI-HQ----PAARLQRLMQRARLVCLVVRQPGEWGEIV-QLS--LPELMQDMSNAI---------RYSTPC 635
Cdd:PRK05677 104 ntNPLYTAREMeHQfndsGAKALVCLANMAHLAEKVLPKTGVKHVIVtEVAdmLPPLKRLLINAVvkhvkkmvpAYHLPQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 636 AL-------------------LPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFA--VGSQDRLLSVTTPTFDI 694
Cdd:PRK05677 184 AVkfndalakgagqpvteanpQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGsnLNEGCEILIAPLPLYHI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 695 -SF-LEYLLPLISGASLYLTEAERAADSfrMIPLIADYR-------PTLMQAtpsfwhgllmagwrgdpeLC-------- 757
Cdd:PRK05677 264 yAFtFHCMAMMLIGNHNILISNPRDLPA--MVKELGKWKfsgfvglNTLFVA------------------LCnneafrkl 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 758 -------VLAGGEALPTKVAEELLRCCG-SLWNLYGPTETtiwSLKSQITQAENI---TLGAPIANTRIYILDNEGHPVP 826
Cdd:PRK05677 324 dfsalklTLSGGMALQLATAERWKEVTGcAICEGYGMTET---SPVVSVNPSQAIqvgTIGIPVPSTLCKVIDDDGNELP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 827 QGVDGELYIAGDGVAQGYDGQPELNAQFFLSEPgvpggrMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERT 906
Cdd:PRK05677 401 LGEVGELCVKGPQVMKGYWQRPEATDEILDSDG------WLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDV 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1288439980 907 LARHPHVDAAVVACIERAPLHKALAAFIITSEPPSLF-EQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRL 982
Cdd:PRK05677 475 LAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTkEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
505-978 |
6.99e-18 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 90.41 E-value: 6.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 505 RIIEQRCVQHPKQLAIQQHDGT-LTYAELWARvQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGacYVPFDI 583
Cdd:PRK06814 636 ALIEAAKIHGFKKLAVEDPVNGpLTYRKLLTG-AFVLGRKLKKNTPPGENVGVMLPNANGAAVTFFALQSAG--RVPAMI 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 584 HQPA--------------------------ARLQRLM----QRARLVCL--VVRQPGEWGEI---VQLSLPELMQDMSNa 628
Cdd:PRK06814 713 NFSAgianilsackaaqvktvltsrafiekARLGPLIealeFGIRIIYLedVRAQIGLADKIkglLAGRFPLVYFCNRD- 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 629 irystpcallPDMQAYLLFTSGSTGEPKGVCVVHRgllNLLLDMQRTFAV---GSQDRLLSVtTPTFDiSF-LE--YLLP 702
Cdd:PRK06814 792 ----------PDDPAVILFTSGSEGTPKGVVLSHR---NLLANRAQVAARidfSPEDKVFNA-LPVFH-SFgLTggLVLP 856
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 703 LISGASLYLTEAERaadSFRMIP-LIADYRPTLMQATPSFwhgllMAGW------------RgdpelCVLAGGEalptKV 769
Cdd:PRK06814 857 LLSGVKVFLYPSPL---HYRIIPeLIYDTNATILFGTDTF-----LNGYaryahpydfrslR-----YVFAGAE----KV 919
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 770 AEELLRccgsLW---------NLYGPTETtiwslksqitqAENITLGAPIANT-----RI-----YILDneghPVPqGVD 830
Cdd:PRK06814 920 KEETRQ----TWmekfgirilEGYGVTET-----------APVIALNTPMHNKagtvgRLlpgieYRLE----PVP-GID 979
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 831 --GELYIAGDGVAQGYdgqpeLNAqfflSEPGV---PGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIEr 905
Cdd:PRK06814 980 egGRLFVRGPNVMLGY-----LRA----ENPGVlepPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVE- 1049
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 906 TLARH--PHVDAAVVACI-----ERAPLhkalaafIITSEPPSLFEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKID 978
Cdd:PRK06814 1050 ELAAElwPDALHAAVSIPdarkgERIIL-------LTTASDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
514-988 |
8.48e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 88.59 E-value: 8.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 514 HPKQLA-IQQHDGT-LTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQ 591
Cdd:PRK13391 10 TPDKPAvIMASTGEvVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 592 RLMQ--RARLVCLVVRQPGEWGEIVQLS---LPELMQDMSNAI----RYSTPCALLPD-------MQAYLLFTSGSTGEP 655
Cdd:PRK13391 90 YIVDdsGARALITSAAKLDVARALLKQCpgvRHRLVLDGDGELegfvGYAEAVAGLPAtpiadesLGTDMLYSSGTTGRP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 656 KGvcvVHRGL--------LNLLLDMQRTFAVGSQDRLLSvTTPTFDISFLEYLLPLIS-GASLYLTE---AERAadsfrm 723
Cdd:PRK13391 170 KG---IKRPLpeqppdtpLPLTAFLQRLWGFRSDMVYLS-PAPLYHSAPQRAVMLVIRlGGTVIVMEhfdAEQY------ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 724 IPLIADYRPTLMQATPSFWHGLLM--AGWRGDPELCVLA----GGEALPTKVAEELLRCCGS-LWNLYGPTETTIWS-LK 795
Cdd:PRK13391 240 LALIEEYGVTHTQLVPTMFSRMLKlpEEVRDKYDLSSLEvaihAAAPCPPQVKEQMIDWWGPiIHEYYAATEGLGFTaCD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 796 SQITQAENITLGAPIANTrIYILDNEGHPVPQGVDGELYIAGdGVAQGYDGQPELNAqfflsEPGVPGGRMFRTGDLVRS 875
Cdd:PRK13391 320 SEEWLAHPGTVGRAMFGD-LHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTA-----EARHPDGTWSTVGDIGYV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 876 DAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHV-DAAVVAcIERAPLHKALAAFIITSEP----PSLFEQLKNEL 950
Cdd:PRK13391 393 DEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVaDAAVFG-VPNEDLGEEVKAVVQPVDGvdpgPALAAELIAFC 471
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1288439980 951 RQQLPDYMVPtlwqRVADF----PNTDNGKIDRKRLAENFVA 988
Cdd:PRK13391 472 RQRLSRQKCP----RSIDFedelPRLPTGKLYKRLLRDRYWG 509
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
526-982 |
1.34e-17 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 88.41 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 526 TLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVP-FDIHQPAA---RLQ---------- 591
Cdd:PRK04319 73 KYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPlFEAFMEEAvrdRLEdseakvlitt 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 592 -RLMQR---ARLVCL----VVRQPGEWGEIVqLSLPELMQDMSNaiRYSTPCALLPDMqAYLLFTSGSTGEPKGVCVVHR 663
Cdd:PRK04319 153 pALLERkpaDDLPSLkhvlLVGEDVEEGPGT-LDFNALMEQASD--EFDIEWTDREDG-AILHYTSGSTGKPKGVLHVHN 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 664 GLL------NLLLDMQrtfavgSQDRLLS------VTTPTFDIsfleyLLPLISGASLYLTEAERAADsfRMIPLIADYR 731
Cdd:PRK04319 229 AMLqhyqtgKYVLDLH------EDDVYWCtadpgwVTGTSYGI-----FAPWLNGATNVIDGGRFSPE--RWYRILEDYK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 732 -------PT----LMQATPSfwhglLMAGWRGDPELCVLAGGEAL-PtkvaeELLRccgslW--NLYG-PTETTIWslks 796
Cdd:PRK04319 296 vtvwytaPTairmLMGAGDD-----LVKKYDLSSLRHILSVGEPLnP-----EVVR-----WgmKVFGlPIHDNWW---- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 797 qitQAEniTLGAPIANTR---IY--------------ILDNEGHPVPQGVDGELYI-AG-DGVAQGYDGQPELNAQFFLs 857
Cdd:PRK04319 357 ---MTE--TGGIMIANYPamdIKpgsmgkplpgieaaIVDDQGNELPPNRMGNLAIkKGwPSMMRGIWNNPEKYESYFA- 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 858 epgvpgGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHV-DAAVVACIE--RAPLHKALAAFI 934
Cdd:PRK04319 431 ------GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVaEAGVIGKPDpvRGEIIKAFVALR 504
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1288439980 935 ITSEPPslfEQLKNELRQQLPDYMVPTLWQRVADF----PNTDNGKIDRKRL 982
Cdd:PRK04319 505 PGYEPS---EELKEEIRGFVKKGLGAHAAPREIEFkdklPKTRSGKIMRRVL 553
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
515-918 |
2.04e-17 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 87.62 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 515 PKQLAIQQHDG-TLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRL 593
Cdd:PRK07514 16 RDAPFIETPDGlRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 594 MQRARlVCLVVRQPGEWGEIVQL------------------SLPELMQDMSNAIRySTPCAllPDMQAYLLFTSGSTGEP 655
Cdd:PRK07514 96 IGDAE-PALVVCDPANFAWLSKIaaaagaphvetldadgtgSLLEAAAAAPDDFE-TVPRG--ADDLAAILYTSGTTGRS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 656 KGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSvTTPTFDIS--FLEYLLPLISGASLYLTEAERAADSFRMIPliadyRPT 733
Cdd:PRK07514 172 KGAMLSHGNLLSNALTLVDYWRFTPDDVLIH-ALPIFHTHglFVATNVALLAGASMIFLPKFDPDAVLALMP-----RAT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 734 LMQATPSFWHGLLmAGWRGDPELC-----VLAGGEALPTKVAEE---------LLRccgslwnlYGPTETTIwsLKSQIT 799
Cdd:PRK07514 246 VMMGVPTFYTRLL-QEPRLTREAAahmrlFISGSAPLLAETHREfqertghaiLER--------YGMTETNM--NTSNPY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 800 QAENI--TLGAPIANTRIYILDNE-GHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFlsepgVPGGrMFRTGDLVRSD 876
Cdd:PRK07514 315 DGERRagTVGFPLPGVSLRVTDPEtGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEF-----RADG-FFITGDLGKID 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1288439980 877 AQGQLFFVGR-KDSQIKlRGYRIELGEIERTLARHPHV-DAAVV 918
Cdd:PRK07514 389 ERGYVHIVGRgKDLIIS-GGYNVYPKEVEGEIDELPGVvESAVI 431
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
527-954 |
3.42e-17 |
|
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: 86.75 E-value: 3.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 527 LTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLMQRARLVCLVVRQ 606
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 607 PGEW--------GEIVQLSLPeLMQDMSNAIRYSTPCALLPDMQ----------AYLLFTSGSTGEPKGVCVVHRGLLNL 668
Cdd:cd05932 87 LDDWkamapgvpEGLISISLP-PPSAANCQYQWDDLIAQHPPLEerptrfpeqlATLIYTSGTTGQPKGVMLTFGSFAWA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 669 LLDMQRTFAVGSQDRLLSVT--TPTFDISFLEyLLPLISGASLYLTEAeraADSFrmiplIAD---YRPTLMQATPSFW- 742
Cdd:cd05932 166 AQAGIEHIGTEENDRMLSYLplAHVTERVFVE-GGSLYGGVLVAFAES---LDTF-----VEDvqrARPTLFFSVPRLWt 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 743 ---HGL-------------------------LMAGWRGDPelCVLAGGEALPtkVAEELL---RCCG-SLWNLYGPTETT 790
Cdd:cd05932 237 kfqQGVqdkipqqklnlllkipvvnslvkrkVLKGLGLDQ--CRLAGCGSAP--VPPALLewyRSLGlNILEAYGMTENF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 791 IWSlksqitqaeniTLGAPIANTRIYIldneGHPVP-----QGVDGELYIAGDGVAQGYDGQPELNAQFFlSEPGvpggr 865
Cdd:cd05932 313 AYS-----------HLNYPGRDKIGTV----GNAGPgvevrISEDGEILVRSPALMMGYYKDPEATAEAF-TADG----- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 866 MFRTGDLVRSDAQGQLFFVGRKDSQIKL-RGYRIELGEIERTLARHPHVDAavvACIERAPLHKALAAFIITSEP-PSLF 943
Cdd:cd05932 372 FLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEM---VCVIGSGLPAPLALVVLSEEArLRAD 448
|
490
....*....|.
gi 1288439980 944 EQLKNELRQQL 954
Cdd:cd05932 449 AFARAELEASL 459
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
524-968 |
8.00e-17 |
|
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: 85.10 E-value: 8.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 524 DGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGAcyvpfdihqPAArlqrlmqrarlvCLV 603
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGA---------VAA------------LIN 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 604 VRQPGEwgeivqlslpelmqDMSNAIRYSTPCALLPDmQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDR 683
Cdd:cd05940 60 YNLRGE--------------SLAHCLNVSSAKHLVVD-AALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 684 LLSvTTPTFDISFLEYLLP--LISGASLYLTEAERAADSFRMIpliADYRPTLMQatpsfwhgllmagWRGdpELC-VLA 760
Cdd:cd05940 125 LYT-CLPLYHSTALIVGWSacLASGATLVIRKKFSASNFWDDI---RKYQATIFQ-------------YIG--ELCrYLL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 761 GGEALPTKVAEELLRCCG-----SLWN-------------LYGPTETTI--WSLKSQI-TQAENITLGAPIANTRIYILD 819
Cdd:cd05940 186 NQPPKPTERKHKVRMIFGnglrpDIWEefkerfgvpriaeFYAATEGNSgfINFFGKPgAIGRNPSLLRKVAPLALVKYD 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 820 NE-GHP----------VPQGVDGEL--YIAGDGVAQGYDGQPELNAQFfLSEPGVPGGRMFRTGDLVRSDAQGQLFFVGR 886
Cdd:cd05940 266 LEsGEPirdaegrcikVPRGEPGLLisRINPLEPFDGYTDPAATEKKI-LRDVFKKGDAWFNTGDLMRLDGEGFWYFVDR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 887 KDSQIKLRGYRIELGEIERTLARHPHVDAAVV--ACIERAPLHKALAAFIITSEPPSLFEQLKNELRQQLPDYMVPtLWQ 964
Cdd:cd05940 345 LGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPGTDGRAGMAAIVLQPNEEFDLSALAAHLEKNLPGYARP-LFL 423
|
....
gi 1288439980 965 RVAD 968
Cdd:cd05940 424 RLQP 427
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
500-983 |
8.22e-17 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 85.83 E-value: 8.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 500 PQDVL-RIIEQrCVQHPKQLAIQQHDGT--LTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGA 576
Cdd:PRK05857 13 PSTVLdRVFEQ-ARQQPEAIALRRCDGTsaLRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 577 CYVPFDIHQPAARLQRLMQRARLVCLVvrqPGEWGEIVQLSLPELMQDMSnAIRYSTPC--------------ALLPDMQ 642
Cdd:PRK05857 92 IAVMADGNLPIAAIERFCQITDPAAAL---VAPGSKMASSAVPEALHSIP-VIAVDIAAvtresehsldaaslAGNADQG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 643 A----YLLFTSGSTGEPKGVCVVHRGLLnLLLDMQRTFAVGSQDRLLSVTT----PTFDISFLEYLLPLISGASLYLTEA 714
Cdd:PRK05857 168 SedplAMIFTSGTTGEPKAVLLANRTFF-AVPDILQKEGLNWVTWVVGETTysplPATHIGGLWWILTCLMHGGLCVTGG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 715 ERAAdSFRMIpLIAD------YRPTLMQATPSfwhgLLMAGWRGDPELCVLAGGEALPTKVAEELLRCCG-SLWNLYGPT 787
Cdd:PRK05857 247 ENTT-SLLEI-LTTNavattcLVPTLLSKLVS----ELKSANATVPSLRLVGYGGSRAIAADVRFIEATGvRTAQVYGLS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 788 ETTIWSL-----KSQITQAENITLGAPIANTRIYILD-NEGHP-VPQGVD----GELYIAGDGVAQGYDGQPElNAQFFL 856
Cdd:PRK05857 321 ETGCTALclptdDGSIVKIEAGAVGRPYPGVDVYLAAtDGIGPtAPGAGPsasfGTLWIKSPANMLGYWNNPE-RTAEVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 857 SEPGVpggrmfRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAvvACIERAPLH----KALAA 932
Cdd:PRK05857 400 IDGWV------NTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREA--ACYEIPDEEfgalVGLAV 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1288439980 933 FIITSEPPSLFEQLKNEL----RQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLA 983
Cdd:PRK05857 472 VASAELDESAARALKHTIaarfRRESEPMARPSTIVIVTDIPRTQSGKVMRASLA 526
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
528-919 |
8.80e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 85.82 E-value: 8.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 528 TYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPfdIHQPAAR----------LQRL-MQR 596
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTM--LHQPTPRtdlavwaedtLRVIgMIG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 597 ARLVCLvvrqpgewGEIVQLSLPELMQDmsnAIRYSTPCALL-----------PDMQAYLLFTSGSTGEPKGVCVVHRGL 665
Cdd:PRK07768 109 AKAVVV--------GEPFLAAAPVLEEK---GIRVLTVADLLaadpidpvetgEDDLALMQLTSGSTGSPKAVQITHGNL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 666 L-NLLLDMQRTFAVGSQDRLLSvTTPTF-DISFLEYL-LPLISGASL-YLTEAERAADSFRMIPLIADYRPTlMQATPSF 741
Cdd:PRK07768 178 YaNAEAMFVAAEFDVETDVMVS-WLPLFhDMGMVGFLtVPMYFGAELvKVTPMDFLRDPLLWAELISKYRGT-MTAAPNF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 742 WHGLL---MAgwRGDPEL--------CVLAGGEALPTKVAEELLRCCG-------SLWNLYGPTETTIW----------- 792
Cdd:PRK07768 256 AYALLarrLR--RQAKPGafdlsslrFALNGAEPIDPADVEDLLDAGArfglrpeAILPAYGMAEATLAvsfspcgaglv 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 793 ------SLKSQITQAEN---------ITLGAPIANTRIYILDNEGHPVP-QGVdGELYIAGDGVAQGY---DGqpelnaq 853
Cdd:PRK07768 334 vdevdaDLLAALRRAVPatkgntrrlATLGPPLPGLEVRVVDEDGQVLPpRGV-GVIELRGESVTPGYltmDG------- 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1288439980 854 fflSEPGVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAA-VVA 919
Cdd:PRK07768 406 ---FIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGnAVA 469
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
640-916 |
2.29e-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: 341266 [Multi-domain] Cd Length: 359 Bit Score: 82.53 E-value: 2.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 640 DMQAYLlFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSvTTPTFDI--SFLEYLLPLISGASLYLTEAE-- 715
Cdd:cd05944 3 DVAAYF-HTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLC-GLPLFHVngSVVTLLTPLASGAHVVLAGPAgy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 716 RAADSFRMI-PLIADYRPTLMQATPSFWHGLLMAgwRGDPELCVL----AGGEALPTKVAEELLRCCG-SLWNLYGPTET 789
Cdd:cd05944 81 RNPGLFDNFwKLVERYRITSLSTVPTVYAALLQV--PVNADISSLrfamSGAAPLPVELRARFEDATGlPVVEGYGLTEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 790 TiwSLKSQITQAENITLGA-----PIANTRIYILDNEGHPV-PQGVD--GELYIAGDGVAQGYDgQPELNAQFFLsepgv 861
Cdd:cd05944 159 T--CLVAVNPPDGPKRPGSvglrlPYARVRIKVLDGVGRLLrDCAPDevGEICVAGPGVFGGYL-YTEGNKNAFV----- 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1288439980 862 pGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAA 916
Cdd:cd05944 231 -ADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFA 284
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
526-985 |
2.67e-16 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 84.42 E-value: 2.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 526 TLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGAcyvpfdIH-------QPAARLQRLMQ-RA 597
Cdd:PRK00174 98 KITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGA------VHsvvfggfSAEALADRIIDaGA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 598 RLV-------------------------------CLVVRQPGE---WGEIVQLSLPELMQDMSnairysTPCALLPdMQA 643
Cdd:PRK00174 172 KLVitadegvrggkpiplkanvdealancpsvekVIVVRRTGGdvdWVEGRDLWWHELVAGAS------DECEPEP-MDA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 644 ----YLLFTSGSTGEPKGVcvVHR--G-LLNLLLDMQRTFAVGSQDrllsVTTPTFDI------SFLEYLlPLISGASLY 710
Cdd:PRK00174 245 edplFILYTSGSTGKPKGV--LHTtgGyLVYAAMTMKYVFDYKDGD----VYWCTADVgwvtghSYIVYG-PLANGATTL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 711 LTE-AERAADSFRMIPLIADYR-------PTLMQAtpsfwhglLMAGwrgdpelcvlagGEALPTKVAEELLRCCGSL-- 780
Cdd:PRK00174 318 MFEgVPNYPDPGRFWEVIDKHKvtifytaPTAIRA--------LMKE------------GDEHPKKYDLSSLRLLGSVge 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 781 ------WNLY----G----PTETTIWslksqitQAEN----IT-L-GA----PIANTRIY------ILDNEGHPVPQGVD 830
Cdd:PRK00174 378 pinpeaWEWYykvvGgercPIVDTWW-------QTETggimITpLpGAtplkPGSATRPLpgiqpaVVDEEGNPLEGGEG 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 831 GELYIAGD--GVAQGYDGQPELNAQ-FFLSEPGvpggrMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTL 907
Cdd:PRK00174 451 GNLVIKDPwpGMMRTIYGDHERFVKtYFSTFKG-----MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESAL 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 908 ARHPHV-DAAVVAcierAPlH----KALAAFII--TSEPPSlfEQLKNELRQQL---------PD--YMVPTLwqrvadf 969
Cdd:PRK00174 526 VAHPKVaEAAVVG----RP-DdikgQGIYAFVTlkGGEEPS--DELRKELRNWVrkeigpiakPDviQFAPGL------- 591
|
570
....*....|....*....
gi 1288439980 970 PNTDNGKIDR---KRLAEN 985
Cdd:PRK00174 592 PKTRSGKIMRrilRKIAEG 610
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
515-978 |
2.80e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 84.17 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 515 PKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGAcyVPFDI--HQPAARLQR 592
Cdd:PRK07798 17 PDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARA--VPVNVnyRYVEDELRY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 593 LMQRARLVCLVVRQpgEWGEIVQLSLPEL--------MQDMS------NAIRY-------STPCALLP----DMqaYLLF 647
Cdd:PRK07798 95 LLDDSDAVALVYER--EFAPRVAEVLPRLpklrtlvvVEDGSgndllpGAVDYedalaagSPERDFGErspdDL--YLLY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 648 TSGSTGEPKGVCVVH----RGLLNllldmQRTFAVG---------SQDRLLSVTTPTFDISfleyllPLISGASLY---- 710
Cdd:PRK07798 171 TGGTTGMPKGVMWRQedifRVLLG-----GRDFATGepiedeeelAKRAAAGPGMRRFPAP------PLMHGAGQWaafa 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 711 --------LTEAERAADSFRMIPLIADYRPTLMQATpsfwhGLLMAG-------WRGDPELCVLA----GGEALPTKVAE 771
Cdd:PRK07798 240 alfsgqtvVLLPDVRFDADEVWRTIEREKVNVITIV-----GDAMARplldaleARGPYDLSSLFaiasGGALFSPSVKE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 772 ELLRccgSLWNL-----YGPTETTIWSlkSQITQAENITLGAPI--ANTRIYILDNEGHPVPQGVDGELYIAGDG-VAQG 843
Cdd:PRK07798 315 ALLE---LLPNVvltdsIGSSETGFGG--SGTVAKGAVHTGGPRftIGPRTVVLDEDGNPVEPGSGEIGWIARRGhIPLG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 844 YDGQPELNAQFFlsePGVPGGRMFRTGDLVRSDAQGQLFFVGRkDSQ-IKLRGYRIELGEIERTLARHPHVDAAVVACI- 921
Cdd:PRK07798 390 YYKDPEKTAETF---PTIDGVRYAIPGDRARVEADGTITLLGR-GSVcINTGGEKVFPEEVEEALKAHPDVADALVVGVp 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 922 -ERapLHKALAAFIITSEPPSL-FEQLKNELRQQLPDYMVP-TLWqRVADFPNTDNGKID 978
Cdd:PRK07798 466 dER--WGQEVVAVVQLREGARPdLAELRAHCRSSLAGYKVPrAIW-FVDEVQRSPAGKAD 522
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
627-984 |
2.92e-16 |
|
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: 84.12 E-value: 2.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 627 NAIRYSTPCALLPDMQAYLLFTSGSTGEPKGVCVVHRGLLnLLLDMQRTFAVGSQ----DRLLSVTTPTFDISFLEYLLP 702
Cdd:cd17642 171 NEYDFKPPSFDRDEQVALIMNSSGSTGLPKGVQLTHKNIV-ARFSHARDPIFGNQiipdTAILTVIPFHHGFGMFTTLGY 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 703 LISGASL-YLTEAERAAdsfrMIPLIADYR-------PTLMqatpSFWHGLLMAGWRGDPELCVLAGGEALPTKVAEELL 774
Cdd:cd17642 250 LICGFRVvLMYKFEEEL----FLRSLQDYKvqsallvPTLF----AFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAV 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 775 RccgSLWNL------YGPTETTIWSLksqITQAENITLGA-----PIANTRIYILDNeGHPVPQGVDGELYIAGDGVAQG 843
Cdd:cd17642 322 A---KRFKLpgirqgYGLTETTSAIL---ITPEGDDKPGAvgkvvPFFYAKVVDLDT-GKTLGPNERGELCVKGPMIMKG 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 844 YDGQPElNAQFFLSEPGvpggrMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIER 923
Cdd:cd17642 395 YVNNPE-ATKALIDKDG-----WLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPD 468
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1288439980 924 APLHKALAAFIITSEPPSLFEQlknELRQQLPDYMVPTLWQR-----VADFPNTDNGKIDRKRLAE 984
Cdd:cd17642 469 EDAGELPAAVVVLEAGKTMTEK---EVMDYVASQVSTAKRLRggvkfVDEVPKGLTGKIDRRKIRE 531
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
527-988 |
3.57e-16 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 83.59 E-value: 3.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 527 LTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLMQ--RARLV---- 600
Cdd:PRK12406 12 RSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEdsGARVLiaha 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 601 ---------------CLVVRQPGEwgeIVQ--------LSLPELMQDMSNAIRYSTPCALLPDMQ-AYLLFTSGSTGEPK 656
Cdd:PRK12406 92 dllhglasalpagvtVLSVPTPPE---IAAayrispalLTPPAGAIDWEGWLAQQEPYDGPPVPQpQSMIYTSGTTGHPK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 657 GVcvvhrgllnllldmQRTFAVGSQdrllsvTTPTFDISFLEYLLP-----LISGAsLYLT-------EAERAADSFRMI 724
Cdd:PRK12406 169 GV--------------RRAAPTPEQ------AAAAEQMRALIYGLKpgiraLLTGP-LYHSapnayglRAGRLGGVLVLQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 725 P---------LIADYRPTLMQATPSFWHGL--LMAGWRGDPELC----VLAGGEALPTKVAEELLRCCGSLWN-LYGPTE 788
Cdd:PRK12406 228 PrfdpeellqLIERHRITHMHMVPTMFIRLlkLPEEVRAKYDVSslrhVIHAAAPCPADVKRAMIEWWGPVIYeYYGSTE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 789 TTIWSL-KSQITQAENITLGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQ-GYDGQPELNAQfflsepgVPGGRM 866
Cdd:PRK12406 308 SGAVTFaTSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAE-------IDRGGF 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 867 FRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIitsEP-----PS 941
Cdd:PRK12406 381 ITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVV---EPqpgatLD 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1288439980 942 LfEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAENFVA 988
Cdd:PRK12406 458 E-ADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPYWA 503
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
55-318 |
4.24e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 84.83 E-value: 4.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 55 WFLQKYDSTATNYNLYVVYRLHGVVDMPMLTEALRHVQARHAILRTRIIVRNDR-PCQVIDDASSLVLDTVTLAAQAPTS 133
Cdd:PRK05691 2800 WFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGRwQAEYRAVTAQELLWQVTVADFAECA 2879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 134 ALDAVIQQVIntrfDLARGPLWGVTQIIQPDQGCHLVFCAHHIIIDGISLRLLFDELQQQYARLHAGNETSLPPPPLQYA 213
Cdd:PRK05691 2880 ALFADAQRSL----DLQQGPLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAGAEPALPAKTSAFR 2955
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 214 DYAFWQREWFQDTLLANELAYWRARLQDAPllSTFPSLHPRPAQPSTHGSRFSITLDETLSLALKHVA----RTQETTpf 289
Cdd:PRK05691 2956 DWAARLQAYAGSESLREELGWWQAQLGGPR--AELPCDRPQGGNLNRHAQTVSVRLDAERTRQLLQQApaayRTQVND-- 3031
|
250 260
....*....|....*....|....*....
gi 1288439980 290 vLMLTAFQLVLMRYAQQQRLVIGMPVSGR 318
Cdd:PRK05691 3032 -LLLTALARVLCRWSGQPSVLVQLEGHGR 3059
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1126-1595 |
4.48e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 84.83 E-value: 4.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1126 DVEHFNVTRFTHAVNALIARHEMLRARVLPDGTQQILAQV-------PAYQLEQRDLSALSpnARNDALmAIRDRLSHHV 1198
Cdd:PRK12467 2676 DVEGLDVERFRTAWQAVIDRHEILRSGFLWDGELEEPLQVvykqarlPFSRLDWRDRADLE--QALDAL-AAADRQQGFD 2752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1199 hpADRWPLFDFSYSACTAQHGRLHFSLDLLIADALSMRTLQQELMMLYR-EPhvsLPLLPFSFRDYVQALlveQASEAyA 1277
Cdd:PRK12467 2753 --LLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRYFgQP---PPAREGRYRDYIAWL---QAQDA-E 2823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1278 RDQAYWQRALPQLyGPPTLpvqgdLAQLSAIRFVR-------RRHRLSAHNWGVLSALAQRTRITKTALLLTVFSQVLAR 1350
Cdd:PRK12467 2824 ASEAFWKEQLAAL-EEPTR-----LARALYPAPAEavaghgaHYLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQR 2897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1351 WSLSPTFTLNLTLFNRPQGYPNAEAVIGDFTAVSLLNVCYDSQHSYAHNAQRIQVQLWE--DLEH------RRFSGiRAS 1422
Cdd:PRK12467 2898 FTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPRAEQTVSDWLQQVQAQNLAlrEFEHtpladiQRWAG-QGG 2976
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1423 EALIHSGRFHAPMPVvftsmldidGETTAQDPRDTTRFTLCPDANITQTPQVWLDHQVIELagELHFNWDavEQLFDTTL 1502
Cdd:PRK12467 2977 EALFDSILVFENYPI---------SEALKQGAPSGLRFGAVSSREQTNYPLTLAVGLGDTL--ELEFSYD--RQHFDAAA 3043
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1503 LDQMFGAYCHALQALVAMPQSWWGVNSSLAlPTVSAPVTQAPAPTA-------LLHHGLLRQAALTPQETALISPIRELT 1575
Cdd:PRK12467 3044 IERLAESFDRLLQAMLNNPAARLGELPTLA-AHERRQVLHAWNATAaaypserLVHQLIEAQVARTPEAPALVFGDQQLS 3122
|
490 500
....*....|....*....|
gi 1288439980 1576 YRQLSTAADHVARALLALGV 1595
Cdd:PRK12467 3123 YAELNRRANRLAHRLIAIGV 3142
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
86-318 |
6.11e-16 |
|
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: 82.10 E-value: 6.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 86 EALRHVQARHAILRTRIIVRN-DRPCQVIDDASSLVLDTVTLAAQAPtsALDAVIQQVI--NTRFDLARGPLWGVTQIIQ 162
Cdd:cd19544 43 AALQQVIDRHDILRTAILWEGlSEPVQVVWRQAELPVEELTLDPGDD--ALAQLRARFDprRYRLDLRQAPLLRAHVAED 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 163 PDQG-CHLVFCAHHIIIDGISLRLLFDELQQqyarLHAGNETSLpPPPLQYADYAFWQREwfQDTLLANElAYWRARLQD 241
Cdd:cd19544 121 PANGrWLLLLLFHHLISDHTSLELLLEEIQA----ILAGRAAAL-PPPVPYRNFVAQARL--GASQAEHE-AFFREMLGD 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 242 -----AP--LLSTfpslhprpaqpSTHGSRF---SITLDETLSLALKHVARTQETTPFVLMLTAFQLVLMRYAQQQRLVI 311
Cdd:cd19544 193 vdeptAPfgLLDV-----------QGDGSDIteaRLALDAELAQRLRAQARRLGVSPASLFHLAWALVLARCSGRDDVVF 261
|
....*..
gi 1288439980 312 GMPVSGR 318
Cdd:cd19544 262 GTVLSGR 268
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
1097-1519 |
1.66e-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: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1097 FPLTDVQRAYWLGRQTGATSIATHIYHEFDvEHFNVTRFTHAVNALIARHEMLRARVLPDGTQQILAQVPayqleqrdLS 1176
Cdd:cd19542 2 YPCTPMQEGMLLSQLRSPGLYFNHFVFDLD-SSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTFLQVV--------LK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1177 ALSPNAR-----NDALMAI-RDRLSHHVHPADrwPLFDFSYSACTAQHGRLHFSLDLLIADALSMRTLQQELMMLYReph 1250
Cdd:cd19542 73 SLDPPIEevetdEDSLDALtRDLLDDPTLFGQ--PPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYN--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1251 vSLPLLPF-SFRDYVQALLVEQASEAYardqAYWQRALpQLYGPPTLPVqgdlaqLSAIRFVRRRHRLSAHNWGVLSALA 1329
Cdd:cd19542 148 -GQLLPPApPFSDYISYLQSQSQEESL----QYWRKYL-QGASPCAFPS------LSPKRPAERSLSSTRRSLAKLEAFC 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1330 QRTRITKTALLLTVFSQVLARWSLSPTFTLNLTLFNRPQGYPNAEAVIGDFTAVSLLNVCYDSQHSYAHNAQRIQVQLWE 1409
Cdd:cd19542 216 ASLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1410 DLEHRRFSgirASEALIHSGRfhAPMPVVFTSMLDI--DGETTAQDPRDTTRFTLCPDANITQTPqVWLDhqVIELAGEL 1487
Cdd:cd19542 296 SLPHQHLS---LREIQRALGL--WPSGTLFNTLVSYqnFEASPESELSGSSVFELSAAEDPTEYP-VAVE--VEPSGDSL 367
|
410 420 430
....*....|....*....|....*....|..
gi 1288439980 1488 HFNWDAVEQLFDTTLLDQMFGAYCHALQALVA 1519
Cdd:cd19542 368 KVSLAYSTSVLSEEQAEELLEQFDDILEALLA 399
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
1131-1352 |
1.66e-15 |
|
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: 80.86 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1131 NVTRFTHAVNALIARHEMLRAR-VLPDGT--QQILAQVPAyQLEQRDLSALSPNARNDALMAIRDRLSHhvHPAD--RWP 1205
Cdd:cd19531 37 DVAALERALNELVARHEALRTTfVEVDGEpvQVILPPLPL-PLPVVDLSGLPEAEREAEAQRLAREEAR--RPFDlaRGP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1206 LFDFSYSACTAQHGRLHFSLDLLIADALSMRTLQQELMMLYR----EPHVSLPLLPFSFRDYV---QALLveqASEAYAR 1278
Cdd:cd19531 114 LLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAaflaGRPSPLPPLPIQYADYAvwqREWL---QGEVLER 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1279 DQAYWQRalpQLYGPPTL----------PVQ---GDlaqlsairfvRRRHRLSAHNWGVLSALAQRTRITKTALLLTVFS 1345
Cdd:cd19531 191 QLAYWRE---QLAGAPPVlelptdrprpAVQsfrGA----------RVRFTLPAELTAALRALARREGATLFMTLLAAFQ 257
|
....*..
gi 1288439980 1346 QVLARWS 1352
Cdd:cd19531 258 VLLHRYS 264
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
526-940 |
1.91e-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: 81.11 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 526 TLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWfvgacyvpfdihqpaarlqrlMQRARLVClVVR 605
Cdd:cd17639 5 YMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCW---------------------SQNIPIVT-VYA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 606 QPGEWGEIVQLSLPElmqdmSNAIrYSTPCallPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQR--TFAVGSQDR 683
Cdd:cd17639 63 TLGEDALIHSLNETE-----CSAI-FTDGK---PDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDrvPELLGPDDR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 684 LLS------VTTPTFDISFLEYLLPLISGASLYLTEAERA---ADsfrmiplIADYRPTLMQATPS-------------- 740
Cdd:cd17639 134 YLAylplahIFELAAENVCLYRGGTIGYGSPRTLTDKSKRgckGD-------LTEFKPTLMVGVPAiwdtirkgvlakln 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 741 ---------FWHG--LLMAGWRGDPELCV--------------------LAGGEALPTKVAEELLRCCGSLWNLYGPTET 789
Cdd:cd17639 207 pmgglkrtlFWTAyqSKLKALKEGPGTPLldelvfkkvraalggrlrymLSGGAPLSADTQEFLNIVLCPVIQGYGLTET 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 790 TIWSLKSQITQAENITLGAPIANTRIYILDNE--GH----PVPQGvdgELYIAGDGVAQGYDGQPELNAQFFLsepgvpG 863
Cdd:cd17639 287 CAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEegGYstdkPPPRG---EILIRGPNVFKGYYKNPEKTKEAFD------G 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1288439980 864 GRMFRTGDLVRSDAQGQLFFVGRKDSQIKLR-GYRIELGEIERTLARHPHVDAavvACIERAPLHKALAAFIITSEPP 940
Cdd:cd17639 358 DGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNN---ICVYADPDKSYPVAIVVPNEKH 432
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
505-960 |
2.98e-15 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 81.07 E-value: 2.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 505 RIIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIH 584
Cdd:PRK08279 41 DVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 585 QPAARLQRLMQRARLVCLVV----------------RQPGEWGE-IVQLSLPELMQDMSNAIRYSTP------CALLPDM 641
Cdd:PRK08279 121 QRGAVLAHSLNLVDAKHLIVgeelveafeearadlaRPPRLWVAgGDTLDDPEGYEDLAAAAAGAPTtnpasrSGVTAKD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 642 QAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSVttptfdisfleylLPL--------------ISGA 707
Cdd:PRK08279 201 TAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCC-------------LPLyhntggtvawssvlAAGA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 708 SLYLteaeraADSF---RMIPLIADYRPTLMQATpsfwhGllmagwrgdpELC-VLAGGEALPTKVAEELLRCCG----- 778
Cdd:PRK08279 268 TLAL------RRKFsasRFWDDVRRYRATAFQYI-----G----------ELCrYLLNQPPKPTDRDHRLRLMIGnglrp 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 779 SLWN-------------LYGPTETTIwSLksqiTQAENI---------TLGAPIA------NTRIYILDNEGH--PVPQG 828
Cdd:PRK08279 327 DIWDefqqrfgiprileFYAASEGNV-GF----INVFNFdgtvgrvplWLAHPYAivkydvDTGEPVRDADGRciKVKPG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 829 VDGELyIAGDGVAQGYDG--QPELNAQFFLSEPGVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERT 906
Cdd:PRK08279 402 EVGLL-IGRITDRGPFDGytDPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1288439980 907 LARHPHVDAAVVACIErAPLH--KALAAFIITSEPPSL-FEQLKNELRQQLPDYMVP 960
Cdd:PRK08279 481 LSGFPGVEEAVVYGVE-VPGTdgRAGMAAIVLADGAEFdLAALAAHLYERLPAYAVP 536
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
526-991 |
3.35e-15 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 80.66 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 526 TLTYAELWARVQFIAMRFRAH-GIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDihqPAARLQRLMQRAR--LVCL 602
Cdd:PLN02574 66 SISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMN---PSSSLGEIKKRVVdcSVGL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 603 VVRQPGEWGEIVQL-----SLPELMQDMSNAIRYSTPCALL-------------PDMQAYLLFTSGSTGEPKGVCVVHRG 664
Cdd:PLN02574 143 AFTSPENVEKLSPLgvpviGVPENYDFDSKRIEFPKFYELIkedfdfvpkpvikQDDVAAIMYSSGTTGASKGVVLTHRN 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 665 LLNLLLDMQR----TFAVGSQDRLLSVTTPTFDISFLE-YLLPLIS-GASLYLTeaeRAADSFRMIPLIADYRPTLMQAT 738
Cdd:PLN02574 223 LIAMVELFVRfeasQYEYPGSDNVYLAALPMFHIYGLSlFVVGLLSlGSTIVVM---RRFDASDMVKVIDRFKVTHFPVV 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 739 PSFWHGLLMA--GWRGDPELC---VLAGGEALPTKVAEELLRCCG--SLWNLYGPTETTIWSLK----SQITQAENITLG 807
Cdd:PLN02574 300 PPILMALTKKakGVCGEVLKSlkqVSCGAAPLSGKFIQDFVQTLPhvDFIQGYGMTESTAVGTRgfntEKLSKYSSVGLL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 808 APiaNTRIYILDNE-GHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEPgvpggrMFRTGDLVRSDAQGQLFFVGR 886
Cdd:PLN02574 380 AP--NMQAKVVDWStGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDG------WLRTGDIAYFDEDGYLYIVDR 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 887 KDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEPPSLF-EQLKNELRQQLPDYMVPTLWQR 965
Cdd:PLN02574 452 LKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSqEAVINYVAKQVAPYKKVRKVVF 531
|
490 500
....*....|....*....|....*.
gi 1288439980 966 VADFPNTDNGKIDRKRLAENFVADSS 991
Cdd:PLN02574 532 VQSIPKSPAGKILRRELKRSLTNSVS 557
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
500-1080 |
4.38e-15 |
|
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: 80.90 E-value: 4.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 500 PQDVLRIIEQRCVQHPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYV 579
Cdd:COG3319 4 AAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 580 PFDIHQPAARLQRLMQRARLVCLVVRQPGEW-GEIVQLSLPELMQDMSNAIRYSTPCALLPDMQAYLLFTSGSTGEPKGV 658
Cdd:COG3319 84 LALALAAAAAALLLAALALLLALLAALALALlALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAGV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 659 CVVHRGLLNLLLDMQRTFAVGSQDRLLSVTTPTFDISFLEYLLPLISGASLYLTEAERAADSFRMIPLIADYRPTLMQAT 738
Cdd:COG3319 164 LVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 739 PSFWHGLLMAGWRGDPELCVLAGGEALPTKVAEELLRCCGSLWNLYG-------PTETTIWSLKSQITQAENITLGAPIA 811
Cdd:COG3319 244 LAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAaggtattAAVTTTAAAAAPGVAGALGPIGGGPG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 812 NTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFFLSEP--GVPGGRMFRTGDLVRSDAQGQLFFVGRKDS 889
Cdd:COG3319 324 LLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPagAGARGRLRRGGDRGRRLGGGLLLGLGRLRL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 890 QIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEPPSLFEQLKNELRQQLPDYMVPTLWQRVADF 969
Cdd:COG3319 404 QRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLLLLL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 970 PNTDNGKIDRKRLAEnfvADSSLVSPQTQALSDTEQMLLALWMRYLPIKNVDPECDFFRLGGHSLLAVTLVAEINRTFHC 1049
Cdd:COG3319 484 LLLLLAALLLAAAAP---AAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLR 560
|
570 580 590
....*....|....*....|....*....|.
gi 1288439980 1050 ALTLKDIFHYSTLRALSARIAQQSITDAAAS 1080
Cdd:COG3319 561 LLLLLALLLAPTLAALAAALAAAAAAAALSP 591
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
538-984 |
5.15e-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: 79.73 E-value: 5.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 538 FIAMRFRAH---GIQPGDRIGVLLPRHrdvIATMLATWFVGACYVPfdihqPAARLQRLMQRARLVCLVVRQPGEwgeiv 614
Cdd:cd05929 26 ALNRNARAAaaeGVWIADGVYIYLINS---ILTVFAAAAAWKCGAC-----PAYKSSRAPRAEACAIIEIKAAAL----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 615 qLSLPELMQDMSNAIR-YSTPCALLPDMQA-------YLLFTSGSTGEPKGVCVVHRGLLN---LLLDMQRTFAVGSQDR 683
Cdd:cd05929 93 -VCGLFTGGGALDGLEdYEAAEGGSPETPIedeaagwKMLYSGGTTGRPKGIKRGLPGGPPdndTLMAAALGFGPGADSV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 684 LLSV-----TTPtfdisFLEYLLPLISGASLYLTEAERAADSFRmipLIADYRPTLMQATPSFWHGLL-----------M 747
Cdd:cd05929 172 YLSPaplyhAAP-----FRWSMTALFMGGTLVLMEKFDPEEFLR---LIERYRVTFAQFVPTMFVRLLklpeavrnaydL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 748 AGWRGdpelcVLAGGEALPTKVAEELLRCCGS-LWNLYGPTE---TTIwslksqITQAENIT----LGAPIANtRIYILD 819
Cdd:cd05929 244 SSLKR-----VIHAAAPCPPWVKEQWIDWGGPiIWEYYGGTEgqgLTI------INGEEWLThpgsVGRAVLG-KVHILD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 820 NEGHPVPQGVDGELYIA-GDGVAQGYDgqPELnaqfflSEPGVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRI 898
Cdd:cd05929 312 EDGNEVPPGEIGEVYFAnGPGFEYTND--PEK------TAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 899 ELGEIERTLARHPHV-DAAVVAcIERAPLHKALAAFIIT----SEPPSLFEQLKNELRQQLPDYMVPTLWQRVADFPNTD 973
Cdd:cd05929 384 YPQEIENALIAHPKVlDAAVVG-VPDEELGQRVHAVVQPapgaDAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDD 462
|
490
....*....|.
gi 1288439980 974 NGKIDRKRLAE 984
Cdd:cd05929 463 TGKLYRRLLRD 473
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
514-982 |
7.57e-15 |
|
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: 79.27 E-value: 7.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 514 HPKQLAIQQHDGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRhrdvIATMLATWF----VGACYVPFDIHQPAAR 589
Cdd:cd12118 17 YPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPN----TPAMYELHFgvpmAGAVLNALNTRLDAEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 590 LQRLMQRARLVCLVVRQPGEWGEIVQLS----LPELMQDMSNAIRystpcallpdmqayLLFTSGSTGEPKGVCVVHRGL 665
Cdd:cd12118 93 IAFILRHSEAKVLFVDREFEYEDLLAEGdpdfEWIPPADEWDPIA--------------LNYTSGTTGRPKGVVYHHRGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 666 LNLLLDMQRTFAVGSQDRLLSvTTPTFDIS---FLeYLLPLISGASLYLTEAErAADSFRmipLIADYRPTLMQATPSFW 742
Cdd:cd12118 159 YLNALANILEWEMKQHPVYLW-TLPMFHCNgwcFP-WTVAAVGGTNVCLRKVD-AKAIYD---LIEKHKVTHFCGAPTVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 743 HGLL--MAGWRG--DPELCVLAGGEALPTKVAEELLRCCGSLWNLYGPTETT------IWSLKS-QITQAENITLGAP-- 809
Cdd:cd12118 233 NMLAnaPPSDARplPHRVHVMTAGAPPPAAVLAKMEELGFDVTHVYGLTETYgpatvcAWKPEWdELPTEERARLKARqg 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 810 ---IANTRIYILDNEGH-PVPQ-GVD-GELYIAGDGVAQGYDGQPELNAQFFlsepgvPGGrMFRTGDLVRSDAQGQLFF 883
Cdd:cd12118 313 vryVGLEEVDVLDPETMkPVPRdGKTiGEIVFRGNIVMKGYLKNPEATAEAF------RGG-WFHSGDLAVIHPDGYIEI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 884 VGRKDSQIKLRGYRIELGEIERTLARHPHV-DAAVVA-CIERapLHKALAAFIITSEPPSL-FEQLKNELRQQLPDYMVP 960
Cdd:cd12118 386 KDRSKDIIISGGENISSVEVEGVLYKHPAVlEAAVVArPDEK--WGEVPCAFVELKEGAKVtEEEIIAFCREHLAGFMVP 463
|
490 500
....*....|....*....|..
gi 1288439980 961 TLWQrVADFPNTDNGKIDRKRL 982
Cdd:cd12118 464 KTVV-FGELPKTSTGKIQKFVL 484
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1090-1595 |
1.09e-14 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 80.09 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1090 PEHRHQPFPLTDVQRAYWLGRQ--TGATSIATHIYHEFDVEhFNVTRFTHAVNALIARHEMLRARVLPDG---TQQILAQ 1164
Cdd:PRK10252 1 AEPMSQHLPLVAAQPGIWMAEKlsPLPSAWSVAHYVELTGE-LDAPLLARAVVAGLAEADTLRMRFTEDNgevWQWVDPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1165 VPAYQLEQRDLSAlSPNARNDALMAIRDRLSHHVHPADRWPLFDFSYSACTAQHGRLHFSLDLLIADALSMRTLQQELMM 1244
Cdd:PRK10252 80 LTFPLPEIIDLRT-QPDPHAAAQALMQADLQQDLRVDSGKPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1245 LYR-----EPHVSLPLLPFSfrDYVQALLVEQASEAYARDQAYWQRALPQLYGPPTLPVQGDLAQLSAIRFVRRRHRLSA 1319
Cdd:PRK10252 159 IYCawlrgEPTPASPFTPFA--DVVEEYQRYRASEAWQRDAAFWAEQRRQLPPPASLSPAPLPGRSASADILRLKLEFTD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1320 hnwGVLSAL-AQRTRITKTALLLTVFSQVLARWSLSPTFTLNLtLFNRPQGYPnAEAVIGDFTAVSLLNVCYDSQHSYAH 1398
Cdd:PRK10252 237 ---GAFRQLaAQASGVQRPDLALALVALWLGRLCGRMDYAAGF-IFMRRLGSA-ALTATGPVLNVLPLRVHIAAQETLPE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1399 NAQRIQVQLWEDLEHRRFsgiRASEALIHSGRFHAPMPV--------VFTSMLDIDG-----ETTAQDPRDTTRFTLCPD 1465
Cdd:PRK10252 312 LATRLAAQLKKMRRHQRY---DAEQIVRDSGRAAGDEPLfgpvlnikVFDYQLDFPGvqaqtHTLATGPVNDLELALFPD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1466 anitqtpqvwldhqvieLAGELHFNWDAVEQLFDTTLLDQMFGAYCHALQALVAMPQSWWGvNSSLALPTVSAPV----- 1540
Cdd:PRK10252 389 -----------------EHGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCG-DVDILLPGEYAQLaqvna 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1288439980 1541 TQAPAPTALLHHGLLRQAALTPQETALISPIRELTYRQLSTAADHVARALLALGV 1595
Cdd:PRK10252 451 TAVEIPETTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGV 505
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
499-984 |
1.55e-14 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 78.70 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 499 GPQDVLRI-------IEQRCVQHPKQLAIQQHDGTL--TYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATML 569
Cdd:PRK08315 7 GPTDVPLLeqtigqlLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 570 ATWFVGACYVPFDihqPAARLQRL-----------------------------------------MQRARLVCL--VVR- 605
Cdd:PRK08315 87 ATAKIGAILVTIN---PAYRLSELeyalnqsgckaliaadgfkdsdyvamlyelapelatcepgqLQSARLPELrrVIFl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 606 ----QPG--EWGEIVQLS-------LPELMQDMSN--AIrystpcallpDMQayllFTSGSTGEPKGVCVVHRGLLNLLL 670
Cdd:PRK08315 164 gdekHPGmlNFDELLALGravddaeLAARQATLDPddPI----------NIQ----YTSGTTGFPKGATLTHRNILNNGY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 671 DMQRTFAVGSQDRL----------------LSVTT---------PTFDisfleyllPLisgASLYLTEAERAAdsfrmip 725
Cdd:PRK08315 230 FIGEAMKLTEEDRLcipvplyhcfgmvlgnLACVThgatmvypgEGFD--------PL---ATLAAVEEERCT------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 726 liADYR-PTL---MQATPSFWH--------GLlMAGwrgdpELCvlaggealPtkvaEELLRCCGSLWNL------YGPT 787
Cdd:PRK08315 292 --ALYGvPTMfiaELDHPDFARfdlsslrtGI-MAG-----SPC--------P----IEVMKRVIDKMHMsevtiaYGMT 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 788 ETTIWSLKSQITQAENI---TLGAPIANTRIYILDNE-GHPVPQGVDGELYIAGDGVAQGYDGQPELNAqfflsEPGVPG 863
Cdd:PRK08315 352 ETSPVSTQTRTDDPLEKrvtTVGRALPHLEVKIVDPEtGETVPRGEQGELCTRGYSVMKGYWNDPEKTA-----EAIDAD 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 864 GRMfRTGDLVRSDAQGQLFFVGR-KDSQIklRG----Y-RielgEIERTLARHPHV-DAAVVAcierAPLHK---ALAAF 933
Cdd:PRK08315 427 GWM-HTGDLAVMDEEGYVNIVGRiKDMII--RGgeniYpR----EIEEFLYTHPKIqDVQVVG----VPDEKygeEVCAW 495
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1288439980 934 IITSEPPSLFEQlknELRQ----QLPDYMVPTLWQRVADFPNTDNGKIDRKRLAE 984
Cdd:PRK08315 496 IILRPGATLTEE---DVRDfcrgKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMRE 547
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
1120-1521 |
1.68e-14 |
|
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: 77.49 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1120 HIYHEFDVEHF----NVTRFTHAVNALIARHEMLRARVLPDGTQQILAQV-PAYQLEQRDLSALSPNARNDALMAIRDRL 1194
Cdd:cd19536 22 SVYLHNYTYTVgrrlNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVhRQAQVPVTELDLTPLEEQLDPLRAYKEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1195 SHHVHPADRWPLFDFSYSACTAQ-HGRLHFSLDLLIADALSMRTLQQELMMLYREP--HVSLPLLPFS-FRDYVqALLVE 1270
Cdd:cd19536 102 KIRRFDLGRAPLVRAALVRKDEReRFLLVISDHHSILDGWSLYLLVKEILAVYNQLleYKPLSLPPAQpYRDFV-AHERA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1271 QASEAyaRDQAYWQRALPQLYGPPTLP----VQGDLAQLSAIRFVRRRHRLSAhnwgvlsALAQRTRITKTALLLTVFSQ 1346
Cdd:cd19536 181 SIQQA--ASERYWREYLAGATLATLPAlseaVGGGPEQDSELLVSVPLPVRSR-------SLAKRSGIPLSTLLLAAWAL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1347 VLARWSLSPTFTLNLTLFNRPQGYPNAEAVIGDFTAVSLLNVCYdSQHSYAHNAQRIQVQLWEDLEHRrfsgiRASEALI 1426
Cdd:cd19536 252 VLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTL-SEETVEDLLKRAQEQELESLSHE-----QVPLADI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1427 HSgrfHAPMPVVFTSML---DIDGETTAQDPRDTTRFTLCPDANITQTP-QVWLdhQVIELAGELHFNWDAVEQLFDTTL 1502
Cdd:cd19536 326 QR---CSEGEPLFDSIVnfrHFDLDFGLPEWGSDEGMRRGLLFSEFKSNyDVNL--SVLPKQDRLELKLAYNSQVLDEEQ 400
|
410
....*....|....*....
gi 1288439980 1503 LDQMFGAYCHALQALVAMP 1521
Cdd:cd19536 401 AQRLAAYYKSAIAELATAP 419
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
500-986 |
2.75e-14 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 77.90 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 500 PQDVLRIIEQRCVQHPKQLAIQQHDG---TLTYAELWARVQFIAMRFRAH-GIQPGDRIGVLLPRHRDVIATMLATWFVG 575
Cdd:PRK05620 9 PLSLTRILEYGSTVHGDTTVTTWGGAeqeQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 576 ACYVPFDIHQPAARLQRLMQRARLVCLVV--RQPGEWGEI---------VQLSLPELMQDMSNAIRYSTPC----ALL-- 638
Cdd:PRK05620 89 AVFNPLNKQLMNDQIVHIINHAEDEVIVAdpRLAEQLGEIlkecpcvraVVFIGPSDADSAAAHMPEGIKVysyeALLdg 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 639 -------PDMQ----AYLLFTSGSTGEPKGVCVVHRGLL--NLLLDMQRTFAVGSQDRLLsVTTPTFDIsfLEYLLPL-- 703
Cdd:PRK05620 169 rstvydwPELDettaAAICYSTGTTGAPKGVVYSHRSLYlqSLSLRTTDSLAVTHGESFL-CCVPIYHV--LSWGVPLaa 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 704 -ISGASLYLTEAERAADSFRMIplIADYRPTLMQATPSFWHGLLMAGWRGDPELCVL----AGGEALP---TKVAEEllR 775
Cdd:PRK05620 246 fMSGTPLVFPGPDLSAPTLAKI--IATAMPRVAHGVPTLWIQLMVHYLKNPPERMSLqeiyVGGSAVPpilIKAWEE--R 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 776 CCGSLWNLYGPTETtiwSLKSQITQAENITLGAPIANTRI----------YILDNEGHpVPQGVD---GELYIAGDGVAQ 842
Cdd:PRK05620 322 YGVDVVHVWGMTET---SPVGTVARPPSGVSGEARWAYRVsqgrfpasleYRIVNDGQ-VMESTDrneGEIQVRGNWVTA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 843 GYDGQPELN----AQFFLSEPGVPGGRMF------RTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPH 912
Cdd:PRK05620 398 SYYHSPTEEgggaASTFRGEDVEDANDRFtadgwlRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPE 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1288439980 913 V-DAAVVACIERAPLHKALAAFIITSE-PPS--LFEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAENF 986
Cdd:PRK05620 478 VvECAVIGYPDDKWGERPLAVTVLAPGiEPTreTAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHL 555
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
494-980 |
3.42e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 77.78 E-value: 3.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 494 NVPW-LGPQDVLRIIEQRCVQHPKQLAIQQHDGT------LTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIA 566
Cdd:PRK12582 41 RHPLgPYPRSIPHLLAKWAAEAPDRPWLAQREPGhgqwrkVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 567 TMLATWFVGACYVP------------------FDIHQPA-------ARLQRLMQRARLV---CLVVRQPGEwgEIVQLSL 618
Cdd:PRK12582 121 MTLAAMQAGVPAAPvspayslmshdhaklkhlFDLVKPRvvfaqsgAPFARALAALDLLdvtVVHVTGPGE--GIASIAF 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 619 PELMQDMSNAIRYSTPCALLPDMQAYLLFTSGSTGEPKGVCVVHRGLL-NLLLDMQ-RTFAvgsqdrllsvttPTFDISF 696
Cdd:PRK12582 199 ADLAATPPTAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQRMMCaNIAMQEQlRPRE------------PDPPPPV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 697 LEYLLP--------------LISGASLYLTEAERAADSFRmiPLIADYR---PTLMQATPSFWhGLLMAGWRGDPELC-- 757
Cdd:PRK12582 267 SLDWMPwnhtmggnanfnglLWGGGTLYIDDGKPLPGMFE--ETIRNLReisPTVYGNVPAGY-AMLAEAMEKDDALRrs 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 758 ------VLA-GGEALPTKVAEEL----LRCCGS---LWNLYGPTET------TIWslksqITQAENItLGAPIANTRIYI 817
Cdd:PRK12582 344 ffknlrLMAyGGATLSDDLYERMqalaVRTTGHripFYTGYGATETaptttgTHW-----DTERVGL-IGLPLPGVELKL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 818 ldneghpVPQGVDGELYIAGDGVAQGYDGQPELNAQFFlSEPGvpggrMFRTGDLVR----SD-AQGqLFFVGRKDSQIK 892
Cdd:PRK12582 418 -------APVGDKYEVRVKGPNVTPGYHKDPELTAAAF-DEEG-----FYRLGDAARfvdpDDpEKG-LIFDGRVAEDFK 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 893 L-RGYRIELGEIERTL--ARHPHVDAAVVACIERA-------PLHKALAAFIitSEPPSLFEQLKNE------LRQQLPD 956
Cdd:PRK12582 484 LsTGTWVSVGTLRPDAvaACSPVIHDAVVAGQDRAfigllawPNPAACRQLA--GDPDAAPEDVVKHpavlaiLREGLSA 561
|
570 580 590
....*....|....*....|....*....|..
gi 1288439980 957 Y--MVPTLWQRVADF------PNTDNGKIDRK 980
Cdd:PRK12582 562 HnaEAGGSSSRIARAllmtepPSIDAGEITDK 593
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
526-888 |
3.62e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 77.29 E-value: 3.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 526 TLTYAELWARVQFIAMRFRAHGiQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQR----LMQRARLVC 601
Cdd:PRK05850 35 TLTWSQLYRRTLNVAEELRRHG-STGDRAVILAPQGLEYIVAFLGALQAGLIAVPLSVPQGGAHDERvsavLRDTSPSVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 602 L------------VVRQPGEWG-EIVQLSLPelmqDMSNAIRYSTPCALLPDMqAYLLFTSGSTGEPKGVCVVHRgllNL 668
Cdd:PRK05850 114 LttsavvddvteyVAPQPGQSApPVIEVDLL----DLDSPRGSDARPRDLPST-AYLQYTSGSTRTPAGVMVSHR---NV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 669 LLDMQRTFAVGSQDRLLSVTTPTFDISFLEY----------LLPLISGASLYLTEA----ERAAdsfRMIPLIADYRPTL 734
Cdd:PRK05850 186 IANFEQLMSDYFGDTGGVPPPDTTVVSWLPFyhdmglvlgvCAPILGGCPAVLTSPvaflQRPA---RWMQLLASNPHAF 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 735 mQATPSFWHGLL--------MAGWRGDPELCVLAGGE----ALPTKVAEELLRccgslWNL--------YGPTETTI--- 791
Cdd:PRK05850 263 -SAAPNFAFELAvrktsdddMAGLDLGGVLGIISGSErvhpATLKRFADRFAP-----FNLretairpsYGLAEATVyva 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 792 ---WSLKSQIT----------QAEN---------ITLGAPIANTrIYILDNEGH-PVPQGVDGELYIAGDGVAQGYDGQP 848
Cdd:PRK05850 337 trePGQPPESVrfdyeklsagHAKRcetgggtplVSYGSPRSPT-VRIVDPDTCiECPAGTVGEIWVHGDNVAAGYWQKP 415
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1288439980 849 ELNAQFF---LSEP--GVPGGRMFRTGDL-VRSDaqGQLFFVGR-KD 888
Cdd:PRK05850 416 EETERTFgatLVDPspGTPEGPWLRTGDLgFISE--GELFIVGRiKD 460
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
639-910 |
5.56e-14 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 76.78 E-value: 5.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 639 PDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSVTTPtfdisFLEY------LLPLISGASLYLt 712
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPP-----FHAYgfnsctLFPLLSGVPVVF- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 713 eAERAADSFRMIPLIADYRPTLMQATPSFWHGLLMAGWRGDPELC----VLAGGEALPTKVAEELLRCCG--SLWNLYGP 786
Cdd:PRK06334 256 -AYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPslrfVVIGGDAFKDSLYQEALKTFPhiQLRQGYGT 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 787 TETT-IWSLKSQITQAENITLGAPIANTRIYILDNEGH-PVPQGVDGELYIAGDGVAQGYDGQPElnAQFFLSepgVPGG 864
Cdd:PRK06334 335 TECSpVITINTVNSPKHESCVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLGEDF--GQGFVE---LGGE 409
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1288439980 865 RMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARH 910
Cdd:PRK06334 410 TWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
1098-1380 |
6.24e-14 |
|
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: 75.88 E-value: 6.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1098 PLTDVQRAYWLGRQTGATSIATHIYHEFDVEH-FNVTRFTHAVNALIARHEMLRARVLPDGT----QQILAQVPAyQLEQ 1172
Cdd:cd19539 3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGpLDVEALREALRDVVARHEALRTLLVRDDGgvprQEILPPGPA-PLEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1173 RDLSALSPNARNDALMAIRDRLSHHVHPADRWPLfdfsySACTAQHGRLHFSLDLLI----ADALSMRTLQQELMMLYRE 1248
Cdd:cd19539 82 RDLSDPDSDRERRLEELLRERESRGFDLDEEPPI-----RAVLGRFDPDDHVLVLVAhhtaFDAWSLDVFARDLAALYAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1249 PHVS----LPLLPFSFRDYVQALLVEQASEAYARDQAYWQRALPQLyGPPTLPvqGDLAQLSAIRFVRRRHR--LSAHNW 1322
Cdd:cd19539 157 RRKGpaapLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRGA-EPTALP--TDRPRPAGFPYPGADLRfeLDAELV 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1288439980 1323 GVLSALAQRTRITKTALLLTVFSQVLARWSLSPTFTLNLTLFNRPQgyPNAEAVIGDF 1380
Cdd:cd19539 234 AALRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNH--PRFESTVGFF 289
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
524-1006 |
6.90e-14 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 76.86 E-value: 6.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 524 DGTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGAC----YVPFDIHQPAARLQRLMQRARL 599
Cdd:PLN02654 118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVhsvvFAGFSAESLAQRIVDCKPKVVI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 600 VCLVVR---QPGEWGEIVQLSLPE-----------LMQDMSNAIR--------------------YSTPCAL-LPDMQ-- 642
Cdd:PLN02654 198 TCNAVKrgpKTINLKDIVDAALDEsakngvsvgicLTYENQLAMKredtkwqegrdvwwqdvvpnYPTKCEVeWVDAEdp 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 643 AYLLFTSGSTGEPKGVCVVHRGLLnllLDMQRTFAVGSQDRLLSVTTPTFDI------SFLEYLlPLISGASLYLTE-AE 715
Cdd:PLN02654 278 LFLLYTSGSTGKPKGVLHTTGGYM---VYTATTFKYAFDYKPTDVYWCTADCgwitghSYVTYG-PMLNGATVLVFEgAP 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 716 RAADSFRMIPLIADYRPTLMQATPSFWHGLLMAGwrgdpelcvlaggEALPTKVAEELLRCCGSL------------WNL 783
Cdd:PLN02654 354 NYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDG-------------DEYVTRHSRKSLRVLGSVgepinpsawrwfFNV 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 784 YG----PTETTIWSLKS---QIT--------QAENITLgaPIANTRIYILDNEGHPVPQGVDGELYIAGD--GVAQGYDG 846
Cdd:PLN02654 421 VGdsrcPISDTWWQTETggfMITplpgawpqKPGSATF--PFFGVQPVIVDEKGKEIEGECSGYLCVKKSwpGAFRTLYG 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 847 QPE-LNAQFFLSEPGvpggrMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAP 925
Cdd:PLN02654 499 DHErYETTYFKPFAG-----YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEV 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 926 LHKALAAFIITSEPPSLFEQLKNEL----RQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAEnfvadssLVSPQTQALS 1001
Cdd:PLN02654 574 KGQGIYAFVTLVEGVPYSEELRKSLiltvRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK-------IASRQLDELG 646
|
....*
gi 1288439980 1002 DTEQM 1006
Cdd:PLN02654 647 DTSTL 651
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
644-978 |
7.01e-14 |
|
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: 75.11 E-value: 7.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 644 YLLFTSGSTGEPKGVcvvhrgllnllldMQRtfavgsQDRLLSVTTPTFDISFLEYLLPLISGAslyltEAERAADSfRM 723
Cdd:cd05924 7 YILYTGGTTGMPKGV-------------MWR------QEDIFRMLMGGADFGTGEFTPSEDAHK-----AAAAAAGT-VM 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 724 IPLiadyrPTLMQATPSF-WHGLLMAG---------------WR-------------GD------------------PEL 756
Cdd:cd05924 62 FPA-----PPLMHGTGSWtAFGGLLGGqtvvlpddrfdpeevWRtiekhkvtsmtivGDamarplidalrdagpydlSSL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 757 CVLA-GGEALPTKVAEELLRCCGS--LWNLYGPTET---TIWSLKSQITQAENITLGAPiantRIYILDNEGHPVPQGVD 830
Cdd:cd05924 137 FAISsGGALLSPEVKQGLLELVPNitLVDAFGSSETgftGSGHSAGSGPETGPFTRANP----DTVVLDDDGRVVPPGSG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 831 GELYIAGDG-VAQGYDGQPELNAQFFlsePGVPGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLAR 909
Cdd:cd05924 213 GVGWIARRGhIPLGYYGDEAKTAETF---PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKS 289
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1288439980 910 HPHVDAAVVACIERAPLHKALAAFIITSEP--PSLfEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKID 978
Cdd:cd05924 290 HPAVYDVLVVGRPDERWGQEVVAVVQLREGagVDL-EELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
547-979 |
1.02e-13 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 75.99 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 547 GIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLMQRARLVCLVVRQP-GEWGEIVQLS-LPELM-- 622
Cdd:PLN02860 53 GLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETcSSWYEELQNDrLPSLMwq 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 623 -------------------QDMSNAIRYSTPCALL---PDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGS 680
Cdd:PLN02860 133 vflespsssvfiflnsfltTEMLKQRALGTTELDYawaPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 681 QDRLLSvTTPTFDISFLEYLLP-LISGASLYLT---EAERAADSfrmiplIADYRPTLMQATPSFWHGLL-----MAGWR 751
Cdd:PLN02860 213 DDVYLH-TAPLCHIGGLSSALAmLMVGACHVLLpkfDAKAALQA------IKQHNVTSMITVPAMMADLIsltrkSMTWK 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 752 GDPEL-CVLAGGEALPTKVAEE--LLRCCGSLWNLYGPTETTiwslkSQIT--QAENITLGAPIANTRIYILDNEGH-PV 825
Cdd:PLN02860 286 VFPSVrKILNGGGSLSSRLLPDakKLFPNAKLFSAYGMTEAC-----SSLTfmTLHDPTLESPKQTLQTVNQTKSSSvHQ 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 826 PQGV--------------------DGELYIAGDGVAQGYDGQP-----ELNAQFFLSepgvpggrmfrTGDLVRSDAQGQ 880
Cdd:PLN02860 361 PQGVcvgkpaphvelkigldessrVGRILTRGPHVMLGYWGQNsetasVLSNDGWLD-----------TGDIGWIDKAGN 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 881 LFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFI--------ITSEPPSLF-------EQ 945
Cdd:PLN02860 430 LWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVrlrdgwiwSDNEKENAKknltlssET 509
|
490 500 510
....*....|....*....|....*....|....*...
gi 1288439980 946 LKNELRQQ-LPDYMVP---TLWQRvaDFPNTDNGKIDR 979
Cdd:PLN02860 510 LRHHCREKnLSRFKIPklfVQWRK--PFPLTTTGKIRR 545
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1096-1361 |
1.31e-13 |
|
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: 74.98 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1096 PFPLTDVQRayWLGRQTGATsiATHIYHEFDV---EHFNVTRFTHAVNALIARHEMLRARVLPD--GTQQILAQVPAyQL 1170
Cdd:cd19534 1 EVPLTPIQR--WFFEQNLAG--RHHFNQSVLLrvpQGLDPDALRQALRALVEHHDALRMRFRREdgGWQQRIRGDVE-EL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1171 EQRDLSALSPNARNDALMAIRDRLSHHVHPADrWPLFDFSYSACTAQHGRLHFSLDLLIADALSMRTLQQELMMLYREPH 1250
Cdd:cd19534 76 FRLEVVDLSSLAQAAAIEALAAEAQSSLDLEE-GPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1251 VSLPL-LPF--SFRDYVQALLVEQASEAYARDQAYWQRALPQLYGPptLPVQGDLAQLSAIRFVRrrhRLSAHNwgvLSA 1327
Cdd:cd19534 155 AGEPIpLPSktSFQTWAELLAEYAQSPALLEELAYWRELPAADYWG--LPKDPEQTYGDARTVSF---TLDEEE---TEA 226
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1288439980 1328 L------AQRTRITKtaLLLTVFSQVLARWSLSPTFTLNL 1361
Cdd:cd19534 227 LlqeanaAYRTEIND--LLLAALALAFQDWTGRAPPAIFL 264
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
634-982 |
1.84e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 75.05 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 634 PCAllpdmqAYLLFTSGSTGEPKG----------------VCVVHRGLlnllldmqrtFAVGSQDRLLSvTTPTFDISFL 697
Cdd:PRK13390 148 PCG------AVMLYSSGTTGFPKGiqpdlpgrdvdapgdpIVAIARAF----------YDISESDIYYS-SAPIYHAAPL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 698 EYLLPLIS-GASLYLTEAERAADSFRMIpliADYRPTLMQATPSFWHGLL-----------MAGWRGdpelcVLAGGEAL 765
Cdd:PRK13390 211 RWCSMVHAlGGTVVLAKRFDAQATLGHV---ERYRITVTQMVPTMFVRLLkldadvrtrydVSSLRA-----VIHAAAPC 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 766 PTKVAEELLRCCGSL-WNLYGPTET-TIWSLKSQITQAENITLGAPIANTrIYILDNEGHPVPQGVDGELYIAGDGVAQG 843
Cdd:PRK13390 283 PVDVKHAMIDWLGPIvYEYYSSTEAhGMTFIDSPDWLAHPGSVGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFR 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 844 YDGQPELNAQffLSEPGVPggrmFRT--GDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACI 921
Cdd:PRK13390 362 YLNDPEKTAA--AQHPAHP----FWTtvGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGV 435
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1288439980 922 ERAPLHKALAAFIITSEPPSLFEQLKNEL----RQQLPDYMVPTLWQRVADFPNTDNGKIDRKRL 982
Cdd:PRK13390 436 PDPEMGEQVKAVIQLVEGIRGSDELARELidytRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
507-924 |
3.23e-13 |
|
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: 74.39 E-value: 3.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 507 IEQRCVQHPKQLAIQQHDG-----TLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPF 581
Cdd:cd05921 1 LAHWARQAPDRTWLAEREGnggwrRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 582 D-----IHQPAARLQRLMQR--ARLV---------------------CLVVRQPGEwgEIVQLSLPELMQ-----DMSNA 628
Cdd:cd05921 81 SpayslMSQDLAKLKHLFELlkPGLVfaqdaapfaralaaifplgtpLVVSRNAVA--GRGAISFAELAAtpptaAVDAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 629 IRystpcALLPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSVTTPTFDISF---LEYLLPLIS 705
Cdd:cd05921 159 FA-----AVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPPVLVDWLPWNHTFggnHNFNLVLYN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 706 GASLYLTEAERAADSF-RMIPLIADYRPTLMQATPSFWHGLLMAgWRGDPELC---------VLAGGEALPTKVAEEL-- 773
Cdd:cd05921 234 GGTLYIDDGKPMPGGFeETLRNLREISPTVYFNVPAGWEMLVAA-LEKDEALRrrffkrlklMFYAGAGLSQDVWDRLqa 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 774 --LRCCG---SLWNLYGPTETTIWSLKSQITQAENITLGAPIANTRIYIldneghpVPQGVDGELYIAGDGVAQGYDGQP 848
Cdd:cd05921 313 laVATVGeriPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKL-------VPSGGKYEVRVKGPNVTPGYWRQP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 849 ELNAQFFlSEPGvpggrMFRTGDLVR----SDAQGQLFFVGRKDSQIKLR-GYRIELGEIeRT---LARHPHVDAAVVAC 920
Cdd:cd05921 386 ELTAQAF-DEEG-----FYCLGDAAKladpDDPAKGLVFDGRVAEDFKLAsGTWVSVGPL-RAravAACAPLVHDAVVAG 458
|
....
gi 1288439980 921 IERA 924
Cdd:cd05921 459 EDRA 462
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
46-396 |
3.66e-13 |
|
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: 73.50 E-value: 3.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 46 PLSFNQERLWFLQKYDSTATNYNLYVVYRLHGVVDMPMLTEALRHVQARHAILRTRIIVRN-DRPCQVIDDASSLVLDTV 124
Cdd:cd19547 3 PLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDrAEPLQYVRDDLAPPWALL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 125 TLAAQAPTSALDAVIQQVINTR---FDLARGPLWGVTQIIQPDQGCHLVFCAHHIIIDGISLRLLFDELQQQYARLHAGN 201
Cdd:cd19547 83 DWSGEDPDRRAELLERLLADDRaagLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAHGR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 202 ETSLPPPPlQYADYAFWQRewfQDTLLANELA-YWRARLQDapllstfpsLHPRP--AQPSTHGSRFSITLD---ETLSL 275
Cdd:cd19547 163 EPQLSPCR-PYRDYVRWIR---ARTAQSEESErFWREYLRD---------LTPSPfsTAPADREGEFDTVVHefpEQLTR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 276 ALKHVARTQETTPFVLMLTAFQLVLMRYAQQQRLVIGMPVSGRiRPELQSS---IGYYASTAVIYTDFNGVEVGREALQR 352
Cdd:cd19547 230 LVNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGR-PPELEGSehmVGIFINTIPLRIRLDPDQTVTGLLET 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1288439980 353 VKASVKETQGRQQLPFENLVNMLDLPRsLSHSPLFQILYIYHNH 396
Cdd:cd19547 309 IHRDLATTAAHGHVPLAQIKSWASGER-LSGGRVFDNLVAFENY 351
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
499-986 |
1.32e-12 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 72.48 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 499 GPQDVLRIIEQRCVQHPKQLAIQQH-DGTL---TYAELWARVQFIAMRFRAHGIQPGDRIGVL---LPRHrdviatmLAT 571
Cdd:PRK06018 8 WPLLCHRIIDHAARIHGNREVVTRSvEGPIvrtTYAQIHDRALKVSQALDRDGIKLGDRVATIawnTWRH-------LEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 572 WF----VGACYvpfdiHQPAARLqrlmqRARLVCLVVRQPGEWGEIVQLSLPELMQDMSNAI----RY-------STPCA 636
Cdd:PRK06018 81 WYgimgIGAIC-----HTVNPRL-----FPEQIAWIINHAEDRVVITDLTFVPILEKIADKLpsveRYvvltdaaHMPQT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 637 LLPDMQAY-----------------------LLFTSGSTGEPKGVCVVHRG-LLNLLLDMQR-TFAVGSQDRLLSVtTPT 691
Cdd:PRK06018 151 TLKNAVAYeewiaeadgdfawktfdentaagMCYTSGTTGDPKGVLYSHRSnVLHALMANNGdALGTSAADTMLPV-VPL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 692 FDISF--LEYLLPLiSGASLYLTEAEraADSFRMIPLIADYRPTLMQATPSFWHGLLMAGWRGDPEL----CVLAGGEAL 765
Cdd:PRK06018 230 FHANSwgIAFSAPS-MGTKLVMPGAK--LDGASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLphlkMVVCGGSAM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 766 PTKVAEELLRCCGSLWNLYGPTET----TIWSLKSQITQAEN-------ITLGAPIANTRIYILDNEGHPVPQgvDGE-- 832
Cdd:PRK06018 307 PRSMIKAFEDMGVEVRHAWGMTEMsplgTLAALKPPFSKLPGdarldvlQKQGYPPFGVEMKITDDAGKELPW--DGKtf 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 833 --LYIAGDGVAQGY--DGQPELNAQFFlsepgvpggrmFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLA 908
Cdd:PRK06018 385 grLKVRGPAVAAAYyrVDGEILDDDGF-----------FDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAV 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 909 RHPHVdaavvacieraplhkALAAFIITSEP-----PSLFEQLK---NELRQQLPDYM---VPTLW-----QRVADFPNT 972
Cdd:PRK06018 454 GHPKV---------------AEAAVIGVYHPkwderPLLIVQLKpgeTATREEILKYMdgkIAKWWmpddvAFVDAIPHT 518
|
570
....*....|....
gi 1288439980 973 DNGKIDRKRLAENF 986
Cdd:PRK06018 519 ATGKILKTALREQF 532
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
863-982 |
2.10e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 71.22 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 863 GGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAFIITSEPPSL 942
Cdd:PRK08308 289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDP 368
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1288439980 943 fEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRL 982
Cdd:PRK08308 369 -VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1126-1595 |
2.68e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 72.30 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1126 DVEHFNVTRFTHAVNALIARHEMLRARVLPDGTQQILAQVPAYQLEQ--RDLSALSPNARNDALMAIRDRLSHHVHPADR 1203
Cdd:PRK12316 4132 DVQGLDVERFRAAWQAALDRHDVLRSGFVWQGELGRPLQVVHKQVSLpfAELDWRGRADLQAALDALAAAERERGFDLQR 4211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1204 WPLFDFSYSACTAQHGRLHFSLDLLIADALSMRTLQQELMMLYREPHVSLPLLpfSFRDYVQALLVEQASEAyardQAYW 1283
Cdd:PRK12316 4212 APLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERYSGRPPAQPGG--RYRDYIAWLQRQDAAAS----EAFW 4285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1284 QRALPQLYGPPTLPVQGDLAQL-SAIRFVRRRHRLSAHNWGVLSALAQRTRITKTALLLTVFSQVLARWSLSPTFTLNLT 1362
Cdd:PRK12316 4286 REQLAALDEPTRLAQAIARADLrSANGYGEHVRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGAT 4365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1363 LFNRPQGYPNAEAVIGDFTAVSLLNVCYDSQHSYAHNAQRIQVQLWEDLEH--------RRFSGiRASEALIHSGRFHAP 1434
Cdd:PRK12316 4366 VAGRPAELPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLALREHehtplyeiQRWAG-QGGEALFDSLLVFEN 4444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1435 MPVvftsmldidGETTAQDPRDTTRFTLCPDANITQTPqvwLDHQV-IELAGELHFNWDavEQLFDTTLLDQMFGAYCHA 1513
Cdd:PRK12316 4445 YPV---------SEALQQGAPGGLRFGEVTNHEQTNYP---LTLAVgLGETLSLQFSYD--RGHFDAATIERLARHLTNL 4510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1514 LQALVAMPQSWWGVNSSLALPTVSAPV-----TQAPAPTALLHHGLLR-QAALTPQETALISPIRELTYRQLSTAADHVA 1587
Cdd:PRK12316 4511 LEAMAEDPQRRLGELQLLEKAEQQRIValwnrTDAGYPATRCVHQLVAeRARMTPDAVAVVFDEEKLTYAELNRRANRLA 4590
|
....*...
gi 1288439980 1588 RALLALGV 1595
Cdd:PRK12316 4591 HALIARGV 4598
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
526-982 |
2.87e-12 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 71.17 E-value: 2.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 526 TLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGAC-------YVPFDIHQPAA---------- 588
Cdd:PLN02246 50 VYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVtttanpfYTPAEIAKQAKasgakliitq 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 589 -----RLQRLMQRARLVCLVVRQPGEwgeiVQLSLPELMQDMSNAIRystPCALLPDMQAYLLFTSGSTGEPKGVCVVHR 663
Cdd:PLN02246 130 scyvdKLKGLAEDDGVTVVTIDDPPE----GCLHFSELTQADENELP---EVEISPDDVVALPYSSGTTGLPKGVMLTHK 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 664 GLL------------NLLLdmqrtfavGSQDRLLSVtTPTFDISFLEYLL--PLISGASLYLTeaeRAADSFRMIPLIAD 729
Cdd:PLN02246 203 GLVtsvaqqvdgenpNLYF--------HSDDVILCV-LPMFHIYSLNSVLlcGLRVGAAILIM---PKFEIGALLELIQR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 730 YRPTLMQATPSfwhglLMAGWRGDPEL---------CVLAGGEALpTKVAEELLRccGSLWNL-----YGPTET------ 789
Cdd:PLN02246 271 HKVTIAPFVPP-----IVLAIAKSPVVekydlssirMVLSGAAPL-GKELEDAFR--AKLPNAvlgqgYGMTEAgpvlam 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 790 ------TIWSLKSQitqaeniTLGAPIANTRIYILDNE-GHPVPQGVDGELYIAGDGVAQGYDGQPELNAQfFLSEPGvp 862
Cdd:PLN02246 343 clafakEPFPVKSG-------SCGTVVRNAELKIVDPEtGASLPRNQPGEICIRGPQIMKGYLNDPEATAN-TIDKDG-- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 863 ggrMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHV-DAAVVACIERA----PLhkalaAFIITS 937
Cdd:PLN02246 413 ---WLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIaDAAVVPMKDEVagevPV-----AFVVRS 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1288439980 938 EPPSLFEqlkNELRQQLPDYMVptLWQR------VADFPNTDNGKIDRKRL 982
Cdd:PLN02246 485 NGSEITE---DEIKQFVAKQVV--FYKRihkvffVDSIPKAPSGKILRKDL 530
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
1118-1352 |
3.74e-12 |
|
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: 70.31 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1118 ATHIYHE---FDVEH-FNVTRFTHAVNALIARHEMLRARVLPDGTQQ----ILAQVPAyQLEQRDLSALSPNARNDALMA 1189
Cdd:cd19543 20 GSGAYVEqmvITLEGpLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEplqvVLKDRKL-PWRELDLSHLSEAEQEAELEA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1190 IRDRLSHHVHPADRWPLFDFSYSACTAQHGRLHFSLDLLIADALSMRTLQQELMMLYREP-HVSLPLLPF--SFRDYVQA 1266
Cdd:cd19543 99 LAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALgEGQPPSLPPvrPYRDYIAW 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1267 LLVEQASEAyardQAYWQRALPQLYGPPTLPVQGDLAQLSAIRFVRRRHRLSAHNWGVLSALAQRTRITKTALLLTVFSQ 1346
Cdd:cd19543 179 LQRQDKEAA----EAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQELARQHGVTLNTVVQGAWAL 254
|
....*.
gi 1288439980 1347 VLARWS 1352
Cdd:cd19543 255 LLSRYS 260
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
796-1077 |
6.53e-12 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 68.24 E-value: 6.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 796 SQITQAENITLGAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQ-PELNAQFFLSEPGVPGGRMFRTGDLVR 874
Cdd:COG3433 10 PPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLaAAARAPFIPVPYPAQPGRQADDLRLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 875 SDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERA-PLHKALAAFIITSEPPSLFEQLknELRQQ 953
Cdd:COG3433 90 RRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAgVGLLLIVGAVAALDGLAAAAAL--AALDK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 954 LPDYMVPTLWQRVADFPNTDNGKIDRKRLAENFVADSSLVSPQTQALSD---TEQMLLALWMRYLPIK--NVDPECDFFR 1028
Cdd:COG3433 168 VPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALEtalTEEELRADVAELLGVDpeEIDPDDNLFD 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1288439980 1029 LGGHSLLAVTLVAEINRTfHCALTLKDIFHYSTLRALSARIAQQSITDA 1077
Cdd:COG3433 248 LGLDSIRLMQLVERWRKA-GLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1129-1352 |
8.50e-12 |
|
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: 69.02 E-value: 8.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1129 HFNVTRFTHAVNALIARHEMLRARVLPDG-----TQQILAQvPAYQLEQRdlsalsPNARNDALMAIRDRLSHHVHPADR 1203
Cdd:cd19532 35 PLDVARLERAVRAVGQRHEALRTCFFTDPedgepMQGVLAS-SPLRLEHV------QISDEAEVEEEFERLKNHVYDLES 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1204 WPLF---DFSYSActaqhgRLHFsldLLIA------DALSMRTLQQELMMLYRepHVSLPLLPFSFRDYVQALLVEQASE 1274
Cdd:cd19532 108 GETMrivLLSLSP------TEHY---LIFGyhhiamDGVSFQIFLRDLERAYN--GQPLLPPPLQYLDFAARQRQDYESG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1275 AYARDQAYWQRALPQLygPPTLPVQgDLAQ------LSAIRFVRRRHRLSAHNWGVLSALAQRTRITKTALLLTVFSQVL 1348
Cdd:cd19532 177 ALDEDLAYWKSEFSTL--PEPLPLL-PFAKvksrppLTRYDTHTAERRLDAALAARIKEASRKLRVTPFHFYLAALQVLL 253
|
....
gi 1288439980 1349 ARWS 1352
Cdd:cd19532 254 ARLL 257
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
1098-1416 |
9.07e-12 |
|
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: 68.94 E-value: 9.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1098 PLTDVQRAYWLGRQ----TGATSIAThiYHEFDVEhFNVTRFTHAVNALIARHEMLRARVL--PDGTQQILAQVPAYQLE 1171
Cdd:cd19533 3 PLTSAQRGVWFAEQldpeGSIYNLAE--YLEITGP-VDLAVLERALRQVIAEAETLRLRFTeeEGEPYQWIDPYTPVPIR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1172 QRDLSAlSPNARNDALMAIRDRLSHHVhPADRWPLFDFSYSACTAQHGRLHFSLDLLIADALSMRTLQQELMMLYRE--P 1249
Cdd:cd19533 80 HIDLSG-DPDPEGAAQQWMQEDLRKPL-PLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTAllK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1250 HVSLPLLPF-SFRDYVQALLVEQASEAYARDQAYWQRALPQLYGPPTLPVQGDLAQLSAIRFvRRRHRLSAHNwgVLSAL 1328
Cdd:cd19533 158 GRPAPPAPFgSFLDLVEEEQAYRQSERFERDRAFWTEQFEDLPEPVSLARRAPGRSLAFLRR-TAELPPELTR--TLLEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1329 AQRTRITKTALLLTVFSQVLARWSLSPTFTLNLTLFNRpqGYPNAEAVIGDFTAVSLLNVCYDSQHSYAHNAQRIQVQLW 1408
Cdd:cd19533 235 AEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGR--LGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELR 312
|
....*...
gi 1288439980 1409 EDLEHRRF 1416
Cdd:cd19533 313 SLLRHQRY 320
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
639-984 |
1.00e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 69.32 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 639 PDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLsVTTPTFDISFL--EYLLPLISGASLYLtEAER 716
Cdd:PRK07867 151 PDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCY-VSMPLFHSNAVmaGWAVALAAGASIAL-RRKF 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 717 AADSFrmIPLIADYRPTLMQ----------ATPSfwhgllMAGWRGDPeLCVLAGGEALPTKVAEELLRCCGSLWNLYGP 786
Cdd:PRK07867 229 SASGF--LPDVRRYGATYANyvgkplsyvlATPE------RPDDADNP-LRIVYGNEGAPGDIARFARRFGCVVVDGFGS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 787 TETTIwslksQITQAENI---TLGAPIANTRIYILDNeGHPVPQGVD------------GELY-IAGDGVAQGYDGQPEL 850
Cdd:PRK07867 300 TEGGV-----AITRTPDTppgALGPLPPGVAIVDPDT-GTECPPAEDadgrllnadeaiGELVnTAGPGGFEGYYNDPEA 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 851 NAQfflsepGVPGGrMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPH-VDAAVVACIERAPLHKA 929
Cdd:PRK07867 374 DAE------RMRGG-VYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDaTEVAVYAVPDPVVGDQV 446
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 930 LAAFIITsePPSLFEQLKNE--LRQQlPDY---MVPTLWQRVADFPNTDNGKIDRKRLAE 984
Cdd:PRK07867 447 MAALVLA--PGAKFDPDAFAefLAAQ-PDLgpkQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
508-886 |
1.14e-11 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 69.52 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 508 EQRCVQHPKQLAIQQHDG-----TLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVP-- 580
Cdd:PRK08180 46 VHWAQEAPDRVFLAERGAdggwrRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPvs 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 581 ----------------FDIHQP-------AARLQRLMQRARL--VCLVVRQPGEWGEIVqLSLPELMQDMSNAIRYSTPC 635
Cdd:PRK08180 126 payslvsqdfgklrhvLELLTPglvfaddGAAFARALAAVVPadVEVVAVRGAVPGRAA-TPFAALLATPPTAAVDAAHA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 636 ALLPDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVgsqdrlLSVTTPTfdisFLEYL-------------LP 702
Cdd:PRK08180 205 AVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPF------LAEEPPV----LVDWLpwnhtfggnhnlgIV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 703 LISGASLYLTE----AERAADSFRMIPLIAdyrPTLMQATPSFWHGLLMAgWRGDPELC---------VLAGGEALPTKV 769
Cdd:PRK08180 275 LYNGGTLYIDDgkptPGGFDETLRNLREIS---PTVYFNVPKGWEMLVPA-LERDAALRrrffsrlklLFYAGAALSQDV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 770 AEELLRC----CG-SLWNL--YGPTET--TIWSLKSQITQAENItlGAPIANTRIYIldneghpVPQGVDGELYIAGDGV 840
Cdd:PRK08180 351 WDRLDRVaeatCGeRIRMMtgLGMTETapSATFTTGPLSRAGNI--GLPAPGCEVKL-------VPVGGKLEVRVKGPNV 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1288439980 841 AQGYDGQPELNAQFFlSEPGvpggrMFRTGDLVR----SDAQGQLFFVGR 886
Cdd:PRK08180 422 TPGYWRAPELTAEAF-DEEG-----YYRSGDAVRfvdpADPERGLMFDGR 465
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
1001-1072 |
1.70e-11 |
|
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: 61.41 E-value: 1.70e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1288439980 1001 SDTEQMLLALWMRYL--PIKNVDPECDFFR-LGGHSLLAVTLVAEINRTFHCALTLKDIFHYSTLRALSARIAQQ 1072
Cdd:COG0236 4 EELEERLAEIIAEVLgvDPEEITPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
758-986 |
1.94e-11 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 67.38 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 758 VLAGGEALPTKVAEELLRCCGSLWNLYGPTETTiwslksqitqAENITLGAPIANTRIYIldneghpvpqgVDGELYIAG 837
Cdd:PRK07824 156 VLVGGGPAPAPVLDAAAAAGINVVRTYGMSETS----------GGCVYDGVPLDGVRVRV-----------EDGRIALGG 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 838 DGVAQGYDGQPELNAqffLSEPGvpggrMFRTGDLVRSDAqGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAV 917
Cdd:PRK07824 215 PTLAKGYRNPVDPDP---FAEPG-----WFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCA 285
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 918 VACIERAPLHKALAAFIITSEPPS-LFEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAENF 986
Cdd:PRK07824 286 VFGLPDDRLGQRVVAAVVGDGGPApTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRF 355
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
645-984 |
4.78e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 67.36 E-value: 4.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 645 LLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDrLLSVTTPTFDISFLEYLLP--LISGASLYLTEAERAAdsfR 722
Cdd:PRK13388 155 LIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDD-VCYVSMPLFHSNAVMAGWApaVASGAAVALPAKFSAS---G 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 723 MIPLIADYRPTLMQ----------ATPSfwhgllmagwR---GDPELCVLAGGEALPTKVAEELLRCCGSLWNLYGPTET 789
Cdd:PRK13388 231 FLDDVRRYGATYFNyvgkplayilATPE----------RpddADNPLRVAFGNEASPRDIAEFSRRFGCQVEDGYGSSEG 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 790 TIwslksQITQAENI---TLGAPIANTRIY-----------ILDNEGHPV-PQGVDGELY-IAGDGVAQGYDGQPELNAQ 853
Cdd:PRK13388 301 AV-----IVVREPGTppgSIGRGAPGVAIYnpetltecavaRFDAHGALLnADEAIGELVnTAGAGFFEGYYNNPEATAE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 854 fflsepGVPGGrMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIERAPLHKALAAF 933
Cdd:PRK13388 376 ------RMRHG-MYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAA 448
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1288439980 934 IITSEP----PSLFEQLkneLRQQ--LPDYMVPTLWQRVADFPNTDNGKIDRKRLAE 984
Cdd:PRK13388 449 LVLRDGatfdPDAFAAF---LAAQpdLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
526-967 |
5.26e-11 |
|
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: 67.48 E-value: 5.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 526 TLTYAELWARVQFIAMRFRA-HGIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRLMQRA------- 597
Cdd:cd17632 67 TITYAELWERVGAVAAAHDPeQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETeprllav 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 598 -------------------RLVCLVVRQPG----EWGEIVQLSLPE---------LMQDMSNAIRYSTPCALLPDMQ--A 643
Cdd:cd17632 147 saehldlaveavleggtppRLVVFDHRPEVdahrAALESARERLAAvgipvttltLIAVRGRDLPPAPLFRPEPDDDplA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 644 YLLFTSGSTGEPKGVCVVHRgllnLLLDMQRTFAVGSQDRLLSVTTPTF-DISFLEYLLPLI----SGASLYLTEAERAA 718
Cdd:cd17632 227 LLIYTSGSTGTPKGAMYTER----LVATFWLKVSSIQDIRPPASITLNFmPMSHIAGRISLYgtlaRGGTAYFAAASDMS 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 719 DSFRMIPLIadyRPTLMQATPSFWHgLLMAGWRGDPELCVLAGG--EALPTKVAEEL----------LRCCGS------- 779
Cdd:cd17632 303 TLFDDLALV---RPTELFLVPRVCD-MLFQRYQAELDRRSVAGAdaETLAERVKAELrervlggrllAAVCGSaplsaem 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 780 -----------LWNLYGPTETTIWSLKSQITQaenitlgAPIANTRI-------YILDNEGHPvpqgvDGELYIAGDGVA 841
Cdd:cd17632 379 kafmeslldldLHDGYGSTEAGAVILDGVIVR-------PPVLDYKLvdvpelgYFRTDRPHP-----RGELLVKTDTLF 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 842 QGYDGQPELNAQFFlSEPGvpggrMFRTGDLVRSDAQGQLFFVGRKDSQIKL-RGYRIELGEIERTLARHPHVDAAVV-A 919
Cdd:cd17632 447 PGYYKRPEVTAEVF-DEDG-----FYRTGDVMAELGPDRLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVRQIFVyG 520
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1288439980 920 CIERAPLhkaLAAFIITSEPPSLF--EQLKNELRQQLpdymvptlwQRVA 967
Cdd:cd17632 521 NSERAYL---LAVVVPTQDALAGEdtARLRAALAESL---------QRIA 558
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
526-990 |
1.06e-10 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 66.16 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 526 TLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGACyvpFDIHQPAARLQRLMQRARL--VCLV 603
Cdd:PLN02330 55 AVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGV---FSGANPTALESEIKKQAEAagAKLI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 604 VRQPGEWGEIVQLSLPELM---QDMSNAIRYSTpcaLLP------DMQAY----------LLFTSGSTGEPKGVCVVHRG 664
Cdd:PLN02330 132 VTNDTNYGKVKGLGLPVIVlgeEKIEGAVNWKE---LLEaadragDTSDNeeilqtdlcaLPFSSGTTGISKGVMLTHRN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 665 LL-NLLLDMqrtFAVGSQdRLLSVTT----PTFDI--------------------------SFLEYLL-------PLISG 706
Cdd:PLN02330 209 LVaNLCSSL---FSVGPE-MIGQVVTlgliPFFHIygitgiccatlrnkgkvvvmsrfelrTFLNALItqevsfaPIVPP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 707 ASLYLTEaERAADSFRMIPLiaDYRPTLMQATPsfwhgllMAgwrgdPELcVLAGGEALPTKVAEELlrccgslwnlYGP 786
Cdd:PLN02330 285 IILNLVK-NPIVEEFDLSKL--KLQAIMTAAAP-------LA-----PEL-LTAFEAKFPGVQVQEA----------YGL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 787 TETTIWSL------KSQITQAENiTLGAPIANTRIYILDNE-GHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFfLSEP 859
Cdd:PLN02330 339 TEHSCITLthgdpeKGHGIAKKN-SVGFILPNLEVKFIDPDtGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRT-IDED 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 860 GvpggrMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHV-DAAVVACIERAPLHKALAAFIITSE 938
Cdd:PLN02330 417 G-----WLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVeDAAVVPLPDEEAGEIPAACVVINPK 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1288439980 939 PPSLFEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAENFVADS 990
Cdd:PLN02330 492 AKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLSIN 543
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
528-986 |
1.51e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 65.88 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 528 TYAELWARVQFIAMRFRAHGIQPGDRIGVLL------------------------PR-HRDVIAtmlatWFVGAC---YV 579
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPGDRVGTLAwngyrhleayygvsgsgavchtinPRlFPEQIA-----YIVNHAedrYV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 580 PFD------IHQPAARLQRLmQRARLVCLVVRQPGewGEIVQLSLPELMQDMSNAirYSTPcaLLPDMQA-YLLFTSGST 652
Cdd:PRK07008 116 LFDltflplVDALAPQCPNV-KGWVAMTDAAHLPA--GSTPLLCYETLVGAQDGD--YDWP--RFDENQAsSLCYTSGTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 653 GEPKGVCVVHRG--LLNLLLDMQRTFAVGSQDRLLSVtTPTFDISF--LEYLLPL-----------ISGASLY-LTEAER 716
Cdd:PRK07008 189 GNPKGALYSHRStvLHAYGAALPDAMGLSARDAVLPV-VPMFHVNAwgLPYSAPLtgaklvlpgpdLDGKSLYeLIEAER 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 717 AadsfrmipliadyrpTLMQATPSFWHGLLM----AGWRGDPELCVLAGGEALPTKVAEELLRCCG-SLWNLYGPTET-- 789
Cdd:PRK07008 268 V---------------TFSAGVPTVWLGLLNhmreAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGvEVIHAWGMTEMsp 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 790 --TIWSLK---SQITQAENITL----GAPIANTRIYILDNEGHPVP-QGVD-GELYIAGDGVAQGYdgqpelnaqfFLSE 858
Cdd:PRK07008 333 lgTLCKLKwkhSQLPLDEQRKLlekqGRVIYGVDMKIVGDDGRELPwDGKAfGDLQVRGPWVIDRY----------FRGD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 859 --PGVPGgrMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHV-DAAVVACI-----ERaPLhkal 930
Cdd:PRK07008 403 asPLVDG--WFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVaEAACIACAhpkwdER-PL---- 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1288439980 931 aafIITSEPPSlFEQLKNEL---------RQQLPDYMVptlwqRVADFPNTDNGKIDRKRLAENF 986
Cdd:PRK07008 476 ---LVVVKRPG-AEVTREELlafyegkvaKWWIPDDVV-----FVDAIPHTATGKLQKLKLREQF 531
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
527-939 |
2.26e-10 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 65.41 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 527 LTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGAcyVPFDIHQPAA---------RLQRLMQRA 597
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGL--VPVPLPLPMGfggresyiaQLRGMLASA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 598 RLVCLVVrqPGEWGEIVQLSLP--ELMQDMSNAIRYSTP---CAL---LPDMQAYLLFTSGSTGEPKGVCVVHRGLL-NL 668
Cdd:PRK09192 128 QPAAIIT--PDELLPWVNEATHgnPLLHVLSHAWFKALPeadVALprpTPDDIAYLQYSSGSTRFPRGVIITHRALMaNL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 669 LLDMQRTFAVGSQDRLLSVTTPTFDISFLEYLL-PLISGASL-YLTEAERAADSFRMIPLIADYRPTLMQAtPSFWH--- 743
Cdd:PRK09192 206 RAISHDGLKVRPGDRCVSWLPFYHDMGLVGFLLtPVATQLSVdYLPTRDFARRPLQWLDLISRNRGTISYS-PPFGYelc 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 744 ----------GLLMAGWRgdpelcvLA--GGEALPTKVAEELLRCCGSL-------WNLYGPTETTI---WSLKSQITQA 801
Cdd:PRK09192 285 arrvnskdlaELDLSCWR-------VAgiGADMIRPDVLHQFAEAFAPAgfddkafMPSYGLAEATLavsFSPLGSGIVV 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 802 ENITL-------------------------GAPIANTRIYILDNEGHPVPQGVDGELYIAGDGVAQGYDGQPElnAQFFL 856
Cdd:PRK09192 358 EEVDRdrleyqgkavapgaetrrvrtfvncGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEE--SQDVL 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 857 SepgvPGGRMfRTGDL-VRSDaqGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVacieraplhkalAAFII 935
Cdd:PRK09192 436 A----ADGWL-DTGDLgYLLD--GYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRSGDA------------AAFSI 496
|
....
gi 1288439980 936 TSEP 939
Cdd:PRK09192 497 AQEN 500
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
1007-1064 |
2.88e-10 |
|
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: 57.19 E-value: 2.88e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1007 LLALWMRYL--PIKNVDPECDFFRLGGHSLLAVTLVAEINRTFHCALTLKDIFHYSTLRA 1064
Cdd:pfam00550 3 LRELLAEVLgvPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
1132-1350 |
8.96e-10 |
|
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: 62.84 E-value: 8.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1132 VTRFTHAVNALIARHEMLRARVLPDGTQQIL------AQVPayqLEQRDLsalspnarnDALMAIRDRLSHHVHPADRW- 1204
Cdd:cd19544 38 LDAFLAALQQVIDRHDILRTAILWEGLSEPVqvvwrqAELP---VEELTL---------DPGDDALAQLRARFDPRRYRl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1205 -----PLFDFSYsACTAQHGRLHFSLDL--LIADALSMRTLQQELMMLYREPHVSLPlLPFSFRDYV-QALLVEQASEAy 1276
Cdd:cd19544 106 dlrqaPLLRAHV-AEDPANGRWLLLLLFhhLISDHTSLELLLEEIQAILAGRAAALP-PPVPYRNFVaQARLGASQAEH- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1277 ardQAYWQRALpqlyG---PPTLP-----VQGDLAQLsairfVRRRHRLSAHNWGVLSALAQRTRITKTALLLTVFSQVL 1348
Cdd:cd19544 183 ---EAFFREML----GdvdEPTAPfglldVQGDGSDI-----TEARLALDAELAQRLRAQARRLGVSPASLFHLAWALVL 250
|
..
gi 1288439980 1349 AR 1350
Cdd:cd19544 251 AR 252
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
516-934 |
9.65e-10 |
|
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: 63.21 E-value: 9.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 516 KQLAIQQhdgTLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGAcyVPFDIHQPA-------- 587
Cdd:cd17641 4 KDFGIWQ---EFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGA--LSLGIYQDSmaeevayl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 588 -----AR------------LQRLMQRARLVCLVV----------RQPG--------EWGEIVQLSLPELMQDMSNAIRYS 632
Cdd:cd17641 79 lnytgARvviaedeeqvdkLLEIADRIPSVRYVIycdprgmrkyDDPRlisfedvvALGRALDRRDPGLYEREVAAGKGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 633 TPCALLPdmqayllfTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQDRLLSVTtPTFDISFLEYLL--PLISGASL- 709
Cdd:cd17641 159 DVAVLCT--------TSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVL-PLPWIGEQMYSVgqALVCGFIVn 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 710 YLTEAERAADSFRMI--------P-----LIADYRPTLMQATP----SFWHGL------LMAGWRGDPELCVL------- 759
Cdd:cd17641 230 FPEEPETMMEDLREIgptfvllpPrvwegIAADVRARMMDATPfkrfMFELGMklglraLDRGKRGRPVSLWLrlaswla 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 760 ---------------------AGGEALPTKVAEeLLRCCG-SLWNLYGPTETTIWSLKSQITQAENITLGAPIANTRIYI 817
Cdd:cd17641 310 dallfrplrdrlgfsrlrsaaTGGAALGPDTFR-FFHAIGvPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 818 lDNEGhpvpqgvdgELYIAGDGVAQGYDGQPELNAQFFLsepgvpGGRMFRTGDLVRSDAQGQLFFVGR-KDSQIKLRGY 896
Cdd:cd17641 389 -DEVG---------EILVRSPGVFVGYYKNPEATAEDFD------EDGWLHTGDAGYFKENGHLVVIDRaKDVGTTSDGT 452
|
490 500 510
....*....|....*....|....*....|....*...
gi 1288439980 897 RIELGEIERTLARHPHVDAAVVACIERaplhKALAAFI 934
Cdd:cd17641 453 RFSPQFIENKLKFSPYIAEAVVLGAGR----PYLTAFI 486
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
526-984 |
2.90e-09 |
|
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: 61.29 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 526 TLTYAELWARVQFIAMRFR-AHGIQPGDRIGVLLPRHRDVIATMLATWFVGACyvpfdihqPAARLQRLMQRARLVCLvv 604
Cdd:cd05937 5 TWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA--------PAFINYNLSGDPLIHCL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 605 rqpgewgeivqlslpelmqdmsnaiRYSTpCALL---PDMQAYLLFTSGSTGEPKGVCVVHRGLLNLLLDMQRTFAVGSQ 681
Cdd:cd05937 75 -------------------------KLSG-SRFVivdPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 682 DRLLSvTTPTF--DISFLEYLLPLISGASLYLTEA-----------ERAADSFRMIPLIADYrptLMQATPSFW---HGL 745
Cdd:cd05937 129 DRTYT-CMPLYhgTAAFLGACNCLMSGGTLALSRKfsasqfwkdvrDSGATIIQYVGELCRY---LLSTPPSPYdrdHKV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 746 LMA---GWRGD-----------PELCVL-AGGEALptkvaeellrccGSLWNLY-GPTET-------TIWSLKSQITQAe 802
Cdd:cd05937 205 RVAwgnGLRPDiwerfrerfnvPEIGEFyAATEGV------------FALTNHNvGDFGAgaighhgLIRRWKFENQVV- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 803 nitlgaPIA---NTRIYILDNE-GHPV--PQGVDGELYIA----GDGVAQGYDGQPELNAQFFLSEPGVPGGRMFRTGDL 872
Cdd:cd05937 272 ------LVKmdpETDDPIRDPKtGFCVraPVGEPGEMLGRvpfkNREAFQGYLHNEDATESKLVRDVFRKGDIYFRTGDL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 873 VRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHVDAAVVACIeRAPLHKALAAF-IITSEPPSL------FEQ 945
Cdd:cd05937 346 LRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGV-KVPGHDGRAGCaAITLEESSAvpteftKSL 424
|
490 500 510
....*....|....*....|....*....|....*....
gi 1288439980 946 LKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAE 984
Cdd:cd05937 425 LASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
755-990 |
3.96e-09 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 61.30 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 755 ELCVlaGGEALPTKVA---EELLRCCGSlwNLYGPTETTIWSLKS-QITQAENITLGAPIANTRIYILDNEGHPVPQGVD 830
Cdd:PTZ00237 384 EIWC--GGEVIEESIPeyiENKLKIKSS--RGYGQTEIGITYLYCyGHINIPYNATGVPSIFIKPSILSEDGKELNVNEI 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 831 GELYIA---GDGVAQGYDGQPELNAQFFLSEPGvpggrMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTL 907
Cdd:PTZ00237 460 GEVAFKlpmPPSFATTFYKNDEKFKQLFSKFPG-----YYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSI 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 908 ARHPHVDAAVVACIERAPLHKALAAFIITSEPPSL----FEQLKNE----LRQQLPDYMVPTLWQRVADFPNTDNGKIDR 979
Cdd:PTZ00237 535 LKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNqsidLNKLKNEinniITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
250
....*....|.
gi 1288439980 980 KRLAeNFVADS 990
Cdd:PTZ00237 615 QIIS-KFLNDS 624
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
526-977 |
3.34e-08 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 58.27 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 526 TLTYAELWARVQFIAMRFRAHGIQPGDRIGVLLPRHRDVIATMLATWFVGA----C------------------------ 577
Cdd:PRK03584 114 ELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAiwssCspdfgvqgvldrfgqiepkvliav 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 578 --Y----VPFDIHQPAARLQRLMQRARLVCLVvrqpGEWGEIVQLSLPELMQDMSNAIRYSTPCAL----LP-DMQAYLL 646
Cdd:PRK03584 194 dgYryggKAFDRRAKVAELRAALPSLEHVVVV----PYLGPAAAAAALPGALLWEDFLAPAEAAELefepVPfDHPLWIL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 647 FTSGSTGEPKgvCVVHRG---LLNLLLDMQRTFAVGSQDRLLSVTTPT-----FDISfleyllPLISGASLYLTE----A 714
Cdd:PRK03584 270 YSSGTTGLPK--CIVHGHggiLLEHLKELGLHCDLGPGDRFFWYTTCGwmmwnWLVS------GLLVGATLVLYDgspfY 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 715 ERAADSFRmipLIADYRPTLMQATPSFWHGLLMAGwrgdpelcvLAGGEA--LPTkvaeelLRCCGS----LwnlygPTE 788
Cdd:PRK03584 342 PDPNVLWD---LAAEEGVTVFGTSAKYLDACEKAG---------LVPGEThdLSA------LRTIGStgspL-----PPE 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 789 TTIW---SLKSQItQAENIT----------LGAPIA------------NTRIYILDNEGHPVPQGVdGELYIA------- 836
Cdd:PRK03584 399 GFDWvyeHVKADV-WLASISggtdicscfvGGNPLLpvyrgeiqcrglGMAVEAWDEDGRPVVGEV-GELVCTkpfpsmp 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 837 ----GDGvaqgyDGQPELNAQF--FlsePGVpggrmFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARH 910
Cdd:PRK03584 477 lgfwNDP-----DGSRYRDAYFdtF---PGV-----WRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEAL 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 911 PHVDAAVVACIE------RAPLhkalaaFIITSEPPSLFEQLKNELRQQL---------PDYMVPtlwqrVADFPNTDNG 975
Cdd:PRK03584 544 PEVLDSLVIGQEwpdgdvRMPL------FVVLAEGVTLDDALRARIRTTIrtnlsprhvPDKIIA-----VPDIPRTLSG 612
|
..
gi 1288439980 976 KI 977
Cdd:PRK03584 613 KK 614
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
624-919 |
2.89e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 55.16 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 624 DMSNAIRYSTPCALLP---DMQAYLLFTSGSTGEPKGVcVVHRG--LLNLLLDMQRTFAVGSQDRLLSVTTPTFDISFLE 698
Cdd:PRK05851 133 DLATAAHTNRSASLTPpdsGGPAVLQGTAGSTGTPRTA-ILSPGavLSNLRGLNARVGLDAATDVGCSWLPLYHDMGLAF 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 699 YLLPLISGASLYLT-EAERAADSFRMIPLIADYRPTlMQATPSFWHGLL--MAGWRGDPEL----CVLAGGEALP----T 767
Cdd:PRK05851 212 LLTAALAGAPLWLApTTAFSASPFRWLSWLSDSRAT-LTAAPNFAYNLIgkYARRVSDVDLgalrVALNGGEPVDcdgfE 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 768 KVAEELLRC---CGSLWNLYGPTETT---------IWSLKSQITQAENIT------LGAPIANTRIYILDNEGHPVPQGV 829
Cdd:PRK05851 291 RFATAMAPFgfdAGAAAPSYGLAESTcavtvpvpgIGLRVDEVTTDDGSGarrhavLGNPIPGMEVRISPGDGAAGVAGR 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 830 D-GELYIAGDGVAQGYDGQPELNAqfflsepgvpgGRMFRTGDL-VRSDaqGQLFFVGRKDSQIKLRGYRIELGEIERTL 907
Cdd:PRK05851 371 EiGEIEIRGASMMSGYLGQAPIDP-----------DDWFPTGDLgYLVD--GGLVVCGRAKELITVAGRNIFPTEIERVA 437
|
330
....*....|...
gi 1288439980 908 ARHPHV-DAAVVA 919
Cdd:PRK05851 438 AQVRGVrEGAVVA 450
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
527-925 |
3.01e-07 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 55.13 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 527 LTYAELWARVQFIAMRFRAHgIQPGDRIGVLLPRHRDVIATMLATWFVGACYVP-FDIHQP--AARLQRLMQRAR----L 599
Cdd:PRK12476 69 LTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPlFAPELPghAERLDTALRDAEptvvL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 600 VCLVVRQPGEwgeivqlslpELMQDMSNAIRYS---------------TPCALLPDMQAYLLFTSGSTGEPKGVCVVHRG 664
Cdd:PRK12476 148 TTTAAAEAVE----------GFLRNLPRLRRPRviaidaipdsagesfVPVELDTDDVSHLQYTSGSTRPPVGVEITHRA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 665 LLNLLLDMqrTFAVGSQDR-LLSVT-TPTF-DISFLEYLLPLISGASLYLTE----AERAADSFRMIPLIADYRPTLmQA 737
Cdd:PRK12476 218 VGTNLVQM--ILSIDLLDRnTHGVSwLPLYhDMGLSMIGFPAVYGGHSTLMSptafVRRPQRWIKALSEGSRTGRVV-TA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 738 TPSF---W---HGLLMAGWRGDPELCVLAGGEALPTKVAEELLRCCGSLWNL--------YGPTETT------------- 790
Cdd:PRK12476 295 APNFayeWaaqRGLPAEGDDIDLSNVVLIIGSEPVSIDAVTTFNKAFAPYGLprtafkpsYGIAEATlfvatiapdaeps 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 791 -IWSLKSQITQAE-------------NITLGAPIANTRIYILD-NEGHPVPQGVDGELYIAGDGVAQGYDGQPELNAQFF 855
Cdd:PRK12476 375 vVYLDREQLGAGRavrvaadapnavaHVSCGQVARSQWAVIVDpDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTF 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 856 LSEPGV------------PGGRMFRTGDL-VRSDaqGQLFFVGRKDSQIKLRGYRIELGEIERTLA------RHPHVDA- 915
Cdd:PRK12476 455 GAKLQSrlaegshadgaaDDGTWLRTGDLgVYLD--GELYITGRIADLIVIDGRNHYPQDIEATVAeaspmvRRGYVTAf 532
|
490 500
....*....|....*....|
gi 1288439980 916 ----------AVVAciERAP 925
Cdd:PRK12476 533 tvpaednerlVIVA--ERAA 550
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
526-922 |
3.22e-07 |
|
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: 55.05 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 526 TLTYAELWARVQFIAMRFRAH-GIQPGDRIGVLLPRHRDVIATMLATWFVGACYVPFDIHQPAARLQRL-----MQRARL 599
Cdd:cd05905 14 TLTWGKLLSRAEKIAAVLQKKvGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLlgtckVRVALT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 600 VCLVVRQP-------GEWGEIVQLSLPELMQDMSNA-------IRYSTPCALL-PDMQAYLLFTSGSTGEPKGVCVVHRG 664
Cdd:cd05905 94 VEACLKGLpkkllksKTAAEIAKKKGWPKILDFVKIpkskrskLKKWGPHPPTrDGDTAYIEYSFSSDGSLSGVAVSHSS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 665 LLNLLLDMQRTFAVGSQDRLLSVTTPTFDISF-LEYLLPLISGASLYLteaeraadsfrmIPliadyrPTLMQATPSFW- 742
Cdd:cd05905 174 LLAHCRALKEACELYESRPLVTVLDFKSGLGLwHGCLLSVYSGHHTIL------------IP------PELMKTNPLLWl 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 743 HGL-------LMAGWRgDPELCVLAGGEALPTKVAEEL-LRC-------CGSLWNLY----------------------- 784
Cdd:cd05905 236 QTLsqykvrdAYVKLR-TLHWCLKDLSSTLASLKNRDVnLSSlrmcmvpCENRPRISscdsflklfqtlglspravstef 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 785 --------------GPTETTIWSLKSQITQAE----------NITL---GAPIANTRIYILDNEGhPVPQGVD--GELYI 835
Cdd:cd05905 315 gtrvnpficwqgtsGPEPSRVYLDMRALRHGVvrlderdkpnSLPLqdsGKVLPGAQVAIVNPET-KGLCKDGeiGEIWV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 836 AGDGVAQGYDGQP-ELNAQF-----FLSEPGVPGGRMFRTGDL----------VRSDAQGQLFFVGRKDSQIKLRGYRIE 899
Cdd:cd05905 394 NSPANASGYFLLDgETNDTFkvfpsTRLSTGITNNSYARTGLLgflrptkctdLNVEEHDLLFVVGSIDETLEVRGLRHH 473
|
490 500
....*....|....*....|....
gi 1288439980 900 LGEIERT-LARHPHVDAAVVACIE 922
Cdd:cd05905 474 PSDIEATvMRVHPYRGRCAVFSIT 497
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
902-976 |
4.46e-07 |
|
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: 48.69 E-value: 4.46e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1288439980 902 EIERTLARHPHV-DAAVVAcIERAPLHKALAAFIITSEPPSLFEQ-LKNELRQQLPDYMVPTLWQRVADFPNTDNGK 976
Cdd:pfam13193 1 EVESALVSHPAVaEAAVVG-VPDELKGEAPVAFVVLKPGVELLEEeLVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
784-989 |
8.65e-07 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 53.46 E-value: 8.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 784 YGPTETT--IWSLKSQITQAENITLGAPIANTRIYILDNEghpvpqgvDGELYIAGDGVAQGYdGQPELNAQfflsepgv 861
Cdd:PRK07445 261 YGMTETAsqIATLKPDDFLAGNNSSGQVLPHAQITIPANQ--------TGNITIQAQSLALGY-YPQILDSQ-------- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 862 pggRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERT-LARHPHVDAAVVAcIERAPLHKALAAFIITSEPP 940
Cdd:PRK07445 324 ---GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAiLATGLVQDVCVLG-LPDPHWGEVVTAIYVPKDPS 399
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1288439980 941 SLFEQLKNELRQQLPDYMVPTLWQRVADFPNTDNGKIDRKRLAENFVAD 989
Cdd:PRK07445 400 ISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQR 448
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
996-1072 |
8.90e-07 |
|
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: 48.40 E-value: 8.90e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1288439980 996 QTQALSDTEQMLLALWMRYLPIKNVDPECDFFRLGGHSLLAVTLVAEINRTFHCALTLKDIFHYSTLRALSARIAQQ 1072
Cdd:smart00823 9 RRRLLLDLVREQVAAVLGHAAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAAE 85
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
527-918 |
1.38e-06 |
|
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: 52.99 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 527 LTYAELWARVQFIAMRFRAHGI--QPGDRIGVLLPRHRDVIATMLATWFVGACYVPF-DIHQPAArLQRLMQRARLVCLV 603
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLyDTLGPEA-IEYILNHAEISIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 604 VrQPGewgeIVQLSLPELMQDMSNAIRYSTPCAllPDMQAYLLFTSGSTGEPKGVCVVHRGLLN----LLLDMQRTFAVG 679
Cdd:cd05927 85 C-DAG----VKVYSLEEFEKLGKKNKVPPPPPK--PEDLATICYTSGTTGNPKGVMLTHGNIVSnvagVFKILEILNKIN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 680 SQDRLlsvttptfdISFleylLPLisgASLYlteaERAADSFRM------------IPLIAD----YRPTLMQATPSFW- 742
Cdd:cd05927 158 PTDVY---------ISY----LPL---AHIF----ERVVEALFLyhgakigfysgdIRLLLDdikaLKPTVFPGVPRVLn 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 743 --HGLLMAGWRGDPEL--------------------------------------------CVLAGGEALPTKVaEELLR- 775
Cdd:cd05927 218 riYDKIFNKVQAKGPLkrklfnfalnyklaelrsgvvraspfwdklvfnkikqalggnvrLMLTGSAPLSPEV-LEFLRv 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 776 --CCGSLWNlYGPTETTIWSLKSqiTQAENI--TLGAPIANTRIYILDneghpVPQ-GVD-------GELYIAGDGVAQG 843
Cdd:cd05927 297 alGCPVLEG-YGQTECTAGATLT--LPGDTSvgHVGGPLPCAEVKLVD-----VPEmNYDakdpnprGEVCIRGPNVFSG 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1288439980 844 YDGQPELNAQFFLSEpGvpggrMFRTGDLVRSDAQGQLFFVGRKDSQIKL-RGYRIELGEIERTLARHPHVDAAVV 918
Cdd:cd05927 369 YYKDPEKTAEALDED-G-----WLHTGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSPFVAQIFV 438
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1550-1595 |
1.03e-05 |
|
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: 49.81 E-value: 1.03e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1288439980 1550 LHHGLLRQAALTPQETALISPIRELTYRQLSTAADHVARALLALGV 1595
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGV 46
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
645-982 |
2.84e-05 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 48.69 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 645 LLFTSGSTGEPKGVCVVHRGLLnlLLDMQRTFAVGSQDRLLSV-TTPTFDISFLEYL--LPLISGASLYLTEAERAAdsf 721
Cdd:PLN02479 200 LGYTSGTTASPKGVVLHHRGAY--LMALSNALIWGMNEGAVYLwTLPMFHCNGWCFTwtLAALCGTNICLRQVTAKA--- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 722 rMIPLIADYRPTLMQATPSFWHGLLMAGWRGD----PELC-VLAGGEALPTKVAEELLRCCGSLWNLYGPTET----TI- 791
Cdd:PLN02479 275 -IYSAIANYGVTHFCAAPVVLNTIVNAPKSETilplPRVVhVMTAGAAPPPSVLFAMSEKGFRVTHTYGLSETygpsTVc 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 792 -----WSLKSQITQAE-NITLGAP-IANTRIYILDNE-GHPVPQ--GVDGELYIAGDGVAQGYDGQPELNAQFFlsepgv 861
Cdd:PLN02479 354 awkpeWDSLPPEEQARlNARQGVRyIGLEGLDVVDTKtMKPVPAdgKTMGEIVMRGNMVMKGYLKNPKANEEAF------ 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 862 pGGRMFRTGDLVRSDAQGQLFFVGRKDSQIKLRGYRIELGEIERTLARHPHV-DAAVVAcieRAPLH--KALAAFII--- 935
Cdd:PLN02479 428 -ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVlEASVVA---RPDERwgESPCAFVTlkp 503
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1288439980 936 ---TSEPPSLFEQLKNELRQQLPDYMVPtlwqRVADF---PNTDNGKIDRKRL 982
Cdd:PLN02479 504 gvdKSDEAALAEDIMKFCRERLPAYWVP----KSVVFgplPKTATGKIQKHVL 552
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
1550-1595 |
3.25e-05 |
|
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: 48.47 E-value: 3.25e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1288439980 1550 LHHGLLRQAALTPQETALISPIRELTYRQLSTAADHVARALLALGV 1595
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGV 46
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
1552-1595 |
4.41e-05 |
|
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: 48.04 E-value: 4.41e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1288439980 1552 HGLL-RQAALTPQETALISPIRELTYRQLSTAADHVARALLALGV 1595
Cdd:cd17646 1 HALVaEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGV 45
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
784-939 |
6.47e-05 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 47.80 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 784 YGPTETTIWSLKSQITQAENITLGAPIANTRIYILD-NEG------HPVPQGvdgELYIAGDGVAQGY-DGQPELNAQFF 855
Cdd:PLN02387 452 YGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSwEEGgylisdKPMPRG---EIVIGGPSVTLGYfKNQEKTDEVYK 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 856 LSEPGVpggRMFRTGDLVRSDAQGQLFFVGRKDSQIKLR-GYRIELGEIERTLARHPHVDAAVVaciERAPLHKALAAFI 934
Cdd:PLN02387 529 VDERGM---RWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAALSVSPYVDNIMV---HADPFHSYCVALV 602
|
....*
gi 1288439980 935 ITSEP 939
Cdd:PLN02387 603 VPSQQ 607
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1556-1595 |
6.79e-05 |
|
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: 47.20 E-value: 6.79e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1288439980 1556 RQAALTPQETALISPIRELTYRQLSTAADHVARALLALGV 1595
Cdd:cd12117 5 EQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGV 44
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
549-985 |
8.72e-05 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 47.40 E-value: 8.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 549 QPGDRIGVLLPRhrdviATMLATWFVGACY---VPFDIHQPA--ARLQRLMQRARLVCLVV-RQPGEWGEIVQLS----- 617
Cdd:PRK08043 253 VEGERIGLMLPN-----ATISAAVIFGASLrrrIPAMMNYTAgvKGLTSAITAAEIKTIFTsRQFLDKGKLWHLPeqltq 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 618 -----LPELMQDMSNAIRYSTPCALL----------PDMQAYLLFTSGSTGEPKGVCVVHRGLL-NllLDMQRTFA-VGS 680
Cdd:PRK08043 328 vrwvyLEDLKDDVTTADKLWIFAHLLmprlaqvkqqPEDAALILFTSGSEGHPKGVVHSHKSLLaN--VEQIKTIAdFTP 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 681 QDRLLSvTTPTFDiSF---LEYLLPLISGASLYLTEAERaadSFRMIP-LIADYRPTLMQATPSFW-------HGLLMAG 749
Cdd:PRK08043 406 NDRFMS-ALPLFH-SFgltVGLFTPLLTGAEVFLYPSPL---HYRIVPeLVYDRNCTVLFGTSTFLgnyarfaNPYDFAR 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 750 WRgdpelCVLAGGEALPTKVAEellrccgsLWNL---------YGPTETtiwslksqitqAENITLGAPIA---NTRIYI 817
Cdd:PRK08043 481 LR-----YVVAGAEKLQESTKQ--------LWQDkfglrilegYGVTEC-----------APVVSINVPMAakpGTVGRI 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 818 L---DNEGHPVPqGVD--GELYIAGDGVAQGY---DGQPELNAQFFLSEPGVPGGRMFRTGDLVRSDAQGQLFFVGRKDS 889
Cdd:PRK08043 537 LpgmDARLLSVP-GIEqgGRLQLKGPNIMNGYlrvEKPGVLEVPTAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKR 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 890 QIKLRGYRIELGEIER-TLARHPHVDAAVVAcieRAPLHKALAAFIITSEPPSLFEQLKNELRQQ-LPDYMVPTLWQRVA 967
Cdd:PRK08043 616 FAKIAGEMVSLEMVEQlALGVSPDKQHATAI---KSDASKGEALVLFTTDSELTREKLQQYAREHgVPELAVPRDIRYLK 692
|
490 500
....*....|....*....|.
gi 1288439980 968 DFPNTDNGKID---RKRLAEN 985
Cdd:PRK08043 693 QLPLLGSGKPDfvtLKSMVDE 713
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1556-1595 |
2.98e-04 |
|
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: 45.41 E-value: 2.98e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1288439980 1556 RQAALTPQETALISPIRELTYRQLSTAADHVARALLALGV 1595
Cdd:cd17651 3 RQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGV 42
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1550-1595 |
2.99e-04 |
|
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: 45.52 E-value: 2.99e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1288439980 1550 LHHGLLRQAALTPQETALISPIRELTYRQLSTAADHVARALLALGV 1595
Cdd:COG1021 27 LGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGL 72
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
1554-1595 |
4.03e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 44.92 E-value: 4.03e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1288439980 1554 LLRQAALTPQETALISPIRELTYRQLSTAADHVARALLALGV 1595
Cdd:PRK08316 17 LRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGL 58
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
1554-1595 |
5.80e-04 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 44.42 E-value: 5.80e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1288439980 1554 LLRQAALTPQETALISPIREL--TYRQLSTAADHVARALLALGV 1595
Cdd:PRK08315 22 LDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGI 65
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1554-1595 |
6.93e-04 |
|
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: 44.14 E-value: 6.93e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1288439980 1554 LLRQAALTPQETALISPIRELTYRQLSTAADHVARALLALGV 1595
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGV 42
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1554-1595 |
1.11e-03 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 43.45 E-value: 1.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1288439980 1554 LLRQAALTPQETAL-ISPIRELTYRQLSTAADHVARALLALGV 1595
Cdd:pfam00501 1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGV 43
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
753-899 |
1.63e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 43.17 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 753 DPELCV-LAGGEALPTKVAEELlrccGSLWNL-----YGPTETT--IWSLKSQITQAENItlGAPIA-NTRIYILDNEGH 823
Cdd:PTZ00342 460 NPNLEViLNGGGKLSPKIAEEL----SVLLNVnyyqgYGLTETTgpIFVQHADDNNTESI--GGPISpNTKYKVRTWETY 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 824 P----VPQGvdgELYIAGDGVAQGYDGQPELNAQFFLSEpgvpggRMFRTGDLVRSDAQGQLFFVGRKDSQIKL-RGYRI 898
Cdd:PTZ00342 534 KatdtLPKG---ELLIKSDSIFSGYFLEKEQTKNAFTED------GYFKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYI 604
|
.
gi 1288439980 899 E 899
Cdd:PTZ00342 605 E 605
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
1554-1595 |
2.15e-03 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 42.73 E-value: 2.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1288439980 1554 LLRQAALTPQETALISP------IRELTYRQLSTAADHVARALLALGV 1595
Cdd:PRK13295 30 LDACVASCPDKTAVTAVrlgtgaPRRFTYRELAALVDRVAVGLARLGV 77
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1554-1595 |
4.43e-03 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 41.62 E-value: 4.43e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1288439980 1554 LLRQAALTPQETALISPI----RELTYRQLSTAADHVARALLALGV 1595
Cdd:COG1022 17 LRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALGV 62
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
1097-1363 |
5.25e-03 |
|
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: 41.13 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1097 FPLTDVQRA-YWLGRQTGATSIATHIYhEFDvEHFNVTRFTHAVNALIARHEMLRARVLPD----GTQQILAQVPAYQLE 1171
Cdd:cd19545 2 YPCTPLQEGlMALTARQPGAYVGQRVF-ELP-PDIDLARLQAAWEQVVQANPILRTRIVQSdsggLLQVVVKESPISWTE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1172 QRDLSALSPNARnDALMAIRDRLSHHvhpADRWPLFDFSYSACTAQHGrlhfsldllIADALSMRTLQQELMMLYREPHV 1251
Cdd:cd19545 80 STSLDEYLEEDR-AAPMGLGGPLVRL---ALVEDPDTERYFVWTIHHA---------LYDGWSLPLILRQVLAAYQGEPV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 1252 SLPLlpfSFRDYVQALLVEQASEAyardQAYWQRalpQLYGP-----PTLPVQGDLAQLSAIRFVRRRHRLSAhnwgvls 1326
Cdd:cd19545 147 PQPP---PFSRFVKYLRQLDDEAA----AEFWRS---YLAGLdpavfPPLPSSRYQPRPDATLEHSISLPSSA------- 209
|
250 260 270
....*....|....*....|....*....|....*..
gi 1288439980 1327 alaqRTRITKTALLLTVFSQVLARWSLSPTFTLNLTL 1363
Cdd:cd19545 210 ----SSGVTLATVLRAAWALVLSRYTGSDDVVFGVTL 242
|
|
| PRK09294 |
PRK09294 |
phthiocerol/phthiodiolone dimycocerosyl transferase; |
46-243 |
5.49e-03 |
|
phthiocerol/phthiodiolone dimycocerosyl transferase;
Pssm-ID: 181765 [Multi-domain] Cd Length: 416 Bit Score: 41.23 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 46 PLSFNQERLWFLQKYDStatnynlYVVyRLHGVVDMPMLTEALRHVQARHAILRTRIIVRND-RPCQVIDDA--SSLVLD 122
Cdd:PRK09294 9 KLAPSEEVFARYEAFTG-------YTA-HLRGVLDIDALSDAFDALLRAHPVLAAHLEQDSDgGWELVADDLlhPGIVVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288439980 123 TVTLAAQAPTSALDaviQQVINTRFDLARGplwgvtqiiqpDQGCHLVFCAHHIIIDGISLRLLFDELQQQYARLhagNE 202
Cdd:PRK09294 81 DGDAARPLPELQLD---QGVSLLALDVVPD-----------DGGARVTLYIHHSIADAHHSASLLDELWSRYTDV---VT 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1288439980 203 TSLPPPPL-----QYADYAFWQR----------EWFQDTLLANELAYWR-ARLQDAP 243
Cdd:PRK09294 144 TGDPGPIRpqpapQSLEAVLAQRgirrqalsgaERFMPAMYAYELPPTPtAAVLAKP 200
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1562-1595 |
7.06e-03 |
|
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: 40.59 E-value: 7.06e-03
10 20 30
....*....|....*....|....*....|....
gi 1288439980 1562 PQETALISPIRELTYRQLSTAADHVARALLALGV 1595
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGV 34
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
1550-1595 |
9.24e-03 |
|
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: 40.60 E-value: 9.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1288439980 1550 LHHGLLRQAALTPQETALISPIRELTYRQLSTAADHVARALLALGV 1595
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGV 46
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1554-1595 |
9.74e-03 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 40.33 E-value: 9.74e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1288439980 1554 LLRQAALTPQETALISPIRELTYRQLSTAADHVARALLALGV 1595
Cdd:PRK03640 8 LKQRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGV 49
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
1553-1595 |
9.84e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 40.30 E-value: 9.84e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1288439980 1553 GLLRQAALT-PQETALISPIRELTYRQLSTAADHVARALLALGV 1595
Cdd:PRK07788 53 GLVAHAARRaPDRAALIDERGTLTYAELDEQSNALARGLLALGV 96
|
|
| |
