|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
44-2119 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 1578.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 44 PGPVPLAPGQAGIWFSEQLRPGTPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVFRlGPDGEPVQQTAPAAPVA 123
Cdd:PRK12467 47 FERIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFV-QDEEGFRQVIDASLSLT 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 124 LPVIDVT-------EADLPQALRTAAEQPFDLERGPLLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLLLADLARAYA-- 194
Cdd:PRK12467 126 IPLDDLAneqgrarESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSay 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 195 --GELPAGVAAP-AFRDVAAWQHGRLAAGELDDQLRYWRQRLAG-LPDLEIPGDRQRPADRDWRAHSVRRELPAATEAAV 270
Cdd:PRK12467 206 sqGREPSLPALPiQYADYAIWQRSWLEAGERERQLAYWQEQLGGeHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 271 RRLAAAHDTTPFTVLLAAYGTFLHRLTGQDDFAVGVPVAGRGRTDLESVVGLFAGMVPVRLDLTGRPSFDEVLSRTVAGS 350
Cdd:PRK12467 286 KALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTA 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 351 RNDFAHPQIPFDRLVRELRRDRIAGSQLLVQAMAGTESTAVALTFGEAAG----TEQPVDVA--LAKCDLDLSVLDDGDR 424
Cdd:PRK12467 366 LGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQNTATGGRDREGAQlpglTVEELSWArhTAQFDLALDTYESAQG 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 425 LAVTLVAAADLFTPAAAEQLAGQFLSLLAGLTGAPDRLVSEVDLLDTDELHTVLCRWNDTARPLPAASLRERFQQWCRRT 504
Cdd:PRK12467 446 LWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAPDCVHQLIEAQARQH 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 505 PGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLL 584
Cdd:PRK12467 526 PERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYML 605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 585 SDARPVLVVTDAATADRLG-PDDITGLVVLEETD-TGGYPATEP-PAVPAGHSAYVIYTSGSTGRPKGVVITRAALDNFL 661
Cdd:PRK12467 606 DDSGVRLLLTQSHLLAQLPvPAGLRSLCLDEPADlLCGYSGHNPeVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYV 685
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 662 AAMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALIDLAGRHRVTLAQATPTLWQALvpeL 741
Cdd:PRK12467 686 CVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQAL---L 762
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 742 SGPALAGIR----VLVGGEALPAELA---RRLGDaGAEVTNMYGPTETTIWSTSGPTSEDSIRRGS--IGVPIDNTQVYV 812
Cdd:PRK12467 763 QASRVALPRpqraLVCGGEALQVDLLarvRALGP-GARLINHYGPTETTVGVSTYELSDEERDFGNvpIGQPLANLGLYI 841
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 813 LDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFGPPGTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGF 892
Cdd:PRK12467 842 LDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGF 921
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 893 RIELGEIETTLInAGPVRRAAAVVREDRPGDLRLVAYVIPDGP-------VAPDALRTELSRTLPDYMIPAVIVPVPDFP 965
Cdd:PRK12467 922 RIELGEIEARLL-AQPGVREAVVLAQPGDAGLQLVAYLVPAAVadgaehqATRDELKAQLRQVLPDYMVPAHLLLLDSLP 1000
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 966 TTPNGKLDRAALPAPDYGT-RSTARPPRDDRERFLCTAFAEVLGLPEVAVSDNFFELGGHSLLAFRLLARIRDEFGAGFS 1044
Cdd:PRK12467 1001 LTPNGKLDRKALPKPDASAvQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVP 1080
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1045 LRRLLAAPTVAAVAAELAAETSTGDDAvhLAPVPRDEPLPLSPMQESIWLADQVSAGDSVYNVPLALRLIGPLDRGALRR 1124
Cdd:PRK12467 1081 LRTLFEHQTLAGFAQAVAAQQQGAQPA--LPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALER 1158
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1125 TLNRVVDRHEMLRTRIHPgPDGMPVQVADPAGGGA---ALTERDAAPGTDLAQLLLAEAALGFTLATEHPLRAVLWRLDE 1201
Cdd:PRK12467 1159 SFDALVARHESLRTTFVQ-EDGRTRQVIHPVGSLTleePLLLAADKDEAQLKVYVEAEARQPFDLEQGPLLRVGLLRLAA 1237
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1202 REHVLLLTAHHVAVDAWSMDLIQRDLTELYAADTGHREPELDEPALAQADYAVWQRQSAQRGRYAAELDFWRTELTGAVA 1281
Cdd:PRK12467 1238 DEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQP 1317
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1282 T-EVAGDLPRPATPGGGGGAVEFALAPRQIQGIRELARRCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGRGNPRLD 1360
Cdd:PRK12467 1318 VlELPTDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETE 1397
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1361 NLVGCLVNTVVLRGDLSGAPTFHELLRRTHARTADALAHQELPFEHLV----ADRGAGNGPLFRIMYSFSSQ-EPAGRSA 1435
Cdd:PRK12467 1398 GLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVealqPERSLSHSPLFQVMFNHQRDdHQAQAQL 1477
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1436 GDVDLEPVPVPVTTCKFDLVLTVVDGGSTLEGVLEYADDLYLPGTAERLVTSLTNLLAAAVRTPELAVTRLAITSESDTV 1515
Cdd:PRK12467 1478 PGLSVESLSWESQTAQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERR 1557
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1516 RT-SRWGRSEQHVGDDRTVHQLVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLD 1594
Cdd:PRK12467 1558 QIlEGWNATHTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLI--ALG---VGPEVLVGIAVE 1632
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1595 RSPELVVAMLAVLKAGGYFIPVDPGYPMARLTRIADTVTPALVLTRTGQGGCLPGAEvfgDVPVVALDRVADRLTAMPDQ 1674
Cdd:PRK12467 1633 RSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLPD---GLRSLVLDQEDDWLEGYSDS 1709
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1675 RPEVTVDPRGLAYSIFTSGSTGQPKGVAVEHIGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMSALFEPLVSGRGVTL 1754
Cdd:PRK12467 1710 NPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVI 1789
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1755 MPADATLAdlAEELSGPLAYDYIRL---TPSHLRHLVGHWTGQELPPAARGWVVGGETLDPALVKQLLELRPDAEVINHY 1831
Cdd:PRK12467 1790 APPGAHRD--PEQLIQLIERQQVTTlhfVPSMLQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLY 1867
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1832 GPTETVIGRVVHPVREAGELAVDSpLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPD 1911
Cdd:PRK12467 1868 GPTETAVDVTHWTCRRKDLEGRDS-VPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVAD 1946
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1912 PAGEPGARMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRD----QQLVGWFIP-- 1985
Cdd:PRK12467 1947 PFGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDgangKQLVAYVVPtd 2026
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1986 ----AEDHPPVTV-SALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRALPGPTSGRPelEDRYQAPRTPGEQLLAE 2060
Cdd:PRK12467 2027 pglvDDDEAQVALrAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASEL--QQAYVAPQSELEQRLAA 2104
|
2090 2100 2110 2120 2130
....*....|....*....|....*....|....*....|....*....|....*....
gi 653678460 2061 LWSTVLGTDRIGIEDNFFDLGGTSISVIQLSGACRRAGVEISPKDVFEQPTVRGQAMRA 2119
Cdd:PRK12467 2105 IWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLAAVA 2163
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
32-2129 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 1323.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 32 GPAHGGGLPVQPPGPVPLAPGQAGIWFSEQLRPGTPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVFrLGPDGE 111
Cdd:PRK05691 661 GAAQAAIARLPRGQALPQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRF-YERDGV 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 112 PVQQTAPAAPVALPVIDVTeaDLPQALRTA---------AEQPFDLERGPLLRACLHRIGAKQHVLLVTVHHIVLDGWSC 182
Cdd:PRK05691 740 ALQRIDAQGEFALQRIDLS--DLPEAEREAraaqireeeARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSL 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 183 GLLLADLARAYAGE---LPAGVAAPAFR--DVAAWQHGRLAAGELDDQLRYWRQRLAG-LPDLEIPGDRQRPADRDWRAH 256
Cdd:PRK05691 818 NILLDEFSRLYAAAcqgQTAELAPLPLGyaDYGAWQRQWLAQGEAARQLAYWKAQLGDeQPVLELATDHPRSARQAHSAA 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 257 SVRRELPAATEAAVRRLAAAHDTTPFTVLLAAYGTFLHRLTGQDDFAVGVPVAGRGRTDLESVVGLFAGMVPVRLDLTGR 336
Cdd:PRK05691 898 RYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGR 977
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 337 PSFDEVLSRTVAGSRNDFAHPQIPFDRLVRELRRdriAGSQLLVQAMAGTES---TAVALTFGEAAgTEQPVDVALAKCD 413
Cdd:PRK05691 978 LPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQ---AREQGLFQVMFNHQQrdlSALRRLPGLLA-EELPWHSREAKFD 1053
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 414 LDL-SVLDDGDRLAVTLVAAADLFTPAAAEQLAGQFLSLLAGLTGAPDRLVSEVDLLDTDELHTvLCRWNDTARPLPAAS 492
Cdd:PRK05691 1054 LQLhSEEDRNGRLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQ-LAQWGQAPCAPAQAW 1132
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 493 LRERFQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPID 572
Cdd:PRK05691 1133 LPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLD 1212
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 573 PDFPVERIAYLLSDARPVLVVTDAATADRLGPDDITGLVVLEETDTGGYPATEPP-AVPAGHSAYVIYTSGSTGRPKGVV 651
Cdd:PRK05691 1213 PDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALDSLHLDSWPSQAPGlHLHGDNLAYVIYTSGSTGQPKGVG 1292
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 652 ITRAALDNFLAAMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALIDLAGRHRVTLAQATP 731
Cdd:PRK05691 1293 NTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVP 1372
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 732 TLWQALVPElsgPALAGI----RVLVGGEALPAELARRLGDAGAEVT--NMYGPTETTIWSTSGPTSEDSIRRGSIGVPI 805
Cdd:PRK05691 1373 PLLQLFIDE---PLAAACtslrRLFSGGEALPAELRNRVLQRLPQVQlhNRYGPTETAINVTHWQCQAEDGERSPIGRPL 1449
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 806 DNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFGPPGTRMYRTGDLVRWSAAGDLEYLGRTDH 885
Cdd:PRK05691 1450 GNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGEDGARLYRTGDRARWNADGALEYLGRLDQ 1529
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 886 QVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDlRLVAYVIPDG--PVAPDALRTELSRTLPDYMIPAVIVPVPD 963
Cdd:PRK05691 1530 QVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGA-QLVGYYTGEAgqEAEAERLKAALAAELPEYMVPAQLIRLDQ 1608
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 964 FPTTPNGKLDRAALPAPDYGTRSTARpPRDDRERFLCTAFAEVLGLPEVAVSDNFFELGGHSLLAFRLLARIRDEFGAGF 1043
Cdd:PRK05691 1609 MPLGPSGKLDRRALPEPVWQQREHVE-PRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVEL 1687
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1044 SLRRLLAAPTVAAVAAELAAETSTGDDAVH--LAPVPRDEPLPLSPMQESIWLADQVSAGDSVYNVPLALRLIGPLDRGA 1121
Cdd:PRK05691 1688 PLRALFEASELGAFAEQVARIQAAGERNSQgaIARVDRSQPVPLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDR 1767
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1122 LRRTLNRVVDRHEMLRTRIhPGPDGMPVQ-VADPAGGGAALTERDAAPGTDLAQLLLAEAALG----FTLATEHPLRAVL 1196
Cdd:PRK05691 1768 FEAALQALILRHETLRTTF-PSVDGVPVQqVAEDSGLRMDWQDFSALPADARQQRLQQLADSEahqpFDLERGPLLRACL 1846
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1197 WRLDEREHVLLLTAHHVAVDAWSMDLIQRDLTELYAADTGHREPELDEPALAQADYAVWQRQSAQRGRYAAELDFWRTEL 1276
Cdd:PRK05691 1847 VKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDRESPLEPLPVQYLDYSVWQRQWLESGERQRQLDYWKAQL 1926
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1277 -TGAVATEVAGDLPRPATPGGGGGAVEFALAPRQIQGIRELARRCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGRG 1355
Cdd:PRK05691 1927 gNEHPLLELPADRPRPPVQSHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRI 2006
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1356 NPRLDNLVGCLVNTVVLRGDLSGAPTFHELLRRTHARTADALAHQELPFEHLV----ADRGAGNGPLFRIM-----YSF- 1425
Cdd:PRK05691 2007 RPESEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVealqPPRSAAYNPLFQVMcnvqrWEFq 2086
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1426 SSQEPAGrsagdVDLEPVPVPVTTCKFDLVLTVVDGGSTLEGVLEYADDLYLPGTAERLVTSLTNLLAAAVRTPELAVTR 1505
Cdd:PRK05691 2087 QSRQLAG-----MTVEYLVNDARATKFDLNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAE 2161
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1506 LAITSESD-TVRTSRWGRSEQHVGDDRTVHQLVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHtgalgAPPVG 1584
Cdd:PRK05691 2162 LPLLAAAEqQQLLDSLAGEAGEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALR-----ERGVG 2236
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1585 PETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMARLTRIADTVTPALVLtrtGQGGCLpgaEVFGDVPV-VA--- 1660
Cdd:PRK05691 2237 PQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLL---SDRALF---EALGELPAgVArwc 2310
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1661 LDRVADRLTAMPDQRPEVTVDPRGLAYSIFTSGSTGQPKGVAVEHIGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMS 1740
Cdd:PRK05691 2311 LEDDAAALAAYSDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASE 2390
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1741 ALFEPLVSGRGVTLMPADATLADLAEELSGPLAYDYIRLTPSHLRHLVGHWTGQELPPAARGWVVGGETLDPALVKQLLE 1820
Cdd:PRK05691 2391 RLLVPLLCGARVVLRAQGQWGAEEICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGGEALTGEHLQRIRQ 2470
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1821 LRPDAEVINHYGPTETVIGRVVHPVREAGELAVDSpLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGR 1900
Cdd:PRK05691 2471 AFAPQLFFNAYGPTETVVMPLACLAPEQLEEGAAS-VPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDR 2549
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1901 PALTAEKFLPDPAGEPGARMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRD---- 1976
Cdd:PRK05691 2550 PGLTAERFVADPFAADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDtpsg 2629
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1977 QQLVGWFIPA-----EDHPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRALPGPTsgrPEL-EDRYQAP 2050
Cdd:PRK05691 2630 KQLAGYLVSAvagqdDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPD---PELnRQAYQAP 2706
|
2090 2100 2110 2120 2130 2140 2150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 653678460 2051 RTPGEQLLAELWSTVLGTDRIGIEDNFFDLGGTSISVIQLSGACRRAGVEISPKDVFEQPTVrgQAMRAIARSRDDAYA 2129
Cdd:PRK05691 2707 RSELEQQLAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTV--QTLAAVATHSEAAQA 2783
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
38-2116 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 1296.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 38 GLPVqPPGPV----PLAPGQAGIWFSEQLRPGTPLYSVPLAVRLTGpLDVDALRAALDAVTARHEALRTVF-RLGPDGEP 112
Cdd:PRK12316 1545 ALPL-PAGEIadiyPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFlWQDGLEQP 1622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 113 VQQTAPAapVALPVIDV---TEADLPQALRTAA----EQPFDLERGPLLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLL 185
Cdd:PRK12316 1623 LQVIHKQ--VELPFAELdwrGREDLGQALDALAqaerQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQL 1700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 186 LADLARAYAGELPAGvAAPAFRDVAAW-QHGRLAAGElddqlRYWRQRLAGLPDLEIPGDRQRPADRDWRAHSVRRELPA 264
Cdd:PRK12316 1701 LGEVLQRYAGQPVAA-PGGRYRDYIAWlQRQDAAASE-----AFWKEQLAALEEPTRLAQAARTEDGQVGYGDHQQLLDP 1774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 265 ATEAAVRRLAAAHDTTPFTVLLAAYGTFLHRLTGQDDFAVGVPVAGRGR--TDLESVVGLFAGMVPV----RLDLTGRPS 338
Cdd:PRK12316 1775 AQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAelPGIEQQIGLFINTLPViaapRPDQSVADW 1854
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 339 FDEVLSRTVAgsRNDFAHPQIpfdrlvRELRRDRIAGSQLLVQAMAGTESTAVA----------LTFGEAAGTEQ---PV 405
Cdd:PRK12316 1855 LQEVQALNLA--LREHEHTPL------YDIQRWAGQGGEALFDSLLVFENYPVAealkqgapagLVFGRVSNHEQtnyPL 1926
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 406 DVALAKcdldlsvlddGDRLAVTLVAAADLFTPAAAEQLAGQFLSLLAGLTGAPDRLVSEVDLLDTDELHTVLCRWNDTA 485
Cdd:PRK12316 1927 TLAVTL----------GETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTP 1996
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 486 RPLPAA-SLRERFQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKA 564
Cdd:PRK12316 1997 EAYPRGpGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKA 2076
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 565 GAAYLPIDPDFPVERIAYLLSDARPVLVVTDAATADRLGPDdiTGLVVLEETDTG---GYPATEP-PAVPAGHSAYVIYT 640
Cdd:PRK12316 2077 GGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLP--AGVARLPLDRDAewaDYPDTAPaVQLAGENLAYVIYT 2154
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 641 SGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADaDTARNPAALIDLAG 720
Cdd:PRK12316 2155 SGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRD-DELWDPEQLYDEME 2233
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 721 RHRVTLAQATPTLWQALVPEL--SGPALAGIRVLVGGEALPAELARRLGDA--GAEVTNMYGPTETTIWST---SGPTSE 793
Cdd:PRK12316 2234 RHGVTILDFPPVYLQQLAEHAerDGRPPAVRVYCFGGEAVPAASLRLAWEAlrPVYLFNGYGPTEAVVTPLlwkCRPQDP 2313
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 794 DSIRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFGPPGTRMYRTGDLVRWSA 873
Cdd:PRK12316 2314 CGAAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGERLYRTGDLARYRA 2393
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 874 AGDLEYLGRTDHQVKLRGFRIELGEIETTLInAGPVRRAAAVVREDRPGDLRLVAYVIPDGPVA--PDALRTELSRTLPD 951
Cdd:PRK12316 2394 DGVVEYLGRIDHQVKIRGFRIELGEIEARLQ-AHPAVREAVVVAQDGASGKQLVAYVVPDDAAEdlLAELRAWLAARLPA 2472
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 952 YMIPAVIVPVPDFPTTPNGKLDRAALPAPDYGTRSTA-RPPRDDRERFLCTAFAEVLGLPEVAVSDNFFELGGHSLLAFR 1030
Cdd:PRK12316 2473 YMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAyVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQ 2552
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1031 LLARIRDEFGAGFSLRRLLAAPTVAAVAAELAAETSTgdDAVHLAPVPRDEPLPLSPMQESIWLADQVSAGDSVYNVPLA 1110
Cdd:PRK12316 2553 VVSRVRQDLGLEVPLRILFERPTLAAFAASLESGQTS--RAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSA 2630
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1111 LRLIGPLDRGALRRTLNRVVDRHEMLRTRIHPGPDGMPVQVADPAGGGAALTERDAAPGTDLAQLLLAEAALGFTLATEH 1190
Cdd:PRK12316 2631 LHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGP 2710
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1191 PLRAVLWRLDEREHVLLLTAHHVAVDAWSMDLIQRDLTELYAADTGHREPELDEPALAQADYAVWQRQSAQRGRYAAELD 1270
Cdd:PRK12316 2711 LLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYADYAAWQRAWMDSGEGARQLD 2790
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1271 FWRTELTGA-VATEVAGDLPRPATPGGGGGAVEFALAPRQIQGIRELARRCGTTVSTVVLSALQTLLYRITGGADVVIGS 1349
Cdd:PRK12316 2791 YWRERLGGEqPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGV 2870
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1350 TVSGRGNPRLDNLVGCLVNTVVLRGDLSGAPTFHELLRRTHARTADALAHQELPFEHLVA----DRGAGNGPLFRIMYSF 1425
Cdd:PRK12316 2871 PIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEalqpERSLSHSPLFQVMYNH 2950
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1426 SSQEPAGRSAGDVDLEPVPVPVTTCKFDLVLTVVDGGSTLEGVLEYADDLYLPGTAERLVTSLTNLLAAAVRTPELAVTR 1505
Cdd:PRK12316 2951 QSGERAAAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDE 3030
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1506 LAITSESDTVR-TSRWGRSEQHVGDDRTVHQLVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHtgalgAPPVG 1584
Cdd:PRK12316 3031 LAMLDAEERGQlLEAWNATAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLI-----ERGVG 3105
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1585 PETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMARLTRIADTVTPALVLTRTGqggcLPGAEVFGdVPVVALDRV 1664
Cdd:PRK12316 3106 PDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSH----LRLPLAQG-VQVLDLDRG 3180
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1665 ADRLTampDQRPEVTVDPRGLAYSIFTSGSTGQPKGVAVEHIGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMSALFE 1744
Cdd:PRK12316 3181 DENYA---EANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFW 3257
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1745 PLVSGRGVTLM-PADATLADLAEELSGPLAYDYIRLTPSHLRHLVGHWTGQELpPAARGWVVGGETLDPALVKQLLELRP 1823
Cdd:PRK12316 3258 PLMSGARVVLAgPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRC-TSLKRIVCGGEALPADLQQQVFAGLP 3336
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1824 daeVINHYGPTETVIGRVVHPVREAGElavdSPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPAL 1903
Cdd:PRK12316 3337 ---LYNLYGPTEATITVTHWQCVEEGK----DAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGL 3409
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1904 TAEKFLPDPAgEPGARMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVL-VRDQQLVGW 1982
Cdd:PRK12316 3410 TAERFVPDPF-VPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLaVDGRQLVAY 3488
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1983 FIPaEDHPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRALPGPTSGrpELEDRYQAPRTPGEQLLAELW 2062
Cdd:PRK12316 3489 VVP-EDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAA--LLQQDYVAPVNELERRLAAIW 3565
|
2090 2100 2110 2120 2130
....*....|....*....|....*....|....*....|....*....|....
gi 653678460 2063 STVLGTDRIGIEDNFFDLGGTSISVIQLSGACRRAGVEISPKDVFEQPTVRGQA 2116
Cdd:PRK12316 3566 ADVLKLEQVGLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQGLA 3619
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
39-1336 |
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: 963.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 39 LPVQPPGPVPLAPGQAGIWFSEQLRPGTPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVFRLgPDGEPVQQTAP 118
Cdd:COG1020 10 PPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRT-RAGRPVQVIQP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 119 AAPVALPVIDVT-------EADLPQALRTAAEQPFDLERGPLLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLLLADLAR 191
Cdd:COG1020 89 VVAAPLPVVVLLvdlealaEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 192 AY-----AGELPAGVAAPAFRDVAAWQHGRLAAGELDDQLRYWRQRLAGLPD-LEIPGDRQRPADRDWRAHSVRRELPAA 265
Cdd:COG1020 169 LYlaayaGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPlLELPTDRPRPAVQSYRGARVSFRLPAE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 266 TEAAVRRLAAAHDTTPFTVLLAAYGTFLHRLTGQDDFAVGVPVAGRGRTDLESVVGLFAGMVPVRLDLTGRPSFDEVLSR 345
Cdd:COG1020 249 LTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLAR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 346 TVAGSRNDFAHPQIPFDRLVRELRRDRIAGSQLLVQAMAGTESTAV-ALTFGEAAGTEQPVDVALAKCDLDLSVLDDGDR 424
Cdd:COG1020 329 VRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPAdELELPGLTLEPLELDSGTAKFDLTLTVVETGDG 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 425 LAVTLVAAADLFTPAAAEQLAGQFLSLLAGLTGAPDRLVSEVDLLDTDELHTVLCRWNDTARPLPA-ASLRERFQQWCRR 503
Cdd:COG1020 409 LRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPAdATLHELFEAQAAR 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 504 TPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYL 583
Cdd:COG1020 489 TPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYM 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 584 LSDARPVLVVTDAATADRLgPDDITGLVVLEETDTGGYPATEPPA-VPAGHSAYVIYTSGSTGRPKGVVITRAALDNFLA 662
Cdd:COG1020 569 LEDAGARLVLTQSALAARL-PELGVPVLALDALALAAEPATNPPVpVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLA 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 663 AMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALIDLAGRHRVTLAQATPTLWQALVPELS 742
Cdd:COG1020 648 WMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAP 727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 743 GPALAGIRVLVGGEALPAELARRLGDA--GAEVTNMYGPTETTIWSTSGPTSEDSIRRGS--IGVPIDNTQVYVLDANLH 818
Cdd:COG1020 728 EALPSLRLVLVGGEALPPELVRRWRARlpGARLVNLYGPTETTVDSTYYEVTPPDADGGSvpIGRPIANTRVYVLDAHLQ 807
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 819 PAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFGPPGTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGE 898
Cdd:COG1020 808 PVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGE 887
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 899 IETTLINAGPVRRAAAVVREDRPGDLRLVAYVIPDG--PVAPDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAA 976
Cdd:COG1020 888 IEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAgaAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLA 967
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 977 LPAPDYGTRSTARPPRDDRERFLCTAFAEVLGLPEVAVSDNFFELGGHSLLAFRLLARIRDEFGAGFSLRRLLAAPTVAA 1056
Cdd:COG1020 968 LPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAA 1047
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1057 VAAELAAETSTGDDAVHLAPVPRDEPLPLSPMQESIWLADQVSAGDSVYNVPLALRLIGPLDRGALRRTLNRVVDRHEML 1136
Cdd:COG1020 1048 AAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRA 1127
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1137 RTRIHPGPDGMPVQVADPAGGGAALTERDAAPGTDLAQLLLAEAALGFTLATEHPLRAVLWRLDEREHVLLLTAHHVAVD 1216
Cdd:COG1020 1128 RRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLL 1207
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1217 AWSMDLIQRDLTELYAADTGHREPELDEPALAQADYAVWQRQSAQRGRYAAELDFWRTELTGAVATEVAGDLPRPATPGG 1296
Cdd:COG1020 1208 LLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALARAR 1287
|
1290 1300 1310 1320
....*....|....*....|....*....|....*....|
gi 653678460 1297 GGGAVEFALAPRQIQGIRELARRCGTTVSTVVLSALQTLL 1336
Cdd:COG1020 1288 AARTARALALLLLLALLLLLALALALLLLLLLLLALLLLA 1327
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
31-1347 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 869.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 31 QGPAHGGGLPVQPPG-PVPLAPGQAGIWFSEQLRPGTPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVFRLgPD 109
Cdd:PRK12467 1100 QQQGAQPALPDVDRDqPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQ-ED 1178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 110 GEPVQQTAPAAPVA-----LPVIDVTEADLPQALRTAAEQPFDLERGPLLRACLHRIGAKQHVLLVTVHHIVLDGWSCGL 184
Cdd:PRK12467 1179 GRTRQVIHPVGSLTleeplLLAADKDEAQLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQV 1258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 185 LLADLARAYA----GELPAGVAAP-AFRDVAAWQHGRLAAGELDDQLRYWRQRLAG-LPDLEIPGDRQRPADRDWRAHSV 258
Cdd:PRK12467 1259 LVDELVALYAaysqGQSLQLPALPiQYADYAVWQRQWMDAGERARQLAYWKAQLGGeQPVLELPTDRPRPAVQSHRGARL 1338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 259 RRELPAATEAAVRRLAAAHDTTPFTVLLAAYGTFLHRLTGQDDFAVGVPVAGRGRTDLESVVGLFAGMVPVRLDLTGRPS 338
Cdd:PRK12467 1339 AFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQAS 1418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 339 FDEVLSRTVAGSRNDFAHPQIPFDRLVRELRRDRIAGSQLLVQAMAG--TESTAVALTFGEAAGTEQPVDVALAKCDLDL 416
Cdd:PRK12467 1419 FQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNhqRDDHQAQAQLPGLSVESLSWESQTAQFDLTL 1498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 417 SVLDDGDRLAVTLVAAADLFTPAAAEQLAGQFLSLLAGLTGAPDRLVSEVDLLDTDELHTVLCRWNDTARPLPAA-SLRE 495
Cdd:PRK12467 1499 DTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLArLVHQ 1578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 496 RFQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDF 575
Cdd:PRK12467 1579 LIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEY 1658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 576 PVERIAYLLSDARPVLVVTDAATADRLG-PDDITGLVVLEETD-TGGYPATEPPAVPAGHS-AYVIYTSGSTGRPKGVVI 652
Cdd:PRK12467 1659 PRERLAYMIEDSGIELLLTQSHLQARLPlPDGLRSLVLDQEDDwLEGYSDSNPAVNLAPQNlAYVIYTSGSTGRPKGAGN 1738
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 653 TRAALDNFLAAMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALIDLAGRHRVTLAQATPT 732
Cdd:PRK12467 1739 RHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPS 1818
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 733 LWQALV--PELSGPALAGIRVLVGGEALPAELAR----RLGDAGaeVTNMYGPTETTIWSTSGP-TSEDSIRRGS--IGV 803
Cdd:PRK12467 1819 MLQQLLqmDEQVEHPLSLRRVVCGGEALEVEALRpwleRLPDTG--LFNLYGPTETAVDVTHWTcRRKDLEGRDSvpIGQ 1896
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 804 PIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFGPPGTRMYRTGDLVRWSAAGDLEYLGRT 883
Cdd:PRK12467 1897 PIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGTVGSRLYRTGDLARYRADGVIEYLGRI 1976
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 884 DHQVKLRGFRIELGEIETTLINAGPVRRaAAVVREDRPGDLRLVAYVIPDGPVAPDA----------LRTELSRTLPDYM 953
Cdd:PRK12467 1977 DHQVKIRGFRIELGEIEARLREQGGVRE-AVVIAQDGANGKQLVAYVVPTDPGLVDDdeaqvalraiLKNHLKASLPEYM 2055
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 954 IPAVIVPVPDFPTTPNGKLDRAALPAPDYGTRSTA-RPPRDDRERFLCTAFAEVLGLPEVAVSDNFFELGGHSLLAFRLL 1032
Cdd:PRK12467 2056 VPAHLVFLARMPLTPNGKLDRKALPAPDASELQQAyVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVV 2135
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1033 ARIRDEfGAGFSLRRLLAAPTVAAVAAELaaetSTGDDAVHLAPVPRDEPLPLSPMQESIWlaDQVSAGDSVYNVPLALR 1112
Cdd:PRK12467 2136 SRARQA-GIRFTPKDLFQHQTVQSLAAVA----QEGDGTVSIDQGPVTGDLPLLPIQQMFF--ADDIPERHHWNQSVLLE 2208
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1113 LIGPLDRGALRRTLNRVVDRHEMLRTRIHPGPDGMPVQVADPAGGGAALTERDAAPGTDLAQLLLAEAALGFTLATEHPL 1192
Cdd:PRK12467 2209 PREALDAELLEAALQALLVHHDALRLGFVQEDGGWSAMHRAPEQERRPLLWQVVVADKEELEALCEQAQRSLDLEEGPLL 2288
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1193 RAVLWRLDEREHVLLLTAHHVAVDAWSMDLIQRDLTELYAADTGHREPELDEPALAQADYAVWQRQSAQRGRYAAELDFW 1272
Cdd:PRK12467 2289 RAVLATLPDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAASAALADELGYW 2368
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 653678460 1273 RTELTGAvATEVAGDLPRPATPGGGGGAVEFALAPRQI-QGIRELARRCGTTVSTVVLSALQTLLYRITGGADVVI 1347
Cdd:PRK12467 2369 QAQLQGA-STELPCDHPQGGLQRRHAASVTTHLDSEWTrRLLQEAPAAYRTQVNDLLLTALARVIARWTGQASTLI 2443
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
41-1347 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 862.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 41 VQPPGPVPLAPGQAGIWFSEQLRPGTPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVFRLGPDgEPVQQTAPAA 120
Cdd:PRK12316 44 VSSAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGAD-DSLAQVPLDR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 121 PVALPVIDVT---EADLPQALRTAAE----QPFDLERGPLLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLLLADLARAY 193
Cdd:PRK12316 123 PLEVEFEDCSglpEAEQEARLRDEAQreslQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 194 AG-ELPAGVAAPA----FRDVAAWQHGRLAAGELDDQLRYWRQRLAG-LPDLEIPGDRQRPADRDWRAHSVRRELPAATE 267
Cdd:PRK12316 203 SAyATGAEPGLPAlpiqYADYALWQRSWLEAGEQERQLEYWRAQLGEeHPVLELPTDHPRPAVPSYRGSRYEFSIDPALA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 268 AAVRRLAAAHDTTPFTVLLAAYGTFLHRLTGQDDFAVGVPVAGRGRTDLESVVGLFAGMVPVRLDLTGRPSFDEVLS--- 344
Cdd:PRK12316 283 EALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAgvk 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 345 RTVAGSRndfAHPQIPFDRLVRELRRDRIAGSQLLVQAM---------AGTESTAVALTFGEAagteqPVDVALAKCDLD 415
Cdd:PRK12316 363 DTVLGAQ---AHQDLPFERLVEALKVERSLSHSPLFQVMynhqplvadIEALDTVAGLEFGQL-----EWKSRTTQFDLT 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 416 LSVLDDGDRLAVTLVAAADLFTPAAAEQLAGQFLSLLAGLTGAPDRLVSEVDLLDTDELHTVLCRWNDTARPLP-AASLR 494
Cdd:PRK12316 435 LDTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPlQRGVH 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 495 ERFQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPD 574
Cdd:PRK12316 515 RLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPE 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 575 FPVERIAYLLSDARPVLVVTDAATADRLGPDDITGLVVLEETDT--GGYPaTEPP--AVPAGHSAYVIYTSGSTGRPKGV 650
Cdd:PRK12316 595 YPAERLAYMLEDSGVQLLLSQSHLGRKLPLAAGVQVLDLDRPAAwlEGYS-EENPgtELNPENLAYVIYTSGSTGKPKGA 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 651 VITRAALDNFLAAMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALIDLAGRHRVTLAQAT 730
Cdd:PRK12316 674 GNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFV 753
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 731 PTLWQALVPELSGPALAGIRVLV-GGEALPAELARRLGD--AGAEVTNMYGPTETTIWSTSGPTSEDSIRRGSIGVPIDN 807
Cdd:PRK12316 754 PSMLQAFLQDEDVASCTSLRRIVcSGEALPADAQEQVFAklPQAGLYNLYGPTEAAIDVTHWTCVEEGGDSVPIGRPIAN 833
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 808 TQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFGpPGTRMYRTGDLVRWSAAGDLEYLGRTDHQV 887
Cdd:PRK12316 834 LACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFV-AGERMYRTGDLARYRADGVIEYAGRIDHQV 912
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 888 KLRGFRIELGEIETTLINAGPVRRAAAVVREDRpgdlRLVAYVIPD--GPVAPDALRTELSRTLPDYMIPAVIVPVPDFP 965
Cdd:PRK12316 913 KLRGLRIELGEIEARLLEHPWVREAAVLAVDGK----QLVGYVVLEseGGDWREALKAHLAASLPEYMVPAQWLALERLP 988
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 966 TTPNGKLDRAALPAPDYGTRSTAR-PPRDDRERFLCTAFAEVLGLPEVAVSDNFFELGGHSLLAFRLLARIRDEfGAGFS 1044
Cdd:PRK12316 989 LTPNGKLDRKALPAPEASVAQQGYvAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQA-GIQLS 1067
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1045 LRRLLAAPTVAAVAAELAAETSTGDDAvhlapVPRDEPLPLSPMQEsiWLADQVSAGDSVYNVPLALRLIGPLDRGALRR 1124
Cdd:PRK12316 1068 PRDLFQHQTIRSLALVAKAGQATAADQ-----GPASGEVALAPVQR--WFFEQAIPQRQHWNQSLLLQARQPLDPDRLGR 1140
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1125 TLNRVVDRHEMLRTRIHpGPDGMPVQVADPAGGGAALTERDAApgtDLAQLLLAEAALGFTLATEHP--LRAVLWRLDER 1202
Cdd:PRK12316 1141 ALERLVAHHDALRLRFR-EEDGGWQQAYAAPQAGEVLWQRQAA---SEEELLALCEEAQRSLDLEQGplLRALLVDMADG 1216
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1203 EHVLLLTAHHVAVDAWSMDLIQRDLTELYaadtghREPELDEPALAQAdYAVW-QRQSAQRGRYAAELDFWRTELTGAvA 1281
Cdd:PRK12316 1217 SQRLLLVIHHLVVDGVSWRILLEDLQRAY------ADLDADLPARTSS-YQAWaRRLHEHAGARAEELDYWQAQLEDA-P 1288
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 653678460 1282 TEVAGDLPRPATPGGGGGAVEFALAPRQIQGIRELARRC-GTTVSTVVLSALQTLLYRITGGADVVI 1347
Cdd:PRK12316 1289 HELPCENPDGALENRHERKLELRLDAERTRQLLQEAPAAyRTQVNDLLLTALARVTCRWSGQASVLV 1355
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
40-1354 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 805.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 40 PVQPPGPVPLAPGQAGIWFSEQLRPGTPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVFRlgPDGEPVQQTAPA 119
Cdd:PRK12316 2596 KVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFV--EVGEQTRQVILP 2673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 120 A----PVALPVIDVTEADLPQALRTAAEQPFDLERGPLLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLLLADLARAYAG 195
Cdd:PRK12316 2674 NmslrIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAG 2753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 196 -----ELPAGVAAPAFRDVAAWQHGRLAAGELDDQLRYWRQRLAGL-PDLEIPGDRQRPADRDWRAHSVRRELPAATEAA 269
Cdd:PRK12316 2754 arrgeQPTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEqPVLELPLDRPRPALQSHRGARLDVALDVALSRE 2833
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 270 VRRLAAAHDTTPFTVLLAAYGTFLHRLTGQDDFAVGVPVAGRGRTDLESVVGLFAGMVPVRLDLTGRPSFDEVLSRTVAG 349
Cdd:PRK12316 2834 LLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQ 2913
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 350 SRNDFAHPQIPFDRLVRELRRDRIAGSQLLVQAMAGTESTAVA-LTFGEAAGTEQPVDVALAKCDLDLSVLDDGDRLAVT 428
Cdd:PRK12316 2914 ALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERAaAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGAS 2993
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 429 LVAAADLFTPAAAEQLAGQFLSLLAGLTGAPDRLVSEVDLLDTDELHTVLCRWNDTARPLPAASLRER-FQQWCRRTPGA 507
Cdd:PRK12316 2994 LTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAAEYPLERGVHRlFEEQVERTPDA 3073
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 508 VAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDA 587
Cdd:PRK12316 3074 VALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDS 3153
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 588 RPVLVVTDAATadRLGPDDITGLVVLEETDTGGYPATEPPAVPAGHSAYVIYTSGSTGRPKGVVITRAALDNFLAAMAER 667
Cdd:PRK12316 3154 GAQLLLSQSHL--RLPLAQGVQVLDLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQA 3231
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 668 FPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALIDLAGRHRVTLAQATPTLWQALVPELSGPALA 747
Cdd:PRK12316 3232 YGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCT 3311
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 748 GIR-VLVGGEALPAELARRLgDAGAEVTNMYGPTETTIWSTSGPTSEDSIRRGSIGVPIDNTQVYVLDANLHPAPIGVLG 826
Cdd:PRK12316 3312 SLKrIVCGGEALPADLQQQV-FAGLPLYNLYGPTEATITVTHWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALG 3390
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 827 ELHIAGEGLARGYWNRPGLTAEKFLPDPFgPPGTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINA 906
Cdd:PRK12316 3391 ELYLGGEGLARGYHNRPGLTAERFVPDPF-VPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEH 3469
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 907 GPVRRAAAVVREDRpgdlRLVAYVIPDGPVA--PDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAALPAPDYGT 984
Cdd:PRK12316 3470 PWVREAVVLAVDGR----QLVAYVVPEDEAGdlREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAAL 3545
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 985 RSTAR-PPRDDRERFLCTAFAEVLGLPEVAVSDNFFELGGHSLLAFRLLARIRdEFGAGFSLRRLLAAPTVAAVAAELAa 1063
Cdd:PRK12316 3546 LQQDYvAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRAR-QAGIRFTPKDLFQHQTIQGLARVAR- 3623
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1064 etstGDDAVHLAPVPRDEPLPLSPMQESIWlaDQVSAGDSVYNVPLALRLIGPLDRGALRRTLNRVVDRHEMLRTRIHPG 1143
Cdd:PRK12316 3624 ----VGGGVAVDQGPVSGETLLLPIQQQFF--EEPVPERHHWNQSLLLKPREALDAAALEAALQALVEHHDALRLRFVED 3697
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1144 PDGMPVQVADPAGGGAALTERDAApGTDLAQLLLAEAALGFTLATEHPLRAVLWRLDEREHVLLLTAHHVAVDAWSMDLI 1223
Cdd:PRK12316 3698 AGGWTAEHLPVELGGALLWRAELD-DAEELERLGEEAQRSLDLADGPLLRALLATLADGSQRLLLVIHHLVVDGVSWRIL 3776
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1224 QRDLTELYAADTGHREPELDEPALAQADYAVWQRQSAQRGRYAAELDFWRTELTGaVATEVAGDLPRPATPGGGGGAVEF 1303
Cdd:PRK12316 3777 LEDLQQAYQQLLQGEAPRLPAKTSSFKAWAERLQEHARGEALKAELAYWQEQLQG-VSSELPCDHPQGALQNRHAASVQT 3855
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*....
gi 653678460 1304 ALAprqiqgiRELARRC--------GTTVSTVVLSALQTLLYRITGGADVVIGSTVSGR 1354
Cdd:PRK12316 3856 RLD-------RELTRRLlqqapaayRTQVNDLLLTALARVVCRWTGEASALVQLEGHGR 3907
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1069-2393 |
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: 796.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1069 DDAVHLAPVPRDEPLPLSPMQESIWLADQVSAGDSVYNVPLALRLIGPLDRGALRRTLNRVVDRHEMLRTRIHPGPDGMP 1148
Cdd:COG1020 4 AAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1149 VQVADPAGGGA----ALTERDAAPGTDLAQLLLAEAALGFTLATEHPLRAVLWRLDEREHVLLLTAHHVAVDAWSMDLIQ 1224
Cdd:COG1020 84 QVIQPVVAAPLpvvvLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1225 RDLTELYAADTGHREPELDEPALAQADYAVWQRQSAQRGRYAAELDFWRTELTGAVAT-EVAGDLPRPATPGGGGGAVEF 1303
Cdd:COG1020 164 AELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLlELPTDRPRPAVQSYRGARVSF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1304 ALAPRQIQGIRELARRCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGRGNPRLDNLVGCLVNTVVLRGDLSGAPTFH 1383
Cdd:COG1020 244 RLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1384 ELLRRTHARTADALAHQELPFEHLVAD----RGAGNGPLFRIMYSFSSQEPAGRSAGDVDLEPVPVPVTTCKFDLVLTVV 1459
Cdd:COG1020 324 ELLARVRETLLAAYAHQDLPFERLVEElqpeRDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLTLTVV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1460 DGGSTLEGVLEYADDLYLPGTAERLVTSLTNLLAAAVRTPELAVTRLAITSESDTVR-TSRWGRSEQHVGDDRTVHQLVE 1538
Cdd:COG1020 404 ETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQlLAEWNATAAPYPADATLHELFE 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1539 AQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDP 1618
Cdd:COG1020 484 AQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLR--ALG---VGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDP 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1619 GYPMARLTRIADTVTPALVLTRTGQGGCLPGAevfgDVPVVALDRVAdrLTAMPDQRPEVTVDPRGLAYSIFTSGSTGQP 1698
Cdd:COG1020 559 AYPAERLAYMLEDAGARLVLTQSALAARLPEL----GVPVLALDALA--LAAEPATNPPVPVTPDDLAYVIYTSGSTGRP 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1699 KGVAVEHIGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMSALFEPLVSGRGVTLMPADATL--ADLAEELSGPlAYDY 1776
Cdd:COG1020 633 KGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRdpAALAELLARH-RVTV 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1777 IRLTPSHLRHLVGHwtGQELPPAARGWVVGGETLDPALVKQLLELRPDAEVINHYGPTETVIGRVVHPVREAGelAVDSP 1856
Cdd:COG1020 712 LNLTPSLLRALLDA--APEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPD--ADGGS 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1857 LPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPAGEPGARMYRTGDLVRWRGDGLLD 1936
Cdd:COG1020 788 VPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGARLYRTGDLARWLPDGNLE 867
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1937 FVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRD----QQLVGWFIPAEDHPPVTVSALRRFCAEQLPEFMVPN 2012
Cdd:COG1020 868 FLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREdapgDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPA 947
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 2013 QWVALDAFPLTPHGKVNHRALPGPTSGRPelEDRYQAPRTPGEQLLAELWSTVLGTDRIGIEDNFFDLGGTSISVIQLSG 2092
Cdd:COG1020 948 AVVLLLPLPLTGNGKLDRLALPAPAAAAA--AAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALAR 1025
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 2093 ACRRAGVEISPKDVFEQPTVRGQAMRAIARSRDDAYAPVLDTVFGAGHTGTT-RTVVTLRGEGDGRPVFCVHPSGGGVAW 2171
Cdd:COG1020 1026 AARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLsLLALLLALLLLLALLALLALLLLLLLL 1105
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 2172 YLPLARALPAGHPVHAFQPLGMDGREAPAETIEDMAAGYLADLRLVQPEGPYVVVGWSLGGTIAFEMARQLDRLGEPVQL 2251
Cdd:COG1020 1106 LLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALL 1185
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 2252 ILLEPTLPEVARTIDLHRPARDSYLRGADLAERILRLPAGDPEGDRLRAELTRLLEDAGYSAGEISLGDALPMRACGQML 2331
Cdd:COG1020 1186 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALA 1265
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 653678460 2332 AAFAEYRPLPLPDESKVRTQFVVSAECTDATPERPSGTSHTAYGSYAAGWQKLLGRAAAPRT 2393
Cdd:COG1020 1266 LLALALLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLA 1327
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1076-2123 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 784.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1076 PVPRD----EPLPLSPMQESIWLADQVSAGDSVYNVPLALRLIGPLDRGALRRTLNRVVDRHEMLRTRIHPGPDGMPVQV 1151
Cdd:PRK12467 39 PIPQVrsafERIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1152 ADPAGGGAALTERDAAPGTDL----AQLLLAEAALGFTLATEHPLRAVLWRLDEREHVLLLTAHHVAVDAWSMDLIQRDL 1227
Cdd:PRK12467 119 DASLSLTIPLDDLANEQGRAResqiEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEEL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1228 TELYAADTGHREPELDEPALAQADYAVWQRQSAQRGRYAAELDFWRTEL-TGAVATEVAGDLPRPATPGGGGGAVEFALA 1306
Cdd:PRK12467 199 VQLYSAYSQGREPSLPALPIQYADYAIWQRSWLEAGERERQLAYWQEQLgGEHTVLELPTDRPRPAVPSYRGARLRVDLP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1307 PRQIQGIRELARRCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGRGNPRLDNLVGCLVNTVVLRGDLSGAPTFHELL 1386
Cdd:PRK12467 279 QALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1387 RRTHARTADALAHQELPFEHLVA----DRGAGNGPLFRIMYSFSSQEPAGRSA-----GDVDLEPVPVPVTTCKFDLVLT 1457
Cdd:PRK12467 359 QQVKRTALGAQAHQDLPFEQLVEalqpERSLSHSPLFQVMFNHQNTATGGRDRegaqlPGLTVEELSWARHTAQFDLALD 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1458 VVDGGSTLEGVLEYADDLYLPGTAERLVTSLTNLLAAAVRTPELAVTRLAITSESDTVRTSRWGRSEQHVGDDRTVHQLV 1537
Cdd:PRK12467 439 TYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAPDCVHQLI 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1538 EAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHtgalgAPPVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVD 1617
Cdd:PRK12467 519 EAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLI-----AAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLD 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1618 PGYPMARLTRIADTVTPALVLTRTGQGGCLPgaeVFGDVPVVALDRVADRLTAMPDQRPEVTVDPRGLAYSIFTSGSTGQ 1697
Cdd:PRK12467 594 PEYPQDRLAYMLDDSGVRLLLTQSHLLAQLP---VPAGLRSLCLDEPADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQ 670
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1698 PKGVAVEHIGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMSALFEPLVSGRGVTLMPADATLAdlAEELSGPLA---Y 1774
Cdd:PRK12467 671 PKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARD--AEAFAALMAdqgV 748
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1775 DYIRLTPSHLRHLVGHwTGQELPPAARGWVVGGETLDPALVKQLLELRPDAEVINHYGPTETVIGRVVHPVREAGelAVD 1854
Cdd:PRK12467 749 TVLKIVPSHLQALLQA-SRVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYELSDEE--RDF 825
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1855 SPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPAGEPGARMYRTGDLVRWRGDGL 1934
Cdd:PRK12467 826 GNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGADGGRLYRTGDLARYRADGV 905
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1935 LDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRD----QQLVGWFIPAED----HPPVTVSALRRFCAEQLP 2006
Cdd:PRK12467 906 IEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPgdagLQLVAYLVPAAVadgaEHQATRDELKAQLRQVLP 985
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 2007 EFMVPNQWVALDAFPLTPHGKVNHRALPGPTSGRPelEDRYQAPRTPGEQLLAELWSTVLGTDRIGIEDNFFDLGGTSIS 2086
Cdd:PRK12467 986 DYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAV--QATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLL 1063
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 653678460 2087 VIQ-LSGACRRAGVEISPKDVFEQPTVRGQAMRAIARS 2123
Cdd:PRK12467 1064 ATQvISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQ 1101
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1075-2119 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 774.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1075 APVPRDEPLPLSPMQESIWLADQVSAGDSVYNVPLALRLIGPLDRGALRRTLNRVVDRHEMLRTRIHPG--------PDG 1146
Cdd:PRK12316 42 AGVSSAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGaddslaqvPLD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1147 MPVQVADPAGGGAALTERDAApgtdLAQLLLAEAALGFTLATEHPLRAVLWRLDEREHVLLLTAHHVAVDAWSMDLIQRD 1226
Cdd:PRK12316 122 RPLEVEFEDCSGLPEAEQEAR----LRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1227 LTELYAADTGHREPELDEPALAQADYAVWQRQSAQRGRYAAELDFWRTELTGAVAT-EVAGDLPRPATPGGGGGAVEFAL 1305
Cdd:PRK12316 198 FSRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRAQLGEEHPVlELPTDHPRPAVPSYRGSRYEFSI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1306 APRQIQGIRELARRCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGRGNPRLDNLVGCLVNTVVLRGDLSGAPTFHEL 1385
Cdd:PRK12316 278 DPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1386 LRRTHARTADALAHQELPFEHLV----ADRGAGNGPLFRIMYSFSSQ--EPAGRS-AGDVDLEPVPVPVTTCKFDLVLTV 1458
Cdd:PRK12316 358 LAGVKDTVLGAQAHQDLPFERLVealkVERSLSHSPLFQVMYNHQPLvaDIEALDtVAGLEFGQLEWKSRTTQFDLTLDT 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1459 VDGGSTLEGVLEYADDLYLPGTAERLVTSLTNLLAAAVRTPELAVTRLAITSESDTVRTSR-WGRSEQHVGDDRTVHQLV 1537
Cdd:PRK12316 438 YEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEgWNATAAEYPLQRGVHRLF 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1538 EAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVD 1617
Cdd:PRK12316 518 EEQVERTPEAPALAFGEETLDYAELNRRANRLAHALI--ERG---VGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLD 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1618 PGYPMARLTRIADTVTPALVLTRTGQGGCLPgaeVFGDVPVVALDRVADRLTAMPDQRPEVTVDPRGLAYSIFTSGSTGQ 1697
Cdd:PRK12316 593 PEYPAERLAYMLEDSGVQLLLSQSHLGRKLP---LAAGVQVLDLDRPAAWLEGYSEENPGTELNPENLAYVIYTSGSTGK 669
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1698 PKGVAVEHIGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMSALFEPLVSG-RGVTLMPADATLADLAEELSGPLAYDY 1776
Cdd:PRK12316 670 PKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGaRLVVAAPGDHRDPAKLVELINREGVDT 749
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1777 IRLTPSHLRHLVgHWTGQELPPAARGWVVGGETLDPALVKQLLELRPDAEVINHYGPTETVIGRVVHPVREAGELAVdsp 1856
Cdd:PRK12316 750 LHFVPSMLQAFL-QDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGGDSV--- 825
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1857 lPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPAGEpGARMYRTGDLVRWRGDGLLD 1936
Cdd:PRK12316 826 -PIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVA-GERMYRTGDLARYRADGVIE 903
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1937 FVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRD-QQLVGWFIPaEDHPPVTVSALRRFCAEQLPEFMVPNQWV 2015
Cdd:PRK12316 904 YAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDgKQLVGYVVL-ESEGGDWREALKAHLAASLPEYMVPAQWL 982
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 2016 ALDAFPLTPHGKVNHRALPGPTSGRPELEdrYQAPRTPGEQLLAELWSTVLGTDRIGIEDNFFDLGGTSISVIQLSGACR 2095
Cdd:PRK12316 983 ALERLPLTPNGKLDRKALPAPEASVAQQG--YVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRAR 1060
|
1050 1060
....*....|....*....|....
gi 653678460 2096 RAGVEISPKDVFEQPTVRGQAMRA 2119
Cdd:PRK12316 1061 QAGIQLSPRDLFQHQTIRSLALVA 1084
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
492-2108 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 752.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 492 SLRERFQQWCRRTPGAVAVI------EGDTTLSYRELDERANRLARLLMERGAGAETfvAVLL-PRSADLLVTLLAVIKA 564
Cdd:PRK05691 10 TLVQALQRRAAQTPDRLALRfladdpGEGVVLSYRDLDLRARTIAAALQARASFGDR--AVLLfPSGPDYVAAFFGCLYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 565 GAAYLPIDPDFPV-----ERIAYLLSDARPVLVVTDAATAD------RLGPDDITGLVVLEETDTGGYPATEPPAVPAGH 633
Cdd:PRK05691 88 GVIAVPAYPPESArrhhqERLLSIIADAEPRLLLTVADLRDsllqmeELAAANAPELLCVDTLDPALAEAWQEPALQPDD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 634 SAYVIYTSGSTGRPKGVVITRAAL--DNFLAAMAERFPLTAEDRVLATTTVSFDIaGL--ELYLPLRSGAGVVL-ADADT 708
Cdd:PRK05691 168 IAFLQYTSGSTALPKGVQVSHGNLvaNEQLIRHGFGIDLNPDDVIVSWLPLYHDM-GLigGLLQPIFSGVPCVLmSPAYF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 709 ARNPAALIDLAGRHRVTLAQATPTLWQALVPELSGPALAGI-----RVLVGG-----EALPAELARRLGDAGAEVTNM-- 776
Cdd:PRK05691 247 LERPLRWLEAISEYGGTISGGPDFAYRLCSERVSESALERLdlsrwRVAYSGsepirQDSLERFAEKFAACGFDPDSFfa 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 777 -YGPTETTIWSTSGPT--------------SEDSIRRG------SIGVPIDNTQVYVLDAN-LHPAPIGVLGELHIAGEG 834
Cdd:PRK05691 327 sYGLAEATLFVSGGRRgqgipaleldaealARNRAEPGtgsvlmSCGRSQPGHAVLIVDPQsLEVLGDNRVGEIWASGPS 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 835 LARGYWNRPGLTAEKFLPDPfgppGTRMYRTGDLvRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRR--- 911
Cdd:PRK05691 407 IAHGYWRNPEASAKTFVEHD----GRTWLRTGDL-GFLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVRkgr 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 912 --AAAVVREDRPG------DLRLVAYVIPdgpvaPDALRTELSRTLPD--YMIPAVIVPVPD--FPTTPNGKLDRAA--- 976
Cdd:PRK05691 482 vaAFAVNHQGEEGigiaaeISRSVQKILP-----PQALIKSIRQAVAEacQEAPSVVLLLNPgaLPKTSSGKLQRSAcrl 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 977 ------------LPAPDYGTRSTARPPRDDRERFLCTAFAEVLGLPEVAVSDNFFELGGHSLLAFRLLARIRDEFGAGFS 1044
Cdd:PRK05691 557 rladgsldsyalFPALQAVEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDELGIDLN 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1045 LRRLLAAPTVAAVAAELAAETSTGDDAVH-LAPVPRDEPLPLSPMQESIWLADQVSAGDSVYNVPLALRLIGPLDRGALR 1123
Cdd:PRK05691 637 LRQLFEAPTLAAFSAAVARQLAGGGAAQAaIARLPRGQALPQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALR 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1124 RTLNRVVDRHEMLRTRIHPgPDGMPVQVADPAG---------GGAALTERDAAPGTDLAQLLLAEaalgFTLATEHPLRA 1194
Cdd:PRK05691 717 ASFQRLVERHESLRTRFYE-RDGVALQRIDAQGefalqridlSDLPEAEREARAAQIREEEARQP----FDLEKGPLLRV 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1195 VLWRLDEREHVLLLTAHHVAVDAWSMDLIQRDLTELYAADTGHREPELDEPALAQADYAVWQRQSAQRGRYAAELDFWRT 1274
Cdd:PRK05691 792 TLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGAWQRQWLAQGEAARQLAYWKA 871
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1275 ELTGAVAT-EVAGDLPRPATPGGGGGAVEFALAPRQIQGIRELARRCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSG 1353
Cdd:PRK05691 872 QLGDEQPVlELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNAN 951
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1354 RGNPRLDNLVGCLVNTVVLRGDLSGAPTFHELLRRTHARTADALAHQELPFEHLV-ADRGAGNGPLFRIMYSFSSQEP-A 1431
Cdd:PRK05691 952 RPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVeALPQAREQGLFQVMFNHQQRDLsA 1031
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1432 GRSAGDVDLEPVPVPVTTCKFDLVL-TVVDGGSTLEGVLEYADDLYLPGTAERLVTSLTNLLAAAVRTPELAVTRLAITS 1510
Cdd:PRK05691 1032 LRRLPGLLAEELPWHSREAKFDLQLhSEEDRNGRLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLD 1111
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1511 ESDTVRTSRWGRSEQhVGDDRTVHQLVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHAL-HTGalgappVGPETPV 1589
Cdd:PRK05691 1112 AAERAQLAQWGQAPC-APAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLrDKG------VGPDVCV 1184
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1590 LLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMARLTRIADTVTPALVLTRTGQGGCLPGAEvfgDVPVVALDRVadRLT 1669
Cdd:PRK05691 1185 AIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAE---GVSAIALDSL--HLD 1259
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1670 AMPDQRPEVTVDPRGLAYSIFTSGSTGQPKGVAVEHIGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMSALFEPLVSG 1749
Cdd:PRK05691 1260 SWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITG 1339
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1750 -RGVTLMPAD----ATLADLAEELSgplaYDYIRLTPSHLRHLVghwtgqELPPAA-----RGWVVGGETLDPALVKQLL 1819
Cdd:PRK05691 1340 cRLVLAGPGEhrdpQRIAELVQQYG----VTTLHFVPPLLQLFI------DEPLAAactslRRLFSGGEALPAELRNRVL 1409
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1820 ELRPDAEVINHYGPTETVIgRVVH--PVREAGELAvdsplPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGY 1897
Cdd:PRK05691 1410 QRLPQVQLHNRYGPTETAI-NVTHwqCQAEDGERS-----PIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGY 1483
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1898 LGRPALTAEKFLPDPAGEPGARMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRD- 1976
Cdd:PRK05691 1484 LGRPALTAERFVPDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREg 1563
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1977 ---QQLVGWFiPAEDHPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRALPGPTSGRPEledrYQAPRTP 2053
Cdd:PRK05691 1564 aagAQLVGYY-TGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQRE----HVEPRTE 1638
|
1690 1700 1710 1720 1730
....*....|....*....|....*....|....*....|....*....|....*.
gi 653678460 2054 GEQLLAELWSTVLGTDRIGIEDNFFDLGGTSISVIQLSGACRRA-GVEISPKDVFE 2108
Cdd:PRK05691 1639 LQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQAcDVELPLRALFE 1694
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
38-1049 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 704.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 38 GLPVqPPGPV----PLAPGQAGIWFSEQLRPGTPLYSVPLAVRLTGpLDVDALRAALDAVTARHEALRTVF-RLGPDGEP 112
Cdd:PRK12316 4091 ALPL-PLGEIediyPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFvWQGELGRP 4168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 113 VQQTAPAAPVALPVIDVT-EADLPQALRTAAEQP----FDLERGPLLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLLLA 187
Cdd:PRK12316 4169 LQVVHKQVSLPFAELDWRgRADLQAALDALAAAErergFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLG 4248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 188 DLARAYAGELPAGvAAPAFRDVAAW-QHGRLAAGElddqlRYWRQRLAGLPDLEIPGDRQRPAD-RDWRAHS-VRRELPA 264
Cdd:PRK12316 4249 EVLERYSGRPPAQ-PGGRYRDYIAWlQRQDAAASE-----AFWREQLAALDEPTRLAQAIARADlRSANGYGeHVRELDA 4322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 265 ATEAAVRRLAAAHDTTPFTVLLAAYGTFLHRLTGQDDFAVGVPVAGRG--RTDLESVVGLFAGMVPVRLDLTGRPSFDEV 342
Cdd:PRK12316 4323 TATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPaeLPGIEGQIGLFINTLPVIATPRAQQSVVEW 4402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 343 LSRTVAGSRNDFAHPQIPFDrlvrELRRDRIAGSQLLVQAMAGTESTAVA----------LTFGEAAGTEQPVdvalakC 412
Cdd:PRK12316 4403 LQQVQRQNLALREHEHTPLY----EIQRWAGQGGEALFDSLLVFENYPVSealqqgapggLRFGEVTNHEQTN------Y 4472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 413 DLDLSVlDDGDRLAVTLVAAADLFTPAAAEQLAGQFLSLLAGLTGAPDRLVSEVDLLDTDELHTVLCRWNDTARPLPAA- 491
Cdd:PRK12316 4473 PLTLAV-GLGETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPATr 4551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 492 SLRERFQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPI 571
Cdd:PRK12316 4552 CVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPL 4631
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 572 DPDFPVERIAYLLSDARPVLVVTDAATADRL-GPDDITGLVVLEETDTGGYPATEPPAVPAGHS-AYVIYTSGSTGRPKG 649
Cdd:PRK12316 4632 DPEYPRERLAYMMEDSGAALLLTQSHLLQRLpIPDGLASLALDRDEDWEGFPAHDPAVRLHPDNlAYVIYTSGSTGRPKG 4711
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 650 VVITRAALDNFLAAMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADaDTARNPAALIDLAGRHRVTLAQA 729
Cdd:PRK12316 4712 VAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRD-DSLWDPERLYAEIHEHRVTVLVF 4790
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 730 TPTLWQALV--PELSGPALAGIRVLVGGEALPAELARRLGDAGAEVT--NMYGPTETTIWSTSGpTSEDSIRRGS----I 801
Cdd:PRK12316 4791 PPVYLQQLAehAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYlfNGYGPTETTVTVLLW-KARDGDACGAaympI 4869
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 802 GVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFGPPGTRMYRTGDLVRWSAAGDLEYLG 881
Cdd:PRK12316 4870 GTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGGRLYRTGDLARYRADGVIDYLG 4949
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 882 RTDHQVKLRGFRIELGEIETTLINAGPVRRaAAVVREDRPGDLRLVAYVIPDGPVAPDA----------LRTELSRTLPD 951
Cdd:PRK12316 4950 RVDHQVKIRGFRIELGEIEARLREHPAVRE-AVVIAQEGAVGKQLVGYVVPQDPALADAdeaqaelrdeLKAALRERLPE 5028
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 952 YMIPAVIVPVPDFPTTPNGKLDRAALPAPDYGTRSTAR-PPRDDRERFLCTAFAEVLGLPEVAVSDNFFELGGHSLLAFR 1030
Cdd:PRK12316 5029 YMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYvAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQ 5108
|
1050
....*....|....*....
gi 653678460 1031 LLARIRDEFGAGFSLRRLL 1049
Cdd:PRK12316 5109 VTSRIQLELGLELPLRELF 5127
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
46-1354 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 703.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 46 PVPLAPGQAGIWFSEQLRPGTPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVFRlGPDGEPVQQTAPAAPV--- 122
Cdd:PRK05691 1728 PVPLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFP-SVDGVPVQQVAEDSGLrmd 1806
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 123 -----ALPViDVTEADLPQALRTAAEQPFDLERGPLLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLL---LADLARAYA 194
Cdd:PRK05691 1807 wqdfsALPA-DARQQRLQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFareLGALYEAFL 1885
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 195 GELPAGVAAPA--FRDVAAWQHGRLAAGELDDQLRYWRQRLAG-LPDLEIPGDRQRPADRDWRAHSVRRELPAATEAAVR 271
Cdd:PRK05691 1886 DDRESPLEPLPvqYLDYSVWQRQWLESGERQRQLDYWKAQLGNeHPLLELPADRPRPPVQSHRGELYRFDLSPELAARVR 1965
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 272 RLAAAHDTTPFTVLLAAYGTFLHRLTGQDDFAVGVPVAGRGRTDLESVVGLFAGMVPVRLDLTGRPSFDEVLSRTVAGSR 351
Cdd:PRK05691 1966 AFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVI 2045
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 352 NDFAHPQIPFDRLVRELRRDRIAGSQLLVQAMAGTESTAVALTfGEAAG--TEQPVDVALA-KCDLDLSVLDDGDRLAVT 428
Cdd:PRK05691 2046 EGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEFQQS-RQLAGmtVEYLVNDARAtKFDLNLEVTDLDGRLGCC 2124
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 429 LVAAADLFTPAAAEQLAGQFLSLLAGLTGAPDRLVSEVDLLDTDELHTVLCRWNDTA-RPLPAASLRERFQQWCRRTPGA 507
Cdd:PRK05691 2125 LTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEAgEARLDQTLHGLFAAQAARTPQA 2204
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 508 VAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDA 587
Cdd:PRK05691 2205 PALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDS 2284
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 588 RPVLVVTDAATADRLG--PDDItGLVVLEETDTG--GYPATEPPAVP-AGHSAYVIYTSGSTGRPKGVVITRAALDNFLA 662
Cdd:PRK05691 2285 GIGLLLSDRALFEALGelPAGV-ARWCLEDDAAAlaAYSDAPLPFLSlPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQ 2363
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 663 AMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLAdADTARNPAALIDLAGRHRVTLAQATPT----LWQALV 738
Cdd:PRK05691 2364 AVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLR-AQGQWGAEEICQLIREQQVSILGFTPSygsqLAQWLA 2442
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 739 PElsGPALAGIRVLVGGEALPAELARRLGDA--GAEVTNMYGPTETTIWSTSGPTSEdSIRRGSIGVPIDNT----QVYV 812
Cdd:PRK05691 2443 GQ--GEQLPVRMCITGGEALTGEHLQRIRQAfaPQLFFNAYGPTETVVMPLACLAPE-QLEEGAASVPIGRVvgarVAYI 2519
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 813 LDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFGPPGTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGF 892
Cdd:PRK05691 2520 LDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGF 2599
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 893 RIELGEIETTLINAGPVRRAAaVVREDRPGDLRLVAYVIPDGPVAPD--------ALRTELSRTLPDYMIPAVIVPVPDF 964
Cdd:PRK05691 2600 RIELGEIESRLLEHPAVREAV-VLALDTPSGKQLAGYLVSAVAGQDDeaqaalreALKAHLKQQLPDYMVPAHLILLDSL 2678
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 965 PTTPNGKLDRAALPAPDYG-TRSTARPPRDDRERFLCTAFAEVLGLPEVAVSDNFFELGGHSLLAFRLLARIRdEFGAGF 1043
Cdd:PRK05691 2679 PLTANGKLDRRALPAPDPElNRQAYQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSRAR-QLGIHF 2757
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1044 SLRRLLAAPTVAAVAAelaaeTSTGDDAVHLAPVPRDEPLPLSPMQEsiWLADQVSAGDSVYNVPLALRLIGPLDRGALR 1123
Cdd:PRK05691 2758 SPRDLFQHQTVQTLAA-----VATHSEAAQAEQGPLQGASGLTPIQH--WFFDSPVPQPQHWNQALLLEPRQALDPALLE 2830
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1124 RTLNRVVDRHEMLRTRIHpGPDGMpVQVADPAGGGAALTERDAAPGTDLAQLLLAEAALGFTLATEHPLRAVLWRLDERE 1203
Cdd:PRK05691 2831 QALQALVEHHDALRLRFS-QADGR-WQAEYRAVTAQELLWQVTVADFAECAALFADAQRSLDLQQGPLLRALLVDGPQGQ 2908
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1204 HVLLLTAHHVAVDAWSMDLIQRDLTELYAADTGHREPELDEPALAQADYAVWQRQSAQRGRYAAELDFWRTELtGAVATE 1283
Cdd:PRK05691 2909 QRLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAGAEPALPAKTSAFRDWAARLQAYAGSESLREELGWWQAQL-GGPRAE 2987
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 653678460 1284 VAGDLPRPATPGGGGGAVEFALAPRQIQGIRELARRC-GTTVSTVVLSALQTLLYRITGGADVVIGSTVSGR 1354
Cdd:PRK05691 2988 LPCDRPQGGNLNRHAQTVSVRLDAERTRQLLQQAPAAyRTQVNDLLLTALARVLCRWSGQPSVLVQLEGHGR 3059
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
40-1040 |
0e+00 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 689.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 40 PVQPPGPVPLAPGQAGIWFSEQLRPGTPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVFRLGpDGEPVQQTAPA 119
Cdd:PRK10252 1 AEPMSQHLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTED-NGEVWQWVDPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 120 APVALP-VIDVTEADLPQALRTAA-----EQPFDLERG-PLLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLLLADLARA 192
Cdd:PRK10252 80 LTFPLPeIIDLRTQPDPHAAAQALmqadlQQDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 193 YA----GELPAGVAAPAFRDVAAwQHGRLAAGELDDQLR-YWRQRLAGLPDLEIPGDrQRPADRDWRAHSVRRELPAATE 267
Cdd:PRK10252 160 YCawlrGEPTPASPFTPFADVVE-EYQRYRASEAWQRDAaFWAEQRRQLPPPASLSP-APLPGRSASADILRLKLEFTDG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 268 AAVRRLAAAHDTTPFTVLLAAYGTFLHRLTGQDDFAVGVPVAGRgrtdLESVVGLFAGMV----PVRLDLTGRPSFDEVL 343
Cdd:PRK10252 238 AFRQLAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRR----LGSAALTATGPVlnvlPLRVHIAAQETLPELA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 344 SRTVAGSRNDFAHPQIPFDRLVRELrrDRIAGSQLL------VQ------AMAGTESTAVALTFGeaagteqPVDvalak 411
Cdd:PRK10252 314 TRLAAQLKKMRRHQRYDAEQIVRDS--GRAAGDEPLfgpvlnIKvfdyqlDFPGVQAQTHTLATG-------PVN----- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 412 cDLDLSVLDDGD-RLAVTLVAAADLFTPAAAEQLAGQFLSLLAGLTGAPDRLVSEVDLLDTDElHTVLCRWNDTARPLPA 490
Cdd:PRK10252 380 -DLELALFPDEHgGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGE-YAQLAQVNATAVEIPE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 491 ASLRERFQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLP 570
Cdd:PRK10252 458 TTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 571 IDPDFPVERIAYLLSDARPVLVVTDAATADRLgpDDITGLVVLEETDTGGYPATEPPAVPA-GHSAYVIYTSGSTGRPKG 649
Cdd:PRK10252 538 LDTGYPDDRLKMMLEDARPSLLITTADQLPRF--ADVPDLTSLCYNAPLAPQGAAPLQLSQpHHTAYIIFTSGSTGRPKG 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 650 VVITRAALDNFLAAMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALIDLAGRHRVTLAQA 729
Cdd:PRK10252 616 VMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHF 695
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 730 TPTLWQALV----PELSGPALAGIR-VLVGGEALPAELARRL-GDAGAEVTNMYGPTETTI---WSTSGPTSEDSIRRGS 800
Cdd:PRK10252 696 VPSMLAAFVasltPEGARQSCASLRqVFCSGEALPADLCREWqQLTGAPLHNLYGPTEAAVdvsWYPAFGEELAAVRGSS 775
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 801 --IGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFGPpGTRMYRTGDLVRWSAAGDLE 878
Cdd:PRK10252 776 vpIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAP-GERMYRTGDVARWLDDGAVE 854
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 879 YLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVR-----EDRPGDLR-LVAYVIPDGPVAPD--ALRTELSRTLP 950
Cdd:PRK10252 855 YLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqaAATGGDARqLVGYLVSQSGLPLDtsALQAQLRERLP 934
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 951 DYMIPAVIVPVPDFPTTPNGKLDRAALPAPDYGTRSTARPPRDDRERFLCTAFAEVLGLPEVAVSDNFFELGGHSLLAFR 1030
Cdd:PRK10252 935 PHMVPVVLLQLDQLPLSANGKLDRKALPLPELKAQVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMK 1014
|
1050
....*....|
gi 653678460 1031 LLARIRDEFG 1040
Cdd:PRK10252 1015 LAAQLSRQFA 1024
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
39-1290 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 685.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 39 LPVqPPGPV----PLAPGQAGIWFSEQLRPGTPLYSVPLAVRLTGpLDVDALRAALDAVTARHEALRTVF-RLGPDGEPV 113
Cdd:PRK12467 2636 LPV-AVGDIediyPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFlWDGELEEPL 2713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 114 QQTAPAAPVALPVIDVTE-ADLPQALRTAAE----QPFDLERGPLLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLLLAD 188
Cdd:PRK12467 2714 QVVYKQARLPFSRLDWRDrADLEQALDALAAadrqQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGE 2793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 189 LARAYAGELPAGVAApAFRDVAAWqhgrLAAGELDDQLRYWRQRLAGL--PDLEIPGDRQRPADRDWRAHSVRRELPAAT 266
Cdd:PRK12467 2794 VLQRYFGQPPPAREG-RYRDYIAW----LQAQDAEASEAFWKEQLAALeePTRLARALYPAPAEAVAGHGAHYLHLDATQ 2868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 267 EAAVRRLAAAHDTTPFTVLLAAYGTFLHRLTGQDDFAVGVPVAGR--GRTDLESVVGLFAGMVPVRLDLTGRPSFDEVLS 344
Cdd:PRK12467 2869 TRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRpaQLRGAEQQLGLFINTLPVIASPRAEQTVSDWLQ 2948
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 345 RTVAGSRNDFAHPQIPfdrlVRELRRDRIAGSQLLVQAMAGTESTAVA----------LTFGEAAGTEQ---PVDVALAK 411
Cdd:PRK12467 2949 QVQAQNLALREFEHTP----LADIQRWAGQGGEALFDSILVFENYPISealkqgapsgLRFGAVSSREQtnyPLTLAVGL 3024
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 412 cdldlsvlddGDRLAVTLVAAADLFTPAAAEQLAGQFLSLLAGLTGAPDRLVSEVDLLDTDELHTVLCRWNDTARPLPA- 490
Cdd:PRK12467 3025 ----------GDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPSe 3094
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 491 ASLRERFQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLP 570
Cdd:PRK12467 3095 RLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVP 3174
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 571 IDPDFPVERIAYLLSDARPVLVVTDAATADRLGPDDITGLVVLEETDTGGYPATEPPAVPAGHS-AYVIYTSGSTGRPKG 649
Cdd:PRK12467 3175 LDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPAPAGDTALTLDRLDLNGYSENNPSTRVMGENlAYVIYTSGSTGKPKG 3254
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 650 VVITRAALDNFLAAMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTaRNPAALIDLAGRHRVTLAQA 729
Cdd:PRK12467 3255 VGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDL-WDPEELWQAIHAHRISIACF 3333
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 730 TPTLWQALVPELSGPALAGI-RVLVGGEALP----AELARRLGDAGaeVTNMYGPTETTIWSTSGPTSEDSIRRGS---I 801
Cdd:PRK12467 3334 PPAYLQQFAEDAGGADCASLdIYVFGGEAVPpaafEQVKRKLKPRG--LTNGYGPTEAVVTVTLWKCGGDAVCEAPyapI 3411
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 802 GVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFGPPGTRMYRTGDLVRWSAAGDLEYLG 881
Cdd:PRK12467 3412 GRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSGSGGRLYRTGDLARYRADGVIEYLG 3491
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 882 RTDHQVKLRGFRIELGEIETTLINAGPVRRaAAVVREDRPGDLRLVAYVIPDGPVAP--DALRTELSRTLPDYMIPAVIV 959
Cdd:PRK12467 3492 RIDHQVKIRGFRIELGEIEARLLQHPSVRE-AVVLARDGAGGKQLVAYVVPADPQGDwrETLRDHLAASLPDYMVPAQLL 3570
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 960 PVPDFPTTPNGKLDRAALPAPDYGTRSTARPPRDDRERFLCTAFAEVLGLPEVAVSDNFFELGGHSLLAFRLLARIRDEF 1039
Cdd:PRK12467 3571 VLAAMPLGPNGKVDRKALPDPDAKGSREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSL 3650
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1040 GAGFSLRRLLaaptvaavaaelaaetstgddavhLAPVPRDeplplspmqesiwLADQVSAGDsvynvpLALRLIGPLDR 1119
Cdd:PRK12467 3651 GLKLSLRDLM------------------------SAPTIAE-------------LAGYSPLGD------VPVNLLLDLNR 3687
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1120 gaLRRTLNRVVDRHEMLRTrihpGPDGMPVQVAdpagggaalterdaapgtdlaqlllaeaalgftlatehplravlwrL 1199
Cdd:PRK12467 3688 --LETGFPALFCRHEGLGT----VFDYEPLAVI----------------------------------------------L 3715
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1200 DEREHVLLLTAHHVAVDAWSmdliqrdltelyaadtghrEPELDEPALAQADYAVWQRQSAQRGRYAAELDfwrteltGA 1279
Cdd:PRK12467 3716 EGDRHVLGLTCRHLLDDGWQ-------------------DTSLQAMAVQYADYILWQQAKGPYGLLGWSLG-------GT 3769
|
1290
....*....|.
gi 653678460 1280 VATEVAGDLPR 1290
Cdd:PRK12467 3770 LARLVAELLER 3780
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1070-2113 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 621.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1070 DAVHLAPVPRDEPLPLSPMQESIWLADQVSAGDSVYNVPLALRLIGpLDRGALRRTLNRVVDRHEMLRTRI-HPGPDGMP 1148
Cdd:PRK12316 4090 DALPLPLGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFvWQGELGRP 4168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1149 VQVADPAGGgAALTERDAAPGTDLAQLLLAEAAL----GFTLATEHPLRAVLWRLDEREHVLLLTAHHVAVDAWSMDLIQ 1224
Cdd:PRK12316 4169 LQVVHKQVS-LPFAELDWRGRADLQAALDALAAAererGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLL 4247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1225 RDLTELYAADTghrepeLDEPALAQADYAVW-QRQSAqrgryAAELDFWRTELTGAVA-TEVAGDLPRP-ATPGGGGGAV 1301
Cdd:PRK12316 4248 GEVLERYSGRP------PAQPGGRYRDYIAWlQRQDA-----AASEAFWREQLAALDEpTRLAQAIARAdLRSANGYGEH 4316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1302 EFALAPRQIQGIRELARRCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGRGN--PRLDNLVGCLVNTVVLRGDLSGA 1379
Cdd:PRK12316 4317 VRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAelPGIEGQIGLFINTLPVIATPRAQ 4396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1380 PTFHELLRRTHARTADALAHQELPFEHLVADRGAGNGPLFRIMYSFSS---------QEPAGRSAGDVDLEPVpvpvTTC 1450
Cdd:PRK12316 4397 QSVVEWLQQVQRQNLALREHEHTPLYEIQRWAGQGGEALFDSLLVFENypvsealqqGAPGGLRFGEVTNHEQ----TNY 4472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1451 KFDLVltvVDGGSTLEGVLEYADDLYLPGTAERLVTSLTNLLAAAVRTPELAVTRLAITSESDTVRT-SRWGRSEQHVGD 1529
Cdd:PRK12316 4473 PLTLA---VGLGETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIvALWNRTDAGYPA 4549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1530 DRTVHQLVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKA 1609
Cdd:PRK12316 4550 TRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALI--ARG---VGPEVLVGIAMERSAEMMVGLLAVLKA 4624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1610 GGYFIPVDPGYPMARLTRIADTVTPALVLTRTGQGGCLPGAEvfgDVPVVALDRvADRLTAMPDQRPEVTVDPRGLAYSI 1689
Cdd:PRK12316 4625 GGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPD---GLASLALDR-DEDWEGFPAHDPAVRLHPDNLAYVI 4700
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1690 FTSGSTGQPKGVAVEHIGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMSALFEPLVSGRGVTLMPADATLADLAEELS 1769
Cdd:PRK12316 4701 YTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPERLYAEI 4780
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1770 GPLAYDYIRLTPSHLRHLVGHWTGQELPPAARGWVVGGETLDPALVKQLLELRPDAEVINHYGPTETVIGRVVHPVReAG 1849
Cdd:PRK12316 4781 HEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKAR-DG 4859
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1850 ELAVDSPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPAGEPGARMYRTGDLVRW 1929
Cdd:PRK12316 4860 DACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGGRLYRTGDLARY 4939
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1930 RGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRD----QQLVGWFIPAEDH--PPVTVSA-----LR 1998
Cdd:PRK12316 4940 RADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEgavgKQLVGYVVPQDPAlaDADEAQAelrdeLK 5019
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1999 RFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRALPGPTSGrpELEDRYQAPRTPGEQLLAELWSTVLGTDRIGIEDNFF 2078
Cdd:PRK12316 5020 AALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDAS--LLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFF 5097
|
1050 1060 1070
....*....|....*....|....*....|....*.
gi 653678460 2079 DLGGTSISVIQLSGACRRA-GVEISPKDVFEQPTVR 2113
Cdd:PRK12316 5098 ELGGHSLLAIQVTSRIQLElGLELPLRELFQTPTLA 5133
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
505-977 |
0e+00 |
|
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: 602.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 505 PGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLL 584
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 585 SDARPVLVVTDAatadrlgpdditglvvleetdtggypateppavpaGHSAYVIYTSGSTGRPKGVVITRAALDNFLAAM 664
Cdd:cd05930 81 EDSGAKLVLTDP-----------------------------------DDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWM 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 665 AERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALIDLAGRHRVTLAQATPTLWQALVPELSGP 744
Cdd:cd05930 126 QEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 745 ALAGIR-VLVGGEALPAELARRLGDA--GAEVTNMYGPTETTIWSTSGPTSEDSIRRGS--IGVPIDNTQVYVLDANLHP 819
Cdd:cd05930 206 ALPSLRlVLVGGEALPPDLVRRWRELlpGARLVNLYGPTEATVDATYYRVPPDDEEDGRvpIGRPIPNTRVYVLDENLRP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 820 APIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFGpPGTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEI 899
Cdd:cd05930 286 VPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFG-PGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEI 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 900 ETTLINAGPVRRAAAVVREDRPGDLRLVAYVIPDGPVAPD--ALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:cd05930 365 EAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDeeELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
505-977 |
0e+00 |
|
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: 587.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 505 PGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLL 584
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 585 SDARPVLVVTDAATADRLgPDDITGLVVLEETDTGGYPATEPPAVPaGHSAYVIYTSGSTGRPKGVVITRAALDNFLAAM 664
Cdd:cd12116 81 EDAEPALVLTDDALPDRL-PAGLPVLLLALAAAAAAPAAPRTPVSP-DDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 665 AERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALIDLAGRHRVTLAQATPTLWQALVPelSG- 743
Cdd:cd12116 159 RERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLD--AGw 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 744 PALAGIRVLVGGEALPAELARRLGDAGAEVTNMYGPTETTIWSTSGPTsEDSIRRGSIGVPIDNTQVYVLDANLHPAPIG 823
Cdd:cd12116 237 QGRAGLTALCGGEALPPDLAARLLSRVGSLWNLYGPTETTIWSTAARV-TAAAGPIPIGRPLANTQVYVLDAALRPVPPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 824 VLGELHIAGEGLARGYWNRPGLTAEKFLPDPFGPPGTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTL 903
Cdd:cd12116 316 VPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAAL 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 653678460 904 INAGPVRRAAAVVREDRpGDLRLVAYVIPDGPVAPD--ALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:cd12116 396 AAHPGVAQAAVVVREDG-GDRRLVAYVVLKAGAAPDaaALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1076-2279 |
3.50e-178 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 583.93 E-value: 3.50e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1076 PVPRDEPLPLSPMQESIWLADQVSAGDSVYNVPLALRLIGPLDRGALRRTLNRVVDRHEMLRTRIHPGPDGmPVQVADPA 1155
Cdd:PRK10252 1 AEPMSQHLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGE-VWQWVDPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1156 GGGAALTERD----AAPGTDLAQLLLAEAALGFTLATEHPL-RAVLWRLDEREHVLLLTAHHVAVDAWSMDLIQRDLTEL 1230
Cdd:PRK10252 80 LTFPLPEIIDlrtqPDPHAAAQALMQADLQQDLRVDSGKPLvFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1231 YAADTgHREPELDEP----ALAQADYAVWqRQSAQRGRYAAeldFWRTELTG--AVATEVAGDLP-RPATPGGGGGAVEF 1303
Cdd:PRK10252 160 YCAWL-RGEPTPASPftpfADVVEEYQRY-RASEAWQRDAA---FWAEQRRQlpPPASLSPAPLPgRSASADILRLKLEF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1304 ALAprqiqGIRELARRCGTTVSTVVLSALQTL-LYRITGGADVVIGSTVSGR-GNPRLdNLVGCLVNTVVLRGDLSGAPT 1381
Cdd:PRK10252 235 TDG-----AFRQLAAQASGVQRPDLALALVALwLGRLCGRMDYAAGFIFMRRlGSAAL-TATGPVLNVLPLRVHIAAQET 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1382 FHELLRRTHARTADALAHQELPFEHLVADRG--AGN----GPLFRIMYSFSSQEPAGRSAGDVDLEPVPVPvttckfDLV 1455
Cdd:PRK10252 309 LPELATRLAAQLKKMRRHQRYDAEQIVRDSGraAGDeplfGPVLNIKVFDYQLDFPGVQAQTHTLATGPVN------DLE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1456 LTV---VDGGSTLEgvLEYADDLYLPGTAERLVTSLTNLLAAAVRTPELAVTRLAITSESDTVRTSRWGRSeQHVGDDRT 1532
Cdd:PRK10252 383 LALfpdEHGGLSIE--ILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQLAQVNAT-AVEIPETT 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1533 VHQLVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGY 1612
Cdd:PRK10252 460 LSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLR--ERG---VKPGDSVAVALPRSVFLTLALHAIVEAGAA 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1613 FIPVDPGYPMARLTRIADTVTPALVLTRTGQggclpgAEVFGDVPVVALDRVADRLTAmPDQRPEVTVDPRGLAYSIFTS 1692
Cdd:PRK10252 535 WLPLDTGYPDDRLKMMLEDARPSLLITTADQ------LPRFADVPDLTSLCYNAPLAP-QGAAPLQLSQPHHTAYIIFTS 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1693 GSTGQPKGVAVEHIGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMSALFEPLVSGRGVTLMPADA-----TLADL-AE 1766
Cdd:PRK10252 608 GSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAhrdplAMQQFfAE 687
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1767 ElsgplAYDYIRLTPSHLRHLVGHWTGQELPPAA---RGWVVGGETLDPALVKQLlELRPDAEVINHYGPTETVIGRVVH 1843
Cdd:PRK10252 688 Y-----GVTTTHFVPSMLAAFVASLTPEGARQSCaslRQVFCSGEALPADLCREW-QQLTGAPLHNLYGPTEAAVDVSWY 761
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1844 PV-REAGELAVDSPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPAGePGARMYR 1922
Cdd:PRK10252 762 PAfGEELAAVRGSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFA-PGERMYR 840
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1923 TGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVR-----------DQQLVGWFIPAEDHPP 1991
Cdd:PRK10252 841 TGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqaaatggdARQLVGYLVSQSGLPL 920
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1992 vTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRALPGP-----TSGRpeledryqAPRTPGEQLLAELWSTVL 2066
Cdd:PRK10252 921 -DTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPelkaqVPGR--------APKTGTETIIAAAFSSLL 991
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 2067 GTDRIGIEDNFFDLGGTSISVIQLSGACRRA-GVEISPKDVFEQPTVRGQAmRAIARSRDDAYAPVLDtvfgaghtgttr 2145
Cdd:PRK10252 992 GCDVVDADADFFALGGHSLLAMKLAAQLSRQfARQVTPGQVMVASTVAKLA-TLLDAEEDESRRLGFG------------ 1058
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 2146 TVVTLRgEGDGRPVFCVHPSgGGVAW-YLPLARALPAGHPVHAFQPLGMDGREAPAETIEDMAAGYLADLRLVQPEGPYV 2224
Cdd:PRK10252 1059 TILPLR-EGDGPTLFCFHPA-SGFAWqFSVLSRYLDPQWSIYGIQSPRPDGPMQTATSLDEVCEAHLATLLEQQPHGPYH 1136
|
1210 1220 1230 1240 1250 1260 1270
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 653678460 2225 VVGWSLGGTIAFEMARQLDRLGEPVQLILLEPTLP----------------EVARTIDLHRPARDSYLRGA 2279
Cdd:PRK10252 1137 LLGYSLGGTLAQGIAARLRARGEEVAFLGLLDTWPpetqnwrekeangldpEVLAEIDREREAFLAAQQGS 1207
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1070-2264 |
3.27e-176 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 606.39 E-value: 3.27e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1070 DAVHLAPVPRDEPLPLSPMQESIWLADQVSAGDSVYNVPLALRLIGpLDRGALRRTLNRVVDRHEMLRTR-IHPGPDGMP 1148
Cdd:PRK12467 2634 DRLPVAVGDIEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGfLWDGELEEP 2712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1149 VQV-----------------ADPAGGGAALTERDAApgtdlaqlllaeaaLGFTLATEHPLRAVLWRLDEREHVLLLTAH 1211
Cdd:PRK12467 2713 LQVvykqarlpfsrldwrdrADLEQALDALAAADRQ--------------QGFDLLSAPLLRLTLVRTGEDRHHLIYTNH 2778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1212 HVAVDAWSMDLIQRDLTELYAADTghrepeLDEPALAQADYAVW-QRQSAQRGRyaaelDFWRTELtGAVA--TEVAGDL 1288
Cdd:PRK12467 2779 HILMDGWSGSQLLGEVLQRYFGQP------PPAREGRYRDYIAWlQAQDAEASE-----AFWKEQL-AALEepTRLARAL 2846
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1289 -PRPATPGGGGGAVEFALAPRQIQGIRELARRCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGR--GNPRLDNLVGC 1365
Cdd:PRK12467 2847 yPAPAEAVAGHGAHYLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRpaQLRGAEQQLGL 2926
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1366 LVNTVVLRGDLSGAPTFHELLRRTHARTADALAHQELPFEHLVADRGAGNGPLFRIMYSFSSQ--EPAGRSAGDVDLEPV 1443
Cdd:PRK12467 2927 FINTLPVIASPRAEQTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQGGEALFDSILVFENYpiSEALKQGAPSGLRFG 3006
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1444 PVP---VTTCKFDLVLTVvdgGSTLEGVLEYADDLYLPGTAERLVTSLTNLLAAAVRTPE--LAVTRLAITSESDTVRTS 1518
Cdd:PRK12467 3007 AVSsreQTNYPLTLAVGL---GDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAarLGELPTLAAHERRQVLHA 3083
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1519 rWGRSEQHVGDDRTVHQLVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPE 1598
Cdd:PRK12467 3084 -WNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLI--AIG---VGPDVLVGVAVERSVE 3157
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1599 LVVAMLAVLKAGGYFIPVDPGYPMARLTRIADTVTPALVLTRTGQGGCLPGAEVfgdVPVVALDRVAdrLTAMPDQRPEV 1678
Cdd:PRK12467 3158 MIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPAPAG---DTALTLDRLD--LNGYSENNPST 3232
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1679 TVDPRGLAYSIFTSGSTGQPKGVAVEHIGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMSALFEPLVSGRGVTLmpAD 1758
Cdd:PRK12467 3233 RVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVV--RD 3310
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1759 ATLADLAEELSGPLAYDY--IRLTPSHLRHLVGHWTGQELPPAARgWVVGGETLDPALVKQLLELRPDAEVINHYGPTET 1836
Cdd:PRK12467 3311 NDLWDPEELWQAIHAHRIsiACFPPAYLQQFAEDAGGADCASLDI-YVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEA 3389
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1837 VIgRVVHPVREAGELAVDSPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPAGEP 1916
Cdd:PRK12467 3390 VV-TVTLWKCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSGS 3468
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1917 GARMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRD----QQLVGWFIPaEDHPPV 1992
Cdd:PRK12467 3469 GGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDgaggKQLVAYVVP-ADPQGD 3547
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1993 TVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRALPGPTSgrpELEDRYQAPRTPGEQLLAELWSTVLGTDRIG 2072
Cdd:PRK12467 3548 WRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDA---KGSREYVAPRSEVEQQLAAIWADVLGVEQVG 3624
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 2073 IEDNFFDLGGTSISVIQLSGACRRA-GVEISPKDVFEQPTVRGQAmrAIARSRDDAYAPVLDTVfgaghtgttrtvvtlR 2151
Cdd:PRK12467 3625 VTDNFFELGGDSLLALQVLSRIRQSlGLKLSLRDLMSAPTIAELA--GYSPLGDVPVNLLLDLN---------------R 3687
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 2152 GEGDGRPVFCVHPSGGGVAWYLPLARALPAGHPVHAFQPLGMDGREAPAETIEDMAAGYLADLRLVQPEGPYVVVGWSLG 2231
Cdd:PRK12467 3688 LETGFPALFCRHEGLGTVFDYEPLAVILEGDRHVLGLTCRHLLDDGWQDTSLQAMAVQYADYILWQQAKGPYGLLGWSLG 3767
|
1210 1220 1230
....*....|....*....|....*....|....
gi 653678460 2232 GTIAFEMARQLDRLGEPVQLI-LLEPTLPEVART 2264
Cdd:PRK12467 3768 GTLARLVAELLEREGESEAFLgLFDNTLPLPDEF 3801
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
495-977 |
3.44e-173 |
|
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: 540.71 E-value: 3.44e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 495 ERFQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPD 574
Cdd:cd17646 2 ALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 575 FPVERIAYLLSDARPVLVVTDAATADRLGPDDitGLVVLEETDTGGYPATEPPAVPAGHS-AYVIYTSGSTGRPKGVVIT 653
Cdd:cd17646 82 YPADRLAYMLADAGPAVVLTTADLAARLPAGG--DVALLGDEALAAPPATPPLVPPRPDNlAYVIYTSGSTGRPKGVMVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 654 RAALDNFLAAMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALIDLAGRHRVTLAQATPTL 733
Cdd:cd17646 160 HAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 734 WQALVPELSGPALAGIR-VLVGGEALPAELARRLGDA-GAEVTNMYGPTETTIWSTSGPTSEDSIRRG-SIGVPIDNTQV 810
Cdd:cd17646 240 LRVFLAEPAAGSCASLRrVFCSGEALPPELAARFLALpGAELHNLYGPTEAAIDVTHWPVRGPAETPSvPIGRPVPNTRL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 811 YVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFGpPGTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLR 890
Cdd:cd17646 320 YVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFG-PGSRMYRTGDLARWRPDGALEFLGRSDDQVKIR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 891 GFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIPDG---PVAPDALRTELSRTLPDYMIPAVIVPVPDFPTT 967
Cdd:cd17646 399 GFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAgaaGPDTAALRAHLAERLPEYMVPAAFVVLDALPLT 478
|
490
....*....|
gi 653678460 968 PNGKLDRAAL 977
Cdd:cd17646 479 ANGKLDRAAL 488
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
495-981 |
5.45e-168 |
|
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: 526.51 E-value: 5.45e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 495 ERFQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPD 574
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 575 FPVERIAYLLSDARPVLVVTDAATADRLgpdDITGLVVLEETDTGGYPATE--PPAVPAGHSAYVIYTSGSTGRPKGVVI 652
Cdd:cd17655 81 YPEERIQYILEDSGADILLTQSHLQPPI---AFIGLIDLLDEDTIYHEESEnlEPVSKSDDLAYVIYTSGSTGKPKGVMI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 653 TRAALDNFLAAMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALIDLAGRHRVTLAQATPT 732
Cdd:cd17655 158 EHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 733 LWQALVPELSGPALAGIRVLVGGEALPAELARRLGD---AGAEVTNMYGPTETTIWSTSGPTSEDSIRRGS--IGVPIDN 807
Cdd:cd17655 238 HLKLLDAADDSEGLSLKHLIVGGEALSTELAKKIIElfgTNPTITNAYGPTETTVDASIYQYEPETDQQVSvpIGKPLGN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 808 TQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgPPGTRMYRTGDLVRWSAAGDLEYLGRTDHQV 887
Cdd:cd17655 318 TRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPF-VPGERMYRTGDLARWLPDGNIEFLGRIDHQV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 888 KLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIPDGPVAPDALRTELSRTLPDYMIPAVIVPVPDFPTT 967
Cdd:cd17655 397 KIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLT 476
|
490
....*....|....
gi 653678460 968 PNGKLDRAALPAPD 981
Cdd:cd17655 477 PNGKVDRKALPEPD 490
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
495-977 |
2.61e-167 |
|
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: 524.07 E-value: 2.61e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 495 ERFQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPD 574
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 575 FPVERIAYLLSDARPVLVVTDAATADRLGPDdiTGLVVLEETDTGGYPATEPPAVPAGHSAYVIYTSGSTGRPKGVVITR 654
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGL--EVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 655 AALDNfLAAMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALIDLAGRHRVTLAQATPTLW 734
Cdd:cd12117 159 RGVVR-LVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 735 QALVPELSGpALAGIR-VLVGGEALPAELARRLGDAGAE--VTNMYGPTETTIWSTSGPTSEDSIRRGS--IGVPIDNTQ 809
Cdd:cd12117 238 NQLADEDPE-CFAGLReLLTGGEVVSPPHVRRVLAACPGlrLVNGYGPTENTTFTTSHVVTELDEVAGSipIGRPIANTR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 810 VYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFGPPGtRMYRTGDLVRWSAAGDLEYLGRTDHQVKL 889
Cdd:cd12117 317 VYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGE-RLYRTGDLARWLPDGRLEFLGRIDDQVKI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 890 RGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIPDGPVAPDALRTELSRTLPDYMIPAVIVPVPDFPTTPN 969
Cdd:cd12117 396 RGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTAN 475
|
....*...
gi 653678460 970 GKLDRAAL 977
Cdd:cd12117 476 GKVDRRAL 483
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
505-978 |
3.62e-167 |
|
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: 521.81 E-value: 3.62e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 505 PGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLL 584
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 585 SDARPVLVVTDAatadrlgpdditglvvleetdtggypateppavpaGHSAYVIYTSGSTGRPKGVVITRAALDNFLAAM 664
Cdd:cd17652 81 ADARPALLLTTP-----------------------------------DNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 665 AERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALIDLAGRHRVTLAQATPTLWQALvPELSGP 744
Cdd:cd17652 126 IAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAAL-PPDDLP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 745 ALAGirVLVGGEALPAELARRLGDaGAEVTNMYGPTETTIWSTSGPTSEDSiRRGSIGVPIDNTQVYVLDANLHPAPIGV 824
Cdd:cd17652 205 DLRT--LVVAGEACPAELVDRWAP-GRRMINAYGPTETTVCATMAGPLPGG-GVPPIGRPVPGTRVYVLDARLRPVPPGV 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 825 LGELHIAGEGLARGYWNRPGLTAEKFLPDPFGPPGTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLI 904
Cdd:cd17652 281 PGELYIAGAGLARGYLNRPGLTAERFVADPFGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALT 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 653678460 905 NAGPVRRAAAVVREDRPGDLRLVAYVIPDGPVAPDA--LRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAALP 978
Cdd:cd17652 361 EHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAaeLRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1065-2189 |
5.33e-157 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 546.86 E-value: 5.33e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1065 TSTGDDAVHLAPVPRDEPLPLSPMQESIW---LADQvSAGDSVYNvplaLRL-IGPLDRGALRRTLNRVVDRHEMLRTRI 1140
Cdd:PRK12316 1539 SQAQLDALPLPAGEIADIYPLSPMQQGMLfhsLYEQ-EAGDYINQ----LRVdVQGLDPDRFRAAWQATVDRHEILRSGF 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1141 HPGPD-GMPVQVAD-----PAGGGAALTERDaaPGTDLAQLLLAEAALGFTLATEHPLRAVLWRLDEREHVLLLTAHHVA 1214
Cdd:PRK12316 1614 LWQDGlEQPLQVIHkqvelPFAELDWRGRED--LGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHIL 1691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1215 VDAWSMDLIQRDLTELYAadtGHREPEldePALAQADYAVW-QRQSAqrgryAAELDFWRTELTGAVA-TEVAGDLPRPA 1292
Cdd:PRK12316 1692 MDGWSNAQLLGEVLQRYA---GQPVAA---PGGRYRDYIAWlQRQDA-----AASEAFWKEQLAALEEpTRLAQAARTED 1760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1293 TPGGGGGAVEfALAPRQIQGIRELARRCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGRGN--PRLDNLVGCLVNTV 1370
Cdd:PRK12316 1761 GQVGYGDHQQ-LLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAelPGIEQQIGLFINTL 1839
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1371 VLRGDLSGAPTFHELLRRTHARTADALAHQELPFEHLVADRGAGNGPLFRIMYSFSS---------QEPAGRSAGDV-DL 1440
Cdd:PRK12316 1840 PVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWAGQGGEALFDSLLVFENypvaealkqGAPAGLVFGRVsNH 1919
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1441 EPVPVPVTtckfdLVLTVvdgGSTLEGVLEYADDLYLPGTAERLVTSLTNLLAAAVRTPELAVTRLAITSESDTVRT-SR 1519
Cdd:PRK12316 1920 EQTNYPLT-----LAVTL---GETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRIlAD 1991
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1520 WGRSEQHVGDDRTVHQLVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPEL 1599
Cdd:PRK12316 1992 WDRTPEAYPRGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLR--ARG---VGPEVRVAIAAERSFEL 2066
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1600 VVAMLAVLKAGGYFIPVDPGYPMARLTRIADTVTPALVLTRTGQGGCLPgaeVFGDVPVVALDRVADrLTAMPDQRPEVT 1679
Cdd:PRK12316 2067 VVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLP---LPAGVARLPLDRDAE-WADYPDTAPAVQ 2142
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1680 VDPRGLAYSIFTSGSTGQPKGVAVEHIGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMSALFEPLVSGrgVTLMPADA 1759
Cdd:PRK12316 2143 LAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNG--ARVLIRDD 2220
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1760 TLADlAEELsgplaYDYIR--------LTPSHLRHLVGHWTGQELPPAARGWVVGGETLDPALVKQLLELRPDAEVINHY 1831
Cdd:PRK12316 2221 ELWD-PEQL-----YDEMErhgvtildFPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGY 2294
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1832 GPTETVIGRVVHPVREAGELAVDSPlPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPD 1911
Cdd:PRK12316 2295 GPTEAVVTPLLWKCRPQDPCGAAYV-PIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPD 2373
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1912 PAGEPGARMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRD----QQLVGWFIPaE 1987
Cdd:PRK12316 2374 PFSASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDgasgKQLVAYVVP-D 2452
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1988 DHPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRALPGPTSGrpELEDRYQAPRTPGEQLLAELWSTVLG 2067
Cdd:PRK12316 2453 DAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVS--QLRQAYVAPQEGLEQRLAAIWQAVLK 2530
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 2068 TDRIGIEDNFFDLGGTSISVIQLSGACRRA-GVEISPKDVFEQPTVrgQAMRAIARSRDDAYAPVLDTVfgaghtgtTRT 2146
Cdd:PRK12316 2531 VEQVGLDDHFFELGGHSLLATQVVSRVRQDlGLEVPLRILFERPTL--AAFAASLESGQTSRAPVLQKV--------TRV 2600
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|...
gi 653678460 2147 VVTLRGEGDGRPVFCVHPSGGGVAWYLPLARALPAGHPVHAFQ 2189
Cdd:PRK12316 2601 QPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALE 2643
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
505-977 |
3.35e-156 |
|
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: 491.44 E-value: 3.35e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 505 PGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLL 584
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 585 SDARPVLVVTDaatadrlgPDDItglvvleetdtggypateppavpaghsAYVIYTSGSTGRPKGVVITRAALDNFLAAM 664
Cdd:cd17643 81 ADSGPSLLLTD--------PDDL---------------------------AYVIYTSGSTGRPKGVVVSHANVLALFAAT 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 665 AERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALIDLAGRHRVTLAQATPTLWQALVPEL--S 742
Cdd:cd17643 126 QRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAAdrD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 743 GPALAGIR-VLVGGEALPAELAR----RLGDAGAEVTNMYGPTETTIWSTSGPTSEDSIRRG---SIGVPIDNTQVYVLD 814
Cdd:cd17643 206 GRDPLALRyVIFGGEALEAAMLRpwagRFGLDRPQLVNMYGITETTVHVTFRPLDAADLPAAaasPIGRPLPGLRVYVLD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 815 ANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFGPPGTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRI 894
Cdd:cd17643 286 ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRI 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 895 ELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIPDGPVAPD--ALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKL 972
Cdd:cd17643 366 ELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADiaELRALLKELLPDYMVPARYVPLDALPLTVNGKL 445
|
....*
gi 653678460 973 DRAAL 977
Cdd:cd17643 446 DRAAL 450
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1545-2033 |
4.88e-156 |
|
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: 490.89 E-value: 4.88e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1545 PGWTALRTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMAR 1624
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLR--ERG---VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1625 LTRIADTVTPALVLTrtgqggclpgaevfgdvpvvaldrvadrltampdqrpevtvDPRGLAYSIFTSGSTGQPKGVAVE 1704
Cdd:cd05930 76 LAYILEDSGAKLVLT-----------------------------------------DPDDLAYVIYTSGSTGKPKGVMVE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1705 HIGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMSALFEPLVSGRGVTLMPADAT-----LADLAEELSgplaYDYIRL 1779
Cdd:cd05930 115 HRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRkdpeaLADLLAEEG----ITVLHL 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1780 TPSHLRHLVGHwTGQELPPAARGWVVGGETLDPALVKQLLELRPDAEVINHYGPTETVIGRVVHPVREAGELavDSPLPL 1859
Cdd:cd05930 191 TPSLLRLLLQE-LELAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDEE--DGRVPI 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1860 GRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPAGePGARMYRTGDLVRWRGDGLLDFVG 1939
Cdd:cd05930 268 GRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFG-PGERMYRTGDLVRWLPDGNLEFLG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1940 RVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVR-----DQQLVGWFIPAEDhPPVTVSALRRFCAEQLPEFMVPNQW 2014
Cdd:cd05930 347 RIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVARedgdgEKRLVAYVVPDEG-GELDEEELRAHLAERLPDYMVPSAF 425
|
490
....*....|....*....
gi 653678460 2015 VALDAFPLTPHGKVNHRAL 2033
Cdd:cd05930 426 VVLDALPLTPNGKVDRKAL 444
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
497-978 |
6.17e-153 |
|
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: 484.15 E-value: 6.17e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 497 FQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFP 576
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 577 VERIAYLLSDARPVLVVTDAATADRLGPDDITGLVVLEETDTGGYPATEPPAVPAGHSAYVIYTSGSTGRPKGVVITRAA 656
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 657 LDNFLAAMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALIDLAGRHRVTLAQATPTLWQA 736
Cdd:cd17651 161 LANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 737 LVPEL--SGPALAGIR-VLVGGEALP-----AELARRLGdaGAEVTNMYGPTETTIwSTSGPTSEDSIRRG---SIGVPI 805
Cdd:cd17651 241 LAEHGrpLGVRLAALRyLLTGGEQLVltedlREFCAGLP--GLRLHNHYGPTETHV-VTALSLPGDPAAWPappPIGRPI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 806 DNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFGpPGTRMYRTGDLVRWSAAGDLEYLGRTDH 885
Cdd:cd17651 318 DNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFV-PGARMYRTGDLARWLPDGELEFLGRADD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 886 QVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIPD--GPVAPDALRTELSRTLPDYMIPAVIVPVPD 963
Cdd:cd17651 397 QVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDpeAPVDAAELRAALATHLPEYMVPSAFVLLDA 476
|
490
....*....|....*
gi 653678460 964 FPTTPNGKLDRAALP 978
Cdd:cd17651 477 LPLTPNGKLDRRALP 491
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
518-915 |
1.16e-147 |
|
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: 465.59 E-value: 1.16e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 518 SYRELDERANRLAR-LLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARPVLVVTDA 596
Cdd:TIGR01733 1 TYRELDERANRLARhLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 597 ATADRLGPDDITGLVV--LEETDTGGYPATEPPAVPAGHS--AYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTA 672
Cdd:TIGR01733 81 ALASRLAGLVLPVILLdpLELAALDDAPAPPPPDAPSGPDdlAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 673 EDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALIDLAGRHR-VTLAQATPTLWQALVPELsGPALAGIR- 750
Cdd:TIGR01733 161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHpVTVLNLTPSLLALLAAAL-PPALASLRl 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 751 VLVGGEALPAELARRLGDA--GAEVTNMYGPTETTIWSTSGPTSEDSIRRGS---IGVPIDNTQVYVLDANLHPAPIGVL 825
Cdd:TIGR01733 240 VILGGEALTPALVDRWRARgpGARLINLYGPTETTVWSTATLVDPDDAPRESpvpIGRPLANTRLYVLDDDLRPVPVGVV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 826 GELHIAGEGLARGYWNRPGLTAEKFLPDPF-GPPGTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLi 904
Cdd:TIGR01733 320 GELYIGGPGVARGYLNRPELTAERFVPDPFaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAAL- 398
|
410
....*....|.
gi 653678460 905 NAGPVRRAAAV 915
Cdd:TIGR01733 399 LRHPGVREAVV 409
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
46-459 |
1.03e-143 |
|
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: 454.89 E-value: 1.03e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 46 PVPLAPGQAGIWFSEQLRPGTPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVFRLGpDGEPVQQTAPAAPVALP 125
Cdd:cd19531 1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEV-DGEPVQVILPPLPLPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 126 VIDVT-------EADLPQALRTAAEQPFDLERGPLLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLLLADLARAYAGEL- 197
Cdd:cd19531 80 VVDLSglpeaerEAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLa 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 198 --PAGVAAPA--FRDVAAWQHGRLAAGELDDQLRYWRQRLAGLPD-LEIPGDRQRPADRDWRAHSVRRELPAATEAAVRR 272
Cdd:cd19531 160 grPSPLPPLPiqYADYAVWQREWLQGEVLERQLAYWREQLAGAPPvLELPTDRPRPAVQSFRGARVRFTLPAELTAALRA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 273 LAAAHDTTPFTVLLAAYGTFLHRLTGQDDFAVGVPVAGRGRTDLESVVGLFAGMVPVRLDLTGRPSFDEVLSRTVAGSRN 352
Cdd:cd19531 240 LARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 353 DFAHPQIPFDRLVRELRRDRIAGSQLLVQAMAGTEST-AVALTFGEAAGTEQPVDVALAKCDLDLSVLDDGDRLAVTLVA 431
Cdd:cd19531 320 AYAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNApAAALELPGLTVEPLEVDSGTAKFDLTLSLTETDGGLRGSLEY 399
|
410 420
....*....|....*....|....*...
gi 653678460 432 AADLFTPAAAEQLAGQFLSLLAGLTGAP 459
Cdd:cd19531 400 NTDLFDAATIERMAGHFQTLLEAIVADP 427
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
493-977 |
8.17e-143 |
|
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: 453.31 E-value: 8.17e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 493 LRERFQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPID 572
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 573 PDFPVERIAYLLSDARPVLVVTDAAtadrlgpdditglvvleetdtggypateppavpagHSAYVIYTSGSTGRPKGVVI 652
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVLTDPD-----------------------------------DLAYVIYTSGSTGRPKGVAI 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 653 TRAALDNFLAAMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADadtarNPAALIDLAGRHRVTLAQATPT 732
Cdd:cd12115 126 EHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLAD-----NVLALPDLPAAAEVTLINTVPS 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 733 LWQALVPElsGPALAGIRVL-VGGEALPAELARRLGDA--GAEVTNMYGPTETTIWSTSGPTSEDSIRRGSIGVPIDNTQ 809
Cdd:cd12115 201 AAAELLRH--DALPASVRVVnLAGEPLPRDLVQRLYARlqVERVVNLYGPSEDTTYSTVAPVPPGASGEVSIGRPLANTQ 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 810 VYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFGpPGTRMYRTGDLVRWSAAGDLEYLGRTDHQVKL 889
Cdd:cd12115 279 AYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFG-PGARLYRTGDLVRWRPDGLLEFLGRADNQVKV 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 890 RGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIPDGPVAP--DALRTELSRTLPDYMIPAVIVPVPDFPTT 967
Cdd:cd12115 358 RGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGlvEDLRRHLGTRLPAYMVPSRFVRLDALPLT 437
|
490
....*....|
gi 653678460 968 PNGKLDRAAL 977
Cdd:cd12115 438 PNGKIDRSAL 447
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
505-978 |
8.87e-142 |
|
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: 450.67 E-value: 8.87e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 505 PGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLL 584
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 585 SDARPVLVVTDaatadrlGPDditglvvleetdtggypateppavpagHSAYVIYTSGSTGRPKGVVITRAALDNFLAAM 664
Cdd:cd17649 81 EDSGAGLLLTH-------HPR---------------------------QLAYVIYTSGSTGTPKGVAVSHGPLAAHCQAT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 665 AERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALIDLAGRHRVTLAQATPTLWQALVPEL--- 741
Cdd:cd17649 127 AERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEAdrt 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 742 -SGPALAGIRVLVGGEALPAELARRLGDAGAEVTNMYGPTETTIWSTSGPTSEDSIRRGS---IGVPIDNTQVYVLDANL 817
Cdd:cd17649 207 gDGRPPSLRLYIFGGEALSPELLRRWLKAPVRLFNAYGPTEATVTPLVWKCEAGAARAGAsmpIGRPLGGRSAYILDADL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 818 HPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFGPPGTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELG 897
Cdd:cd17649 287 NPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 898 EIETTLInAGPVRRAAAVVREDRPGDLRLVAYVIPDGPVA----PDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLD 973
Cdd:cd17649 367 EIEAALL-EHPGVREAAVVALDGAGGKQLVAYVVLRAAAAqpelRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLD 445
|
....*
gi 653678460 974 RAALP 978
Cdd:cd17649 446 RKALP 450
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
1534-2033 |
2.38e-141 |
|
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: 450.96 E-value: 2.38e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1534 HQLVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALhtGALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYF 1613
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLL--RARG---VGPEDRVAVLLPRSADLVVALLAVLKAGAAY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1614 IPVDPGYPMARLTRIADTVTPALVLTRTGQGGCLPGAevfGDVPVValdrVADRLTAMPDQRPEVTVDPRGLAYSIFTSG 1693
Cdd:cd17646 76 LPLDPGYPADRLAYMLADAGPAVVLTTADLAARLPAG---GDVALL----GDEALAAPPATPPLVPPRPDNLAYVIYTSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1694 STGQPKGVAVEHIGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMSALFEPLVSGRGVTLMPAD-----ATLADLAEEL 1768
Cdd:cd17646 149 STGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGghrdpAYLAALIREH 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1769 SGPLAYdyirLTPSHLRHLVGhWTGQELPPAARGWVVGGETLDPALVKQLLELrPDAEVINHYGPTETVIGRVVHPVREA 1848
Cdd:cd17646 229 GVTTCH----FVPSMLRVFLA-EPAAGSCASLRRVFCSGEALPPELAARFLAL-PGAELHNLYGPTEAAIDVTHWPVRGP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1849 GElavDSPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPAGePGARMYRTGDLVR 1928
Cdd:cd17646 303 AE---TPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFG-PGSRMYRTGDLAR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1929 WRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRD-----QQLVGWFIPAEDHPPVTVSALRRFCAE 2003
Cdd:cd17646 379 WRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAapagaARLVGYVVPAAGAAGPDTAALRAHLAE 458
|
490 500 510
....*....|....*....|....*....|
gi 653678460 2004 QLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:cd17646 459 RLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
492-978 |
3.13e-139 |
|
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: 443.80 E-value: 3.13e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 492 SLRERFQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPI 571
Cdd:cd17644 1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 572 DPDFPVERIAYLLSDARPVLVVTDaatadrlgPDDItglvvleetdtggypateppavpaghsAYVIYTSGSTGRPKGVV 651
Cdd:cd17644 81 DPNYPQERLTYILEDAQISVLLTQ--------PENL---------------------------AYVIYTSGSTGKPKGVM 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 652 ITRAALDNFLAAMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALIDLAGRHRVTLAQATP 731
Cdd:cd17644 126 IEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 732 TLWQALVPELSGPALAGIR----VLVGGEALPAELARRLGDAGAE---VTNMYGPTETTIWST----SGPTSEDsIRRGS 800
Cdd:cd17644 206 AYWHLLVLELLLSTIDLPSslrlVIVGGEAVQPELVRQWQKNVGNfiqLINVYGPTEATIAATvcrlTQLTERN-ITSVP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 801 IGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPF-GPPGTRMYRTGDLVRWSAAGDLEY 879
Cdd:cd17644 285 IGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFnSSESERLYKTGDLARYLPDGNIEY 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 880 LGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIPDGPVAPDA--LRTELSRTLPDYMIPAV 957
Cdd:cd17644 365 LGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTveLRQFLKAKLPDYMIPSA 444
|
490 500
....*....|....*....|.
gi 653678460 958 IVPVPDFPTTPNGKLDRAALP 978
Cdd:cd17644 445 FVVLEELPLTPNGKIDRRALP 465
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
38-1046 |
8.87e-135 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 475.43 E-value: 8.87e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 38 GLPVqPPGPV----PLAPGQAGIWFSEQLRPGTPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVF--RLGPDGE 111
Cdd:PRK05691 3246 ALPV-PAAEIedvyPLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFswNAGETML 3324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 112 PVQQTAPAAPV------ALPViDVTEADLPQALRTAAEQPFDLERGPLLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLL 185
Cdd:PRK05691 3325 QVIHKPGRTPIdyldwrGLPE-DGQEQRLQALHKQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLL 3403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 186 LADLARAYA----GELPAGVAAPAFRDVAAWqhgrLAAGELDDQLRYWRQRLAGLP-DLEIPGDRqrPADRDWRAHS--- 257
Cdd:PRK05691 3404 MNDFFEIYTalgeGREAQLPVPPRYRDYIGW----LQRQDLAQARQWWQDNLRGFErPTPIPSDR--PFLREHAGDSggm 3477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 258 ----VRRELPAATEAAVRRLAAAHDTTPFTVLLAAYGTFLHRLTGQDDFAVGVPVAGR--GRTDLESVVGLFAGMVPVRL 331
Cdd:PRK05691 3478 vvgdCYTRLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRpvSMPQMQRTVGLFINSIALRV 3557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 332 DLTG---RPSFDEVLSRTVAGSRNDFAHPQIPfdrLVRELRRDRIAGSQLLVQAMAGTESTAVALT-FGEAAGTEQPVDV 407
Cdd:PRK05691 3558 QLPAagqRCSVRQWLQGLLDSNMELREYEYLP---LVAIQECSELPKGQPLFDSLFVFENAPVEVSvLDRAQSLNASSDS 3634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 408 ALAKCDLDLS-VLDDGDRLAVTLVAAADLFTPAAAEQLAGQFLSLLAGLTGAPDRLVSEVDLLDTDELHTVLCRWNDTAR 486
Cdd:PRK05691 3635 GRTHTNFPLTaVCYPGDDLGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGEQERDFLLDGCNRSER 3714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 487 PLP-AASLRERFQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAG 565
Cdd:PRK05691 3715 DYPlEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAG 3794
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 566 AAYLPIDPDFPVERIAYLLSDAR-PVLVVTDAATA------DRLGPDDITGLVVLEETDTGGYPATEPPAVPAGHS-AYV 637
Cdd:PRK05691 3795 AGYLPLDPGLPAQRLQRIIELSRtPVLVCSAACREqarallDELGCANRPRLLVWEEVQAGEVASHNPGIYSGPDNlAYV 3874
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 638 IYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDRVLATTTVSFDIAGLE-LYLPLrSGAGVVLADADTARNPAALI 716
Cdd:PRK05691 3875 IYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQfLAAPL-FGARVEIVPNAIAHDPQGLL 3953
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 717 DLAGRHRVTLAQATPTLWQALVPElSGPALAGIR-VLVGGEALPAELAR----RLGDAGaeVTNMYGPTETTIWSTSGPT 791
Cdd:PRK05691 3954 AHVQAQGITVLESVPSLIQGMLAE-DRQALDGLRwMLPTGEAMPPELARqwlqRYPQIG--LVNAYGPAECSDDVAFFRV 4030
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 792 SEDSIRrGS---IGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFGPPGTRMYRTGDL 868
Cdd:PRK05691 4031 DLASTR-GSylpIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFGAPGERLYRTGDL 4109
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 869 VRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDlRLVAYVIP-DGPVAPDALRTE--- 944
Cdd:PRK05691 4110 ARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNGK-HLVGYLVPhQTVLAQGALLERikq 4188
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 945 -LSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAALPAPDYG-TRSTA-RPPRDDRERFLCTAFAEVLGLPEVAVSDNFFEL 1021
Cdd:PRK05691 4189 rLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGqLQSQAyLAPRNELEQTLATIWADVLKVERVGVHDNFFEL 4268
|
1050 1060
....*....|....*....|....*
gi 653678460 1022 GGHSLLAFRLLARIRDEFGAGFSLR 1046
Cdd:PRK05691 4269 GGHSLLATQIASRVQKALQRNVPLR 4293
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
1535-2036 |
1.15e-134 |
|
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: 431.75 E-value: 1.15e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1535 QLVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHtgalgAPPVGPETPVLLLLDRSPELVVAMLAVLKAGGYFI 1614
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLR-----EKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1615 PVDPGYPMARLTRIADTVTPALVLTrtgQGGCLPGAEVFGDVPVVALDRVADRltamPDQRPEVTVDPRGLAYSIFTSGS 1694
Cdd:cd17655 76 PIDPDYPEERIQYILEDSGADILLT---QSHLQPPIAFIGLIDLLDEDTIYHE----ESENLEPVSKSDDLAYVIYTSGS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1695 TGQPKGVAVEHIGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMSALFEPLVSGRGVTLMPADatladlaEELSGPLAY 1774
Cdd:cd17655 149 TGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKE-------TVLDGQALT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1775 DYIR--------LTPSHLRHL--VGHWTGQELppaaRGWVVGGETLDPALVKQLLELRPDA-EVINHYGPTETVIGRVVH 1843
Cdd:cd17655 222 QYIRqnritiidLTPAHLKLLdaADDSEGLSL----KHLIVGGEALSTELAKKIIELFGTNpTITNAYGPTETTVDASIY 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1844 PVrEAGELAVDSPlPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPAgEPGARMYRT 1923
Cdd:cd17655 298 QY-EPETDQQVSV-PIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPF-VPGERMYRT 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1924 GDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVR-DQQ----LVGWFIPAEDhppVTVSALR 1998
Cdd:cd17655 375 GDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARkDEQgqnyLCAYIVSEKE---LPVAQLR 451
|
490 500 510
....*....|....*....|....*....|....*...
gi 653678460 1999 RFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRALPGP 2036
Cdd:cd17655 452 EFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPEP 489
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
1533-2033 |
7.72e-132 |
|
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: 421.73 E-value: 7.72e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1533 VHQLVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALhtGALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGY 1612
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARL--RAAG---VGPESRVGVCLERTPDLVVALLAVLKAGAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1613 FIPVDPGYPMARLTRIADTVTPALVLTrtgqggclpgaevfgdvpvvaldrvadrltampdqrpevtvDPRGLAYSIFTS 1692
Cdd:cd12115 76 YVPLDPAYPPERLRFILEDAQARLVLT-----------------------------------------DPDDLAYVIYTS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1693 GSTGQPKGVAVEHIGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMSALFEPLVSGRGVTLMPADATLADLAEELSGPL 1772
Cdd:cd12115 115 GSTGRPKGVAIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLADNVLALPDLPAAAEVTL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1773 aydyIRLTPSHLRHLVGHwtgQELPPAARGWVVGGETLDPALVKQLLELRPDAEVINHYGPTETVIGRVVHPVREAGELA 1852
Cdd:cd12115 195 ----INTVPSAAAELLRH---DALPASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPGASGE 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1853 VdsplPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPAGePGARMYRTGDLVRWRGD 1932
Cdd:cd12115 268 V----SIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFG-PGARLYRTGDLVRWRPD 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1933 GLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVR-----DQQLVGWfIPAEDHPPVTVSALRRFCAEQLPE 2007
Cdd:cd12115 343 GLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIgdaagERRLVAY-IVAEPGAAGLVEDLRRHLGTRLPA 421
|
490 500
....*....|....*....|....*.
gi 653678460 2008 FMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:cd12115 422 YMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
1082-1499 |
1.61e-131 |
|
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: 420.22 E-value: 1.61e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1082 PLPLSPMQESIWLADQVSAGDSVYNVPLALRLIGPLDRGALRRTLNRVVDRHEMLRTRIHPGpDGMPVQVADPAGGgAAL 1161
Cdd:cd19531 1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEV-DGEPVQVILPPLP-LPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1162 TERD------AAPGTDLAQLLLAEAALGFTLATEHPLRAVLWRLDEREHVLLLTAHHVAVDAWSMDLIQRDLTELYAADT 1235
Cdd:cd19531 79 PVVDlsglpeAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1236 GHREPELDEPALAQADYAVWQRQSAQRGRYAAELDFWRTELTGAVAT-EVAGDLPRPATPGGGGGAVEFALAPRQIQGIR 1314
Cdd:cd19531 159 AGRPSPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVlELPTDRPRPAVQSFRGARVRFTLPAELTAALR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1315 ELARRCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGRGNPRLDNLVGCLVNTVVLRGDLSGAPTFHELLRRTHARTA 1394
Cdd:cd19531 239 ALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1395 DALAHQELPFEHLVA----DRGAGNGPLFRIMYSFSSQEPAGRSAGDVDLEPVPVPVTTCKFDLVLTVVDGGSTLEGVLE 1470
Cdd:cd19531 319 EAYAHQDLPFEKLVEalqpERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTETDGGLRGSLE 398
|
410 420
....*....|....*....|....*....
gi 653678460 1471 YADDLYLPGTAERLVTSLTNLLAAAVRTP 1499
Cdd:cd19531 399 YNTDLFDAATIERMAGHFQTLLEAIVADP 427
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
505-977 |
3.47e-131 |
|
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: 421.29 E-value: 3.47e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 505 PGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLL 584
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 585 SDARPVLVVTDAATADrlgPDDITGLVVLEETDTGGYPATEPPAVPAGH-SAYVIYTSGSTGRPKGVVITRAALDNFLAA 663
Cdd:cd12114 81 ADAGARLVLTDGPDAQ---LDVAVFDVLILDLDALAAPAPPPPVDVAPDdLAYVIFTSGSTGTPKGVMISHRAALNTILD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 664 MAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALIDLAGRHRVTLAQATPTLWQAL--VPEL 741
Cdd:cd12114 158 INRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLldVLEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 742 SGPALAGIR-VLVGGEALPAELARRLGD--AGAEVTNMYGPTETTIWSTSGPTSEDSIRRGSI--GVPIDNTQVYVLDAN 816
Cdd:cd12114 238 AQALLPSLRlVLLSGDWIPLDLPARLRAlaPDARLISLGGATEASIWSIYHPIDEVPPDWRSIpyGRPLANQRYRVLDPR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 817 LHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDpfgPPGTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIEL 896
Cdd:cd12114 318 GRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTH---PDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIEL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 897 GEIETTLINAGPVRRAAAVVReDRPGDLRLVAYVIPDG---PVAPDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLD 973
Cdd:cd12114 395 GEIEAALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDNdgtPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVD 473
|
....
gi 653678460 974 RAAL 977
Cdd:cd12114 474 RAAL 477
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1535-2033 |
3.70e-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: 421.22 E-value: 3.70e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1535 QLVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFI 1614
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLR--AAG---VGPGDVVGVLAERSPELVVALLAVLKAGAAYV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1615 PVDPGYPMARLTRIADTVTPALVLTRTGQGGCLPGAEVFGDVpvvaldrvADRLTAMPDQRPEVTVDPRGLAYSIFTSGS 1694
Cdd:cd12117 76 PLDPELPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVI--------DEALDAGPAGNPAVPVSPDDLAYVMYTSGS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1695 TGQPKGVAVEHIGIVRYLSWAAASYPTAGRRgTLAHSSVGFDLTMSALFEPLVSGRGVTLMPADATL--ADLAEELSGPL 1772
Cdd:cd12117 148 TGRPKGVAVTHRGVVRLVKNTNYVTLGPDDR-VLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLdpDALGALIAEEG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1773 AyDYIRLTPSHLRHLVghwtgQELPPAARGW---VVGGETLDPALVKQLLELRPDAEVINHYGPTETVIGRVVHPVREag 1849
Cdd:cd12117 227 V-TVLWLTAALFNQLA-----DEDPECFAGLrelLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTE-- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1850 ELAVDSPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPAGePGARMYRTGDLVRW 1929
Cdd:cd12117 299 LDEVAGSIPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFG-PGERLYRTGDLARW 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1930 RGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVR-----DQQLVGWFIPAEdhpPVTVSALRRFCAEQ 2004
Cdd:cd12117 378 LPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVRedaggDKRLVAYVVAEG---ALDAAELRAFLRER 454
|
490 500
....*....|....*....|....*....
gi 653678460 2005 LPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:cd12117 455 LPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
505-977 |
9.12e-129 |
|
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: 413.02 E-value: 9.12e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 505 PGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLL 584
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 585 SDARPVLVVTDaatadrlgPDDItglvvleetdtggypateppavpaghsAYVIYTSGSTGRPKGVVITRAALDNFLAAM 664
Cdd:cd17650 81 EDSGAKLLLTQ--------PEDL---------------------------AYVIYTSGTTGKPKGVMVEHRNVAHAAHAW 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 665 AERFPLTAED-RVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALIDLAGRHRVTLAQATPTLWQALVPEL-- 741
Cdd:cd17650 126 RREYELDSFPvRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVyr 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 742 SGPALAGIRVL-VGGEALPAE----LARRLGdAGAEVTNMYGPTETTIWSTSGPTSEDSIRRGS---IGVPIDNTQVYVL 813
Cdd:cd17650 206 NGLDLSAMRLLiVGSDGCKAQdfktLAARFG-QGMRIINSYGVTEATIDSTYYEEGRDPLGDSAnvpIGRPLPNTAMYVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 814 DANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFGPpGTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFR 893
Cdd:cd17650 285 DERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAP-GERMYRTGDLARWRADGNVELLGRVDHQVKIRGFR 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 894 IELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIPDGPVAPDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLD 973
Cdd:cd17650 364 IELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVD 443
|
....
gi 653678460 974 RAAL 977
Cdd:cd17650 444 RRAL 447
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1558-1972 |
1.01e-128 |
|
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: 411.27 E-value: 1.01e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1558 TFAGLDAQANRLAHALHTGALgappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMARLTRIADTVTPALV 1637
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGG----VGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1638 LTRTGQGGCLPGAeVFGDVPVVALDRVADRlTAMPDQRPEVTVDPRGLAYSIFTSGSTGQPKGVAVEHIGIVRYLSWAAA 1717
Cdd:TIGR01733 77 LTDSALASRLAGL-VLPVILLDPLELAALD-DAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1718 SYPTAGRRGTLAHSSVGFDLTMSALFEPLVSGRGVTLMPADATLAD--LAEELSGPLAYDYIRLTPSHLRHLVGHwtGQE 1795
Cdd:TIGR01733 155 RYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDaaLLAALIAEHPVTVLNLTPSLLALLAAA--LPP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1796 LPPAARGWVVGGETLDPALVKQLLELRPDAEVINHYGPTETVIGRVVHPVrEAGELAVDSPLPLGRPLGETRLQVLDAWL 1875
Cdd:TIGR01733 233 ALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLV-DPDDAPRESPVPIGRPLANTRLYVLDDDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1876 EAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDP-AGEPGARMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIEL 1954
Cdd:TIGR01733 312 RPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPfAGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIEL 391
|
410
....*....|....*...
gi 653678460 1955 GEIEARMAEHPGVEQAVV 1972
Cdd:TIGR01733 392 GEIEAALLRHPGVREAVV 409
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1537-2034 |
2.16e-128 |
|
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: 413.66 E-value: 2.16e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1537 VEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPV 1616
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLR--ARG---VGPGDLVALCARRSAELVVALLAILKAGAAYVPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1617 DPGYPMARLTRIADTVTPALVLTRTGQGGCLPGAEVfgdvPVVALDRVADrlTAMPDQRPEVTVDPRGLAYSIFTSGSTG 1696
Cdd:cd17651 76 DPAYPAERLAFMLADAGPVLVLTHPALAGELAVELV----AVTLLDQPGA--AAGADAEPDPALDADDLAYVIYTSGSTG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1697 QPKGVAVEHIGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMSALFEPLVSGRGVTLMPAD-----ATLADLAEELsgp 1771
Cdd:cd17651 150 RPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEvrtdpPALAAWLDEQ--- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1772 lAYDYIRLTPSHLRHLVGH-WTGQELPPAARGWVVGGETLDP-ALVKQLLELRPDAEVINHYGPTETVigrvvhpVREAG 1849
Cdd:cd17651 227 -RISRVFLPTVALRALAEHgRPLGVRLAALRYLLTGGEQLVLtEDLREFCAGLPGLRLHNHYGPTETH-------VVTAL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1850 ELAVD-----SPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPAGePGARMYRTG 1924
Cdd:cd17651 299 SLPGDpaawpAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFV-PGARMYRTG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1925 DLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVR-----DQQLVGWFIPAEDHPPvTVSALRR 1999
Cdd:cd17651 378 DLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLARedrpgEKRLVAYVVGDPEAPV-DAAELRA 456
|
490 500 510
....*....|....*....|....*....|....*
gi 653678460 2000 FCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRALP 2034
Cdd:cd17651 457 ALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
495-977 |
8.20e-128 |
|
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: 411.55 E-value: 8.20e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 495 ERFQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPD 574
Cdd:cd05918 3 DLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 575 FPVERIAYLLSDARPVLVVTDAatadrlgPDDItglvvleetdtggypateppavpaghsAYVIYTSGSTGRPKGVVITR 654
Cdd:cd05918 83 HPLQRLQEILQDTGAKVVLTSS-------PSDA---------------------------AYVIFTSGSTGKPKGVVIEH 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 655 AALDNFLAAMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNpaaliDLAG---RHRVTLAQATP 731
Cdd:cd05918 129 RALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLN-----DLAGfinRLRVTWAFLTP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 732 TLWQALVPElsgpALAGIRVLV-GGEALPAELARRLGDaGAEVTNMYGPTETTIWSTSGPTSEDSiRRGSIGVPIDNTqV 810
Cdd:cd05918 204 SVARLLDPE----DVPSLRTLVlGGEALTQSDVDTWAD-RVRLINAYGPAECTIAATVSPVVPST-DPRNIGRPLGAT-C 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 811 YVLDANLH--PAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPF------GPPGTRMYRTGDLVRWSAAGDLEYLGR 882
Cdd:cd05918 277 WVVDPDNHdrLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAwlkqegSGRGRRLYRTGDLVRYNPDGSLEYVGR 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 883 TDHQVKLRGFRIELGEIETTLINAGPVRR---AAAVVREDRPGDLRLVAYVIPDG-------------------PVAPDA 940
Cdd:cd05918 357 KDTQVKIRGQRVELGEIEHHLRQSLPGAKevvVEVVKPKDGSSSPQLVAFVVLDGsssgsgdgdslflepsdefRALVAE 436
|
490 500 510
....*....|....*....|....*....|....*..
gi 653678460 941 LRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:cd05918 437 LRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1545-2033 |
9.20e-128 |
|
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: 410.91 E-value: 9.20e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1545 PGWTALRTGDRSLTFAGLDAQANRLAHALHTGAlgappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMAR 1624
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARG-----VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1625 LTRIADTVTPALVLTRTGqggcLPgAEVFGDVPVVALDRVADRLtamPDQRPEVTVDPRGLAYSIFTSGSTGQPKGVAVE 1704
Cdd:cd12116 76 LRYILEDAEPALVLTDDA----LP-DRLPAGLPVLLLALAAAAA---APAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1705 HIGIVRYL-SWAAASYPTAGRRgTLAHSSVGFDLTMSALFEPLVSGRGVTLMPADATL--ADLAEELSGPLAyDYIRLTP 1781
Cdd:cd12116 148 HRNLVNFLhSMRERLGLGPGDR-LLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRdpEALARLIEAHSI-TVMQATP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1782 SHLRHLVGhwTGQELPPAARGwVVGGETLDPALVKQLLElrPDAEVINHYGPTETVIGRVVHPVREAgelavDSPLPLGR 1861
Cdd:cd12116 226 ATWRMLLD--AGWQGRAGLTA-LCGGEALPPDLAARLLS--RVGSLWNLYGPTETTIWSTAARVTAA-----AGPIPIGR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1862 PLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPAGEPGARMYRTGDLVRWRGDGLLDFVGRV 1941
Cdd:cd12116 296 PLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGSRLYRTGDLVRRRADGRLEYLGRA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1942 DDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVR----DQQLVGWFIPAEDHPPvTVSALRRFCAEQLPEFMVPNQWVAL 2017
Cdd:cd12116 376 DGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVRedggDRRLVAYVVLKAGAAP-DAAALRAHLRATLPAYMVPSAFVRL 454
|
490
....*....|....*.
gi 653678460 2018 DAFPLTPHGKVNHRAL 2033
Cdd:cd12116 455 DALPLTANGKLDRKAL 470
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
1545-2034 |
4.93e-124 |
|
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: 399.44 E-value: 4.93e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1545 PGWTALRTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMAR 1624
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLR--ALG---VGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1625 LTRIADTVTPALVLTRtgqggclpgaevfgdvpvvaldrvadrltampdqrpevtvDPRGLAYSIFTSGSTGQPKGVAVE 1704
Cdd:cd17649 76 LRYMLEDSGAGLLLTH----------------------------------------HPRQLAYVIYTSGSTGTPKGVAVS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1705 HIGIVRYLSWAAASYP-TAGRRgTLAHSSVGFDLTMSALFEPLVSGRGVTLMPADatLADLAEELSGPLAYDYIR---LT 1780
Cdd:cd17649 116 HGPLAAHCQATAERYGlTPGDR-ELQFASFNFDGAHEQLLPPLICGACVVLRPDE--LWASADELAEMVRELGVTvldLP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1781 PSHLRHLVGHW--TGQELPPAARGWVVGGETLDPALVKQLLELrpDAEVINHYGPTETVIGRVVHPVReAGELAVDSPLP 1858
Cdd:cd17649 193 PAYLQQLAEEAdrTGDGRPPSLRLYIFGGEALSPELLRRWLKA--PVRLFNAYGPTEATVTPLVWKCE-AGAARAGASMP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1859 LGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPAGEPGARMYRTGDLVRWRGDGLLDFV 1938
Cdd:cd17649 270 IGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPGSRLYRTGDLARWRDDGVIEYL 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1939 GRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRD----QQLVGWFIPAEDHP-PVTVSALRRFCAEQLPEFMVPNQ 2013
Cdd:cd17649 350 GRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDgaggKQLVAYVVLRAAAAqPELRAQLRTALRASLPDYMVPAH 429
|
490 500
....*....|....*....|.
gi 653678460 2014 WVALDAFPLTPHGKVNHRALP 2034
Cdd:cd17649 430 LVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
1545-2034 |
1.37e-123 |
|
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: 397.78 E-value: 1.37e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1545 PGWTALRTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMAR 1624
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLA--ARG---VGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1625 LTRIADTVTPALVLTrtgqggclpgaevfgdvpvvaldrvadrltampdqrpevtvDPRGLAYSIFTSGSTGQPKGVAVE 1704
Cdd:cd17652 76 IAYMLADARPALLLT-----------------------------------------TPDNLAYVIYTSGSTGRPKGVVVT 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1705 HIGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMSALFEPLVSGRGVTLMPADATLA--DLAEELsGPLAYDYIRLTPS 1782
Cdd:cd17652 115 HRGLANLAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPgePLADLL-REHRITHVTLPPA 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1783 HLRHLvghwTGQELPPAaRGWVVGGETLDPALVKQLlelRPDAEVINHYGPTETVIGRVVHPVREAGelavdSPLPLGRP 1862
Cdd:cd17652 194 ALAAL----PPDDLPDL-RTLVVAGEACPAELVDRW---APGRRMINAYGPTETTVCATMAGPLPGG-----GVPPIGRP 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1863 LGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPAGEPGARMYRTGDLVRWRGDGLLDFVGRVD 1942
Cdd:cd17652 261 VPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGAPGSRMYRTGDLARWRADGQLEFLGRAD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1943 DQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRD-----QQLVGWFIPAEDhPPVTVSALRRFCAEQLPEFMVPNQWVAL 2017
Cdd:cd17652 341 DQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDdrpgdKRLVAYVVPAPG-AAPTAAELRAHLAERLPGYMVPAAFVVL 419
|
490
....*....|....*..
gi 653678460 2018 DAFPLTPHGKVNHRALP 2034
Cdd:cd17652 420 DALPLTPNGKLDRRALP 436
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
504-978 |
2.55e-122 |
|
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: 395.69 E-value: 2.55e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 504 TPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYL 583
Cdd:cd17656 1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 584 LSDARPVLVVTDAATADRLgpdDITGLVVLEETDTGGYPATE--PPAVPAGHSAYVIYTSGSTGRPKGVVITRAALDNFL 661
Cdd:cd17656 81 MLDSGVRVVLTQRHLKSKL---SFNKSTILLEDPSISQEDTSniDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 662 AAMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALIDLAGRHRVTLAQATPTLWQALVPE- 740
Cdd:cd17656 158 HFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEr 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 741 -LSGPALAGIR-VLVGGEAL--PAELARRLGDAGAEVTNMYGPTETTIWSTSGPTSEDSIRR-GSIGVPIDNTQVYVLDA 815
Cdd:cd17656 238 eFINRFPTCVKhIITAGEQLviTNEFKEMLHEHNVHLHNHYGPSETHVVTTYTINPEAEIPElPPIGKPISNTWIYILDQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 816 NLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgPPGTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIE 895
Cdd:cd17656 318 EQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPF-DPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 896 LGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIPDGPVAPDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRA 975
Cdd:cd17656 397 LGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRK 476
|
...
gi 653678460 976 ALP 978
Cdd:cd17656 477 ALP 479
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
497-978 |
7.62e-121 |
|
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: 389.99 E-value: 7.62e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 497 FQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFP 576
Cdd:cd17645 4 FEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 577 VERIAYLLSDARPVLVVTDaatadrlgPDDItglvvleetdtggypateppavpaghsAYVIYTSGSTGRPKGVVITRAA 656
Cdd:cd17645 84 GERIAYMLADSSAKILLTN--------PDDL---------------------------AYVIYTSGSTGLPKGVMIEHHN 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 657 LDNFLAAMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALIDLAGRHRVTLAqATPTLWQA 736
Cdd:cd17645 129 LVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITIS-FLPTGAAE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 737 LVPELSGPALagiRVLV-GGEALpaelaRRLGDAGAEVTNMYGPTETTIWSTSGPT--SEDSIrrgSIGVPIDNTQVYVL 813
Cdd:cd17645 208 QFMQLDNQSL---RVLLtGGDKL-----KKIERKGYKLVNNYGPTENTVVATSFEIdkPYANI---PIGKPIDNTRVYIL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 814 DANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgPPGTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFR 893
Cdd:cd17645 277 DEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPF-VPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYR 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 894 IELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIPDGPVAPDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLD 973
Cdd:cd17645 356 IEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVD 435
|
....*
gi 653678460 974 RAALP 978
Cdd:cd17645 436 RKALP 440
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1076-2091 |
1.06e-117 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 420.34 E-value: 1.06e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1076 PVPR---DEPLPLSPMQESIWLADQVSAGDSVYNVPLALRLIGPLDRGALRRTLNRVVDRHEMLRTR------------I 1140
Cdd:PRK05691 3248 PVPAaeiEDVYPLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASfswnagetmlqvI 3327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1141 H-PGPDGMPVQ--VADPAGGGA----AL--TERDAapgtdlaqlllaeaalGFTLATEHPLRAVLWRLDEREHVLLLTAH 1211
Cdd:PRK05691 3328 HkPGRTPIDYLdwRGLPEDGQEqrlqALhkQEREA----------------GFDLLNQPPFHLRLIRVDEARYWFMMSNH 3391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1212 HVAVDAWSMDLIQRDLTELYAADTGHREPELDEPALAQaDYAVW-QRQSAQRGRyaaelDFWRTELTG-AVATEVAGDLP 1289
Cdd:PRK05691 3392 HILIDAWCRSLLMNDFFEIYTALGEGREAQLPVPPRYR-DYIGWlQRQDLAQAR-----QWWQDNLRGfERPTPIPSDRP 3465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1290 --RPATPGGGGGAVE---FALAPRQIQGIRELARRCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGR--GNPRLDNL 1362
Cdd:PRK05691 3466 flREHAGDSGGMVVGdcyTRLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRpvSMPQMQRT 3545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1363 VGCLVNTVVLRGDLSGAP---TFHELLRRTHARTADALAHQELPFEHLVADRGAGNG-PLFRIMYSFSSQepagrsagdv 1438
Cdd:PRK05691 3546 VGLFINSIALRVQLPAAGqrcSVRQWLQGLLDSNMELREYEYLPLVAIQECSELPKGqPLFDSLFVFENA---------- 3615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1439 dlePVPVPVTTCKFDLVLTVvDGGST-----LEGVLEYADDLYL----------PGTAERLVTSLTNLLAAAVRTPELAV 1503
Cdd:PRK05691 3616 ---PVEVSVLDRAQSLNASS-DSGRThtnfpLTAVCYPGDDLGLhlsydqryfdAPTVERLLGEFKRLLLALVQGFHGDL 3691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1504 TRLAITSESD-TVRTSRWGRSEQHVGDDRTVHQLVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHtgALGapp 1582
Cdd:PRK05691 3692 SELPLLGEQErDFLLDGCNRSERDYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALR--AAG--- 3766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1583 VGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMARLTRIAD-TVTPALVLTRTgqggCLP-GAEVFGDVPVVA 1660
Cdd:PRK05691 3767 VGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIElSRTPVLVCSAA----CREqARALLDELGCAN 3842
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1661 LDR--VADRLTA--MPDQRPEVTVDPRGLAYSIFTSGSTGQPKGVAVEHIGIV-RYLSwaAASYPTAGRRGTLAHS-SVG 1734
Cdd:PRK05691 3843 RPRllVWEEVQAgeVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLnNQLS--KVPYLALSEADVIAQTaSQS 3920
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1735 FDLTM-SALFEPLVSGRgVTLMPadatlADLAEELSGPLAY---DYIRLTPSHLRHLVGHWTGQELPPAARGWVV-GGET 1809
Cdd:PRK05691 3921 FDISVwQFLAAPLFGAR-VEIVP-----NAIAHDPQGLLAHvqaQGITVLESVPSLIQGMLAEDRQALDGLRWMLpTGEA 3994
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1810 LDPALVKQLLELRPDAEVINHYGPTETVIGRVVHPVREAGELAvdSPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIG 1889
Cdd:PRK05691 3995 MPPELARQWLQRYPQIGLVNAYGPAECSDDVAFFRVDLASTRG--SYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVA 4072
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1890 GDGIARGYLGRPALTAEKFLPDPAGEPGARMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQ 1969
Cdd:PRK05691 4073 GTGVGRGYVGDPLRTALAFVPHPFGAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVRE 4152
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1970 AVVLVRD----QQLVGWFIPAEdhPPVTVSALRRFCAEQ----LPEFMVPNQWVALDAFPLTPHGKVNHRALPGPTSGRP 2041
Cdd:PRK05691 4153 AAVAVQEgvngKHLVGYLVPHQ--TVLAQGALLERIKQRlraeLPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQL 4230
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|
gi 653678460 2042 ELEDrYQAPRTPGEQLLAELWSTVLGTDRIGIEDNFFDLGGTSISVIQLS 2091
Cdd:PRK05691 4231 QSQA-YLAPRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIA 4279
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
505-978 |
9.22e-117 |
|
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: 378.67 E-value: 9.22e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 505 PGAVAVIEGDTTLSYRELDERANRLARLLMERGAG-AETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYL 583
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 584 LSDARPVLVVTDaatadrlgPDDItglvvleetdtggypateppavpaghsAYVIYTSGSTGRPKGVVITRAALDNFLAA 663
Cdd:cd17648 81 LEDTGARVVITN--------STDL---------------------------AYAIYTSGTTGKPKGVLVEHGSVVNLRTS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 664 MAERFPLTAED--RVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALIDLAGRHRVTLAQATPTLWQALvpEL 741
Cdd:cd17648 126 LSERYFGRDNGdeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQY--DL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 742 SG-PALAgiRVLVGGEALPAELARRL-GDAGAEVTNMYGPTETTIWSTSGPTSEDSIRRGSIGVPIDNTQVYVLDANLHP 819
Cdd:cd17648 204 ARlPHLK--RVDAAGEEFTAPVFEKLrSRFAGLIINAYGPTETTVTNHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKR 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 820 APIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFGPPG-------TRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGF 892
Cdd:cd17648 282 VPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQ 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 893 RIELGEIETTLINAGPVRRAAAVVRED-----RPGDLRLVAYVIPDGPVAPDA-LRTELSRTLPDYMIPAVIVPVPDFPT 966
Cdd:cd17648 362 RIEPGEVEAALASYPGVRECAVVAKEDasqaqSRIQKYLVGYYLPEPGHVPESdLLSFLRAKLPRYMVPARLVRLEGIPV 441
|
490
....*....|..
gi 653678460 967 TPNGKLDRAALP 978
Cdd:cd17648 442 TINGKLDVRALP 453
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
46-459 |
1.19e-116 |
|
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: 377.53 E-value: 1.19e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 46 PVPLAPGQAGIWFSEQLRPGTPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVFRLGpDGEPVQQTAPA--APVA 123
Cdd:cd19540 1 RIPLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPED-DGGPYQVVLPAaeARPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 124 LPVIDVTEADLPQALRTAAEQPFDLERGPLLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLLLADLARAY----AGELPA 199
Cdd:cd19540 80 LTVVDVTEDELAARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYaarrAGRAPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 200 GVAAPA-FRDVAAWQHGRL-----AAGELDDQLRYWRQRLAGLPD-LEIPGDRQRPADRDWRAHSVRRELPAATEAAVRR 272
Cdd:cd19540 160 WAPLPVqYADYALWQRELLgdeddPDSLAARQLAYWRETLAGLPEeLELPTDRPRPAVASYRGGTVEFTIDAELHARLAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 273 LAAAHDTTPFTVLLAAYGTFLHRLTGQDDFAVGVPVAGRGRTDLESVVGLFAGMVPVRLDLTGRPSFDEVLSRTVAGSRN 352
Cdd:cd19540 240 LAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 353 DFAHPQIPFDRLVRELRRDRIAGSQLLVQAMAGTESTAVA-LTFGEAAGTEQPVDVALAKCDLDLSVLDDGDR------L 425
Cdd:cd19540 320 AFAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAAtLELPGLTVEPVPVDTGVAKFDLSFTLTERRDAdgapagL 399
|
410 420 430
....*....|....*....|....*....|....
gi 653678460 426 AVTLVAAADLFTPAAAEQLAGQFLSLLAGLTGAP 459
Cdd:cd19540 400 TGELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
1532-2034 |
2.03e-116 |
|
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: 378.32 E-value: 2.03e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1532 TVHQLVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHTgaLGappVGPETPVLLLLDRSPELVVAMLAVLKAGG 1611
Cdd:cd17644 1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQS--LG---VKSESLVGICVERSLEMIIGLLAILKAGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1612 YFIPVDPGYPMARLTRIADTVTPALVLTRtgqggclpgaevfgdvpvvaldrvadrltampdqrpevtvdPRGLAYSIFT 1691
Cdd:cd17644 76 AYVPLDPNYPQERLTYILEDAQISVLLTQ-----------------------------------------PENLAYVIYT 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1692 SGSTGQPKGVAVEHIGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMSALFEPLVSGRGVTLMPAD--ATLADLAeels 1769
Cdd:cd17644 115 SGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEmrSSLEDFV---- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1770 gplayDYIR--------LTPSHLRHLV--GHWTGQELPPAARGWVVGGETLDPALVKQLLE-LRPDAEVINHYGPTETVI 1838
Cdd:cd17644 191 -----QYIQqwqltvlsLPPAYWHLLVleLLLSTIDLPSSLRLVIVGGEAVQPELVRQWQKnVGNFIQLINVYGPTEATI 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1839 GRVVHPVREAGELAVDSPlPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDP-AGEPG 1917
Cdd:cd17644 266 AATVCRLTQLTERNITSV-PIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPfNSSES 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1918 ARMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVR-----DQQLVGWFIPAEDHPPv 1992
Cdd:cd17644 345 ERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVRedqpgNKRLVAYIVPHYEESP- 423
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 653678460 1993 TVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRALP 2034
Cdd:cd17644 424 STVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRALP 465
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1545-2033 |
3.67e-116 |
|
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: 377.03 E-value: 3.67e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1545 PGWTALRTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMAR 1624
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLR--AEG---VGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1625 LTRIADTVTPALVLTrtgqggclpgaevfgdvpvvaldrvadrltampdqrpevtvDPRGLAYSIFTSGSTGQPKGVAVE 1704
Cdd:cd17643 76 IAFILADSGPSLLLT-----------------------------------------DPDDLAYVIYTSGSTGRPKGVVVS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1705 HIGIVRYLSWAAASYP-TAGRRGTLAHSSvGFDLTMSALFEPLVSGRGVTLMPADATLAdlAEELSGPLAYDYIRL---T 1780
Cdd:cd17643 115 HANVLALFAATQRWFGfNEDDVWTLFHSY-AFDFSVWEIWGALLHGGRLVVVPYEVARS--PEDFARLLRDEGVTVlnqT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1781 PSHLRHLV-GHWTGQELPPAARGWVVGGETLDPALVKQLLELRPD--AEVINHYGPTETVIGRVVHPVREAGELAVDSPl 1857
Cdd:cd17643 192 PSAFYQLVeAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLdrPQLVNMYGITETTVHVTFRPLDAADLPAAAAS- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1858 PLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPAGEPGARMYRTGDLVRWRGDGLLDF 1937
Cdd:cd17643 271 PIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGSRMYRTGDLARRLPDGELEY 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1938 VGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVR-----DQQLVGWFIPAEDHPPVTvSALRRFCAEQLPEFMVPN 2012
Cdd:cd17643 351 LGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVRedepgDTRLVAYVVADDGAAADI-AELRALLKELLPDYMVPA 429
|
490 500
....*....|....*....|.
gi 653678460 2013 QWVALDAFPLTPHGKVNHRAL 2033
Cdd:cd17643 430 RYVPLDALPLTVNGKLDRAAL 450
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
502-977 |
1.66e-114 |
|
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: 371.96 E-value: 1.66e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 502 RRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIA 581
Cdd:cd05945 2 AANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 582 YLLSDARPVLVVTDaatadrlgPDDitglvvleetdtggypateppavpaghSAYVIYTSGSTGRPKGVVITRAALDNFL 661
Cdd:cd05945 82 EILDAAKPALLIAD--------GDD---------------------------NAYIIFTSGSTGRPKGVQISHDNLVSFT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 662 AAMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALIDLAGRHRVTLAQATPTLWQALV--P 739
Cdd:cd05945 127 NWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLlsP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 740 ELSGPALAGIR-VLVGGEALPAELARRLGDA--GAEVTNMYGPTETTIWSTS-GPTSEDSIRRGS--IGVPIDNTQVYVL 813
Cdd:cd05945 207 TFTPESLPSLRhFLFCGEVLPHKTARALQQRfpDARIYNTYGPTEATVAVTYiEVTPEVLDGYDRlpIGYAKPGAKLVIL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 814 DANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDpfgpPGTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFR 893
Cdd:cd05945 287 DEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPD----EGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 894 IELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIPDGPVA---PDALRTELSRTLPDYMIPAVIVPVPDFPTTPNG 970
Cdd:cd05945 363 IELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEaglTKAIKAELAERLPPYMIPRRFVYLDELPLNANG 442
|
....*..
gi 653678460 971 KLDRAAL 977
Cdd:cd05945 443 KIDRKAL 449
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
1082-1499 |
2.25e-113 |
|
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: 368.29 E-value: 2.25e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1082 PLPLSPMQESIWLADQVSAGDSVYNVPLALRLIGPLDRGALRRTLNRVVDRHEMLRTrIHPGPDGMPVQ-VADPAGGGAA 1160
Cdd:cd19540 1 RIPLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRT-VFPEDDGGPYQvVLPAAEARPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1161 LTERDAAPGtDLAQLLLAEAALGFTLATEHPLRAVLWRLDEREHVLLLTAHHVAVDAWSMDLIQRDLTELYAADTGHREP 1240
Cdd:cd19540 80 LTVVDVTED-ELAARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGRAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1241 ELDEPALAQADYAVWQR-----QSAQRGRYAAELDFWRTELTGAVA-TEVAGDLPRPATPGGGGGAVEFALAPRQIQGIR 1314
Cdd:cd19540 159 DWAPLPVQYADYALWQRellgdEDDPDSLAARQLAYWRETLAGLPEeLELPTDRPRPAVASYRGGTVEFTIDAELHARLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1315 ELARRCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGRGNPRLDNLVGCLVNTVVLRGDLSGAPTFHELLRRTHARTA 1394
Cdd:cd19540 239 ALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1395 DALAHQELPFEHLVA----DRGAGNGPLFRIMYSFSSQEPAGRSAGDVDLEPVPVPVTTCKFDLVLTVVD------GGST 1464
Cdd:cd19540 319 AAFAHQDVPFERLVEalnpPRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVDTGVAKFDLSFTLTErrdadgAPAG 398
|
410 420 430
....*....|....*....|....*....|....*
gi 653678460 1465 LEGVLEYADDLYLPGTAERLVTSLTNLLAAAVRTP 1499
Cdd:cd19540 399 LTGELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
503-977 |
6.10e-113 |
|
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: 367.02 E-value: 6.10e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 503 RTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAY 582
Cdd:cd17653 9 AHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 583 LLSDARPVLVVTDAAtadrlgPDDitglvvleetdtggypateppavpaghSAYVIYTSGSTGRPKGVVITRAALDNFLA 662
Cdd:cd17653 89 ILRTSGATLLLTTDS------PDD---------------------------LAYIIFTSGSTGIPKGVMVPHRGVLNYVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 663 AMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADAdtarnPAALIDLAgrHRVTLAQATPTLWQALVPElS 742
Cdd:cd17653 136 QPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADP-----SDPFAHVA--RTVDALMSTPSILSTLSPQ-D 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 743 GPALAGIrvLVGGEALPAELARRLGdAGAEVTNMYGPTETTIWSTSGPTSEDsiRRGSIGVPIDNTQVYVLDANLHPAPI 822
Cdd:cd17653 208 FPNLKTI--FLGGEAVPPSLLDRWS-PGRRLYNAYGPTECTISSTMTELLPG--QPVTIGKPIPNSTCYILDADLQPVPE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 823 GVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFGpPGTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETT 902
Cdd:cd17653 283 GVVGEICISGVQVARGYLGNPALTASKFVPDPFW-PGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEV 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 653678460 903 LI-NAGPVRRAAAVVREDrpgdlRLVAYVIPDGpVAPDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:cd17653 362 VLqSQPEVTQAAAIVVNG-----RLVAFVTPET-VDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKAL 431
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
493-979 |
8.12e-113 |
|
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: 367.21 E-value: 8.12e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 493 LRERFQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPID 572
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 573 PDFPVERIAYLLSDARPVLVVTdaatadrlgpdditglvvleetdtggypateppavpaghsAYVIYTSGSTGRPKGVVI 652
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT----------------------------------------ALILYTSGTTGRPKGVML 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 653 TRAALDNFLAAMAERFPLTAEDRVLATTTVSFDIA-GLELYLPLRSGAGVVLADAdtaRNPAALIDLAGRHRVTLAQATP 731
Cdd:COG0318 121 THRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLLPR---FDPERVLELIERERVTVLFGVP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 732 TLWQALV--PELSGPALAGIRVLV-GGEALPAELARRLGDA-GAEVTNMYGPTETTIWSTSGPTSEDSIRRGSIGVPIDN 807
Cdd:COG0318 198 TMLARLLrhPEFARYDLSSLRLVVsGGAPLPPELLERFEERfGVRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 808 TQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFlPDPFgppgtrmYRTGDLVRWSAAGDLEYLGRTDHQV 887
Cdd:COG0318 278 VEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGW-------LRTGDLGRLDEDGYLYIVGRKKDMI 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 888 KLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVI--PDGPVAPDALRTELSRTLPDYMIPAVIVPVPDFP 965
Cdd:COG0318 350 ISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVlrPGAELDAEELRAFLRERLARYKVPRRVEFVDELP 429
|
490
....*....|....
gi 653678460 966 TTPNGKLDRAALPA 979
Cdd:COG0318 430 RTASGKIDRRALRE 443
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
1535-2033 |
1.46e-107 |
|
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: 351.61 E-value: 1.46e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1535 QLVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHAL-HTGalgappVGPETPVLLLLDRSPELVVAMLAVLKAGGYF 1613
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLlQLG------VVPGDVVPLLSDRSLEMLVAILAILKAGAAY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1614 IPVDPGYPMARLTRIADTVTPALVLTRTGqggclpgaevfgdvpvvaldrvadrltampdqrpevtvdPRGLAYSIFTSG 1693
Cdd:cd17653 75 VPLDAKLPSARIQAILRTSGATLLLTTDS---------------------------------------PDDLAYIIFTSG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1694 STGQPKGVAVEHIGIVRYLSWAAAS-YPTAGRRgTLAHSSVGFDLTMSALFEPLvsGRGVTLMPAD--ATLADLAEELsg 1770
Cdd:cd17653 116 STGIPKGVMVPHRGVLNYVSQPPARlDVGPGSR-VAQVLSIAFDACIGEIFSTL--CNGGTLVLADpsDPFAHVARTV-- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1771 playDYIRLTPSHLrhlvghwtgQELPPAA----RGWVVGGETLDPALVKqllELRPDAEVINHYGPTETVIGrVVHPvr 1846
Cdd:cd17653 191 ----DALMSTPSIL---------STLSPQDfpnlKTIFLGGEAVPPSLLD---RWSPGRRLYNAYGPTECTIS-STMT-- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1847 eagELAVDSPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPAgEPGARMYRTGDL 1926
Cdd:cd17653 252 ---ELLPGQPVTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPF-WPGSRMYRTGDY 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1927 VRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARM-AEHPGVEQAVVLVRDQQLVGWFIPAEdhppVTVSALRRFCAEQL 2005
Cdd:cd17653 328 GRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVlQSQPEVTQAAAIVVNGRLVAFVTPET----VDVDGLRSELAKHL 403
|
490 500
....*....|....*....|....*...
gi 653678460 2006 PEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:cd17653 404 PSYAVPDRIIALDSFPLTANGKVDRKAL 431
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
497-890 |
7.16e-107 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 348.92 E-value: 7.16e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 497 FQQWCRRTPGAVAVIEGD-TTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDF 575
Cdd:pfam00501 1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 576 PVERIAYLLSDARPVLVVTDAAT------ADRLGPDDITGLVVLEETDTGGY------------PATEPPAVPAGHSAYV 637
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALkleellEALGKLEVVKLVLVLDRDPVLKEeplpeeakpadvPPPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 638 IYTSGSTGRPKGVVITRAALDNFLAAMA----ERFPLTAEDRVLATTTVSFDIA-GLELYLPLRSGAGVVLADADTARNP 712
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIKrvrpRGFGLGPDDRVLSTLPLFHDFGlSLGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 713 AALIDLAGRHRVTLAQATPTLWQALV--PELSGPALAGIR-VLVGGEALPAELARRLGDA-GAEVTNMYGPTETTIWSTS 788
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLeaGAPKRALLSSLRlVLSGGAPLPPELARRFRELfGGALVNGYGLTETTGVVTT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 789 GPTSEDSIRR-GSIGVPIDNTQVYVLDAN-LHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDpfgppgtRMYRTG 866
Cdd:pfam00501 321 PLPLDEDLRSlGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED-------GWYRTG 393
|
410 420
....*....|....*....|....
gi 653678460 867 DLVRWSAAGDLEYLGRTDHQVKLR 890
Cdd:pfam00501 394 DLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
47-473 |
9.04e-106 |
|
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: 347.01 E-value: 9.04e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 47 VPLAPGQAGIWFSEQLRPGTPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVFRLGPDGEPVQQTAPAAPVALPV 126
Cdd:pfam00668 5 YPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERPFELEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 127 IDV-------TEADLPQALRTAAEQPFDLERGPLLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLLLADLARAYAG---- 195
Cdd:pfam00668 85 IDIsdlseseEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQllkg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 196 -ELPAGvAAPAFRDVAAWQHGRLAAGELDDQLRYWRQRLAG-LPDLEIPGDRQRPADRDWRAHSVRRELPAATEAAVRRL 273
Cdd:pfam00668 165 ePLPLP-PKTPYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGeLPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLRKL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 274 AAAHDTTPFTVLLAAYGTFLHRLTGQDDFAVGVPVAGRGRTDLESVVGLFAGMVPVRLDLTGRPSFDEVLSRTVAGSRND 353
Cdd:pfam00668 244 AKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLSA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 354 FAHPQIPFDRLVRELRRDRIAGSQLLVQAM------AGTESTAVALTFGEAAGTEQPVDVALAKCDLDLSVLDDGDRLAV 427
Cdd:pfam00668 324 EPHQGYPFGDLVNDLRLPRDLSRHPLFDPMfsfqnyLGQDSQEEEFQLSELDLSVSSVIEEEAKYDLSLTASERGGGLTI 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 653678460 428 TLVAAADLFTPAAAEQLAGQFLSLLAGLTGAPDRLVSEVDLLDTDE 473
Cdd:pfam00668 404 KIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAE 449
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
1541-2033 |
5.55e-103 |
|
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: 338.84 E-value: 5.55e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1541 ADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHTGALGAPpvgpeTPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGY 1620
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAG-----DPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1621 PMARLTRIADTVTPALVLtrtgqggclpgaevfgdvpvvaldrvadrltampdqrpevtVDPRGLAYSIFTSGSTGQPKG 1700
Cdd:cd05945 76 PAERIREILDAAKPALLI-----------------------------------------ADGDDNAYIIFTSGSTGRPKG 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1701 VAVEHIGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMSALFEPLVSGRGVTLMPADAT--LADLAEELSgPLAYDYIR 1778
Cdd:cd05945 115 VQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATadPKQLFRFLA-EHGITVWV 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1779 LTPSHLRHLVGHWT-GQELPPAARGWVVGGETLDPALVKQLLELRPDAEVINHYGPTETVIGRVVHPVREAgELAVDSPL 1857
Cdd:cd05945 194 STPSFAAMCLLSPTfTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIEVTPE-VLDGYDRL 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1858 PLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPagepGARMYRTGDLVRWRGDGLLDF 1937
Cdd:cd05945 273 PIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE----GQRAYRTGDLVRLEADGLLFY 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1938 VGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVR-----DQQLVGWFIPAEDHPPVTVSALRRFCAEQLPEFMVPN 2012
Cdd:cd05945 349 RGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKykgekVTELIAFVVPKPGAEAGLTKAIKAELAERLPPYMIPR 428
|
490 500
....*....|....*....|.
gi 653678460 2013 QWVALDAFPLTPHGKVNHRAL 2033
Cdd:cd05945 429 RFVYLDELPLNANGKIDRKAL 449
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
1533-2033 |
4.86e-102 |
|
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: 337.21 E-value: 4.86e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1533 VHQLVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHTgaLGappVGPETPVLLLLDRSPELVVAMLAVLKAGGY 1612
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRS--LG---VGPGVFVPLCFEKSKWAVVAMLAVLKAGGA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1613 FIPVDPGYPMARLTRIADTVTPALVLTrtgqggclpgaevfgdvpvvaldrvadrltampdqrpevtVDPRGLAYSIFTS 1692
Cdd:cd05918 76 FVPLDPSHPLQRLQEILQDTGAKVVLT----------------------------------------SSPSDAAYVIFTS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1693 GSTGQPKGVAVEHIGIV-RYLSWAAASYPTAGRRgTLAHSSVGFDLTMSALFEPLVSGRGVTLMPADATLADLAEELSGp 1771
Cdd:cd05918 116 GSTGKPKGVVIEHRALStSALAHGRALGLTSESR-VLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLNDLAGFINR- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1772 LAYDYIRLTPSHLRHLvghwtGQELPPAARGWVVGGETLDPALVKQLLelrPDAEVINHYGPTETVIGRVVHPVREAGEl 1851
Cdd:cd05918 194 LRVTWAFLTPSVARLL-----DPEDVPSLRTLVLGGEALTQSDVDTWA---DRVRLINAYGPAECTIAATVSPVVPSTD- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1852 avdsPLPLGRPLGeTRLQVLDA----WLeaVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPA------GEPGARMY 1921
Cdd:cd05918 265 ----PRNIGRPLG-ATCWVVDPdnhdRL--VPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAwlkqegSGRGRRLY 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1922 RTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEH-PGVEQAVVLV-------RDQQLVGWFIPAEDHP--- 1990
Cdd:cd05918 338 RTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSlPGAKEVVVEVvkpkdgsSSPQLVAFVVLDGSSSgsg 417
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 653678460 1991 -------------PVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:cd05918 418 dgdslflepsdefRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
1545-2033 |
1.00e-100 |
|
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: 332.12 E-value: 1.00e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1545 PGWTALRTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMAR 1624
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLR--GLG---VAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1625 LTRIADTVTPALVLTrtgqggclpgaevfgdvpvvaldrvadrltampdqrpevtvDPRGLAYSIFTSGSTGQPKGVAVE 1704
Cdd:cd17650 76 LQYMLEDSGAKLLLT-----------------------------------------QPEDLAYVIYTSGTTGKPKGVMVE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1705 HIGIVR-YLSW----AAASYPTAgrrgTLAHSSVGFDLTMSALFEPLVSGRGVTLMPaDATLADLAEelsgplAYDYIR- 1778
Cdd:cd17650 115 HRNVAHaAHAWrreyELDSFPVR----LLQMASFSFDVFAGDFARSLLNGGTLVICP-DEVKLDPAA------LYDLILk 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1779 -------LTPSHLRHLVGHWTGQEL-PPAARGWVVGGETLDPALVKQLL-ELRPDAEVINHYGPTETVIGRVVHPVREAG 1849
Cdd:cd17650 184 sritlmeSTPALIRPVMAYVYRNGLdLSAMRLLIVGSDGCKAQDFKTLAaRFGQGMRIINSYGVTEATIDSTYYEEGRDP 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1850 ELAVDSpLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPAGePGARMYRTGDLVRW 1929
Cdd:cd17650 264 LGDSAN-VPIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFA-PGERMYRTGDLARW 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1930 RGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRD-----QQLVGWFIPAEdhpPVTVSALRRFCAEQ 2004
Cdd:cd17650 342 RADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREdkggeARLCAYVVAAA---TLNTAELRAFLAKE 418
|
490 500
....*....|....*....|....*....
gi 653678460 2005 LPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:cd17650 419 LPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1545-2033 |
6.57e-98 |
|
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: 325.38 E-value: 6.57e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1545 PGWTALRTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMAR 1624
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALK--AAG---VRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1625 LTRIADTVTPALVLTrtgqggCLPGAevFGDVPVVALDRVADRLTAMPDQRPEVTVDPRGLAYSIFTSGSTGQPKGVAVE 1704
Cdd:cd12114 76 REAILADAGARLVLT------DGPDA--QLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMIS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1705 HIGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMSALFEPLVSGRGVTLMPAD-----ATLADLAEEL------SGP-- 1771
Cdd:cd12114 148 HRAALNTILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEArrrdpAHWAELIERHgvtlwnSVPal 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1772 --LAYDYIRLTPSHLRHL-----VGHWTGQELPPAARgwvvggetldpalvkqllELRPDAEVINHYGPTETVIGRVVHP 1844
Cdd:cd12114 228 leMLLDVLEAAQALLPSLrlvllSGDWIPLDLPARLR------------------ALAPDARLISLGGATEASIWSIYHP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1845 VREAgeLAVDSPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPAGEpgaRMYRTG 1924
Cdd:cd12114 290 IDEV--PPDWRSIPYGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHPDGE---RLYRTG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1925 DLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRDQ----QLVGWFIPAEDHPPVTVSALRRF 2000
Cdd:cd12114 365 DLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDpggkRLAAFVVPDNDGTPIAPDALRAF 444
|
490 500 510
....*....|....*....|....*....|...
gi 653678460 2001 CAEQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:cd12114 445 LAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
1534-2034 |
1.16e-96 |
|
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: 320.27 E-value: 1.16e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1534 HQLVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHTGAlgappVGPETPVLLLLDRSPELVVAMLAVLKAGGYF 1613
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKG-----VKPDDQVGIMLDKSLDMIAAILGVLKAGGAY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1614 IPVDPGYPMARLTRIADTVTPALVLTrtgqggclpgaevfgdvpvvaldrvadrltampdqrpevtvDPRGLAYSIFTSG 1693
Cdd:cd17645 76 VPIDPDYPGERIAYMLADSSAKILLT-----------------------------------------NPDDLAYVIYTSG 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1694 STGQPKGVAVEHIGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMSALFEPLVSGRGVTLMPADA-----TLADLAEE- 1767
Cdd:cd17645 115 STGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERrldldALNDYFNQe 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1768 ------LSGPLAYDYIRLTPSHLRHLVghwtgqelppaargwvVGGETLDPALVKQLlelrpdaEVINHYGPTETVIGRV 1841
Cdd:cd17645 195 gitisfLPTGAAEQFMQLDNQSLRVLL----------------TGGDKLKKIERKGY-------KLVNNYGPTENTVVAT 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1842 VHPVREAgelavDSPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPAgEPGARMY 1921
Cdd:cd17645 252 SFEIDKP-----YANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPF-VPGERMY 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1922 RTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRDQQ-----LVGWFIPAEDHPPvtvSA 1996
Cdd:cd17645 326 RTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDAdgrkyLVAYVTAPEEIPH---EE 402
|
490 500 510
....*....|....*....|....*....|....*...
gi 653678460 1997 LRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRALP 2034
Cdd:cd17645 403 LREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKALP 440
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
1084-1499 |
1.54e-95 |
|
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: 316.63 E-value: 1.54e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1084 PLSPMQESIWLADQVSAGDSVYNVPLALRLIGPLDRGALRRTLNRVVDRHEMLRTRIHPGPDGMPVQVADPAGGgAALTE 1163
Cdd:cd19539 3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGP-APLEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1164 RDAAPGTDLAQLLL-----AEAALGFTLATEHPLRAVLWRLDEREHVLLLTAHHVAVDAWSMDLIQRDLTELYAADTGHR 1238
Cdd:cd19539 82 RDLSDPDSDRERRLeellrERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1239 EPELDEPALAQADYAVWQRQSAQRGRYAAELDFWRTELTGAVATEVAGDLPRPATPGGGGGAVEFALAPRQIQGIRELAR 1318
Cdd:cd19539 162 AAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRGAEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELAK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1319 RCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGRGNPRLDNLVGCLVNTVVLRGDLSGAPTFHELLRRTHARTADALA 1398
Cdd:cd19539 242 RARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1399 HQELPFEHLVA----DRGAGNGPLFRIMYSF-SSQEPAGRSAGDVDLEPVPVPVTTCKFDLVLTVVDGGSTLEGVLEYAD 1473
Cdd:cd19539 322 HQELPFQQLVAelpvDRDAGRHPLVQIVFQVtNAPAGELELAGGLSYTEGSDIPDGAKFDLNLTVTEEGTGLRGSLGYAT 401
|
410 420
....*....|....*....|....*.
gi 653678460 1474 DLYLPGTAERLVTSLTNLLAAAVRTP 1499
Cdd:cd19539 402 SLFDEETIQGFLADYLQVLRQLLANP 427
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
1544-2034 |
2.08e-93 |
|
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: 312.49 E-value: 2.08e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1544 TPGWTALRTGDRSLTFAGLDAQANRLAHALHTgaLGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMA 1623
Cdd:cd17656 1 TPDAVAVVFENQKLTYRELNERSNQLARFLRE--KG---VKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1624 RLTRIADTVTPALVLTRTGqggcLPGAEVFGDVPVVALDrvaDRLTAMPDQRPEVTVDPRGLAYSIFTSGSTGQPKGVAV 1703
Cdd:cd17656 76 RRIYIMLDSGVRVVLTQRH----LKSKLSFNKSTILLED---PSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1704 EHIGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMSALFEPLVSGRGVTLMPADATLaDLaEELSGPLAYDYIRLT--P 1781
Cdd:cd17656 149 EHKNMVNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKR-DV-EQLFDLVKRHNIEVVflP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1782 SHLRHLVGHWTG--QELPPAARGWVVGGETLdpaLVKQLLE---LRPDAEVINHYGPTET--VIGRVVHPVREAGELAvd 1854
Cdd:cd17656 227 VAFLKFIFSEREfiNRFPTCVKHIITAGEQL---VITNEFKemlHEHNVHLHNHYGPSEThvVTTYTINPEAEIPELP-- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1855 splPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPAgEPGARMYRTGDLVRWRGDGL 1934
Cdd:cd17656 302 ---PIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPF-DPNERMYRTGDLARYLPDGN 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1935 LDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRDQQ-----LVGWFIPAEDhppVTVSALRRFCAEQLPEFM 2009
Cdd:cd17656 378 IEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDkgekyLCAYFVMEQE---LNISQLREYLAKQLPEYM 454
|
490 500
....*....|....*....|....*
gi 653678460 2010 VPNQWVALDAFPLTPHGKVNHRALP 2034
Cdd:cd17656 455 IPSFFVPLDQLPLTPNGKVDRKALP 479
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
1545-2034 |
5.80e-93 |
|
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: 310.10 E-value: 5.80e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1545 PGWTALRTGDRSLTFAGLDAQANRLAHALHTGALGAPpvgpETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMAR 1624
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRP----DDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1625 LTRIADTVTPALVLTrtgqggclpgaevfgdvpvvaldrvadrltampdqrpevtvDPRGLAYSIFTSGSTGQPKGVAVE 1704
Cdd:cd17648 77 IQFILEDTGARVVIT-----------------------------------------NSTDLAYAIYTSGTTGKPKGVLVE 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1705 HIGIVRYLSWAAASYPTAGRR--GTLAHSSVGFDLTMSALFEPLVSGRGVTLMP-----ADATLADLAEE-----LSGPL 1772
Cdd:cd17648 116 HGSVVNLRTSLSERYFGRDNGdeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPdemrfDPDRFYAYINRekvtyLSGTP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1773 A----YDYIRLTpsHLRHLVghwtgqelppaargwvVGGETLDPALVKQLLELRPdAEVINHYGPTETVIGRVVHPvrEA 1848
Cdd:cd17648 196 SvlqqYDLARLP--HLKRVD----------------AAGEEFTAPVFEKLRSRFA-GLIINAYGPTETTVTNHKRF--FP 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1849 GELAVDSPLplGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPAGEPG-------ARMY 1921
Cdd:cd17648 255 GDQRFDKSL--GRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnARLY 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1922 RTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVR----------DQQLVGWFIPAEDHpp 1991
Cdd:cd17648 333 KTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKedasqaqsriQKYLVGYYLPEPGH-- 410
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 653678460 1992 VTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRALP 2034
Cdd:cd17648 411 VPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRALP 453
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
47-459 |
2.37e-88 |
|
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: 295.83 E-value: 2.37e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 47 VPLAPGQAGIWFSEQLRPGTPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVFRLGPDGEPVQQTAPAAPVALPV 126
Cdd:cd19539 2 IPLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGPAPLEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 127 IDVTEADLPQA------LRTAAEQPFDLERGPLLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLLLADLARAYAGeLPAG 200
Cdd:cd19539 82 RDLSDPDSDRErrleelLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAA-RRKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 201 VAAP------AFRDVAAWQHGRLAAGELDDQLRYWRQRLAGLPDLEIPGDRQRPADRDWRAHSVRRELPAATEAAVRRLA 274
Cdd:cd19539 161 PAAPlpelrqQYKEYAAWQREALAAPRAAELLDFWRRRLRGAEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 275 AAHDTTPFTVLLAAYGTFLHRLTGQDDFAVGVPVAGRGRTDLESVVGLFAGMVPVRLDLTGRPSFDEVLSRTVAGSRNDF 354
Cdd:cd19539 241 KRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 355 AHPQIPFDRLVRELRRDRIAGSQLLVQAMAGTESTAvALTFGEAAGTEQPVDVAL---AKCDLDLSVLDDGDRLAVTLVA 431
Cdd:cd19539 321 RHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAP-AGELELAGGLSYTEGSDIpdgAKFDLNLTVTEEGTGLRGSLGY 399
|
410 420
....*....|....*....|....*...
gi 653678460 432 AADLFTPAAAEQLAGQFLSLLAGLTGAP 459
Cdd:cd19539 400 ATSLFDEETIQGFLADYLQVLRQLLANP 427
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
47-452 |
1.20e-87 |
|
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: 293.79 E-value: 1.20e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 47 VPLAPGQAGIWFSEQLRPGTPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVFrlgP--DGEPVQQTAPAAPVAL 124
Cdd:cd19538 2 IPLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVF---PeeDGVPYQLILEEDEATP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 125 P--VIDVTEADLPQALRTAAEQPFDLERGPLLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLLLADLARAY----AGELP 198
Cdd:cd19538 79 KleIKEVDEEELESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYrarcKGEAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 199 AGVAAPA-FRDVAAWQ-----HGRLAAGELDDQLRYWRQRLAGLPD-LEIPGDRQRPADRDWRAHSVRRELPAATEAAVR 271
Cdd:cd19538 159 ELAPLPVqYADYALWQqellgDESDPDSLIARQLAYWKKQLAGLPDeIELPTDYPRPAESSYEGGTLTFEIDSELHQQLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 272 RLAAAHDTTPFTVLLAAYGTFLHRLTGQDDFAVGVPVAGRGRTDLESVVGLFAGMVPVRLDLTGRPSFDEVLSRTVAGSR 351
Cdd:cd19538 239 QLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 352 NDFAHPQIPFDRLVRELRRDRIAGSQLLVQAMAGTESTAVA-LTFGEAAGTEQPVDVALAKCDLDLSV---LDDG--DRL 425
Cdd:cd19538 319 EAYEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPsLDLPGLEAKLELRTVGSAKFDLTFELreqYNDGtpNGI 398
|
410 420
....*....|....*....|....*..
gi 653678460 426 AVTLVAAADLFTPAAAEQLAGQFLSLL 452
Cdd:cd19538 399 EGFIEYRTDLFDHETIEALAQRYLLLL 425
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
47-459 |
2.67e-87 |
|
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: 292.44 E-value: 2.67e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 47 VPLAPGQAGIWFSEQLRPGTPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVFRLGP-DGEPVQQTAPAAPVALP 125
Cdd:cd19532 2 EPMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPeDGEPMQGVLASSPLRLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 126 VIDVT-EADLPQALRTAAEQPFDLERGPLLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLLLADLARAYAGElPAGVAAP 204
Cdd:cd19532 82 HVQISdEAEVEEEFERLKNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQ-PLLPPPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 205 AFRDVAAWQHGRLAAGELDDQLRYWRQRLAGLPD----LEIPGDRQRPADRDWRAHSVRRELPAATEAAVRRLAAAHDTT 280
Cdd:cd19532 161 QYLDFAARQRQDYESGALDEDLAYWKSEFSTLPEplplLPFAKVKSRPPLTRYDTHTAERRLDAALAARIKEASRKLRVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 281 PFTVLLAAYGTFLHRLTGQDDFAVGVPVAGRGRTDLESVVGLFAGMVPVRLDLTGRPSFDEVLSRTVAGSRNDFAHPQIP 360
Cdd:cd19532 241 PFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDKAYAALAHSRVP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 361 FDRLVRELRRDRIAGSQLLVQA-----MAGTESTavalTFGEAAGTEqpVDVALAK--CDLDLSVLDDGDRLA-VTLVAA 432
Cdd:cd19532 321 FDVLLDELGVPRSATHSPLFQVfinyrQGVAESR----PFGDCELEG--EEFEDARtpYDLSLDIIDNPDGDClLTLKVQ 394
|
410 420
....*....|....*....|....*..
gi 653678460 433 ADLFTPAAAEQLAGQFLSLLAGLTGAP 459
Cdd:cd19532 395 SSLYSEEDAELLLDSYVNLLEAFARDP 421
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
229-1039 |
8.44e-84 |
|
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: 305.07 E-value: 8.44e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 229 WRQRLAGLPDLEIPGDRQRPADRDWRAHSVRRELPAATeaavrrLAAAHDTTPFTVLLAAYGTFLHRLTGQDDFAVGVpv 308
Cdd:TIGR03443 2 WSERLDNPTLSVLPHDYLRPANNRLVEATYSLQLPSAE------VTAGGGSTPFIILLAAFAALVYRLTGDEDIVLGT-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 309 agRGRTDLESVVglfagmvpVRLDLTGRPSFDEVLSRTVAGSRNDFAHPQIPFDRLVRElrrdriagsqllVQAMAGTES 388
Cdd:TIGR03443 74 --SSNKSGRPFV--------LRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEH------------IQAAKKLER 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 389 TAV--ALTFGEAAGTEQPVDVALAKCDLDLSVLDDGDRLAVTLVAAADLFTPAAAEQLAGQFLSLLAGLTGAPDRLVSEV 466
Cdd:TIGR03443 132 TPPlfRLAFQDAPDNQQTTYSTGSTTDLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 467 DLLdTDELHTVLcrwndtarPLPAASL---------RERFQQWCRRTPGAVAVIE---------GDTTLSYRELDERANR 528
Cdd:TIGR03443 212 SLI-TPSQKSLL--------PDPTKDLdwsgfrgaiHDIFADNAEKHPDRTCVVEtpsfldpssKTRSFTYKQINEASNI 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 529 LARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARP--VLVVTDAATADRLGPDD 606
Cdd:TIGR03443 283 LAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPraLIVIEKAGTLDQLVRDY 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 607 ITG----------LVVLEE-TDTGGYPATEPPAVPAGHSAY------VI----------YTSGSTGRPKGVVITRAALDN 659
Cdd:TIGR03443 363 IDKelelrteipaLALQDDgSLVGGSLEGGETDVLAPYQALkdtptgVVvgpdsnptlsFTSGSEGIPKGVLGRHFSLAY 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 660 FLAAMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALIDLAGRHRVTLAQATPTLWQALvp 739
Cdd:TIGR03443 443 YFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAMGQLL-- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 740 elSGPALAGIRVL-----VGgEALPAELARRLgDAGAE---VTNMYGPTET-------TIWSTSGPTS-----EDSIrrg 799
Cdd:TIGR03443 521 --SAQATTPIPSLhhaffVG-DILTKRDCLRL-QTLAEnvcIVNMYGTTETqravsyfEIPSRSSDSTflknlKDVM--- 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 800 SIGVPIDNTQVYVLDANLHPAPIGV--LGELHIAGEGLARGYWNRPGLTAEKFLPDPFGPPGT----------------- 860
Cdd:TIGR03443 594 PAGKGMKNVQLLVVNRNDRTQTCGVgeVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVDPSHwidldkennkperefwl 673
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 861 ----RMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIP---- 932
Cdd:TIGR03443 674 gprdRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVPqdks 753
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 933 ---------------DGPVAP---------DALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAALPAPDYGTRSTA 988
Cdd:TIGR03443 754 deleefksevddeesSDPVVKglikyrkliKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTAQLAAV 833
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 653678460 989 RPPRD---------DRERFLCTAFAEVLGLPEVAVS--DNFFELGGHSLLAFRLLARIRDEF 1039
Cdd:TIGR03443 834 AKNRSasaadeeftETEREIRDLWLELLPNRPATISpdDSFFDLGGHSILATRMIFELRKKL 895
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
1083-1499 |
3.89e-83 |
|
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: 281.08 E-value: 3.89e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1083 LPLSPMQESIWLADQVSAGDSVYNVPLALRLIGPLDRGALRRTLNRVVDRHEMLRTrIHPGPDGMPVQ-VADPAGGGAAL 1161
Cdd:cd19538 2 IPLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRT-VFPEEDGVPYQlILEEDEATPKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1162 TERDAAPgTDLAQLLLAEAALGFTLATEHPLRAVLWRLDEREHVLLLTAHHVAVDAWSMDLIQRDLTELYAADTGHREPE 1241
Cdd:cd19538 81 EIKEVDE-EELESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1242 LDEPALAQADYAVWQRQ-----SAQRGRYAAELDFWRTELTGA-VATEVAGDLPRPATPGGGGGAVEFALAPRQIQGIRE 1315
Cdd:cd19538 160 LAPLPVQYADYALWQQEllgdeSDPDSLIARQLAYWKKQLAGLpDEIELPTDYPRPAESSYEGGTLTFEIDSELHQQLLQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1316 LARRCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGRGNPRLDNLVGCLVNTVVLRGDLSGAPTFHELLRRTHARTAD 1395
Cdd:cd19538 240 LAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNLE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1396 ALAHQELPFEHLV----ADRGAGNGPLFRIMYSFSSQEPAGRSAGDVDLEPVPVPVTTCKFDLVLTV-----VDGGSTLE 1466
Cdd:cd19538 320 AYEHQDIPFERLVealnPTRSRSRHPLFQIMLALQNTPQPSLDLPGLEAKLELRTVGSAKFDLTFELreqynDGTPNGIE 399
|
410 420 430
....*....|....*....|....*....|...
gi 653678460 1467 GVLEYADDLYLPGTAERLVTSLTNLLAAAVRTP 1499
Cdd:cd19538 400 GFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
495-977 |
2.26e-80 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 275.62 E-value: 2.26e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 495 ERFQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPD 574
Cdd:PRK04813 6 ETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 575 FPVERIAYLLSDARPVLVV-TDAATADRLGPDDITgLVVLEETDTGGYPATEPPAVPAGHSAYVIYTSGSTGRPKGVVIT 653
Cdd:PRK04813 86 SPAERIEMIIEVAKPSLIIaTEELPLEILGIPVIT-LDELKDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGVQIS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 654 RAALDNFLAAMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALIDlagrhrvTLAQ----- 728
Cdd:PRK04813 165 HDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFE-------TLPQlpinv 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 729 --ATPTLWQA--LVPELSGPALAGIRV-LVGGEALPAELARRLGDA--GAEVTNMYGPTETTIWSTSGPTSEDSIRRGS- 800
Cdd:PRK04813 238 wvSTPSFADMclLDPSFNEEHLPNLTHfLFCGEELPHKTAKKLLERfpSATIYNTYGPTEATVAVTSIEITDEMLDQYKr 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 801 --IGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFlpdpFGPPGTRMYRTGDLVRWsAAGDLE 878
Cdd:PRK04813 318 lpIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAF----FTFDGQPAYHTGDAGYL-EDGLLF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 879 YLGRTDHQVKLRGFRIELGEIETTLiNAGPVRRAAAVVREDRPGDLR-LVAYVIP-DGPVAPD-----ALRTELSRTLPD 951
Cdd:PRK04813 393 YQGRIDFQIKLNGYRIELEEIEQNL-RQSSYVESAVVVPYNKDHKVQyLIAYVVPkEEDFEREfeltkAIKKELKERLME 471
|
490 500
....*....|....*....|....*.
gi 653678460 952 YMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:PRK04813 472 YMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1533-2033 |
4.32e-80 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 272.84 E-value: 4.32e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1533 VHQLVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGY 1612
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALR--ALG---VGPGDRVALLLPNSPEFVVAFLAALRAGAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1613 FIPVDPGYPMARLTRIADTVTPALVLTrtgqggclpgaevfgdvpvvaldrvadrltampdqrpevtvdprglAYSIFTS 1692
Cdd:COG0318 76 VVPLNPRLTAEELAYILEDSGARALVT----------------------------------------------ALILYTS 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1693 GSTGQPKGVAVEHIGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMSA-LFEPLVSGRGVTLMP---ADATLADLAEEl 1768
Cdd:COG0318 110 GTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVgLLAPLLAGATLVLLPrfdPERVLELIERE- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1769 sGPlayDYIRLTPSHLRHLVGH--WTGQELPpAARGWVVGGETLDPALVKQLLElRPDAEVINHYGPTETVIGRVVHPvr 1846
Cdd:COG0318 189 -RV---TVLFGVPTMLARLLRHpeFARYDLS-SLRLVVSGGAPLPPELLERFEE-RFGVRIVEGYGLTETSPVVTVNP-- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1847 eaGELAVDSPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFlpdpagEPGarMYRTGDL 1926
Cdd:COG0318 261 --EDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF------RDG--WLRTGDL 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1927 VRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVL-----VRDQQLVGWFIPAEDHpPVTVSALRRFC 2001
Cdd:COG0318 331 GRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVgvpdeKWGERVVAFVVLRPGA-ELDAEELRAFL 409
|
490 500 510
....*....|....*....|....*....|..
gi 653678460 2002 AEQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:COG0318 410 RERLARYKVPRRVEFVDELPRTASGKIDRRAL 441
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
492-977 |
3.93e-79 |
|
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273780 [Multi-domain] Cd Length: 502 Bit Score: 272.02 E-value: 3.93e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 492 SLRERFQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPI 571
Cdd:TIGR01734 1 KLIEAIQAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 572 DPDFPVERIAYLLSDARPVLVVTDAA-TADRLGPDDITgLVVLEETDTGGYPATEPPAVPAGHSAYVIYTSGSTGRPKGV 650
Cdd:TIGR01734 81 DTSIPSERIEMIIEAAGPELVIHTAElSIDAVGTQIIT-LSALEQAETSGGPVSFDHAVKGDDNYYIIYTSGSTGNPKGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 651 VITRAALDNFLAAMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALIDLAGRHRVTLAQAT 730
Cdd:TIGR01734 160 QISHDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGLNVWVST 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 731 PTLWQA--LVPELSGPALAGI-RVLVGGEALPAELARRLGDA--GAEVTNMYGPTETTIWSTS-GPTSE--DSIRRGSIG 802
Cdd:TIGR01734 240 PSFVDMclLDPNFNQENYPHLtHFLFCGEELPVKTAKALLERfpKATIYNTYGPTEATVAVTSvKITQEilDQYPRLPIG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 803 VPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFlpdpFGPPGTRMYRTGDLVRWSaAGDLEYLGR 882
Cdd:TIGR01734 320 FAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAF----FSHEGQPAYRTGDAGTIT-DGQLFYQGR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 883 TDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDL-RLVAYVIPDGPV------APDALRTELSRTLPDYMIP 955
Cdd:TIGR01734 395 LDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKYNKDHKVeYLIAAIVPETEDfekefqLTKAIKKELKKSLPAYMIP 474
|
490 500
....*....|....*....|..
gi 653678460 956 AVIVPVPDFPTTPNGKLDRAAL 977
Cdd:TIGR01734 475 RKFIYRDQLPLTANGKIDRKAL 496
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
1271-2125 |
8.00e-77 |
|
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: 283.11 E-value: 8.00e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1271 FWRTELTGAVATEVAGDLPRPATpgggGGAVEfALAPRQIQGiRELARRCGTTVSTVVLSALQTLLYRITGGADVVIGST 1350
Cdd:TIGR03443 1 RWSERLDNPTLSVLPHDYLRPAN----NRLVE-ATYSLQLPS-AEVTAGGGSTPFIILLAAFAALVYRLTGDEDIVLGTS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1351 VSGRGNPrldnlvgclvntVVLRGDLSGAPTFHELLRRTHARTADALAHQELPFEHLVADRGAGNG-----PLFRImySF 1425
Cdd:TIGR03443 75 SNKSGRP------------FVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKlertpPLFRL--AF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1426 SSQEpagrsagDVDLEPVPVPVTTckfDLVLTVVDGGSTLEGVLEYADDLYlpgTAER---LVTSLTNLLAAAVRTPELA 1502
Cdd:TIGR03443 141 QDAP-------DNQQTTYSTGSTT---DLTVFLTPSSPELELSIYYNSLLF---SSDRitiVADQLAQLLSAASSNPDEP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1503 VTRLAITSES------DTVRTSRWGrseQHVGddrTVHQLVEAQA----DR-----TPGWTALRTGDRSLTFAGLDAQAN 1567
Cdd:TIGR03443 208 IGKVSLITPSqksllpDPTKDLDWS---GFRG---AIHDIFADNAekhpDRtcvveTPSFLDPSSKTRSFTYKQINEASN 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1568 RLAHAL-HTGalgappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMARLT------------------RI 1628
Cdd:TIGR03443 282 ILAHYLlKTG------IKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTiylsvakpraliviekagTL 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1629 ADTVT-------------PALVLTRTG--QGGCLPGAEvfGDV--PVVALDrvadrltampDQRPEVTVDPRGLAYSIFT 1691
Cdd:TIGR03443 356 DQLVRdyidkelelrteiPALALQDDGslVGGSLEGGE--TDVlaPYQALK----------DTPTGVVVGPDSNPTLSFT 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1692 SGSTGQPKGVAVEHIGIVRYLSWAAASYP-TAGRRGTL----AHSSVGFDLtmsalFEPLVSGRGVTLMPAD--ATLADL 1764
Cdd:TIGR03443 424 SGSEGIPKGVLGRHFSLAYYFPWMAKRFGlSENDKFTMlsgiAHDPIQRDM-----FTPLFLGAQLLVPTADdiGTPGRL 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1765 AEELSgplayDY----IRLTPSHLRHLVGHWTGQeLPPAARGWVVGGetldpALVKQ----LLELRPDAEVINHYGPTET 1836
Cdd:TIGR03443 499 AEWMA-----KYgatvTHLTPAMGQLLSAQATTP-IPSLHHAFFVGD-----ILTKRdclrLQTLAENVCIVNMYGTTET 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1837 viGRVVH----PVREAGELAVDSP---LPLGRPLGETRLQVLDAWLEAVP--VGAVGELFIGGDGIARGYLGRPALTAEK 1907
Cdd:TIGR03443 568 --QRAVSyfeiPSRSSDSTFLKNLkdvMPAGKGMKNVQLLVVNRNDRTQTcgVGEVGEIYVRAGGLAEGYLGLPELNAEK 645
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1908 FLP------------DPAGEPGA---------RMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPG 1966
Cdd:TIGR03443 646 FVNnwfvdpshwidlDKENNKPErefwlgprdRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPL 725
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1967 VEQAVVLVR-----DQQLVGWFIP----------------AEDHPPVtVSALRR----------FCAEQLPEFMVPNQWV 2015
Cdd:TIGR03443 726 VRENVTLVRrdkdeEPTLVSYIVPqdksdeleefksevddEESSDPV-VKGLIKyrklikdireYLKKKLPSYAIPTVIV 804
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 2016 ALDAFPLTPHGKVNHRALPGPTSGRPELEDRYQAPR------TPGEQLLAELWSTVLGT--DRIGIEDNFFDLGGTSISV 2087
Cdd:TIGR03443 805 PLKKLPLNPNGKVDKPALPFPDTAQLAAVAKNRSASaadeefTETEREIRDLWLELLPNrpATISPDDSFFDLGGHSILA 884
|
970 980 990
....*....|....*....|....*....|....*....
gi 653678460 2088 IQLSGACRRA-GVEISPKDVFEQPTVRGQAmRAIARSRD 2125
Cdd:TIGR03443 885 TRMIFELRKKlNVELPLGLIFKSPTIKGFA-KEVDRLKK 922
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1537-1948 |
1.34e-76 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 261.48 E-value: 1.34e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1537 VEAQADRTPGWTALRTGD-RSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIP 1615
Cdd:pfam00501 1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLR--ALG---VGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1616 VDPGYPMARLTRIADTVTPALVLTrTGQGGCLPGAEVFGDVPVVALDRVADRLTAM-------------PDQRPEVTVDP 1682
Cdd:pfam00501 76 LNPRLPAEELAYILEDSGAKVLIT-DDALKLEELLEALGKLEVVKLVLVLDRDPVLkeeplpeeakpadVPPPPPPPPDP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1683 RGLAYSIFTSGSTGQPKGVAVEHIGIVRYLSWAAASYPTAGRRG----TLAHSSVGFDLTMSA-LFEPLVSGRGVTLMPA 1757
Cdd:pfam00501 155 DDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGpddrVLSTLPLFHDFGLSLgLLGPLLAGATVVLPPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1758 DATLADLAeelsgplAYDYIR--------LTPSHLRHLVGHWTG-QELPPAARGWVVGGETLDPALVKQLLELRPDAeVI 1828
Cdd:pfam00501 235 FPALDPAA-------LLELIErykvtvlyGVPTLLNMLLEAGAPkRALLSSLRLVLSGGAPLPPELARRFRELFGGA-LV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1829 NHYGPTETVIGrVVHPVREAGELAvdSPLPLGRPLGETRLQVLD-AWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEK 1907
Cdd:pfam00501 307 NGYGLTETTGV-VTTPLPLDEDLR--SLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEA 383
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 653678460 1908 FLPDpagepgaRMYRTGDLVRWRGDGLLDFVGRVDDQVKLR 1948
Cdd:pfam00501 384 FDED-------GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
46-459 |
5.62e-75 |
|
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: 257.34 E-value: 5.62e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 46 PVPLAPGQAGIWFSEQLRPGTPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVFrLGPDGEPVQQTAPAAPVALP 125
Cdd:cd19066 1 KIPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRF-CEEAGRYEQVVLDKTVRFRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 126 -VIDVTEADLPQA----LRTAAEQ-PFDLERGPLLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLLLADLARAYAG-ELP 198
Cdd:cd19066 80 eIIDLRNLADPEArlleLIDQIQQtIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAaERQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 199 AGVAAP---AFRDVAAWQHGRLAAGELDDQLRYWRQRLAGLPD-LEIPGDRQRPADRDWRAHSVRRELPAATEAAVRRLA 274
Cdd:cd19066 160 KPTLPPpvgSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPpLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREVA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 275 AAHDTTPFTVLLAAYGTFLHRLTGQDDFAVGVPVAGRGRTDLESVVGLFAGMVPVRLDLTGRPSFDEVLSRTVAGSRNDF 354
Cdd:cd19066 240 RESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREAI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 355 AHPQIPFDRLVRELRRDRIAGSQLLVQAMAGTEST-AVALTFGEAAGTEQPVDVAL-AKCDLDLSVLDDGDR-LAVTLVA 431
Cdd:cd19066 320 EHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNqQQLGKTGGFIFTTPVYTSSEgTVFDLDLEASEDPDGdLLLRLEY 399
|
410 420
....*....|....*....|....*...
gi 653678460 432 AADLFTPAAAEQLAGQFLSLLAGLTGAP 459
Cdd:cd19066 400 SRGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
1084-1514 |
9.13e-75 |
|
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: 257.65 E-value: 9.13e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1084 PLSPMQESIWLADQVSAGDSVYNVPLALRLIGPLDRGALRRTLNRVVDRHEMLRTRIHPGPDGMPVQVADPA-------- 1155
Cdd:pfam00668 6 PLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEErpfeleii 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1156 --GGGAALTERDAAPgtdlaQLLLAEAALGFTLATEHPLRAVLWRLDEREHVLLLTAHHVAVDAWSMDLIQRDLTELYAA 1233
Cdd:pfam00668 86 diSDLSESEEEEAIE-----AFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1234 DTghREPELDEPALAQ-ADYAVWQRQSAQRGRYAAELDFWRTELTGAVA-TEVAGDLPRPATPGGGGGAVEFALAPRQIQ 1311
Cdd:pfam00668 161 LL--KGEPLPLPPKTPyKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPvLQLPKDYARPADRSFKGDRLSFTLDEDTEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1312 GIRELARRCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGRGNPRLDNLVGCLVNTVVLRGDLSGAPTFHELLRRTHA 1391
Cdd:pfam00668 239 LLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1392 RTADALAHQELPFEHLVAD----RGAGNGPLFRIMYSF-------SSQEPAGRSAGDVDLEPVPVPVTtcKFDLVLTVVD 1460
Cdd:pfam00668 319 DLLSAEPHQGYPFGDLVNDlrlpRDLSRHPLFDPMFSFqnylgqdSQEEEFQLSELDLSVSSVIEEEA--KYDLSLTASE 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 653678460 1461 GGSTLEGVLEYADDLYLPGTAERLVTSLTNLLAAAVRTPELAVTRLAITSESDT 1514
Cdd:pfam00668 397 RGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEK 450
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
1532-2033 |
1.54e-74 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 258.67 E-value: 1.54e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1532 TVHQLVEAQADRTpgwtALRTGDRSLTFAGLDAQANRLAHALHTGALGAppvgpETPVLLLLDRSPELVVAMLAVLKAGG 1611
Cdd:PRK04813 7 TIEEFAQTQPDFP----AYDYLGEKLTYGQLKEDSDALAAFIDSLKLPD-----KSPIIVFGHMSPEMLATFLGAVKAGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1612 YFIPVDPGYPMARLTRIADTVTPALVLTRTGqggcLPgaEVFGDVPVVALDRVADRLTAMPDQRPEVTVDPRGLAYSIFT 1691
Cdd:PRK04813 78 AYIPVDVSSPAERIEMIIEVAKPSLIIATEE----LP--LEILGIPVITLDELKDIFATGNPYDFDHAVKGDDNYYIIFT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1692 SGSTGQPKGVAVEHIGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMSALFEPLVSGRGVTLMPADAT--LADLAEEL- 1768
Cdd:PRK04813 152 SGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTanFKQLFETLp 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1769 --------SGPLAYDYIRLTPSHlrhlvghwtGQELPPAARGWVVGGETLDPALVKQLLELRPDAEVINHYGPTE-TVIG 1839
Cdd:PRK04813 232 qlpinvwvSTPSFADMCLLDPSF---------NEEHLPNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEaTVAV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1840 RVVHPVREAgeLAVDSPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPdpagEPGAR 1919
Cdd:PRK04813 303 TSIEITDEM--LDQYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT----FDGQP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1920 MYRTGDLVRWRgDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRD-----QQLVGWFIPA----EDHP 1990
Cdd:PRK04813 377 AYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNkdhkvQYLIAYVVPKeedfEREF 455
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 653678460 1991 PVTvSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:PRK04813 456 ELT-KAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
500-977 |
1.16e-71 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 251.95 E-value: 1.16e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 500 WCRRTPGAVAVI-EGDT----TLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPD 574
Cdd:COG0365 18 HAEGRGDKVALIwEGEDgeerTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 575 FPVERIAYLLSDARPVLVVTDAATA----------------------------DRLGPD-DITGLVVLEETDTGGYPATE 625
Cdd:COG0365 98 FGAEALADRIEDAEAKVLITADGGLrggkvidlkekvdealeelpslehvivvGRTGADvPMEGDLDWDELLAAASAEFE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 626 PPAVPAGHSAYVIYTSGSTGRPKGVVIT-RAALDNFLAAMAERFPLTAEDRVLATTTVSFdIAGL--ELYLPLRSGAGVV 702
Cdd:COG0365 178 PEPTDADDPLFILYTSGTTGKPKGVVHThGGYLVHAATTAKYVLDLKPGDVFWCTADIGW-ATGHsyIVYGPLLNGATVV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 703 LAD-ADTARNPAALIDLAGRHRVTLAQATPTLWQALVPE----LSGPALAGIRVLV-GGEALPAELARRLGDA-GAEVTN 775
Cdd:COG0365 257 LYEgRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAgdepLKKYDLSSLRLLGsAGEPLNPEVWEWWYEAvGVPIVD 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 776 MYGPTETT-IWSTSGPTSEdsIRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGE--GLARGYWNRPGLTAEKFLP 852
Cdd:COG0365 337 GWGQTETGgIFISNLPGLP--VKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPwpGMFRGYWNDPERYRETYFG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 853 DPFGppgtrMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIP 932
Cdd:COG0365 415 RFPG-----WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVL 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 653678460 933 -DGPVAPDALRTEL----SRTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:COG0365 490 kPGVEPSDELAKELqahvREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
501-979 |
1.35e-71 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 250.47 E-value: 1.35e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 501 CRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERI 580
Cdd:TIGR03098 10 AARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 581 AYLLSDARPVLVVTDAATADRLGP-----DDITGLVV------------------LEETDTGGYPATEPPAVPAGHSAyV 637
Cdd:TIGR03098 90 AHILADCNVRLLVTSSERLDLLHPalpgcHDLRTLIIvgdpahaseghpgeepasWPKLLALGDADPPHPVIDSDMAA-I 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 638 IYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNpaaLID 717
Cdd:TIGR03098 169 LYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHDYLLPRD---VLK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 718 LAGRHRVTLAQATPTLWQALV----PELSGPALagiRVLVG-GEALPAELARRLGDA--GAEVTNMYGPTEtTIWSTSGP 790
Cdd:TIGR03098 246 ALEKHGITGLAAVPPLWAQLAqldwPESAAPSL---RYLTNsGGAMPRATLSRLRSFlpNARLFLMYGLTE-AFRSTYLP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 791 TSEDSIRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFGPPGTRMYRT----G 866
Cdd:TIGR03098 322 PEEVDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPPFPGELHLPELavwsG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 867 DLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAV-VREDRPGDlRLVAYVIP--DGPVAPDALRT 943
Cdd:TIGR03098 402 DTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFgVPDPTLGQ-AIVLVVTPpgGEELDRAALLA 480
|
490 500 510
....*....|....*....|....*....|....*.
gi 653678460 944 ELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAALPA 979
Cdd:TIGR03098 481 ECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
48-459 |
2.60e-71 |
|
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: 246.84 E-value: 2.60e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 48 PLAPGQAGIWFSEQLRPGTPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVFRlGPDGEPVQQTAPAAPVALPVI 127
Cdd:cd20484 3 PLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIE-EEDGVPFQKIEPSKPLSFQEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 128 D---VTEADLPQALRTAAEQPFDLERGPLLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLLLADLARAYA----GELPAG 200
Cdd:cd20484 82 DissLKESEIIAYLREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQallqGKQPTL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 201 VAAPA-FRDVAAWQHGRLAAGELDDQLRYWRQRLAG-LPDLEIPGDRQRPADRDWRAHSVRRELPAATEAAVRRLAAAHD 278
Cdd:cd20484 162 ASSPAsYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGtLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFARSQS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 279 TTPFTVLLAAYGTFLHRLTGQDDFAVGVPVAGRGRTDLESVVGLFAGMVPVRLDLTGRPSFDEV---LSRTVAgsrNDFA 355
Cdd:cd20484 242 INLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFirkLQLTVL---DGLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 356 HPQIPFDRLVRELRRDR-IAGSQLL--------------VQAMAGTESTAVALTFGEAAGTEqpvdvalAKCDLDLSVLD 420
Cdd:cd20484 319 HAAYPFPAMVRDLNIPRsQANSPVFqvaffyqnflqstsLQQFLAEYQDVLSIEFVEGIHQE-------GEYELVLEVYE 391
|
410 420 430
....*....|....*....|....*....|....*....
gi 653678460 421 DGDRLAVTLVAAADLFTPAAAEQLAGQFLSLLAGLTGAP 459
Cdd:cd20484 392 QEDRFTLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
633-973 |
8.94e-71 |
|
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: 241.81 E-value: 8.94e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 633 HSAYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADtarNP 712
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF---DP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 713 AALIDLAGRHRVTLAQATPTLWQALV--PELSGPALAGIRVLV-GGEALPAELARRLGDA-GAEVTNMYGPTETTIWSTS 788
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLkaPESAGYDLSSLRALVsGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 789 GPTSEDSIRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFlpdpfgppGTRMYRTGDL 868
Cdd:cd04433 158 GPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD--------EDGWYRTGDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 869 VRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIP--DGPVAPDALRTELS 946
Cdd:cd04433 230 GRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLrpGADLDAEELRAHVR 309
|
330 340
....*....|....*....|....*..
gi 653678460 947 RTLPDYMIPAVIVPVPDFPTTPNGKLD 973
Cdd:cd04433 310 ERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
49-282 |
4.85e-68 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 229.93 E-value: 4.85e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 49 LAPGQAGIWFseqLRPGTPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVFRLGpDGEPVQQTAPAAPVALPVID 128
Cdd:COG4908 1 LSPAQKRFLF---LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEE-DGEPVQRIDPDADLPLEVVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 129 VT-------EADLPQALRTAAEQPFDLERGPLLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLLLADLARAYAG-----E 196
Cdd:COG4908 77 LSalpeperEAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAAllegeP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 197 LPAGVAAPAFRDVAAWQHGRLAAGELDDQLRYWRQRLAGLPD-LEIPGDRQRPADRDWRAHSVRRELPAATEAAVRRLAA 275
Cdd:COG4908 157 PPLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPvLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAK 236
|
....*..
gi 653678460 276 AHDTTPF 282
Cdd:COG4908 237 AHGATVN 243
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
48-459 |
3.92e-67 |
|
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: 234.40 E-value: 3.92e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 48 PLAPGQAGIWFSEQLRPGTPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVFRLGPDGEPVQQTAPAAPVALPVI 127
Cdd:cd19543 3 PLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDRKLPWREL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 128 DVT-------EADLPQALRTAAEQPFDLERGPLLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLLLADLARAYA----GE 196
Cdd:cd19543 83 DLShlseaeqEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAalgeGQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 197 LPAGVAAPAFRDVAAWqhgrLAAGELDDQLRYWRQRLAGLPDL-EIPGDRQRPADRDWRAHSVRRELPAATEAAVRRLAA 275
Cdd:cd19543 163 PPSLPPVRPYRDYIAW----LQRQDKEAAEAYWREYLAGFEEPtPLPKELPADADGSYEPGEVSFELSAELTARLQELAR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 276 AHDTTPFTVLLAAYGTFLHRLTGQDDFAVGVPVAGR--GRTDLESVVGLFAGMVPVRLDLTGRPSFDEVLsRTVAGSRND 353
Cdd:cd19543 239 QHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRpaELPGIETMVGLFINTLPVRVRLDPDQTVLELL-KDLQAQQLE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 354 F-AHPQIPfdrLVrELRRDRIAGSQLL----------VQAMAGTESTAVALTFGEAAGTEQPvdvalakcDLDLSVL-DD 421
Cdd:cd19543 318 LrEHEYVP---LY-EIQAWSEGKQALFdhllvfenypVDESLEEEQDEDGLRITDVSAEEQT--------NYPLTVVaIP 385
|
410 420 430
....*....|....*....|....*....|....*...
gi 653678460 422 GDRLAVTLVAAADLFTPAAAEQLAGQFLSLLAGLTGAP 459
Cdd:cd19543 386 GEELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
501-974 |
1.98e-65 |
|
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: 229.80 E-value: 1.98e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 501 CRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERI 580
Cdd:cd17631 5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 581 AYLLSDARPVLVVtdaatadrlgpDDItglvvleetdtggypateppavpaghsAYVIYTSGSTGRPKGVVIT-RAALDN 659
Cdd:cd17631 85 AYILADSGAKVLF-----------DDL---------------------------ALLMYTSGTTGRPKGAMLThRNLLWN 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 660 FLAAMAErFPLTAEDRVLATTTVsFDIAGLELYLP---LRSGAGVVLADADtarnPAALIDLAGRHRVTLAQATPTLWQA 736
Cdd:cd17631 127 AVNALAA-LDLGPDDVLLVVAPL-FHIGGLGVFTLptlLRGGTVVILRKFD----PETVLDLIERHRVTSFFLVPTMIQA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 737 LV--PELSGPALAGIR-VLVGGEALPAELARRLGDAGAEVTNMYGPTETTIwSTSGPTSEDSIRR-GSIGVPIDNTQVYV 812
Cdd:cd17631 201 LLqhPRFATTDLSSLRaVIYGGAPMPERLLRALQARGVKFVQGYGMTETSP-GVTFLSPEDHRRKlGSAGRPVFFVEVRI 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 813 LDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgppgtrmyRTGDLVRWSAAGDLEYLGRTDHQVKLRGF 892
Cdd:cd17631 280 VDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF--------HTGDLGRLDEDGYLYIVDRKKDMIISGGE 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 893 RIELGEIETTLINAGPVRRAAAV-VREDRPGDlRLVAYVI--PDGPVAPDALRTELSRTLPDYMIPAVIVPVPDFPTTPN 969
Cdd:cd17631 352 NVYPAEVEDVLYEHPAVAEVAVIgVPDEKWGE-AVVAVVVprPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNAT 430
|
....*
gi 653678460 970 GKLDR 974
Cdd:cd17631 431 GKILK 435
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
515-980 |
2.94e-64 |
|
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: 229.33 E-value: 2.94e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 515 TTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARPvlvvt 594
Cdd:cd17647 19 RSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKP----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 595 daatadrlgpddiTGLVVLEETDTGGYPATEPPavpaghsayVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAED 674
Cdd:cd17647 94 -------------RGLIVIRAAGVVVGPDSNPT---------LSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSEND 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 675 RVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALIDLAGRHRVTLAQATPTLWQALVPELSGPALAGIRVLVG 754
Cdd:cd17647 152 KFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQATTPFPKLHHAFFV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 755 GEALPAELARRLgDAGAE---VTNMYGPTETT-------IWS-TSGPTSEDSIR------RGsigvpIDNTQVYVLDAN- 816
Cdd:cd17647 232 GDILTKRDCLRL-QTLAEnvrIVNMYGTTETQravsyfeVPSrSSDPTFLKNLKdvmpagRG-----MLNVQLLVVNRNd 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 817 -LHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFGPPG---------------------TRMYRTGDLVRWSAA 874
Cdd:cd17647 306 rTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDhwnyldkdnnepwrqfwlgprDRLYRTGDLGRYLPN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 875 GDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIPDG-------------------- 934
Cdd:cd17647 386 GDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFdkpddesfaqedvpkevstd 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 653678460 935 PVAP---------DALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAALPAP 980
Cdd:cd17647 466 PIVKgligyrkliKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
1082-1499 |
4.86e-64 |
|
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: 225.37 E-value: 4.86e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1082 PLPLSPMQESIWLADQVSAGDSVYNVPLALRLIGPLDRGALRRTLNRVVDRHEMLRTRiHPGPDGMPVQVADPAGGGAAL 1161
Cdd:cd19066 1 KIPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTR-FCEEAGRYEQVVLDKTVRFRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1162 TERDAAPGTDLAQLLL----AEAALGFTLATEHPLRAVLWRLDEREHVLLLTAHHVAVDAWSMDLIQRDLTELYAADTgH 1237
Cdd:cd19066 80 EIIDLRNLADPEARLLelidQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAE-R 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1238 REPELDEPALAQADYAVWQRQSAQRGRYAAELDFWRTELTGAVAT-EVAGDLPRPATPGGGGGAVEFALAPRQIQGIREL 1316
Cdd:cd19066 159 QKPTLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPlPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1317 ARRCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGRGNPRLDNLVGCLVNTVVLRGDLSGAPTFHELLRRTHARTADA 1396
Cdd:cd19066 239 ARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1397 LAHQELPFEHLVAD----RGAGNGPLFRIMYSF-SSQEPAGRSAGDVDLEPVPVPVTTCKFDLVL---TVVDGGstLEGV 1468
Cdd:cd19066 319 IEHQRVPFIELVRHlgvvPEAPKHPLFEPVFTFkNNQQQLGKTGGFIFTTPVYTSSEGTVFDLDLeasEDPDGD--LLLR 396
|
410 420 430
....*....|....*....|....*....|.
gi 653678460 1469 LEYADDLYLPGTAERLVTSLTNLLAAAVRTP 1499
Cdd:cd19066 397 LEYSRGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
43-459 |
7.52e-61 |
|
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: 216.58 E-value: 7.52e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 43 PPGPVPLAPGQAGIWFSEQLRPGTPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVFRlGPDGEPVQQT--APAA 120
Cdd:cd19546 1 RPDEVPATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFP-GDGGDVHQRIldADAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 121 PVALPVIDVTEADLPQALRTAAEQPFDLERGPLLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLLLADLARAY----AGE 196
Cdd:cd19546 80 RPELPVVPATEEELPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYgarrEGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 197 LPAGVAAP-AFRDVAAWQHgRLAAGELD------DQLRYWRQRLAGLPD-LEIPGDRQRPADRDWRAHSVRRELPAATEA 268
Cdd:cd19546 160 APERAPLPlQFADYALWER-ELLAGEDDrdsligDQIAYWRDALAGAPDeLELPTDRPRPVLPSRRAGAVPLRLDAEVHA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 269 AVRRLAAAHDTTPFTVLLAAYGTFLHRLTGQDDFAVGVPVAGR-GRTDLESVVGLFAGMVPVRLDLTGRPSFDEVLSRTV 347
Cdd:cd19546 239 RLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDdEEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 348 AGSRNDFAHPQIPFDRLVRELRRDRIAGSQLLVQ-AMAGTESTAVALTFGEAAG-TEQPVDVALAKCDLDLSVL------ 419
Cdd:cd19546 319 EAVREARRHQDVPFERLAELLALPPSADRHPVFQvALDVRDDDNDPWDAPELPGlRTSPVPLGTEAMELDLSLAlterrn 398
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 653678460 420 --DDGDRLAVTLVAAADLFTPAAAEQLAGQFLSLLAGLTGAP 459
Cdd:cd19546 399 ddGDPDGLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
524-977 |
1.04e-60 |
|
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: 216.92 E-value: 1.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 524 ERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAA----YLPIDPDFPVERIAYLLSDARPVLVVTDAATA 599
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 600 DRL------GPDDITgLVVLEETDTGGYPAtepPAVPAGHS--AYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLT 671
Cdd:cd05922 81 DRLrdalpaSPDPGT-VLDADGIRAARASA---PAHEVSHEdlALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGIT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 672 AEDRVLATTTVSFDIAGLELYLPLRSGAGVVLadADTARNPAALIDLAGRHRVTLAQATPTLWQALVPELSGPA-LAGIR 750
Cdd:cd05922 157 ADDRALTVLPLSYDYGLSVLNTHLLRGATLVL--TNDGVLDDAFWEDLREHGATGLAGVPSTYAMLTRLGFDPAkLPSLR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 751 VL--VGGeALPAELARRLGDA--GAEVTNMYGPTETTIWSTSGPTSEDSIRRGSIGVPIDNTQVYVLDANLHPAPIGVLG 826
Cdd:cd05922 235 YLtqAGG-RLPQETIARLRELlpGAQVYVMYGQTEATRRMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 827 ELHIAGEGLARGYWNRPGLTAEKflpdpfGPPGTRMYrTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINA 906
Cdd:cd05922 314 EIVHRGPNVMKGYWNDPPYRRKE------GRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSI 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 653678460 907 GPVRRAAAVVREDRPGDlRLVAYVIPDGPVAPDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:cd05922 387 GLIIEAAAVGLPDPLGE-KLALFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
509-977 |
7.57e-60 |
|
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: 213.48 E-value: 7.57e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 509 AVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDAR 588
Cdd:cd05919 3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 589 PVLVVTDAatadrlgpDDItglvvleetdtggypateppavpaghsAYVIYTSGSTGRPKGVVITRAALDNFLAAMA-ER 667
Cdd:cd05919 83 ARLVVTSA--------DDI---------------------------AYLLYSSGTTGPPKGVMHAHRDPLLFADAMArEA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 668 FPLTAEDRVLATTTVSFDIA-GLELYLPLRSGAGVVLadADTARNPAALIDLAGRHRVTLAQATPTLWQALVPELSGP-- 744
Cdd:cd05919 128 LGLTPGDRVFSSAKMFFGYGlGNSLWFPLAVGASAVL--NPGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSpd 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 745 ALAGIRVLV-GGEALPAELARRLGDA-GAEVTNMYGPTETT-IWSTSGPtseDSIRRGSIGVPIDNTQVYVLDANLHPAP 821
Cdd:cd05919 206 ALRSLRLCVsAGEALPRGLGERWMEHfGGPILDGIGATEVGhIFLSNRP---GAWRLGSTGRPVPGYEIRLVDEEGHTIP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 822 IGVLGELHIAGEGLARGYWNRPGLTAEKFLPDpfgppgtrMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIET 901
Cdd:cd05919 283 PGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG--------WYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVES 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 902 TLINAGPVRRAAAVVREDRPGDLRLVAYVIPDGPVAPD-----ALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAA 976
Cdd:cd05919 355 LIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQeslarDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFK 434
|
.
gi 653678460 977 L 977
Cdd:cd05919 435 L 435
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
497-977 |
1.44e-59 |
|
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: 213.96 E-value: 1.44e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 497 FQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFP 576
Cdd:cd05936 5 LEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 577 VERIAYLLSDARPVLVVTDAATADRLGPdditglvvleetdtgGYPATEPPAVPAGHSAYVIYTSGSTGRPKGVVITRAA 656
Cdd:cd05936 85 PRELEHILNDSGAKALIVAVSFTDLLAA---------------GAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 657 L-DNFLAAMA-ERFPLTAEDRVLATTTVsFDIAGLE--LYLPLRSGAGVVLAdadTARNPAALIDLAGRHRVTLAQATPT 732
Cdd:cd05936 150 LvANALQIKAwLEDLLEGDDVVLAALPL-FHVFGLTvaLLLPLALGATIVLI---PRFRPIGVLKEIRKHRVTIFPGVPT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 733 LWQALV--PELSGPALAGIRVLV-GGEALPAELARRLGDA-GAEVTNMYGPTETTIWSTSGPtSEDSIRRGSIGVPIDNT 808
Cdd:cd05936 226 MYIALLnaPEFKKRDFSSLRLCIsGGAPLPVEVAERFEELtGVPIVEGYGLTETSPVVAVNP-LDGPRKPGSIGIPLPGT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 809 QVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgppgtrmyRTGDLVRWSAAGDLEYLGRTDHQVK 888
Cdd:cd05936 305 EVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL--------RTGDIGYMDEDGYFFIVDRKKDMII 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 889 LRGFRIELGEIETTLINAGPVRRAAAV-VREDRPGDlRLVAYVI--PDGPVAPDALRTELSRTLPDYMIPAVIVPVPDFP 965
Cdd:cd05936 377 VGGFNVYPREVEEVLYEHPAVAEAAVVgVPDPYSGE-AVKAFVVlkEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELP 455
|
490
....*....|..
gi 653678460 966 TTPNGKLDRAAL 977
Cdd:cd05936 456 KSAVGKILRREL 467
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
48-459 |
2.16e-59 |
|
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: 211.84 E-value: 2.16e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 48 PLAPGQAGIWFSEQLRPGTPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVFRLgPDGEPVQQTAPAAPVALPVI 127
Cdd:cd19533 3 PLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTE-EEGEPYQWIDPYTPVPIRHI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 128 DVTEADLPQA-----LRTAAEQPFDLERGPLLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLL---LADLARAYAGELPA 199
Cdd:cd19533 82 DLSGDPDPEGaaqqwMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFgqrVAEIYTALLKGRPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 200 GvaAPAFRDVAAWQHGRLAAGELDDQLR---YWRQRLAGLPDLEIPGDRQRPADRDWRAHSVrrELPAATEAAVRRLAAA 276
Cdd:cd19533 162 P--PAPFGSFLDLVEEEQAYRQSERFERdraFWTEQFEDLPEPVSLARRAPGRSLAFLRRTA--ELPPELTRTLLEAAEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 277 HDTTPFTVLLAAYGTFLHRLTGQDDFAVGVPVAGRGRTDLESVVGLFAGMVPVRLDLTGRPSFDEVLSRTVAGSRNDFAH 356
Cdd:cd19533 238 HGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELRSLLRH 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 357 PQIPFDRLVRELRR----DRIAGSQLLVQAMagtestAVALTFGEAAGTEQ-----PVDvalakcDLDLSVLD--DGDRL 425
Cdd:cd19533 318 QRYRYEDLRRDLGLtgelHPLFGPTVNYMPF------DYGLDFGGVVGLTHnlssgPTN------DLSIFVYDrdDESGL 385
|
410 420 430
....*....|....*....|....*....|....
gi 653678460 426 AVTLVAAADLFTPAAAEQLAGQFLSLLAGLTGAP 459
Cdd:cd19533 386 RIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1084-1499 |
3.29e-59 |
|
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: 211.16 E-value: 3.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1084 PLSPMQESIWLADQVSAGDSVYNVPLALRLIGPLDRGALRRTLNRVVDRHEMLRTRIHPGP-DGMPVQV--ADPAgggAA 1160
Cdd:cd19532 3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPeDGEPMQGvlASSP---LR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1161 LTERDAAPGTDLAQLLLAEAALGFTLATEHPLRAVLWRLDEREHVLLLTAHHVAVDAWSMDLIQRDLTELYAADTghrep 1240
Cdd:cd19532 80 LEHVQISDEAEVEEEFERLKNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQP----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1241 eLDEPALAQADYAVWQRQSAQRGRYAAELDFWRTELTGAVATevagdLP---------RPATPGGGGGAVEFALAPRQIQ 1311
Cdd:cd19532 155 -LLPPPLQYLDFAARQRQDYESGALDEDLAYWKSEFSTLPEP-----LPllpfakvksRPPLTRYDTHTAERRLDAALAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1312 GIRELARRCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGRGNPRLDNLVGCLVNTVVLRGDLSGAPTFHELLRRTHA 1391
Cdd:cd19532 229 RIKEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1392 RTADALAHQELPF----EHLVADRGAGNGPLFRIMYSFSSQEPAGRSAGDVDLEPVPVPVTTCKFDLVLTVVD---GGST 1464
Cdd:cd19532 309 KAYAALAHSRVPFdvllDELGVPRSATHSPLFQVFINYRQGVAESRPFGDCELEGEEFEDARTPYDLSLDIIDnpdGDCL 388
|
410 420 430
....*....|....*....|....*....|....*
gi 653678460 1465 LEgvLEYADDLYLPGTAERLVTSLTNLLAAAVRTP 1499
Cdd:cd19532 389 LT--LKVQSSLYSEEDAELLLDSYVNLLEAFARDP 421
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
514-977 |
1.69e-55 |
|
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: 201.16 E-value: 1.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 514 DTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARpvlvV 593
Cdd:cd17654 14 DTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCH----V 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 594 TDAATADRLGpdditglvVLEETDTggyPATEPPAVPAGHS-AYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTA 672
Cdd:cd17654 90 SYLLQNKELD--------NAPLSFT---PEHRHFNIRTDEClAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 673 EDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALID-LAGRHRVTLAQATPTLWQALVPELSGP----ALA 747
Cdd:cd17654 159 EDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADiLFKRHRITVLQATPTLFRRFGSQSIKStvlsATS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 748 GIRVL-VGGEALPAEL---ARRLGDAGAEVTNMYGPTETTIWSTSG--PTSEDSIRrgsIGVPIDNTQVYVLDANLHPap 821
Cdd:cd17654 239 SLRVLaLGGEPFPSLVilsSWRGKGNRTRIFNIYGITEVSCWALAYkvPEEDSPVQ---LGSPLLGTVIEVRDQNGSE-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 822 igVLGELHIagEGLARGYwnrpgltaekFLPDPFGPPGTRMYRTGDLVRwSAAGDLEYLGRTDHQVKLRGFRIELGEIET 901
Cdd:cd17654 314 --GTGQVFL--GGLNRVC----------ILDDEVTVPKGTMRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQ 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 902 TLINAGPVrRAAAVVREDrpgDLRLVAYVI---PDGPVAPDALRTELSRT-LPDYMipaviVPVPDFPTTPNGKLDRAAL 977
Cdd:cd17654 379 VIESCLGV-ESCAVTLSD---QQRLIAFIVgesSSSRIHKELQLTLLSSHaIPDTF-----VQIDKLPLTSHGKVDKSEL 449
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
46-453 |
2.39e-55 |
|
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: 200.18 E-value: 2.39e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 46 PVPLAPGQAGIWFSEQLRPGTPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVFRLG-PDGEpvQQTAPAAPVAL 124
Cdd:cd20483 1 PRPMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGdDFGE--QQVLDDPSFHL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 125 PVIDVT-----EADLPQALRTAAEQPFDLERGPLLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLLLADLARAY----AG 195
Cdd:cd20483 79 IVIDLSeaadpEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYdalrAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 196 ELPAGVAAPA--FRDVAAWQHGRLAAGELDDQLRYWRQRLAGLPDLE--IP-GDRQRPADRDWRAHSVRRELPAATEAAV 270
Cdd:cd20483 159 RDLATVPPPPvqYIDFTLWHNALLQSPLVQPLLDFWKEKLEGIPDASklLPfAKAERPPVKDYERSTVEATLDKELLARM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 271 RRLAAAHDTTPFTVLLAAYGTFLHRLTGQDDFAVGVPVAGRGRTDLESVVGLFAGMVPVRLDLTGRPSFDEVLSRTVAGS 350
Cdd:cd20483 239 KRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 351 RNDFAHPQIPFDRLVRELRRDRIAG----SQLLVQ-AMAGTESTAvalTFGEAAGTEQPVDVALAKCDLDLSVLDDGDR- 424
Cdd:cd20483 319 LEAYEHSAVPFDYIVDALDVPRSTShfpiGQIAVNyQVHGKFPEY---DTGDFKFTDYDHYDIPTACDIALEAEEDPDGg 395
|
410 420
....*....|....*....|....*....
gi 653678460 425 LAVTLVAAADLFTPAAAEQLAGQFLSLLA 453
Cdd:cd20483 396 LDLRLEFSTTLYDSADMERFLDNFVTFLT 424
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
497-977 |
3.95e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 202.34 E-value: 3.95e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 497 FQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFP 576
Cdd:PRK06187 12 LRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 577 VERIAYLLSDARPVLVVTDAATADRLGP-----DDITGLVVLEETDTGGY--------------PATEPPAVPAGHSAYV 637
Cdd:PRK06187 92 PEEIAYILNDAEDRVVLVDSEFVPLLAAilpqlPTVRTVIVEGDGPAAPLapevgeyeellaaaSDTFDFPDIDENDAAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 638 -IYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDRVLATTTVsFDIAGLEL-YLPLRSGAGVVLADadtaR-NPAA 714
Cdd:PRK06187 172 mLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPM-FHVHAWGLpYLALMAGAKQVIPR----RfDPEN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 715 LIDLAGRHRVTLAQATPTLWQALVPELSGPA--LAGIR-VLVGGEALPAELARR-LGDAGAEVTNMYGPTETT-IWSTSG 789
Cdd:PRK06187 247 LLDLIETERVTFFFAVPTIWQMLLKAPRAYFvdFSSLRlVIYGGAALPPALLREfKEKFGIDLVQGYGMTETSpVVSVLP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 790 PTSED---SIRRGSIGVPIDNTQVYVLDANLHPAP--IGVLGELHIAGEGLARGYWNRPGLTAEKFLPDpfgppgtrMYR 864
Cdd:PRK06187 327 PEDQLpgqWTKRRSAGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPEATAETIDGG--------WLH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 865 TGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIEtTLINAGPVRRAAAV--VREDRPGDlRLVAYVI--PDGPVAPDA 940
Cdd:PRK06187 399 TGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELE-DALYGHPAVAEVAVigVPDEKWGE-RPVAVVVlkPGATLDAKE 476
|
490 500 510
....*....|....*....|....*....|....*..
gi 653678460 941 LRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:PRK06187 477 LRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
1083-1499 |
8.54e-55 |
|
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: 198.58 E-value: 8.54e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1083 LPLSPMQESIWLADQVSAGDSVYNVPLALRLIGPLDRGALRRTLNRVVDRHEMLRTRIHPGPDGMPVQVADpAGGGAALT 1162
Cdd:cd19543 2 YPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVL-KDRKLPWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1163 ERDAAPGTDLAQLLLAEA------ALGFTLATEHPLRAVLWRLDEREHVLLLTAHHVAVDAWSMDLIQRDLTELYAADTG 1236
Cdd:cd19543 81 ELDLSHLSEAEQEAELEAlaeedrERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1237 HREPELdEPALAQADYAVW-QRQSAQrgryAAElDFWRTELTGAVA-TEVAGDLPRPATPGGGGGAVEFALAPRQIQGIR 1314
Cdd:cd19543 161 GQPPSL-PPVRPYRDYIAWlQRQDKE----AAE-AYWREYLAGFEEpTPLPKELPADADGSYEPGEVSFELSAELTARLQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1315 ELARRCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGR--GNPRLDNLVGCLVNTVVLRGDLSGAPTFHELLRRTHAR 1392
Cdd:cd19543 235 ELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRpaELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1393 TADALAHQELPFehlvAD---RGAGNGPLF-RIM----YSFSSQEPAGRSAGDVDLEPVPVPVTTcKFDLVLTVVDGGsT 1464
Cdd:cd19543 315 QLELREHEYVPL----YEiqaWSEGKQALFdHLLvfenYPVDESLEEEQDEDGLRITDVSAEEQT-NYPLTVVAIPGE-E 388
|
410 420 430
....*....|....*....|....*....|....*
gi 653678460 1465 LEGVLEYADDLYLPGTAERLVTSLTNLLAAAVRTP 1499
Cdd:cd19543 389 LTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
505-977 |
2.93e-54 |
|
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: 199.52 E-value: 2.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 505 PGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLL 584
Cdd:cd05959 18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 585 SDARPVLVVTDAATADRLGP---DDITGLVVLEETDTGG----------YPATEPPAVPAGHS-----AYVIYTSGSTGR 646
Cdd:cd05959 98 EDSRARVVVVSGELAPVLAAaltKSEHTLVVLIVSGGAGpeagalllaeLVAAEAEQLKPAAThaddpAFWLYSSGSTGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 647 PKGVVITRAALdnflAAMAERFP-----LTAEDRVLATTTVSFDIA-GLELYLPLRSGAGVVLADADTArnPAALIDLAG 720
Cdd:cd05959 178 PKGVVHLHADI----YWTAELYArnvlgIREDDVCFSAAKLFFAYGlGNSLTFPLSVGATTVLMPERPT--PAAVFKRIR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 721 RHRVTLAQATPTLWQAL--VPELSGPALAGIRVLV-GGEALPAELARRLGDA-GAEVTNMYGPTETT-IWSTSGPtseDS 795
Cdd:cd05959 252 RYRPTVFFGVPTLYAAMlaAPNLPSRDLSSLRLCVsAGEALPAEVGERWKARfGLDILDGIGSTEMLhIFLSNRP---GR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 796 IRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLpdpfGPpgtrMYRTGDLVRWSAAG 875
Cdd:cd05959 329 VRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ----GE----WTRTGDKYVRDDDG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 876 DLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIP-DGPVAPDALRTELSR----TLP 950
Cdd:cd05959 401 FYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLrPGYEDSEALEEELKEfvkdRLA 480
|
490 500
....*....|....*....|....*..
gi 653678460 951 DYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:cd05959 481 PYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
1079-1492 |
5.75e-53 |
|
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: 193.85 E-value: 5.75e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1079 RDEPLPLSPMQESIWLADQVSAGDSVYNVPLALRLIGPLDRGALRRTLNRVVDRHEMLRTRIhPGPDGMPVQ-VADPAGG 1157
Cdd:cd19546 1 RPDEVPATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTF-PGDGGDVHQrILDADAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1158 GAALTERDAAPgTDLAQLLLAEAALGFTLATEHPLRAVLWRLDEREHVLLLTAHHVAVDAWSMDLIQRDLTELYAADTGH 1237
Cdd:cd19546 80 RPELPVVPATE-EELPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARREG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1238 REPELDEPALAQADYAVWQRQ-----SAQRGRYAAELDFWRTELTGAV-ATEVAGDLPRPATPGGGGGAVEFALAPRQIQ 1311
Cdd:cd19546 159 RAPERAPLPLQFADYALWEREllageDDRDSLIGDQIAYWRDALAGAPdELELPTDRPRPVLPSRRAGAVPLRLDAEVHA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1312 GIRELARRCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGR-GNPRLDNLVGCLVNTVVLRGDLSGAPTFHELLRRTH 1390
Cdd:cd19546 239 RLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDdEEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1391 ARTADALAHQELPFEHLVADRG----AGNGPLFRIMYSFSSQEPAGRSAGDV---DLEPVPVPVTTCKFDLVLTVVD--- 1460
Cdd:cd19546 319 EAVREARRHQDVPFERLAELLAlppsADRHPVFQVALDVRDDDNDPWDAPELpglRTSPVPLGTEAMELDLSLALTErrn 398
|
410 420 430
....*....|....*....|....*....|....*
gi 653678460 1461 ---GGSTLEGVLEYADDLYLPGTAERLVTSLTNLL 1492
Cdd:cd19546 399 ddgDPDGLDGSLRYAADLFDRATAAALARRLVRVL 433
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
1085-1324 |
3.17e-52 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 184.86 E-value: 3.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1085 LSPMQESIWLADQvsaGDSVYNVPLALRLIGPLDRGALRRTLNRVVDRHEMLRTRIHPGpDGMPVQVADPAGGgAALTER 1164
Cdd:COG4908 1 LSPAQKRFLFLEP---GSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEE-DGEPVQRIDPDAD-LPLEVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1165 D------AAPGTDLAQLLLAEAALGFTLATEHPLRAVLWRLDEREHVLLLTAHHVAVDAWSMDLIQRDLTELYAADTGHR 1238
Cdd:COG4908 76 DlsalpePEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1239 EPELDEPALAQADYAVWQRQSAQRGRYAAELDFWRTELTGAV-ATEVAGDLPRPATPGGGGGAVEFALAPRQIQGIRELA 1317
Cdd:COG4908 156 PPPLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPpVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALA 235
|
....*..
gi 653678460 1318 RRCGTTV 1324
Cdd:COG4908 236 KAHGATV 242
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
507-977 |
9.70e-52 |
|
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: 190.19 E-value: 9.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 507 AVAVIEGDTTLSYRELDERANRLARLLMERGAGAE-TFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLS 585
Cdd:cd05941 2 RIAIVDDGDSITYADLVARAARLANRLLALGKDLRgDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 586 DARPVLVVTDAAtadrlgpdditglvvleetdtggypateppavpaghsayVIYTSGSTGRPKGVVITRAALDNFLAAMA 665
Cdd:cd05941 82 DSEPSLVLDPAL---------------------------------------ILYTSGTTGRPKGVVLTHANLAANVRALV 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 666 ERFPLTAEDRVLATTTVsFDIAGLELYL--PLRSGAGVVLADADTARNPAALIDLAgrhRVTLAQATPTLWQALV--PEL 741
Cdd:cd05941 123 DAWRWTEDDVLLHVLPL-HHVHGLVNALlcPLFAGASVEFLPKFDPKEVAISRLMP---SITVFMGVPTIYTRLLqyYEA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 742 SGP--------ALAGIRVLVGGEA-LPAELARRLGDA-GAEVTNMYGPTETTIwSTSGPTSEDsiRR-GSIGVPIDNTQV 810
Cdd:cd05941 199 HFTdpqfaraaAAERLRLMVSGSAaLPVPTLEEWEAItGHTLLERYGMTEIGM-ALSNPLDGE--RRpGTVGMPLPGVQA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 811 YVLDAN-LHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgppgtrmYRTGDLVRWSAAGDLEYLGRT-DHQVK 888
Cdd:cd05941 276 RIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW-------FKTGDLGVVDEDGYYWILGRSsVDIIK 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 889 LRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIPDGPVAP---DALRTELSRTLPDYMIPAVIVPVPDFP 965
Cdd:cd05941 349 SGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAAlslEELKEWAKQRLAPYKRPRRLILVDELP 428
|
490
....*....|..
gi 653678460 966 TTPNGKLDRAAL 977
Cdd:cd05941 429 RNAMGKVNKKEL 440
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
1083-1499 |
2.46e-51 |
|
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: 187.51 E-value: 2.46e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1083 LPLSPMQESIwLADQVSAGDSvYNVPLALRLIGPLDRGALRRTLNRVVDRHEMLRTR-IHPGPDGMPVQVadpagggaal 1161
Cdd:cd19542 2 YPCTPMQEGM-LLSQLRSPGL-YFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVfVESSAEGTFLQV---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1162 TERDAAPG-------TDLAQLLLAEAALGFTLATEHPLRAVLWRLDEREHVLLLTAHHVAVDAWSMDLIQRDLTELYaad 1234
Cdd:cd19542 70 VLKSLDPPieevetdEDSLDALTRDLLDDPTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAY--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1235 tghrEPELDEPALAQADYAvwqrQSAQRGRYAAELDFWRTELTGAVATEVagdlprPATPGGGGGAVEFALAPRQIQGIR 1314
Cdd:cd19542 147 ----NGQLLPPAPPFSDYI----SYLQSQSQEESLQYWRKYLQGASPCAF------PSLSPKRPAERSLSSTRRSLAKLE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1315 ELARRCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGRGNPR--LDNLVGCLVNTVVLRGDLSGAPTFHELLRRTHAR 1392
Cdd:cd19542 213 AFCASLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVpgIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQ 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1393 TADALAHQELPFEHLV-ADRGAGNGPLFRIMYSF----SSQEPAGRSAGDVDLEPVPVPVTtckFDLVLTVVDGGSTLEG 1467
Cdd:cd19542 293 YLRSLPHQHLSLREIQrALGLWPSGTLFNTLVSYqnfeASPESELSGSSVFELSAAEDPTE---YPVAVEVEPSGDSLKV 369
|
410 420 430
....*....|....*....|....*....|..
gi 653678460 1468 VLEYADDLYLPGTAERLVTSLTNLLAAAVRTP 1499
Cdd:cd19542 370 SLAYSTSVLSEEQAEELLEQFDDILEALLANP 401
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
518-978 |
2.55e-51 |
|
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: 188.27 E-value: 2.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 518 SYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARPVLVVTDaa 597
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 598 tadrlgpdditglvvleetdtggypateppavpaghSAYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDrVL 677
Cdd:cd05934 83 ------------------------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDD-VY 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 678 ATTTVSFDIAGLE--LYLPLRSGAGVVLADADTARnpaALIDLAGRHRVTLAQATPTLWQALV--PELSGPALAGIRVLV 753
Cdd:cd05934 126 LTVLPLFHINAQAvsVLAALSVGATLVLLPRFSAS---RFWSDVRRYGATVTNYLGAMLSYLLaqPPSPDDRAHRLRAAY 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 754 GGEALPAELARRLGDAGAEVTNMYGPTETTIWSTSGPtsEDSIRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGE 833
Cdd:cd05934 203 GAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPR--DEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRGL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 834 ---GLARGYWNRPGLTAEKFlpdpfgPPGtrMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVR 910
Cdd:cd05934 281 rgwGFFKGYYNMPEATAEAM------RNG--WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVR 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 911 RAAAV-VREDRPGDLRLVAYVIPDG-PVAPDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAALP 978
Cdd:cd05934 353 EAAVVaVPDEVGEDEVKAVVVLRPGeTLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1685-2028 |
1.11e-50 |
|
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: 183.64 E-value: 1.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1685 LAYSIFTSGSTGQPKGVAVEHIGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMSALFEPLVSGRGVTLMP---ADATL 1761
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPkfdPEAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1762 ADLAEElsGPlayDYIRLTPSHLRHLVGHWTGQELP-PAARGWVVGGETLDPALVKQLLElRPDAEVINHYGPTETvIGR 1840
Cdd:cd04433 82 ELIERE--KV---TILLGVPTLLARLLKAPESAGYDlSSLRALVSGGAPLPPELLERFEE-APGIKLVNGYGLTET-GGT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1841 VVHPVREAGELAVDSplpLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFlpdpagEPGarM 1920
Cdd:cd04433 155 VATGPPDDDARKPGS---VGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD------EDG--W 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1921 YRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQ-AVVLVRDQQ----LVGWFIPAEDHPPvTVS 1995
Cdd:cd04433 224 YRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEaAVVGVPDPEwgerVVAVVVLRPGADL-DAE 302
|
330 340 350
....*....|....*....|....*....|...
gi 653678460 1996 ALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKV 2028
Cdd:cd04433 303 ELRAHVRERLAPYKVPRRVVFVDALPRTASGKI 335
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
495-977 |
6.25e-50 |
|
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: 187.28 E-value: 6.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 495 ERFQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAylpidpd 574
Cdd:COG1021 29 DLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 575 fPV---------ErIAYLLSDARPVLVVTDA--------ATADRL--------------GPDDITGLVVLEETDTGGypa 623
Cdd:COG1021 102 -PVfalpahrraE-ISHFAEQSEAVAYIIPDrhrgfdyrALARELqaevpslrhvlvvgDAGEFTSLDALLAAPADL--- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 624 tEPPAVPAGHSAYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDRVLATTTV-------SFDIAGlelylPLR 696
Cdd:COG1021 177 -SEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAahnfplsSPGVLG-----VLY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 697 SGAGVVLADADTARNPAALIDlagRHRVTLAQATPTLWQALV--PELSGPALAGIRVL-VGGEALPAELARRLGDA-GAE 772
Cdd:COG1021 251 AGGTVVLAPDPSPDTAFPLIE---RERVTVTALVPPLALLWLdaAERSRYDLSSLRVLqVGGAKLSPELARRVRPAlGCT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 773 VTNMYGPTETTIWSTSGPTSEDsIRRGSIGVPI-DNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFL 851
Cdd:COG1021 328 LQQVFGMAEGLVNYTRLDDPEE-VILTTQGRPIsPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFT 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 852 PDPFgppgtrmYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIEtTLINAGP-VRRAAAVVREDRpgDL--RLVA 928
Cdd:COG1021 407 PDGF-------YRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVE-NLLLAHPaVHDAAVVAMPDE--YLgeRSCA 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 653678460 929 YVIPDG-PVAPDALRTEL-SRTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:COG1021 477 FVVPRGePLTLAELRRFLrERGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
507-977 |
1.75e-49 |
|
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: 184.82 E-value: 1.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 507 AVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSD 586
Cdd:cd05926 5 ALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 587 ARPVLVVTDA--------------ATADRLGPDDITGLVVLEETDTGGYPATEPPAVPAGHS-----AYVIYTSGSTGRP 647
Cdd:cd05926 85 LGSKLVLTPKgelgpasraasklgLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGVPlpddlALILHTSGTTGRP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 648 KGVVITRAaldNFLAAM---AERFPLTAEDRVLATTTVsFDIAGL--ELYLPLRSGAGVVLADADTArnpAALIDLAGRH 722
Cdd:cd05926 165 KGVPLTHR---NLAASAtniTNTYKLTPDDRTLVVMPL-FHVHGLvaSLLSTLAAGGSVVLPPRFSA---STFWPDVRDY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 723 RVTLAQATPTLWQALV---PELSGPALAGIRVL-VGGEALPAELARRLGDA-GAEVTNMYGPTETTIWSTSGPTSEDSIR 797
Cdd:cd05926 238 NATWYTAVPTIHQILLnrpEPNPESPPPKLRFIrSCSASLPPAVLEALEATfGAPVLEAYGMTEAAHQMTSNPLPPGPRK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 798 RGSIGVPiDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgppgtrmYRTGDLVRWSAAGDL 877
Cdd:cd05926 318 PGSVGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW-------FRTGDLGYLDADGYL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 878 EYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAV-VREDRPGDLrLVAYVIPDG--PVAPDALRTELSRTLPDYMI 954
Cdd:cd05926 390 FLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFgVPDEKYGEE-VAAAVVLREgaSVTEEELRAFCRKHLAAFKV 468
|
490 500
....*....|....*....|...
gi 653678460 955 PAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:cd05926 469 PKKVYFVDELPKTATGKIQRRKV 491
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
1555-2036 |
1.89e-48 |
|
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: 182.72 E-value: 1.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1555 RSLTFAGLDAQANRLAHALHTGALGAPPVgpetpVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMARLTRIADTVTP 1634
Cdd:cd17647 19 RSFTYRDINEASNIVAHYLIKTGIKRGDV-----VMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1635 -ALVLTRtgQGGCLPGaevfgdvpvvaldrvadrltamPDQRPEVTvdprglaysiFTSGSTGQPKGVAVEHIGIVRYLS 1713
Cdd:cd17647 94 rGLIVIR--AAGVVVG----------------------PDSNPTLS----------FTSGSEGIPKGVLGRHFSLAYYFP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1714 WAAASYPTAGRRGTLAHSSVGFDLTMSALFEPLVSGRGVTLMPAD-----ATLADLAEELSGPLAYdyirLTPSHLRHLV 1788
Cdd:cd17647 140 WMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDdigtpGRLAEWMAKYGATVTH----LTPAMGQLLT 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1789 GHWTGQeLPPAARGWVVGgETLDPALVKQLLELRPDAEVINHYGPTET--VIGRVVHPVREAGELAVDS---PLPLGRPL 1863
Cdd:cd17647 216 AQATTP-FPKLHHAFFVG-DILTKRDCLRLQTLAENVRIVNMYGTTETqrAVSYFEVPSRSSDPTFLKNlkdVMPAGRGM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1864 GETRLQVLDAW--LEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLP------------DPAGE---------PGARM 1920
Cdd:cd17647 294 LNVQLLVVNRNdrTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNnwfvepdhwnylDKDNNepwrqfwlgPRDRL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1921 YRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRDQQ-----LVGWFIPAEDHPPVTVS 1995
Cdd:cd17647 374 YRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKdeeptLVSYIVPRFDKPDDESF 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 653678460 1996 A--------------------------LRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRALPGP 2036
Cdd:cd17647 454 AqedvpkevstdpivkgligyrklikdIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
516-972 |
2.03e-48 |
|
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: 180.27 E-value: 2.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 516 TLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARP-VLVVT 594
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAkVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 595 daataDRLGPDDitglvvleetdtggyPATEPPAVpaghsAYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAED 674
Cdd:cd05903 81 -----ERFRQFD---------------PAAMPDAV-----ALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 675 RVLATTTVSFDIAGLE-LYLPLRSGAGVVLADADTARNPAALIDlagRHRVTLAQATPTLWQAL--VPELSGPALAGIR- 750
Cdd:cd05903 136 VFLVASPMAHQTGFVYgFTLPLLLGAPVVLQDIWDPDKALALMR---EHGVTFMMGATPFLTDLlnAVEEAGEPLSRLRt 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 751 VLVGGEALPAELARRLGDA-GAEVTNMYGPTETTIWSTSGPTSEDSIRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELH 829
Cdd:cd05903 213 FVCGGATVPRSLARRAAELlGAKVCSAYGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 830 IAGEGLARGYWNRPGLTAEkFLPDPFgppgtrmYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPV 909
Cdd:cd05903 293 SRGPSVFLGYLDRPDLTAD-AAPEGW-------FRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGV 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 653678460 910 RRAAAVVREDRPGDLRLVAYVIPDGPVAP--DALRTELSRT-LPDYMIPAVIVPVPDFPTTPNGKL 972
Cdd:cd05903 365 IEAAVVALPDERLGERACAVVVTKSGALLtfDELVAYLDRQgVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
48-459 |
7.82e-48 |
|
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: 177.50 E-value: 7.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 48 PLAPGQAGIwFSEQLRPGtPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVF-RLGPDGEPVQQTAPAAPVALPV 126
Cdd:cd19542 3 PCTPMQEGM-LLSQLRSP-GLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFvESSAEGTFLQVVLKSLDPPIEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 127 IDVTEADLPQALRTAAEQPFDLERgPLLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLLLADLARAYAGELPAgvAAPAF 206
Cdd:cd19542 81 VETDEDSLDALTRDLLDDPTLFGQ-PPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLP--PAPPF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 207 RDVAAwqhgRLAAGELDDQLRYWRQRLAGLPDLEIPG-DRQRPADRdwRAHSVRRELpaateAAVRRLAAAHDTTPFTVL 285
Cdd:cd19542 158 SDYIS----YLQSQSQEESLQYWRKYLQGASPCAFPSlSPKRPAER--SLSSTRRSL-----AKLEAFCASLGVTLASLF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 286 LAAYGTFLHRLTGQDDFAVGVPVAGRG--RTDLESVVGLFAGMVPVRLDLTGRPSFDEVLSRTVAGSRNDFAHPQIPFDR 363
Cdd:cd19542 227 QAAWALVLARYTGSRDVVFGYVVSGRDlpVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLRE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 364 LVRELRRDRIA---GSQLLVQAMAGTESTAVALTFGEAAGTEQ-PVDVALAkcdldLSVLDDGDRLAVTLVAAADLFTPA 439
Cdd:cd19542 307 IQRALGLWPSGtlfNTLVSYQNFEASPESELSGSSVFELSAAEdPTEYPVA-----VEVEPSGDSLKVSLAYSTSVLSEE 381
|
410 420
....*....|....*....|
gi 653678460 440 AAEQLAGQFLSLLAGLTGAP 459
Cdd:cd19542 382 QAEELLEQFDDILEALLANP 401
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
509-980 |
1.41e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 178.64 E-value: 1.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 509 AVIEGDTTLSYRELDERANRLArllmERGAGAETfVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDAR 588
Cdd:PRK07787 18 AVRIGGRVLSRSDLAGAATAVA----ERVAGARR-VAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 589 PVLVVTDAatadrlgPDDITGLVVlEETDTGGYPATEPPAVPAGHSAYVIYTSGSTGRPKGVVITRAALDNFLAAMAERF 668
Cdd:PRK07787 93 AQAWLGPA-------PDDPAGLPH-VPVRLHARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 669 PLTAEDrVLATTTVSFDIAGLELYL--PLRSGAGVVLADADTARNPAALIDLAGrhrvTLAQATPTLWQALV--PELSGp 744
Cdd:PRK07787 165 QWTADD-VLVHGLPLFHVHGLVLGVlgPLRIGNRFVHTGRPTPEAYAQALSEGG----TLYFGVPTVWSRIAadPEAAR- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 745 ALAGIRVLVGGEA-LPAELARRLGDA-GAEVTNMYGPTETTIwSTSgpTSEDSIRR-GSIGVPIDNTQVYVLDANLHPAP 821
Cdd:PRK07787 239 ALRGARLLVSGSAaLPVPVFDRLAALtGHRPVERYGMTETLI-TLS--TRADGERRpGWVGLPLAGVETRLVDEDGGPVP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 822 IGV--LGELHIAGEGLARGYWNRPGLTAEKFLPDPFgppgtrmYRTGDLVRWSAAGDLEYLGR--TDhQVKLRGFRIELG 897
Cdd:PRK07787 316 HDGetVGELQVRGPTLFDGYLNRPDATAAAFTADGW-------FRTGDVAVVDPDGMHRIVGResTD-LIKSGGYRIGAG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 898 EIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIPDGPVAPDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:PRK07787 388 EIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQL 467
|
...
gi 653678460 978 PAP 980
Cdd:PRK07787 468 LSE 470
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
502-977 |
7.15e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 177.79 E-value: 7.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 502 RRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIA 581
Cdd:PRK07656 16 RRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 582 YLL--SDARPVLVVTDAATADRLGPDDITGL--VVLEETDTG----------------GYPATEPPAVPAGHSAYVIYTS 641
Cdd:PRK07656 96 YILarGDAKALFVLGLFLGVDYSATTRLPALehVVICETEEDdphtekmktftdflaaGDPAERAPEVDPDDVADILFTS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 642 GSTGRPKGVVIT-RAALDNFlAAMAERFPLTAEDRVLATTTVsFDIAGLELYL--PLRSGAGVVLAdadTARNPAALIDL 718
Cdd:PRK07656 176 GTTGRPKGAMLThRQLLSNA-ADWAEYLGLTEGDRYLAANPF-FHVFGYKAGVnaPLMRGATILPL---PVFDPDEVFRL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 719 AGRHRVTLAQATPTLWQAL--VPELSGPALAGIRVLV-GGEALPAELARRLGDA-GAE-VTNMYGPTETTIWSTSGPTSE 793
Cdd:PRK07656 251 IETERITVLPGPPTMYNSLlqHPDRSAEDLSSLRLAVtGAASMPVALLERFESElGVDiVLTGYGLSEASGVTTFNRLDD 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 794 D-SIRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgppgtrmYRTGDLVRWS 872
Cdd:PRK07656 331 DrKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGW-------LHTGDLGRLD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 873 AAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAV-VREDRPGDLrLVAYVI--PDGPVAPDALRTELSRTL 949
Cdd:PRK07656 404 EEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIgVPDERLGEV-GKAYVVlkPGAELTEEELIAYCREHL 482
|
490 500
....*....|....*....|....*...
gi 653678460 950 PDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:PRK07656 483 AKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
492-977 |
5.96e-46 |
|
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: 174.44 E-value: 5.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 492 SLRERFQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPI 571
Cdd:cd05920 16 PLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 572 DPDFPVERIAYLLSDARPVLVVTDaataDRLGPDDITGLVVLEetdtggypATEPPAVpaghsAYVIYTSGSTGRPKGVV 651
Cdd:cd05920 96 LPSHRRSELSAFCAHAEAVAYIVP----DRHAGFDHRALAREL--------AESIPEV-----ALFLLSGGTTGTPKLIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 652 ITRAALDNFLAAMAERFPLTAEDRVLATTTVS--FDIAGLELYLPLRSGAGVVLADADTARNPAALIDlagRHRVTLAQA 729
Cdd:cd05920 159 RTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAhnFPLACPGVLGTLLAGGRVVLAPDPSPDAAFPLIE---REGVTVTAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 730 TPTLWQALVPEL--SGPALAGIRVL-VGGEALPAELARRLGDA-GAEVTNMYGPTETTIWSTSGPTSEDSIrRGSIGVPI 805
Cdd:cd05920 236 VPALVSLWLDAAasRRADLSSLRLLqVGGARLSPALARRVPPVlGCTLQQVFGMAEGLLNYTRLDDPDEVI-IHTQGRPM 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 806 D-NTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgppgtrmYRTGDLVRWSAAGDLEYLGRTD 884
Cdd:cd05920 315 SpDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF-------YRTGDLVRRTPDGYLVVEGRIK 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 885 HQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIPDGPvAPDA--LRTEL-SRTLPDYMIPAVIVPV 961
Cdd:cd05920 388 DQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDP-PPSAaqLRRFLrERGLAAYKLPDRIEFV 466
|
490
....*....|....*.
gi 653678460 962 PDFPTTPNGKLDRAAL 977
Cdd:cd05920 467 DSLPLTAVGKIDKKAL 482
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
1539-2424 |
9.57e-46 |
|
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: 180.28 E-value: 9.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1539 AQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHTGALGAPPVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDP 1618
Cdd:COG3319 1 AAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1619 GYPMARLTRIADTVTPALVLTRTGQGGCLPGAEVFGDVPVVALDRVADRLTAMPDQRPEVTVDPRGLAYSIFTSGSTGQP 1698
Cdd:COG3319 81 LAALALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1699 KGVAVEHIGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMSALFEPLVSGRGVTLMPADATLADLAEELSGPLAYDYIR 1778
Cdd:COG3319 161 AGVLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1779 LTPSHLRHLVGHWTGQELPPAARGWVVGGETLDPALVkqLLELRPDAEVINHYGPTETVIGRVVHPVREAGELAVDSPLP 1858
Cdd:COG3319 241 LLLLAALLLLLALALLLLLALLLLLGLLALLLALLLL--LALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1859 LGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPAGEPGARMYRTGDLVRWRGDGLLDFV 1938
Cdd:COG3319 319 GGGPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1939 GRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRDQQLVGWFIPAEDHPPVTVSALRRFCAEQLPEFMVPNQWVALD 2018
Cdd:COG3319 399 GRLRLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 2019 AFPLTPHGKVNHRALPGPTSGRPELEDRYQAPRTPGEQLLAELWSTVLGTDRIGIEDNFFDLGGTSISVIQLSGACRRAG 2098
Cdd:COG3319 479 LLLLLLLLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALL 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 2099 VEISPKDVFEQPTVRGQAMRAIARSRDDAYAPVLdtvfgaghtgttrtvVTLRGEGDGRPVFCVHPSGGGVAWYLPLARA 2178
Cdd:COG3319 559 LRLLLLLALLLAPTLAALAAALAAAAAAAALSPL---------------VPLRAGGSGPPLFCVHPAGGNVLCYRPLARA 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 2179 LPAGHPVHAFQPLGMDGREAPAETIEDMAAGYLADLRLVQPEGPYVVVGWSLGGTIAFEMARQLDRLGEPV-QLILLEPT 2257
Cdd:COG3319 624 LGPDRPVYGLQAPGLDGGEPPPASVEEMAARYVEAIRAVQPEGPYHLLGWSFGGLVAYEMARQLEAQGEEVaLLVLLDSY 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 2258 LPEVARTIDLHRPAR---DSYLRGADLAERILRLPAGDPEgdRLRAELTRLLEDAGYSAGEISLGDALPMRACGQMLAAF 2334
Cdd:COG3319 704 APGALARLDEAELLAallRDLARGVDLPLDAEELRALDPE--ERLARLLERLREAGLPAGLDAERLRRLLRVFRANLRAL 781
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 2335 AEYRPLPLPdeskVRTQFVVSAECTDATPERPsgtshtaygsyAAGWQKLLgrAAAPRTIHLPGIHATMLTTDRCPTVVS 2414
Cdd:COG3319 782 RRYRPRPYD----GPVLLFRAEEDPPGRADDP-----------ALGWRPLV--AGGLEVHDVPGDHFSMLREPHVAELAA 844
|
890
....*....|
gi 653678460 2415 ACVEALRTTD 2424
Cdd:COG3319 845 ALRAALAAAE 854
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
48-459 |
1.30e-45 |
|
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: 171.48 E-value: 1.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 48 PLAPGQAGIWFSEQLRPGTPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVFRLGPDGEPVQQTAPAAPVALPVI 127
Cdd:cd19536 3 PLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQAQVPVTEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 128 DVT---EADLPQALRTAAEQ--PFDLERGPLLRACLHRIGAKQHVLLV-TVHHIVLDGWSCGLLLADLARAYAGeLPAGV 201
Cdd:cd19536 83 DLTpleEQLDPLRAYKEETKirRFDLGRAPLVRAALVRKDERERFLLViSDHHSILDGWSLYLLVKEILAVYNQ-LLEYK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 202 A-----APAFRDVAAWqhgRLAAGELDDQLRYWRQRLAG--LPDLEIPGD-RQRPADRDWrahSVRRELPAAteAAVRRL 273
Cdd:cd19536 162 PlslppAQPYRDFVAH---ERASIQQAASERYWREYLAGatLATLPALSEaVGGGPEQDS---ELLVSVPLP--VRSRSL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 274 AAAHDTTPFTVLLAAYGTFLHRLTGQDDFAVGVPVAGR--GRTDLESVVGLFAGMVPVRLDLTGRpSFDEVLSRTVAGSR 351
Cdd:cd19536 234 AKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRseETTGAERLLGLFLNTLPLRVTLSEE-TVEDLLKRAQEQEL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 352 NDFAHPQIPfdrlVRELRRDriAGSQLLVQAMAGTESTAVALTFGEAAGTEQPVDVAL-----AKCDLDLSVLDDGDRLA 426
Cdd:cd19536 313 ESLSHEQVP----LADIQRC--SEGEPLFDSIVNFRHFDLDFGLPEWGSDEGMRRGLLfsefkSNYDVNLSVLPKQDRLE 386
|
410 420 430
....*....|....*....|....*....|...
gi 653678460 427 VTLVAAADLFTPAAAEQLAGQFLSLLAGLTGAP 459
Cdd:cd19536 387 LKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
1594-2033 |
1.33e-44 |
|
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: 169.57 E-value: 1.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1594 DRSPELVVAMLAVLKAGGYFIPVDPGYPMARLTRIADTvtpalvltrtgqggclpgAEVFGDVpvvaldrVADRLTAMPD 1673
Cdd:cd17654 49 DRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKK------------------CHVSYLL-------QNKELDNAPL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1674 QRPEVTVD-----PRGLAYSIFTSGSTGQPKGVAVEHIGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMSALFEPLVS 1748
Cdd:cd17654 104 SFTPEHRHfnirtDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1749 G-------RGVTLMPAdaTLADLAEELSGPlayDYIRLTPSHLRHLVGHWTGQELPPAA---RGWVVGGE-----TLDPA 1813
Cdd:cd17654 184 GatllivpTSVKVLPS--KLADILFKRHRI---TVLQATPTLFRRFGSQSIKSTVLSATsslRVLALGGEpfpslVILSS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1814 LVKQLLELRpdaeVINHYGPTETVIGRVVHPVREAgelavDSPLPLGRPLGETRLQVLDAWLEAVPvgavGELFIGGdgI 1893
Cdd:cd17654 259 WRGKGNRTR----IFNIYGITEVSCWALAYKVPEE-----DSPVQLGSPLLGTVIEVRDQNGSEGT----GQVFLGG--L 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1894 ARGYlgrpaltaekFLPDPAGEPGARMYRTGDLVRwRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVL 1973
Cdd:cd17654 324 NRVC----------ILDDEVTVPKGTMRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVT 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1974 VRDQQLVGWFIPAEDHPPVTVSALRRFcaeQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:cd17654 393 LSDQQRLIAFIVGESSSSRIHKELQLT---LLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1082-1497 |
4.11e-44 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380471 [Multi-domain] Cd Length: 430 Bit Score: 167.44 E-value: 4.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1082 PLPLSPMQESIWLADQVSAGDSVYNVPLALRLIGPLDRGALRRTLNRVVDRHEMLRTRIHPGPDGMPVQVADPAGggAAL 1161
Cdd:cd20483 1 PRPMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPS--FHL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1162 TERDAAPGTDLAQLLLAEAalgfTLATEHPL--------RAVLWRLDEREHVLLLTAHHVAVDAWSMDLIQRDLTELYAA 1233
Cdd:cd20483 79 IVIDLSEAADPEAALDQLV----RNLRRQELdieegeviRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1234 DTGHREP-ELDEPALAQADYAVWQRQSAQRGRYAAELDFWRTELTGAvaTEVAGDLP-----RPATPGGGGGAVEFALAP 1307
Cdd:cd20483 155 LRAGRDLaTVPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEGI--PDASKLLPfakaeRPPVKDYERSTVEATLDK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1308 RQIQGIRELARRCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGRGNPRLDNLVGCLVNTVVLRGDLSGAPTFHELLR 1387
Cdd:cd20483 233 ELLARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1388 RTHARTADALAHQELPFEHLV----ADRGAGNGPLFRIMYSFSSQEPAGRSAG------DVDLEPVPvpvTTCKFDL-VL 1456
Cdd:cd20483 313 STKTTCLEAYEHSAVPFDYIVdaldVPRSTSHFPIGQIAVNYQVHGKFPEYDTgdfkftDYDHYDIP---TACDIALeAE 389
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 653678460 1457 TVVDGGstLEGVLEYADDLYLPGTAERLVTSLTNLLAAAVR 1497
Cdd:cd20483 390 EDPDGG--LDLRLEFSTTLYDSADMERFLDNFVTFLTSVIR 428
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
517-977 |
1.26e-43 |
|
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: 165.97 E-value: 1.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 517 LSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARPVLVVTDA 596
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 597 atadrlgpDDItglvvleetdtggypateppavpaghsAYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDRV 676
Cdd:cd05972 81 --------EDP---------------------------ALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIH 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 677 LAT------TTVSFDIAGlelylPLRSGAGVVLADAD--TARNpaaLIDLAGRHRVTLAQATPTLWQALV-PELSGPALA 747
Cdd:cd05972 126 WNIadpgwaKGAWSSFFG-----PWLLGATVFVYEGPrfDAER---ILELLERYGVTSFCGPPTAYRMLIkQDLSSYKFS 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 748 GIRVLV-GGEALPAELARRLGDA-GAEVTNMYGPTETTIwsTSGPTSEDSIRRGSIGVPIDNTQVYVLDANLHPAPIGVL 825
Cdd:cd05972 198 HLRLVVsAGEPLNPEVIEWWRAAtGLPIRDGYGQTETGL--TVGNFPDMPVKPGSMGRPTPGYDVAIIDDDGRELPPGEE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 826 GEL--HIAGEGLARGYWNRPGLTAEKFLPDpfgppgtrMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTL 903
Cdd:cd05972 276 GDIaiKLPPPGLFLGYVGDPEKTEASIRGD--------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESAL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 904 INAGPVRRAAAVVREDrPGDLRLV-AYVI-PDGPVAPDALRTEL-----SRTLPdYMIPAVIVPVPDFPTTPNGKLDRAA 976
Cdd:cd05972 348 LEHPAVAEAAVVGSPD-PVRGEVVkAFVVlTSGYEPSEELAEELqghvkKVLAP-YKYPREIEFVEELPKTISGKIRRVE 425
|
.
gi 653678460 977 L 977
Cdd:cd05972 426 L 426
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
635-977 |
1.34e-43 |
|
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: 162.89 E-value: 1.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 635 AYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDRVLATTTVsFDIAGLE-LYLPLRSGAGVVLADadtaRNPA 713
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPL-YHVGGLAiLVRSLLAGAELVLLE----RNQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 714 ALIDLAgRHRVTLAQATPT-LWQALVPELSGPALAGIR-VLVGGEALPAELARRLGDAGAEVTNMYGPTETTiwSTSGPT 791
Cdd:cd17630 78 LAEDLA-PPGVTHVSLVPTqLQRLLDSGQGPAALKSLRaVLLGGAPIPPELLERAADRGIPLYTTYGMTETA--SQVATK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 792 SEDSIRRGSIGVPIDNTQVYVLDAnlhpapigvlGELHIAGEGLARGYWNRPgltaekfLPDPFGPPGTrmYRTGDLVRW 871
Cdd:cd17630 155 RPDGFGRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQ-------LVPEFNEDGW--FTTKDLGEL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 872 SAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIPDGPVAPDALRTELSRTLPD 951
Cdd:cd17630 216 HADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADPAELRAWLKDKLAR 295
|
330 340
....*....|....*....|....*.
gi 653678460 952 YMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:cd17630 296 FKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
510-974 |
5.76e-43 |
|
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: 164.92 E-value: 5.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 510 VIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARP 589
Cdd:cd05914 1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 590 VLV-VTDaatadrlgPDDItglvvleetdtggypateppavpaghsAYVIYTSGSTGRPKGVVITRAALDNFLAAMAERF 668
Cdd:cd05914 81 KAIfVSD--------EDDV---------------------------ALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 669 PLTAEDRVLATTTVSfDIAGL--ELYLPLRSGAGVVLADadtaRNPAALIDLAGRHRVTLAQATPTLWQ-------ALVP 739
Cdd:cd05914 126 LLGKGDKILSILPLH-HIYPLtfTLLLPLLNGAHVVFLD----KIPSAKIIALAFAQVTPTLGVPVPLViekifkmDIIP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 740 ELSGP-------------------------ALAG-IRVLV-GGEALPAELARRLGDAGAEVTNMYGPTETT-IWSTSGPt 791
Cdd:cd05914 201 KLTLKkfkfklakkinnrkirklafkkvheAFGGnIKEFViGGAKINPDVEEFLRTIGFPYTIGYGMTETApIISYSPP- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 792 seDSIRRGSIGVPIDNTQVYVLDanlhPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgppgtrmYRTGDLVRW 871
Cdd:cd05914 280 --NRIRLGSAGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW-------FHTGDLGKI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 872 SAAGDLEYLGRTDHQVKL-RGFRIELGEIETTLINAGPVRRAAAVVREDRpgdLRLVAYVIPDGPVAP------------ 938
Cdd:cd05914 347 DAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESLVVVQEKK---LVALAYIDPDFLDVKalkqrniidaik 423
|
490 500 510
....*....|....*....|....*....|....*..
gi 653678460 939 DALRTELSRTLPDY-MIPAVIVPVPDFPTTPNGKLDR 974
Cdd:cd05914 424 WEVRDKVNQKVPNYkKISKVKIVKEEFEKTPKGKIKR 460
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1532-2033 |
1.21e-42 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 166.44 E-value: 1.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1532 TVHQLVEAQADRTPGWTALR----TGD-RSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAV 1606
Cdd:COG0365 10 IAYNCLDRHAEGRGDKVALIwegeDGEeRTLTYAELRREVNRFANALR--ALG---VKKGDRVAIYLPNIPEAVIAMLAC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1607 LKAGGYFIPVDPGY-PMARLTRIADTvTPALVLTRTGQ---GGCLPGAEVFGDVP--------VVALDRV---------- 1664
Cdd:COG0365 85 ARIGAVHSPVFPGFgAEALADRIEDA-EAKVLITADGGlrgGKVIDLKEKVDEALeelpslehVIVVGRTgadvpmegdl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1665 --ADRLTAMPDQRPEVTVDPRGLAYSIFTSGSTGQPKGV-------AVEHIGIVRY---------------LSWA-AASY 1719
Cdd:COG0365 164 dwDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVvhthggyLVHAATTAKYvldlkpgdvfwctadIGWAtGHSY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1720 PTAGrrgTLAH--SSVGFD-----LTMSALFEpLVSGRGVTLMPADATL--ADLAEELSGPLAYDyirltPSHLRHLVGh 1790
Cdd:COG0365 244 IVYG---PLLNgaTVVLYEgrpdfPDPGRLWE-LIEKYGVTVFFTAPTAirALMKAGDEPLKKYD-----LSSLRLLGS- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1791 wTGQELPPAARGWV---VGgetldpalvkqllelrpdAEVINHYGPTET----VIGRVVHPVReAGELavdsplplGRPL 1863
Cdd:COG0365 314 -AGEPLNPEVWEWWyeaVG------------------VPIVDGWGQTETggifISNLPGLPVK-PGSM--------GKPV 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1864 GETRLQVLDAWLEAVPVGAVGELFIGGD--GIARGYLGRPALTAEKFLPDPAGepgarMYRTGDLVRWRGDGLLDFVGRV 1941
Cdd:COG0365 366 PGYDVAVVDEDGNPVPPGEEGELVIKGPwpGMFRGYWNDPERYRETYFGRFPG-----WYRTGDGARRDEDGYFWILGRS 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1942 DDQVKLRGYRIELGEIEARMAEHPGV-EQAVV----LVRDQQLVGWFIPAEDHPP--VTVSALRRFCAEQLPEFMVPNQW 2014
Cdd:COG0365 441 DDVINVSGHRIGTAEIESALVSHPAVaEAAVVgvpdEIRGQVVKAFVVLKPGVEPsdELAKELQAHVREELGPYAYPREI 520
|
570
....*....|....*....
gi 653678460 2015 VALDAFPLTPHGKVNHRAL 2033
Cdd:COG0365 521 EFVDELPKTRSGKIMRRLL 539
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
506-977 |
3.87e-42 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 163.47 E-value: 3.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 506 GAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLS 585
Cdd:TIGR02262 20 GKTAFIDDISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 586 DARP-VLVVTDA---ATADRLG--PDDITGLVV---------LEETDTGGYPATEPPAVPAGHSAYVIYTSGSTGRPKGV 650
Cdd:TIGR02262 100 DSRArVVFVSGAllpVIKAALGksPHLEHRVVVgrpeagevqLAELLATESEQFKPAATQADDPAFWLYSSGSTGMPKGV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 651 VITRAALDNFLAAMAERFPLTAEDRVLATTTVSFDIAGL--ELYLPLRSGAGVVL-ADADTarnPAALIDLAGRHRVTLA 727
Cdd:TIGR02262 180 VHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFAYGLgnALTFPMSVGATTVLmGERPT---PDAVFDRLRRHQPTIF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 728 QATPTLWQALVPELSGPALAGIRVLV---GGEALPAELARRLGDA-GAEVTNMYGPTETT-IWSTSGPtseDSIRRGSIG 802
Cdd:TIGR02262 257 YGVPTLYAAMLADPNLPSEDQVRLRLctsAGEALPAEVGQRWQARfGVDIVDGIGSTEMLhIFLSNLP---GDVRYGTSG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 803 VPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLpdpfGPpgtrMYRTGDLVRWSAAGDLEYLGR 882
Cdd:TIGR02262 334 KPVPGYRLRLVGDGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTFQ----GE----WTRSGDKYVRNDDGSYTYAGR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 883 TDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVI--PDGPVAPDALRTELSRTLPDYMIPAVIVP 960
Cdd:TIGR02262 406 TDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVlrPGQTALETELKEHVKDRLAPYKYPRWIVF 485
|
490
....*....|....*..
gi 653678460 961 VPDFPTTPNGKLDRAAL 977
Cdd:TIGR02262 486 VDDLPKTATGKIQRFKL 502
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
518-977 |
1.89e-39 |
|
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: 154.13 E-value: 1.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 518 SYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARPVLVVTDaa 597
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTD-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 598 tadrlGPDDitglvvleetdtggypateppavpaghSAYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDRVL 677
Cdd:cd05971 86 -----GSDD---------------------------PALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGDL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 678 ATTTVSFD-IAGL-ELYLPLRSGAGVVLADADTARNPAALIDLAGRHRVTLAQATPT---LWQALVPELSGPALAGIRVL 752
Cdd:cd05971 134 YWTPADWAwIGGLlDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTalkMMRQQGEQLKHAQVKLRAIA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 753 VGGEALPAELARRLGDA-GAEVTNMYGPTETTIWSTSGPtSEDSIRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELhia 831
Cdd:cd05971 214 TGGESLGEELLGWAREQfGVEVNEFYGQTECNLVIGNCS-ALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEI--- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 832 geGLAR-------GYWNRPGLTAEKFLPDPFgppgtrmyRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLI 904
Cdd:cd05971 290 --AVELpdpvaflGYWNNPSATEKKMAGDWL--------LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLL 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 653678460 905 NAGPVRRAAAVVREDRPGDLRLVAYVI-PDGPVAPDALRTEL----SRTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:cd05971 360 KHPAVLMAAVVGIPDPIRGEIVKAFVVlNPGETPSDALAREIqelvKTRLAAHEYPREIEFVNELPRTATGKIRRREL 437
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
512-972 |
1.89e-39 |
|
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: 155.06 E-value: 1.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 512 EGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARPVL 591
Cdd:cd05911 6 DTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 592 VVTDA-------ATADRLGPDD----ITGLV--------VLEETDTGGYPA-TEPPAVPAGHSAYVIYTSGSTGRPKGVV 651
Cdd:cd05911 86 IFTDPdglekvkEAAKELGPKDkiivLDDKPdgvlsiedLLSPTLGEEDEDlPPPLKDGKDDTAAILYSSGTTGLPKGVC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 652 ITRAAL--DNFLAAMAERFPLTAEDRVLATTTVsFDIAGLE--LYLPLRSGAGVVLADADtarnPAALIDLAGRHRVTLA 727
Cdd:cd05911 166 LSHRNLiaNLSQVQTFLYGNDGSNDVILGFLPL-YHIYGLFttLASLLNGATVIIMPKFD----SELFLDLIEKYKITFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 728 QATPTLWQALV--PELSGPALAGIR-VLVGGEALPAELARRLG--DAGAEVTNMYGPTETTiwSTSGPTSEDSIRRGSIG 802
Cdd:cd05911 241 YLVPPIAAALAksPLLDKYDLSSLRvILSGGAPLSKELQELLAkrFPNATIKQGYGMTETG--GILTVNPDGDDKPGSVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 803 VPIDNTQVYVLDANLHPA-PIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgppgtrmYRTGDLVRWSAAGDLEYLG 881
Cdd:cd05911 319 RLLPNVEAKIVDDDGKDSlGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW-------LHTGDIGYFDEDGYLYIVD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 882 RTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIPdgpvAPDALRTELSrtLPDYMIPAV---- 957
Cdd:cd05911 392 RKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVR----KPGEKLTEKE--VKDYVAKKVasyk 465
|
490 500
....*....|....*....|
gi 653678460 958 -----IVPVPDFPTTPNGKL 972
Cdd:cd05911 466 qlrggVVFVDEIPKSASGKI 485
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1084-1499 |
2.14e-39 |
|
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: 153.63 E-value: 2.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1084 PLSPMQESIWLADQVSAGDSVYNVPLALRLIGPLDRGALRRTLNRVVDRHEMLRTRIHPgPDGMPVQVADPAGGgAALTE 1163
Cdd:cd20484 3 PLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEE-EDGVPFQKIEPSKP-LSFQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1164 RD--AAPGTDLAQLLLAEAALGFTLAtEHPL-RAVLWRLDEREHVLLLTAHHVAVDAWSMDLIQRDLTELYAADTGHREP 1240
Cdd:cd20484 81 EDisSLKESEIIAYLREKAKEPFVLE-NGPLmRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1241 ELDEPALAQADYAVWQRQ--SAQRGryAAELDFWRTELTGAVAT-EVAGDLPRPATPGGGGGAVEFALAPRQIQGIRELA 1317
Cdd:cd20484 160 TLASSPASYYDFVAWEQDmlAGAEG--EEHRAYWKQQLSGTLPIlELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1318 RRCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGRGNPRLDNLVGCLVNTVVLRGDLSGAPTFHELLRRTHARTADAL 1397
Cdd:cd20484 238 RSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1398 AHQELPFEHLVAD----RGAGNGPLFRIMYSF-------SSQEPAGRSAGDVDLEPVPVPVTTCKFDLVLTVVDGGSTLE 1466
Cdd:cd20484 318 DHAAYPFPAMVRDlnipRSQANSPVFQVAFFYqnflqstSLQQFLAEYQDVLSIEFVEGIHQEGEYELVLEVYEQEDRFT 397
|
410 420 430
....*....|....*....|....*....|...
gi 653678460 1467 GVLEYADDLYLPGTAERLVTSLTNLLAAAVRTP 1499
Cdd:cd20484 398 LNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
505-931 |
4.62e-39 |
|
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: 154.31 E-value: 4.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 505 PGAVAVIEGDT--TLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAY 582
Cdd:cd05904 19 PSRPALIDAATgrALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 583 LLSDARPVLVVTDAATADRLgPDDITGLVVLEETDTGG---------YPATEPPAVPAGHS--AYVIYTSGSTGRPKGVV 651
Cdd:cd05904 99 QVKDSGAKLAFTTAELAEKL-ASLALPVVLLDSAEFDSlsfsdllfeADEAEPPVVVIKQDdvAALLYSSGTTGRSKGVM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 652 ITRAaldNFLAAMA-----ERFPLTAEDRVLATTTVsFDIAGLELYL--PLRSGAG-VVLADADTarnpAALIDLAGRHR 723
Cdd:cd05904 178 LTHR---NLIAMVAqfvagEGSNSDSEDVFLCVLPM-FHIYGLSSFAlgLLRLGATvVVMPRFDL----EELLAAIERYK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 724 VTLAQATPTLWQALV--PELSGPALAGIR-VLVGGEALPAELARRLGDA--GAEVTNMYGPTETTIWSTSGPTSE-DSIR 797
Cdd:cd05904 250 VTHLPVVPPIVLALVksPIVDKYDLSSLRqIMSGAAPLGKELIEAFRAKfpNVDLGQGYGMTESTGVVAMCFAPEkDRAK 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 798 RGSIGVPIDNTQVYVLDAN-LHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgppgtrmYRTGDLVRWSAAGD 876
Cdd:cd05904 330 YGSVGRLVPNVEAKIVDPEtGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGW-------LHTGDLCYIDEDGY 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 653678460 877 LEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVI 931
Cdd:cd05904 403 LFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVV 457
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1541-2028 |
4.77e-39 |
|
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: 152.76 E-value: 4.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1541 ADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPgy 1620
Cdd:cd17631 5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALR--ALG---VAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNF-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1621 pmaRLTRiadtvtpalvltrtgqggclpgaevfgdvpvvalDRVADRLTampDQRPEVTVDprGLAYSIFTSGSTGQPKG 1700
Cdd:cd17631 78 ---RLTP----------------------------------PEVAYILA---DSGAKVLFD--DLALLMYTSGTTGRPKG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1701 VAVEHigivRYLSWAAASYPTA---GRRGTLAHSSVGFDLTMSALFEPLVSGRGVTLMP-----ADATLADLAEElsgpl 1772
Cdd:cd17631 116 AMLTH----RNLLWNAVNALAAldlGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVIlrkfdPETVLDLIERH----- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1773 AYDYIRLTPSHLRHLVGH--WTGQELPpAARGWVVGGETLDPALVKQLLELrpDAEVINHYGPTETVIGRVVHPvreaGE 1850
Cdd:cd17631 187 RVTSFFLVPTMIQALLQHprFATTDLS-SLRAVIYGGAPMPERLLRALQAR--GVKFVQGYGMTETSPGVTFLS----PE 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1851 LAVDSPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDpagepgarMYRTGDLVRWR 1930
Cdd:cd17631 260 DHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDG--------WFHTGDLGRLD 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1931 GDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGV-EQAVVLVRDQQlvgW------FIPAEDHPPVTVSALRRFCAE 2003
Cdd:cd17631 332 EDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVaEVAVIGVPDEK---WgeavvaVVVPRPGAELDEDELIAHCRE 408
|
490 500
....*....|....*....|....*
gi 653678460 2004 QLPEFMVPNQWVALDAFPLTPHGKV 2028
Cdd:cd17631 409 RLARYKIPKSVEFVDALPRNATGKI 433
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
512-977 |
6.25e-39 |
|
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: 154.33 E-value: 6.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 512 EGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARPVL 591
Cdd:cd12119 21 GEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 592 VVTDAATADRLGP-----DDITGLVVLeeTDTGGYPATEPPAVPA------------------GHSAYVI-YTSGSTGRP 647
Cdd:cd12119 101 VFVDRDFLPLLEAiaprlPTVEHVVVM--TDDAAMPEPAGVGVLAyeellaaespeydwpdfdENTAAAIcYTSGTTGNP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 648 KGVVITRAALdnFLAAMAER----FPLTAEDRVLATTTVsFDIAGLEL-YLPLRSGAGVVLADADTarNPAALIDLAGRH 722
Cdd:cd12119 179 KGVVYSHRSL--VLHAMAALltdgLGLSESDVVLPVVPM-FHVNAWGLpYAAAMVGAKLVLPGPYL--DPASLAELIERE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 723 RVTLAQATPTLWQALVPELSGPA---LAGIRVLVGGEALPAELARRLGDAGAEVTNMYGPTET-TIWSTSGPTS------ 792
Cdd:cd12119 254 GVTFAAGVPTVWQGLLDHLEANGrdlSSLRRVVIGGSAVPRSLIEAFEERGVRVIHAWGMTETsPLGTVARPPSehsnls 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 793 --EDSIRRGSIGVPIDNTQVYVLDANLHPAPI--GVLGELHIAGEGLARGYWNRPGlTAEKFLPDPFgppgtrmYRTGDL 868
Cdd:cd12119 334 edEQLALRAKQGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDE-ESEALTEDGW-------LRTGDV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 869 VRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVI--PDGPVAPDALRTELS 946
Cdd:cd12119 406 ATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVlkEGATVTAEELLEFLA 485
|
490 500 510
....*....|....*....|....*....|.
gi 653678460 947 RTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:cd12119 486 DKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
502-988 |
8.63e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 153.99 E-value: 8.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 502 RRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIA 581
Cdd:PRK06188 23 KRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 582 YLLSDARP-VLVVTDAATADR----------------LGPDDiTGLVVLEETDTGGYPATEPPAVPAgHSAYVIYTSGST 644
Cdd:PRK06188 103 YVLEDAGIsTLIVDPAPFVERalallarvpslkhvltLGPVP-DGVDLLAAAAKFGPAPLVAAALPP-DIAGLAYTGGTT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 645 GRPKGVVITRAALDNFLAAMAERFPLTAEDRVLATTTVSFdiAGLELYLP--LRSGAGVVLADADtarnPAALIDLAGRH 722
Cdd:PRK06188 181 GKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSH--AGGAFFLPtlLRGGTVIVLAKFD----PAEVLRAIEEQ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 723 RVTLAQATPTLWQALV--PELSGPALAGIRVLVGGEA--LPAELA---RRLGDAGAEVtnmYGPTETTIWSTSGPTSE-- 793
Cdd:PRK06188 255 RITATFLVPTMIYALLdhPDLRTRDLSSLETVYYGASpmSPVRLAeaiERFGPIFAQY---YGQTEAPMVITYLRKRDhd 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 794 --DSIRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDpfgppgtrMYRTGDLVRW 871
Cdd:PRK06188 332 pdDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDG--------WLHTGDVARE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 872 SAAGDLEYLGRTDHQVKLRGFRIELGEIETTLiNAGPVRRAAAV--VREDRPGDLrLVAYVI--PDGPVAPDALRTELSR 947
Cdd:PRK06188 404 DEDGFYYIVDRKKDMIVTGGFNVFPREVEDVL-AEHPAVAQVAVigVPDEKWGEA-VTAVVVlrPGAAVDAAELQAHVKE 481
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 653678460 948 TLPDYMIPAVIVPVPDFPTTPNGKLDRAALPAPDYGTRSTA 988
Cdd:PRK06188 482 RKGSVHAPKQVDFVDSLPLTALGKPDKKALRARYWEGRGRA 522
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
57-368 |
8.73e-39 |
|
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: 150.80 E-value: 8.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 57 WFSEQLRPGTPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVFRLGpDGEPVQQTAPAAPVALPVIDVteadlpq 136
Cdd:cd19537 12 WHKYQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPR-DGGLRRSYSSSPPRVQRVDTL------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 137 ALRTAAEQPFDLERGPLLRACLhrigaKQHVLLVTVHHIVLDGWSCGLLLADLARAYAGELPAGVAAPAFrDVAAWQHgR 216
Cdd:cd19537 84 DVWKEINRPFDLEREDPIRVFI-----SPDTLLVVMSHIICDLTTLQLLLREVSAAYNGKLLPPVRREYL-DSTAWSR-P 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 217 LAAGELDdqlrYWRQRLAGLPDLEIPGdrqRPADRDWRAHSVRRELPAATEAAVRRLAAAHDTTPFTVLLAAYGTFLHRL 296
Cdd:cd19537 157 ASPEDLD----FWSEYLSGLPLLNLPR---RTSSKSYRGTSRVFQLPGSLYRSLLQFSTSSGITLHQLALAAVALALQDL 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 653678460 297 TGQDDFAVGVPVAGRGRTDLESVVGLFAGMVPVRL--DLTGRPSFDEVLSRTVAGSRNDFAHPqIPFDRLVREL 368
Cdd:cd19537 230 SDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRIrfPSSSDASAADFLRAVRRSSQAALAHA-IPWHQLLEHL 302
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
489-972 |
2.19e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 153.01 E-value: 2.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 489 PAASLRERFQQWCRR----TPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKA 564
Cdd:PRK07786 11 PYLARRQNWVNQLARhalmQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANML 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 565 GAAYLPIDPDFPVERIAYLLSDARPVLVVTD------AATADRLGPDDITGLVVLEETDTG--GY--------PATEPPA 628
Cdd:PRK07786 91 GAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEaalapvATAVRDIVPLLSTVVVAGGSSDDSvlGYedllaeagPAHAPVD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 629 VPAGHSAYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDRVLATTTVSFDIAGLELYLP-LRSGAGVVLADAD 707
Cdd:PRK07786 171 IPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPgLLLGAPTVIYPLG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 708 tARNPAALIDLAGRHRVTLAQATPTLWQAL--VPELSGPALAgIRVLVGGEAlPAE--LARRLGDA--GAEVTNMYGPTE 781
Cdd:PRK07786 251 -AFDPGQLLDVLEAEKVTGIFLVPAQWQAVcaEQQARPRDLA-LRVLSWGAA-PASdtLLRQMAATfpEAQILAAFGQTE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 782 TTIwSTSGPTSEDSIR-RGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgppgt 860
Cdd:PRK07786 328 MSP-VTCMLLGEDAIRkLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWF----- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 861 rmyRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIPDGPVAP-- 938
Cdd:PRK07786 402 ---HSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAAlt 478
|
490 500 510
....*....|....*....|....*....|....*
gi 653678460 939 -DALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKL 972
Cdd:PRK07786 479 lEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1531-2033 |
2.20e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 152.37 E-value: 2.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1531 RTVHQLVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAG 1610
Cdd:PRK07656 5 MTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALA--ALG---IGKGDRVAIWAPNSPHWVIAALGALKAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1611 GYFIPVDPGYPMARLTRI-ADTVTPALVltrtGQGGCLPGAEVfGDVPVVALDRVA-----------------DRLTAMP 1672
Cdd:PRK07656 80 AVVVPLNTRYTADEAAYIlARGDAKALF----VLGLFLGVDYS-ATTRLPALEHVViceteeddphtekmktfTDFLAAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1673 DQR-PEVTVDPRGLAYSIFTSGSTGQPKGVAVEHIGIVR-YLSWAAASYPTAGRRgTLA-----HSsvgFDLTmSALFEP 1745
Cdd:PRK07656 155 DPAeRAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSnAADWAEYLGLTEGDR-YLAanpffHV---FGYK-AGVNAP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1746 LVSGRGVTLMP---ADATLADLAEE----LSGPLA-----YDYIRLTPSHLRHLvghwtgqelppaaRGWVVGGETLDPA 1813
Cdd:PRK07656 230 LMRGATILPLPvfdPDEVFRLIETEritvLPGPPTmynslLQHPDRSAEDLSSL-------------RLAVTGAASMPVA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1814 LVKQLLELRPDAEVINHYGPTE----TVIGRvvhpvreAGELAVDSPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIG 1889
Cdd:PRK07656 297 LLERFESELGVDIVLTGYGLSEasgvTTFNR-------LDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1890 GDGIARGYLGRPALTAEKFLPDpagepgaRMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQ 1969
Cdd:PRK07656 370 GPNVMKGYYDDPEATAAAIDAD-------GWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAE 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 653678460 1970 AVVL-VRDQQL---VGWFIPAEDHPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:PRK07656 443 AAVIgVPDERLgevGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
517-977 |
2.60e-38 |
|
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: 150.32 E-value: 2.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 517 LSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARPVLVVTDA 596
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 597 ATadrlgpDDItglvvleetdtggypateppavpaghsAYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDRV 676
Cdd:cd05935 82 EL------DDL---------------------------ALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 677 LATTTVsFDIAGLE--LYLPLRSGAGVVLA---DADTARnpaaliDLAGRHRVTLAQATPTLWQALV--PELSGPALAGI 749
Cdd:cd05935 129 LACLPL-FHVTGFVgsLNTAVYVGGTYVLMarwDRETAL------ELIEKYKVTFWTNIPTMLVDLLatPEFKTRDLSSL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 750 RVLVGGEA-LPAELARRLGD-AGAEVTNMYGPTETTIWSTSGPTSedSIRRGSIGVPIDNTQVYVLDA-NLHPAPIGVLG 826
Cdd:cd05935 202 KVLTGGGApMPPAVAEKLLKlTGLRFVEGYGLTETMSQTHTNPPL--RPKLQCLGIP*FGVDARVIDIeTGRELPPNEVG 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 827 ELHIAGEGLARGYWNRPGLTAEKFLPDpfgpPGTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINA 906
Cdd:cd05935 280 EIVVRGPQIFKGYWNRPEETEESFIEI----KGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKH 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 653678460 907 GPVRRAAAV-VREDRPGDlRLVAYVIPD----GPVAPDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:cd05935 356 PAI*EVCVIsVPDERVGE-EVKAFIVLRpeyrGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
490-967 |
4.00e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 152.20 E-value: 4.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 490 AASLRERFQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYL 569
Cdd:PRK06164 9 ADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 570 PIDPDFPVERIAYLLSDARPVLV------------------------------VTDAATADRLGPDDITGLVVLEETDTG 619
Cdd:PRK06164 89 AVNTRYRSHEVAHILGRGRARWLvvwpgfkgidfaailaavppdalpplraiaVVDDAADATPAPAPGARVQLFALPDPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 620 GYPATEPPAVPAGHSAYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDRVLATTTVS--FDIAGleLYLPLRS 697
Cdd:PRK06164 169 PPAAAGERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCgvFGFST--LLGALAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 698 GAGVVLADA-DTARNPAALidlaGRHRVTLAQATPTLWQALVPELSGPA-LAGIRVLVGGEALPA--ELARRLGDAGAEV 773
Cdd:PRK06164 247 GAPLVCEPVfDAARTARAL----RRHRVTHTFGNDEMLRRILDTAGERAdFPSARLFGFASFAPAlgELAALARARGVPL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 774 TNMYGPTETTIWSTSGPTSED-SIRRGSIGVPID-NTQVYVLD-ANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKF 850
Cdd:PRK06164 323 TGLYGSSEVQALVALQPATDPvSVRIEGGGRPASpEARVRARDpQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARAL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 851 LPDPFgppgtrmYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLiNAGPVRRAAAVVREDRPGDLRLVAYV 930
Cdd:PRK06164 403 TDDGY-------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHAL-EALPGVAAAQVVGATRDGKTVPVAFV 474
|
490 500 510
....*....|....*....|....*....|....*....
gi 653678460 931 IPDGPVAPDA--LRTELSRTLPDYMIPAVIVPVPDFPTT 967
Cdd:PRK06164 475 IPTDGASPDEagLMAACREALAGFKVPARVQVVEAFPVT 513
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
515-963 |
7.37e-38 |
|
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: 149.67 E-value: 7.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 515 TTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARPVLVVT 594
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 595 DaatadrlGPDDItglvvleetdtggypateppavpaghsAYVIYTSGSTGRPKGVVITraaLDNFLA---AMAERFPLT 671
Cdd:cd05907 84 E-------DPDDL---------------------------ATIIYTSGTTGRPKGVMLS---HRNILSnalALAERLPAT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 672 AEDRVLA---TTTVSFDIAGleLYLPLRSGAGVVLadadtARNPAALIDLAGRHRVTLAQATPTLWQALVPELSGPALAG 748
Cdd:cd05907 127 EGDRHLSflpLAHVFERRAG--LYVPLLAGARIYF-----ASSAETLLDDLSEVRPTVFLAVPRVWEKVYAAIKVKAVPG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 749 IR--------------VLVGGEALPAELARRLGDAGAEVTNMYGPTETTiwSTSGPTSEDSIRRGSIGVPIDNTQVyvld 814
Cdd:cd05907 200 LKrklfdlavggrlrfAASGGAPLPAELLHFFRALGIPVYEGYGLTETS--AVVTLNPPGDNRIGTVGKPLPGVEV---- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 815 anlhpaPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgppgtrmYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFR- 893
Cdd:cd05907 274 ------RIADDGEILVRGPNVMLGYYKNPEATAEALDADGW-------LHTGDLGEIDEDGFLHITGRKKDLIITSGGKn 340
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 894 IELGEIETTLINAGPVRRaAAVVREDRPgdlRLVAYVIPDgpvaPDALRTELSRTLPDYMIPAVIVPVPD 963
Cdd:cd05907 341 ISPEPIENALKASPLISQ-AVVIGDGRP---FLVALIVPD----PEALEAWAEEHGIAYTDVAELAANPA 402
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
502-972 |
9.04e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 150.85 E-value: 9.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 502 RRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIA 581
Cdd:PRK08316 22 RRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 582 YLLSDARPVLVVTDAATADRL-------GPDDITGLVVLEETDTGG-----------YPATEPPAVPAGHS-AYVIYTSG 642
Cdd:PRK08316 102 YILDHSGARAFLVDPALAPTAeaalallPVDTLILSLVLGGREAPGgwldfadwaeaGSVAEPDVELADDDlAQILYTSG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 643 STGRPKGVVIT-RAALDNFLAAMAErFPLTAEDRVLATTTVsFDIAGLELYL-P-LRSGAGVVLADADTarnPAALIDLA 719
Cdd:PRK08316 182 TESLPKGAMLThRALIAEYVSCIVA-GDMSADDIPLHALPL-YHCAQLDVFLgPyLYVGATNVILDAPD---PELILRTI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 720 GRHRVTLAQATPTLWQALV--PELSGPALAGIR-VLVGGEALPAELARRLGDA--GAEVTNMYGPTETTIWSTS-GPtsE 793
Cdd:PRK08316 257 EAERITSFFAPPTVWISLLrhPDFDTRDLSSLRkGYYGASIMPVEVLKELRERlpGLRFYNCYGQTEIAPLATVlGP--E 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 794 DSIRR-GSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgppgtrmyRTGDLVRWS 872
Cdd:PRK08316 335 EHLRRpGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWF--------HSGDLGVMD 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 873 AAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIPDG--PVAPDALRTELSRTLP 950
Cdd:PRK08316 407 EEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAgaTVTEDELIAHCRARLA 486
|
490 500
....*....|....*....|..
gi 653678460 951 DYMIPAVIVPVPDFPTTPNGKL 972
Cdd:PRK08316 487 GFKVPKRVIFVDELPRNPSGKI 508
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1535-2033 |
1.45e-37 |
|
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: 148.87 E-value: 1.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1535 QLVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFI 1614
Cdd:cd05936 3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQ--NLG---VQPGDRVALMLPNCPQFPIAYFGALKAGAVVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1615 PVDPGYPMARLTRIadtvtpalvLTRTGqggclpgAEVfgdvpVVALDRVADRLTAMPDQRPEVTVDPRGLAYSIFTSGS 1694
Cdd:cd05936 78 PLNPLYTPRELEHI---------LNDSG-------AKA-----LIVAVSFTDLLAAGAPLGERVALTPEDVAVLQYTSGT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1695 TGQPKGVAVEHIGIVRYLSWAAASYPTAGRRGT-------LAHSsvgFDLTMsALFEPLVSGRGVTLMP---ADATLADL 1764
Cdd:cd05936 137 TGVPKGAMLTHRNLVANALQIKAWLEDLLEGDDvvlaalpLFHV---FGLTV-ALLLPLALGATIVLIPrfrPIGVLKEI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1765 AEElsgplaydyiRLT-----PSHLRHLVGHWTGQELPPAA-RGWVVGGETLDPALVKQLLElRPDAEVINHYGPTETVI 1838
Cdd:cd05936 213 RKH----------RVTifpgvPTMYIALLNAPEFKKRDFSSlRLCISGGAPLPVEVAERFEE-LTGVPIVEGYGLTETSP 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1839 GRVVHPVREagelaVDSPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDpagepga 1918
Cdd:cd05936 282 VVAVNPLDG-----PRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDG------- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1919 rMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVL-VRDQQ----LVGWFIPAEDHpPVT 1993
Cdd:cd05936 350 -WLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVgVPDPYsgeaVKAFVVLKEGA-SLT 427
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 653678460 1994 VSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:cd05936 428 EEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
482-942 |
2.31e-37 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 151.02 E-value: 2.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 482 NDTARPLPAASLRERFQQWCRRTPGAVAVIEGD----TTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVT 557
Cdd:COG1022 2 SEFSDVPPADTLPDLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 558 LLAVIKAGAAYLPIDPDFPVERIAYLLSDARP-VLVVTDAATADRLGP--DDITGL---VVLEETDTGGYP--------- 622
Cdd:COG1022 82 DLAILAAGAVTVPIYPTSSAEEVAYILNDSGAkVLFVEDQEQLDKLLEvrDELPSLrhiVVLDPRGLRDDPrllsldell 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 623 -----ATEPPAVPAGHS-------AYVIYTSGSTGRPKGVVITRAaldNFLA---AMAERFPLTAEDRVLatttvsfdia 687
Cdd:COG1022 162 algreVADPAELEARRAavkpddlATIIYTSGTTGRPKGVMLTHR---NLLSnarALLERLPLGPGDRTL---------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 688 gleLYLPL-----RSG------AGVVLAdadTARNPAALIDLAGRHRVTLAQATPTLW-------QALVPELSGP----- 744
Cdd:COG1022 229 ---SFLPLahvfeRTVsyyalaAGATVA---FAESPDTLAEDLREVKPTFMLAVPRVWekvyagiQAKAEEAGGLkrklf 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 745 ----------------------------ALA------------G--IRVLV-GGEALPAELARRLGDAGAEVTNMYGPTE 781
Cdd:COG1022 303 rwalavgrryararlagkspslllrlkhALAdklvfsklrealGgrLRFAVsGGAALGPELARFFRALGIPVLEGYGLTE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 782 ttiwsTSGPTS---EDSIRRGSIGVPIDNTQVYvldanlhpapIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgpp 858
Cdd:COG1022 383 -----TSPVITvnrPGDNRIGTVGPPLPGVEVK----------IAEDGEILVRGPNVMKGYYKNPEATAEAFDADGW--- 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 859 gtrmYRTGDLVRWSAAGDLEYLGRTDHQVKLR-GFRIELGEIETTLinagpvrRA------AAVVREDRPgdlRLVAYVI 931
Cdd:COG1022 445 ----LHTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENAL-------KAsplieqAVVVGDGRP---FLAALIV 510
|
570
....*....|.
gi 653678460 932 PDgpvaPDALR 942
Cdd:COG1022 511 PD----FEALG 517
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
502-972 |
2.35e-37 |
|
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: 150.81 E-value: 2.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 502 RRTPGAVAVI-EGDT-----TLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDF 575
Cdd:cd17634 64 RENGDRTAIIyEGDDtsqsrTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 576 PVERIAYLLSDARPVLVVT---------------DAATADRLGPDDITGLVVLEETD-----TGGY------------PA 623
Cdd:cd17634 144 APEAVAGRIIDSSSRLLITadggvragrsvplkkNVDDALNPNVTSVEHVIVLKRTGsdidwQEGRdlwwrdliakasPE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 624 TEPPAVPAGHSAYVIYTSGSTGRPKGVVITRAALDNFLA-AMAERFPLTAEDRVLATTTVSFDIAGLEL-YLPLRSGAGV 701
Cdd:cd17634 224 HQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAAtTMKYVFDYGPGDIYWCTADVGWVTGHSYLlYGPLACGATT 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 702 VLAD-ADTARNPAALIDLAGRHRVTLAQATPTLWQALVPE----LSGPALAGIRVLVG-GEALPAE----LARRLGDAGA 771
Cdd:cd17634 304 LLYEgVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAgddaIEGTDRSSLRILGSvGEPINPEayewYWKKIGKEKC 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 772 EVTNMYGPTETTIWSTSGPTSEDSIRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGE--GLARGYWNRPGLTAEK 849
Cdd:cd17634 384 PVVDTWWQTETGGFMITPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHERFEQT 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 850 FLPDPFGppgtrMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAY 929
Cdd:cd17634 464 YFSTFKG-----MYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAY 538
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 653678460 930 VI-----PDGPVAPDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKL 972
Cdd:cd17634 539 VVlnhgvEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
499-976 |
3.57e-37 |
|
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: 149.70 E-value: 3.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 499 QWCRRTPGAVAVI------EGDTTLSYRELDERANRLARLLMERGAGAETfVAVLLPRSADLLVTLLAVIKAGAAYLPID 572
Cdd:cd05931 1 RRAAARPDRPAYTflddegGREETLTYAELDRRARAIAARLQAVGKPGDR-VLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 573 PDFP---VERIAYLLSDARPVLVVTDAATADRLGP-------DDITGLVVLEETDTGGYPATEPPAVPAGHSAYVIYTSG 642
Cdd:cd05931 80 PPTPgrhAERLAAILADAGPRVVLTTAAALAAVRAfaasrpaAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 643 STGRPKGVVIT-RAALDNfLAAMAERFPLTAEDRVlatttVSFdiagLELY----------LPLRSGAGVVL-ADADTAR 710
Cdd:cd05931 160 STGTPKGVVVThRNLLAN-VRQIRRAYGLDPGDVV-----VSW----LPLYhdmgliggllTPLYSGGPSVLmSPAAFLR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 711 NPAALIDLAGRHRVTLAQAtPTLWQALV------PELSGPALAGIRV-LVGGEALPAELARRLGDAGAE-------VTNM 776
Cdd:cd05931 230 RPLRWLRLISRYRATISAA-PNFAYDLCvrrvrdEDLEGLDLSSWRVaLNGAEPVRPATLRRFAEAFAPfgfrpeaFRPS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 777 YGPTETTIWSTSGPT------------------------SEDSIRRGSIGVPIDNTQVYVLDANLH-PAPIGVLGELHIA 831
Cdd:cd05931 309 YGLAEATLFVSGGPPgtgpvvlrvdrdalagravavaadDPAARELVSCGRPLPDQEVRIVDPETGrELPDGEVGEIWVR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 832 GEGLARGYWNRPGLTAEKFLPDPfGPPGTRMYRTGDLvRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRR 911
Cdd:cd05931 389 GPSVASGYWGRPEATAETFGALA-ATDEGGWLRTGDL-GFLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALR 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 653678460 912 ----AAAVVREDRPGDLRLVAYVIPD-GPVAPDALRTELSRTLPDY--MIPAVIVPVP--DFPTTPNGKLDRAA 976
Cdd:cd05931 467 pgcvAAFSVPDDGEERLVVVAEVERGaDPADLAAIAAAIRAAVAREhgVAPADVVLVRpgSIPRTSSGKIQRRA 540
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1554-2034 |
3.84e-37 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 146.67 E-value: 3.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1554 DRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMARLTRIADTVT 1633
Cdd:cd05934 1 GRRWTYAELLRESARIAAALA--ALG---IRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1634 PALVLTrtgqggclpgaevfgdvpvvaldrvadrltampdqrpevtvDPrglAYSIFTSGSTGQPKGVAVEHigivRYLS 1713
Cdd:cd05934 76 AQLVVV-----------------------------------------DP---ASILYTSGTTGPPKGVVITH----ANLT 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1714 WAAASYPTAGRRGT---------LAHSSVGFDLTMSALfeplVSGRGVTLMP---ADATLADLAEelSGPLAYDYIRLTP 1781
Cdd:cd05934 108 FAGYYSARRFGLGEddvyltvlpLFHINAQAVSVLAAL----SVGATLVLLPrfsASRFWSDVRR--YGATVTNYLGAML 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1782 SHL----------RHLVGHWTGQELPPAargwvvggetldpalVKQLLELRPDAEVINHYGPTET---VIGRVVHPVRea 1848
Cdd:cd05934 182 SYLlaqppspddrAHRLRAAYGAPNPPE---------------LHEEFEERFGVRLLEGYGMTETivgVIGPRDEPRR-- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1849 gelavdsPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFI---GGDGIARGYLGRPALTAEKFlpdPAGepgarMYRTGD 1925
Cdd:cd05934 245 -------PGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIrglRGWGFFKGYYNMPEATAEAM---RNG-----WFHTGD 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1926 LVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGV-EQAVVLVRDQ---QLVGWFIPAEDHPPVTVSALRRFC 2001
Cdd:cd05934 310 LGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVrEAAVVAVPDEvgeDEVKAVVVLRPGETLDPEELFAFC 389
|
490 500 510
....*....|....*....|....*....|...
gi 653678460 2002 AEQLPEFMVPNQWVALDAFPLTPHGKVNHRALP 2034
Cdd:cd05934 390 EGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
507-977 |
4.82e-37 |
|
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: 146.85 E-value: 4.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 507 AVAVIEGDTTLSYRELDERANRLARLLMerGAGAETF---VAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYL 583
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLV--GELGIVPgnrVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 584 LSDARPVLVVTDAATADRlgpDDITGLVvleetdtggypateppavpaghsayviYTSGSTGRPKGVVitrAALDNFLAA 663
Cdd:cd05958 79 LDKARITVALCAHALTAS---DDICILA---------------------------FTSGTTGAPKATM---HFHRDPLAS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 664 mAERFP-----LTAEDRVLATTTVSFDIA-GLELYLPLRSGAGVVLADADTARNpaaLIDLAGRHRVTLAQATPTLWQAL 737
Cdd:cd05958 126 -ADRYAvnvlrLREDDRFVGSPPLAFTFGlGGVLLFPFGVGASGVLLEEATPDL---LLSAIARYKPTVLFTAPTAYRAM 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 738 V--PELSGPALAGIRVLV-GGEALPAELARRLGDA-GAEVTNMYGPTETTIWSTSgpTSEDSIRRGSIGVPIDNTQVYVL 813
Cdd:cd05958 202 LahPDAAGPDLSSLRKCVsAGEALPAALHRAWKEAtGIPIIDGIGSTEMFHIFIS--ARPGDARPGATGKPVPGYEAKVV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 814 DANLHPAPIGVLGELHIAGEglaRGYWNrpglTAEKFLPDPFGppGTRMYrTGDLVRWSAAGDLEYLGRTDHQVKLRGFR 893
Cdd:cd05958 280 DDEGNPVPDGTIGRLAVRGP---TGCRY----LADKRQRTYVQ--GGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSGGYN 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 894 IELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIPDGPVAPD-----ALRTELSRTLPDYMIPAVIVPVPDFPTTP 968
Cdd:cd05958 350 IAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGpvlarELQDHAKAHIAPYKYPRAIEFVTELPRTA 429
|
....*....
gi 653678460 969 NGKLDRAAL 977
Cdd:cd05958 430 TGKLQRFAL 438
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
517-977 |
5.29e-37 |
|
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: 146.51 E-value: 5.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 517 LSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLL--SDARpvLVVT 594
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLrtSGAR--LVVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 595 DAATADRLGpddiTGLVVLeetdtggypateppavpaghsayvIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAED 674
Cdd:cd05973 79 DAANRHKLD----SDPFVM------------------------MFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPED 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 675 RVLATTT------VSFDIAGlelylPLRSGAGVVLADAdtARNPAALIDLAGRHRVTLAQATPTLWQAL----VPELSGP 744
Cdd:cd05973 131 SFWNAADpgwaygLYYAITG-----PLALGHPTILLEG--GFSVESTWRVIERLGVTNLAGSPTAYRLLmaagAEVPARP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 745 ALAGIRVLVGGEALPAELARRLGDA-GAEVTNMYGPTETTIWSTSGPTSEDSIRRGSIGVPIDNTQVYVLDANLHPAPIG 823
Cdd:cd05973 204 KGRLRRVSSAGEPLTPEVIRWFDAAlGVPIHDHYGQTELGMVLANHHALEHPVHAGSAGRAMPGWRVAVLDDDGDELGPG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 824 VLGELHI--AGEGLA--RGYWNRPGltaekflPDPFGppgtRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEI 899
Cdd:cd05973 284 EPGRLAIdiANSPLMwfRGYQLPDT-------PAIDG----GYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 900 ETTLINAGPVRRAAAVvreDRPGDLR---LVAYVIPDG-----PVAPDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGK 971
Cdd:cd05973 353 ESALIEHPAVAEAAVI---GVPDPERtevVKAFVVLRGghegtPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGK 429
|
....*.
gi 653678460 972 LDRAAL 977
Cdd:cd05973 430 IQRFLL 435
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
1083-1499 |
1.01e-36 |
|
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: 145.20 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1083 LPLSPMQESIWLADQVSAGDSVYNVPLALRLIGPLDRGALRRTLNRVVDRHEMLRTRIHPgPDGMPVQVADPAGGGAA-- 1160
Cdd:cd19533 2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTE-EEGEPYQWIDPYTPVPIrh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1161 --LTErDAAPGTDLAQLLLAEAALGFTLATEHPLRAVLWRLDEREHVLLLTAHHVAVDAWSMDLIQRDLTELYAADTGHR 1238
Cdd:cd19533 81 idLSG-DPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1239 EPElDEPALAQADYAVWQRQSAQRGRYAAELDFWRTELTGAVA-TEVAGDLPRPATPGGGGGAVefaLAPRQIQGIRELA 1317
Cdd:cd19533 160 PAP-PAPFGSFLDLVEEEQAYRQSERFERDRAFWTEQFEDLPEpVSLARRAPGRSLAFLRRTAE---LPPELTRTLLEAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1318 RRCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGRGNPRLDNLVGCLVNTVVLRGDLSGAPTFHELLRRTHARTADAL 1397
Cdd:cd19533 236 EAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELRSLL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1398 AHQELPFEHLVADRG--AGNGPLFRIMYSFSSQEPAGRsAGDVDLEPVPV---PVTtckfDLVLTVVD--GGSTLEGVLE 1470
Cdd:cd19533 316 RHQRYRYEDLRRDLGltGELHPLFGPTVNYMPFDYGLD-FGGVVGLTHNLssgPTN----DLSIFVYDrdDESGLRIDFD 390
|
410 420
....*....|....*....|....*....
gi 653678460 1471 YADDLYLPGTAERLVTSLTNLLAAAVRTP 1499
Cdd:cd19533 391 ANPALYSGEDLARHQERLLRLLEEAAADP 419
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
487-977 |
1.10e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 148.27 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 487 PLPAASLRERFQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGA 566
Cdd:PRK06178 29 PHGERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 567 AYLPIDPDFPVERIAYLLSD--------------------------------------ARPVLVVTDAATADRLGPDDIT 608
Cdd:PRK06178 109 VHVPVSPLFREHELSYELNDagaevllaldqlapvveqvraetslrhvivtsladvlpAEPTLPLPDSLRAPRLAAAGAI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 609 GLVVLEETDTGGYPAtEPPAVPAghSAYVIYTSGSTGRPKGVVITRAaldNFLAAMAERFPLT---AEDRVLATTTVSFD 685
Cdd:PRK06178 189 DLLPALRACTAPVPL-PPPALDA--LAALNYTGGTTGMPKGCEHTQR---DMVYTAAAAYAVAvvgGEDSVFLSFLPEFW 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 686 IAG--LELYLPLRSGAGVVLadadTAR-NPAALIDLAGRHRVTLA-----QATPTLWQALVPELSGPALAGIRVLVGGEA 757
Cdd:PRK06178 263 IAGenFGLLFPLFSGATLVL----LARwDAVAFMAAVERYRVTRTvmlvdNAVELMDHPRFAEYDLSSLRQVRVVSFVKK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 758 LPAELARRLGDAG----AEVTnmYGPTET----TIwsTSGPTSEDSIRRGS---IGVPIDNTQVYVLDANLH-PAPIGVL 825
Cdd:PRK06178 339 LNPDYRQRWRALTgsvlAEAA--WGMTEThtcdTF--TAGFQDDDFDLLSQpvfVGLPVPGTEFKICDFETGeLLPLGAE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 826 GELHIAGEGLARGYWNRPGLTAEKFLPDpfgppgtrMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLIN 905
Cdd:PRK06178 415 GEIVVRTPSLLKGYWNKPEATAEALRDG--------WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQ 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 653678460 906 AGPVRRAAAVVREDRPGDLRLVAYVI--PDGPVAPDALRTELSRTLPDYMIPAVIVpVPDFPTTPNGKLDRAAL 977
Cdd:PRK06178 487 HPAVLGSAVVGRPDPDKGQVPVAFVQlkPGADLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
46-346 |
1.49e-36 |
|
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: 145.09 E-value: 1.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 46 PVPLAPGQAgiWFSEQLRPGTPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVFRLGPDGepVQQTAP---AAPV 122
Cdd:cd19534 1 EVPLTPIQR--WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGG--WQQRIRgdvEELF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 123 ALPVIDVTEADLPQALRTAAEQ---PFDLERGPLLRACL-HRIGAKQHVLLVtVHHIVLDGWSCGLLLADLARAYAGELP 198
Cdd:cd19534 77 RLEVVDLSSLAQAAAIEALAAEaqsSLDLEEGPLLAAALfDGTDGGDRLLLV-IHHLVVDGVSWRILLEDLEAAYEQALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 199 AGVAA----PAFRDVAAWQHGRLAAGELDDQLRYWRQRLAGLPdLEIPGDR-QRPADRDwrahSVRREL-PAATEAAVRR 272
Cdd:cd19534 156 GEPIPlpskTSFQTWAELLAEYAQSPALLEELAYWRELPAADY-WGLPKDPeQTYGDAR----TVSFTLdEEETEALLQE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 273 LAAAHDTTPFTVLLAAYGTFLHRLTGQDDFAVGvpVAGRGRTDLESV------VGLFAGMVPVRLDLTGRPSFDEVLSRT 346
Cdd:cd19534 231 ANAAYRTEINDLLLAALALAFQDWTGRAPPAIF--LEGHGREEIDPGldlsrtVGWFTSMYPVVLDLEASEDLGDTLKRV 308
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
503-977 |
2.43e-36 |
|
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: 146.11 E-value: 2.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 503 RTPGAVAVI--EGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERI 580
Cdd:cd05923 13 RAPDACAIAdpARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 581 AYLLSDARPVLVVTdaaTADRLGPDDITGLVVLEET---------DTGGYPATEPPAVPAGHSAYVIYTSGSTGRPKGVV 651
Cdd:cd05923 93 AELIERGEMTAAVI---AVDAQVMDAIFQSGVRVLAlsdlvglgePESAGPLIEDPPREPEQPAFVFYTSGTTGLPKGAV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 652 ITRAALDNFLAAMAERFPLT--AEDRVLATTTVSFDIAGLELYLPLRSGAG-VVLADADTARNPAALIDlagRHRVTLAQ 728
Cdd:cd05923 170 IPQRAAESRVLFMSTQAGLRhgRHNVVLGLMPLYHVIGFFAVLVAALALDGtYVVVEEFDPADALKLIE---QERVTSLF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 729 ATPTLWQALVP--ELSGPALAGIR-VLVGGEALPAELARRLGDA-GAEVTNMYGPTETTiwstsGPTSEDSIRRGSIGVP 804
Cdd:cd05923 247 ATPTHLDALAAaaEFAGLKLSSLRhVTFAGATMPDAVLERVNQHlPGEKVNIYGTTEAM-----NSLYMRDARTGTEMRP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 805 IDNTQVY---VLDANLHPAPIGVLGELHIAGEGLA--RGYWNRPGLTAEKfLPDpfgppgtRMYRTGDLVRWSAAGDLEY 879
Cdd:cd05923 322 GFFSEVRivrIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKK-LQD-------GWYRTGDVGYVDPSGDVRI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 880 LGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAV-VREDRPGDLRLVAYVIPDGPVAPDALRTE-LSRTLPDYMIPAV 957
Cdd:cd05923 394 LGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIgVADERWGQSVTACVVPREGTLSADELDQFcRASELADFKRPRR 473
|
490 500
....*....|....*....|
gi 653678460 958 IVPVPDFPTTPNGKLDRAAL 977
Cdd:cd05923 474 YFFLDELPKNAMNKVLRRQL 493
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
502-977 |
7.59e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 144.56 E-value: 7.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 502 RRTPGAVAVIE--GDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVER 579
Cdd:PRK09088 6 RLQPQRLAAVDlaLGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 580 IAYLLSDARPVLVVTDAATAD-RLGPDDITGLVVLEETDTggyPATEPPAvPAGHSAYVIYTSGSTGRPKGVVITRAALD 658
Cdd:PRK09088 86 LDALLQDAEPRLLLGDDAVAAgRTDVEDLAAFIASADALE---PADTPSI-PPERVSLILFTSGTSGQPKGVMLSERNLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 659 NFLAAMAERFPLTAEDRVLATTTVsFDIAGL--ELYLPLRSGAGVVLADA-DTARNPAALIDLAgrHRVTLAQATPTLWQ 735
Cdd:PRK09088 162 QTAHNFGVLGRVDAHSSFLCDAPM-FHIIGLitSVRPVLAVGGSILVSNGfEPKRTLGRLGDPA--LGITHYFCVPQMAQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 736 AL--VPELSGPALAGIRVLV-GGEALPAELARRLGDAGAEVTNMYGPTET-TIWSTSGPTSEDSIRRGSIGVPIDNTQVY 811
Cdd:PRK09088 239 AFraQPGFDAAALRHLTALFtGGAPHAAEDILGWLDDGIPMVDGFGMSEAgTVFGMSVDCDVIRAKAGAAGIPTPTVQTR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 812 VLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgppgtrmYRTGDLVRWSAAGDLEYLGRTDHQVKLRG 891
Cdd:PRK09088 319 VVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW-------FRTGDIARRDADGFFWVVDRKKDMFISGG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 892 FRIELGEIETTLINAGPVRRAAAV-VREDRPGDL-RLVAYVIPDGPVAPDALRTELSRTLPDYMIPAVIVPVPDFPTTPN 969
Cdd:PRK09088 392 ENVYPAEIEAVLADHPGIRECAVVgMADAQWGEVgYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTAS 471
|
....*...
gi 653678460 970 GKLDRAAL 977
Cdd:PRK09088 472 GKLQKARL 479
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
1083-1499 |
9.31e-36 |
|
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: 142.59 E-value: 9.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1083 LPLSPMQESIWLADQVSAGDSVYNVPLALRLIGPLDRGALRRTLNRVVDRHEMLRTRIHPGPDGMPVQVADPAgGGAALT 1162
Cdd:cd19536 2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQ-AQVPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1163 ERDAAPGTDLAQL----LLAEAALGFTLATEHPLRAVLWRLDEREHVLL-LTAHHVAVDAWSMDLIQRDLTELYAADTGH 1237
Cdd:cd19536 81 ELDLTPLEEQLDPlrayKEETKIRRFDLGRAPLVRAALVRKDERERFLLvISDHHSILDGWSLYLLVKEILAVYNQLLEY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1238 REPELdEPALAQADYAVWQRQSAQRgryAAELDFWRTELTGAVATEVAGdlPRPATPGGGGGAVEFALAPRQIQGIRELA 1317
Cdd:cd19536 161 KPLSL-PPAQPYRDFVAHERASIQQ---AASERYWREYLAGATLATLPA--LSEAVGGGPEQDSELLVSVPLPVRSRSLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1318 RRCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGR--GNPRLDNLVGCLVNTVVLRGDLSGApTFHELLRRTHARTAD 1395
Cdd:cd19536 235 KRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRseETTGAERLLGLFLNTLPLRVTLSEE-TVEDLLKRAQEQELE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1396 ALAHQELPFeHLVADRGAGNgPLFRIM-------YSFSSQEPAGRSAGDVDLEPVPVPVTtckFDLVLTVVDGGSTLEGV 1468
Cdd:cd19536 314 SLSHEQVPL-ADIQRCSEGE-PLFDSIvnfrhfdLDFGLPEWGSDEGMRRGLLFSEFKSN---YDVNLSVLPKQDRLELK 388
|
410 420 430
....*....|....*....|....*....|.
gi 653678460 1469 LEYADDLYLPGTAERLVTSLTNLLAAAVRTP 1499
Cdd:cd19536 389 LAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
502-977 |
1.00e-35 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 144.23 E-value: 1.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 502 RRTPGAVAVIEGDTTLSYRELDERANRLARLLMER-GAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERI 580
Cdd:PRK06839 13 YLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 581 AYLLSDA--RPVLV-VTDAATADRLG-------PDDITGLVVLEETDTGGYpatEPPAvpaGHSAYVI-YTSGSTGRPKG 649
Cdd:PRK06839 93 IFQLKDSgtTVLFVeKTFQNMALSMQkvsyvqrVISITSLKEIEDRKIDNF---VEKN---ESASFIIcYTSGTTGKPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 650 VVITRA-----ALDNFLAamaerFPLTAEDRVLATTTVsFDIAGLELY-LP-LRSGAGVVLADAdtaRNPAALIDLAGRH 722
Cdd:PRK06839 167 AVLTQEnmfwnALNNTFA-----IDLTMHDRSIVLLPL-FHIGGIGLFaFPtLFAGGVIIVPRK---FEPTKALSMIEKH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 723 RVTLAQATPTLWQALV--PELSGPALAGIRVLV-GGEALPAELARRLGDAGAEVTNMYGPTETTiwstsgPT----SEDS 795
Cdd:PRK06839 238 KVTVVMGVPTIHQALIncSKFETTNLQSVRWFYnGGAPCPEELMREFIDRGFLFGQGFGMTETS------PTvfmlSEED 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 796 IRR--GSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgppgtrmyRTGDLVRWSA 873
Cdd:PRK06839 312 ARRkvGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWL--------CTGDLARVDE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 874 AGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVRED-RPGDLRLVAYVIPDGPVAPDA-LRTELSRTLPD 951
Cdd:PRK06839 384 DGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHvKWGEIPIAFIVKKSSSVLIEKdVIEHCRLFLAK 463
|
490 500
....*....|....*....|....*.
gi 653678460 952 YMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:PRK06839 464 YKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
1552-2033 |
1.45e-35 |
|
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: 143.61 E-value: 1.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1552 TGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMARLTRIADT 1631
Cdd:cd05926 10 GSTPALTYADLAELVDDLARQLA--ALG---IKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1632 VTPALVLTRTGQGG-CLPGA--------EVFGDVPVVALDRVADRLTAMPD----QRPEVTVDPRGLAYSIFTSGSTGQP 1698
Cdd:cd05926 85 LGSKLVLTPKGELGpASRAAsklglailELALDVGVLIRAPSAESLSNLLAdkknAKSEGVPLPDDLALILHTSGTTGRP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1699 KGVAVEHIGIVRYLSWAAASYPTAGRRGTLA-------HSSVGfdltmsALFEPLVSGRGVTLMPA-DATL--ADLAEE- 1767
Cdd:cd05926 165 KGVPLTHRNLAASATNITNTYKLTPDDRTLVvmplfhvHGLVA------SLLSTLAAGGSVVLPPRfSASTfwPDVRDYn 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1768 --------------LSGPLAYDYIRltPSHLRHlvghwtgqelppaARGwvvGGETLDPALVKQLlELRPDAEVINHYGP 1833
Cdd:cd05926 239 atwytavptihqilLNRPEPNPESP--PPKLRF-------------IRS---CSASLPPAVLEAL-EATFGAPVLEAYGM 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1834 TETVIGRVVHPVreagELAVDSPLPLGRPLGeTRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPa 1913
Cdd:cd05926 300 TEAAHQMTSNPL----PPGPRKPGSVGKPVG-VEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDG- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1914 gepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVL-VRDQ---QLVGWFIPAEDH 1989
Cdd:cd05926 374 ------WFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFgVPDEkygEEVAAAVVLREG 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 653678460 1990 PPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:cd05926 448 ASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
1532-2033 |
2.88e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 143.40 E-value: 2.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1532 TVHQLVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGG 1611
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALR--ALG---VKKGDRVAVFDWNSHEYLEAYFAVPKIGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1612 YFIPVDPGYPMARLTRIADTVTPALVLTRTGQGGCLPGAE----------VFGDVPVVALDRVADRLTAM----PDQRPE 1677
Cdd:PRK06187 82 VLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILpqlptvrtviVEGDGPAAPLAPEVGEYEELlaaaSDTFDF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1678 VTVDPRGLAYSIFTSGSTGQPKGVAVEHIGIVRyLSWAAASYPTAGRRGT------LAHS---SVGFDLTMSAL------ 1742
Cdd:PRK06187 162 PDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFL-HSLAVCAWLKLSRDDVylvivpMFHVhawGLPYLALMAGAkqvipr 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1743 -FEP-----LVSGRGVTLMPADAT-LADLaeeLSGPLAY--DYirltpSHLRHLVghwtgqelppaargwvVGGETLDPA 1813
Cdd:PRK06187 241 rFDPenlldLIETERVTFFFAVPTiWQML---LKAPRAYfvDF-----SSLRLVI----------------YGGAALPPA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1814 LVKQLLElRPDAEVINHYGPTETV-IGRVVHPvrEAGELAvDSPLPL--GRPLGETRLQVLDAWLEAVPV--GAVGELFI 1888
Cdd:PRK06187 297 LLREFKE-KFGIDLVQGYGMTETSpVVSVLPP--EDQLPG-QWTKRRsaGRPLPGVEARIVDDDGDELPPdgGEVGEIIV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1889 GGDGIARGYLGRPALTAEKFLPDpagepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGV- 1967
Cdd:PRK06187 373 RGPWLMQGYWNRPEATAETIDGG--------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVa 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 653678460 1968 EQAVVLVRDQQlvgW------FIPAEDHPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:PRK06187 445 EVAVIGVPDEK---WgerpvaVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
500-972 |
1.06e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 141.18 E-value: 1.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 500 WCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVER 579
Cdd:PRK06145 11 HARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 580 IAYLLSDARPVLVVTD---AATADRLGPDDITGLVVLEETD---TGGYPATEPPAVPAGHSAYVIYTSGSTGRPKGVVIT 653
Cdd:PRK06145 91 VAYILGDAGAKLLLVDeefDAIVALETPKIVIDAAAQADSRrlaQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 654 raaLDNFLAAMAER---FPLTAEDRVLATTTV----SFDIAGLelylplrsgagVVLADADTAR-----NPAALIDLAGR 721
Cdd:PRK06145 171 ---YGNLHWKSIDHviaLGLTASERLLVVGPLyhvgAFDLPGI-----------AVLWVGGTLRihrefDPEAVLAAIER 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 722 HRVTLAQATPTLWQAL--VPELSGPALAGIR-VLVGGEALPAELARRLGD--AGAEVTNMYGPTETTIWSTSGPTSEDSI 796
Cdd:PRK06145 237 HRLTCAWMAPVMLSRVltVPDRDRFDLDSLAwCIGGGEKTPESRIRDFTRvfTRARYIDAYGLTETCSGDTLMEAGREIE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 797 RRGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgppgtrmyRTGDLVRWSAAGD 876
Cdd:PRK06145 317 KIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF--------RSGDVGYLDEEGF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 877 LEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAV-VREDRPGDlRLVAYVI--PDGPVAPDALRTELSRTLPDYM 953
Cdd:PRK06145 389 LYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIgVHDDRWGE-RITAVVVlnPGATLTLEALDRHCRQRLASFK 467
|
490
....*....|....*....
gi 653678460 954 IPAVIVPVPDFPTTPNGKL 972
Cdd:PRK06145 468 VPRQLKVRDELPRNPSGKV 486
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
1548-2033 |
1.40e-34 |
|
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: 139.73 E-value: 1.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1548 TALRTGDRSLTFAGLDAQANRLAHALHtgalGAPPVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMARLTR 1627
Cdd:cd05941 3 IAIVDDGDSITYADLVARAARLANRLL----ALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1628 IADTVTPALVLTRtgqggclpgaevfgdvpvvaldrvadrltampdqrpevtvdprglAYSIFTSGSTGQPKGVAVEHIG 1707
Cdd:cd05941 79 VITDSEPSLVLDP---------------------------------------------ALILYTSGTTGRPKGVVLTHAN 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1708 I---VRYLS--WAAASyptagrRGTLAHssvGFDL-----TMSALFEPLVSGRGVTLMPA-DATLADLAEELSGPLAYD- 1775
Cdd:cd05941 114 LaanVRALVdaWRWTE------DDVLLH---VLPLhhvhgLVNALLCPLFAGASVEFLPKfDPKEVAISRLMPSITVFMg 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1776 ----YIRLTPSHLRHLVGHWTGQELPPAARGWVVGGETLDPALVKQLLELRPDAEVINHYGPTETVIGRVV--HPVREAG 1849
Cdd:cd05941 185 vptiYTRLLQYYEAHFTDPQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNplDGERRPG 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1850 elAVDSPLPlgrplG-ETRLqVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDpagepgaRMYRTGDLVR 1928
Cdd:cd05941 265 --TVGMPLP-----GvQARI-VDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDD-------GWFKTGDLGV 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1929 WRGDGLLDFVGRV-DDQVKLRGYRIELGEIEARMAEHPGV-EQAVVLVRD----QQLVGWFIPAEDHPPVTVSALRRFCA 2002
Cdd:cd05941 330 VDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVsECAVIGVPDpdwgERVVAVVVLRAGAAALSLEELKEWAK 409
|
490 500 510
....*....|....*....|....*....|.
gi 653678460 2003 EQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:cd05941 410 QRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
480-981 |
1.48e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 141.60 E-value: 1.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 480 RWNDTARPLPAASlrerfqqwcRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLL 559
Cdd:PRK07788 47 RYGPFAGLVAHAA---------RRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 560 AVIKAGAAYLPIDPDFPVERIAYLLSDARPVLVVTDAATADRLG--PDDITGLVVL-EETDTGGYPA------------- 623
Cdd:PRK07788 118 AAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSalPPDLGRLRAWgGNPDDDEPSGstdetlddliags 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 624 -TEPPAVPAGHSAYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDRVLATTTV--SFDIAGLELYLPLRSgaG 700
Cdd:PRK07788 198 sTAPLPKPPKPGGIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMfhATGWAHLTLAMALGS--T 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 701 VVLadadtAR--NPAALIDLAGRHRVTLAQATPTLWQ---ALVPELSG-PALAGIR-VLVGGEALPAELARRLGDA-GAE 772
Cdd:PRK07788 276 VVL-----RRrfDPEATLEDIAKHKATALVVVPVMLSrilDLGPEVLAkYDTSSLKiIFVSGSALSPELATRALEAfGPV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 773 VTNMYGPTETTIWSTSGPtSEDSIRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYwnrpgltaekflP 852
Cdd:PRK07788 351 LYNLYGSTEVAFATIATP-EDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY------------T 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 853 DPFGPPGTR-MYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVI 931
Cdd:PRK07788 418 DGRDKQIIDgLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVV 497
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 653678460 932 --PDGPVAPDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAALPAPD 981
Cdd:PRK07788 498 kaPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1566-2033 |
2.18e-34 |
|
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: 139.50 E-value: 2.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1566 ANRLAHALHTGALgappVGPETPVLLLLDRSpELVVAMLAVLKAGGY----FIPVDPGYPMARLTRIADTVTPALVLTRT 1641
Cdd:cd05922 3 VSAAASALLEAGG----VRGERVVLILPNRF-TYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1642 GQGGCL-PGAEVFGDVPVVALdrvADRLTAMPDQRPEVTVDPRGLAYSIFTSGSTGQPKGVAVEHIGIvryLSWAAASYP 1720
Cdd:cd05922 78 GAADRLrDALPASPDPGTVLD---ADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNL---LANARSIAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1721 TAGRRGT---LAHSSVGFDLTMSALFEPLVSGRGVTL----MPADATLADLAEELSGPLAydyirLTPSHLRHLvghwTG 1793
Cdd:cd05922 152 YLGITADdraLTVLPLSYDYGLSVLNTHLLRGATLVLtndgVLDDAFWEDLREHGATGLA-----GVPSTYAML----TR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1794 QELPPAA----RGWVVGGETLDPALVKQLLELRPDAEVINHYGPTETVIGRVVHPvreaGELAVDSPLPLGRPLGETRLQ 1869
Cdd:cd05922 223 LGFDPAKlpslRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLP----PERILEKPGSIGLAIPGGEFE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1870 VL--DAWLEavPVGAVGELFIGGDGIARGYLGRPALTAEKflpdpaGEPGARMYrTGDLVRWRGDGLLDFVGRVDDQVKL 1947
Cdd:cd05922 299 ILddDGTPT--PPGEPGEIVHRGPNVMKGYWNDPPYRRKE------GRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1948 RGYRIELGEIEARMAEHPGVEQAVVLVRDQQLV-GWFIPAEDHPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHG 2026
Cdd:cd05922 370 FGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGeKLALFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASG 449
|
....*..
gi 653678460 2027 KVNHRAL 2033
Cdd:cd05922 450 KVDYAAL 456
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
517-981 |
5.71e-34 |
|
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: 137.63 E-value: 5.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 517 LSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARPVLVVTDA 596
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 597 ATADRLGPDDitglvvleetdtggypateppavpaghSAYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDRV 676
Cdd:cd05969 81 ELYERTDPED---------------------------PTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 677 LATTT---VSFDIAGLelYLPLRSGAGVVLADADTarNPAALIDLAGRHRVTLAQATPTLWQALVPELSGPA----LAGI 749
Cdd:cd05969 134 WCTADpgwVTGTVYGI--WAPWLNGVTNVVYEGRF--DAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELArkydLSSL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 750 R-VLVGGEALPAELARrlgdAGAEVTNM-----YGPTETTIWSTSGPTSEDsIRRGSIGVPIDNTQVYVLDANLHPAPIG 823
Cdd:cd05969 210 RfIHSVGEPLNPEAIR----WGMEVFGVpihdtWWQTETGSIMIANYPCMP-IKPGSMGKPLPGVKAAVVDENGNELPPG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 824 VLGELHIAGE--GLARGYWNRPGLTAEKFLpdpfgppgTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIET 901
Cdd:cd05969 285 TKGILALKPGwpSMFRGIWNDEERYKNSFI--------DGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVES 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 902 TLINAGPVRRAAAVVREDRPGDLRLVAYV-IPDGPVAPDALRTEL----SRTLPDYMIPAVIVPVPDFPTTPNGKLDRAA 976
Cdd:cd05969 357 ALMEHPAVAEAGVIGKPDPLRGEIIKAFIsLKEGFEPSDELKEEIinfvRQKLGAHVAPREIEFVDNLPKTRSGKIMRRV 436
|
....*
gi 653678460 977 LPAPD 981
Cdd:cd05969 437 LKAKE 441
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
490-977 |
1.22e-33 |
|
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: 138.57 E-value: 1.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 490 AASLRERFQQWCRRTPGA----VAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAG 565
Cdd:cd05906 9 PRTLLELLLRAAERGPTKgityIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 566 --AAYLPIDPDFP-----VERIAYLLSDARPVLVVTDAATADRLGP-------DDITGLVVLEETDTGGypatEPPAVPA 631
Cdd:cd05906 89 fvPAPLTVPPTYDepnarLRKLRHIWQLLGSPVVLTDAELVAEFAGletlsglPGIRVLSIEELLDTAA----DHDLPQS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 632 GHS--AYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDRVLatTTVSFD-IAGL-ELYL-PLRSGAGVVLADA 706
Cdd:cd05906 165 RPDdlALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFL--NWVPLDhVGGLvELHLrAVYLGCQQVHVPT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 707 DTA-RNPAALIDLAGRHRVTLAQAtP----TLWQALVPELSGPA--LAGIRVLV-GGEALPAE----LARRLGDAGAEVT 774
Cdd:cd05906 243 EEIlADPLRWLDLIDRYRVTITWA-PnfafALLNDLLEEIEDGTwdLSSLRYLVnAGEAVVAKtirrLLRLLEPYGLPPD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 775 NM---YGPTET---TIWSTSGPT--SEDSIRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLT 846
Cdd:cd05906 322 AIrpaFGMTETcsgVIYSRSFPTydHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEAN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 847 AEKFLPDPFgppgtrmYRTGDLVrWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRR---AAAVVREDRPGD 923
Cdd:cd05906 402 AEAFTEDGW-------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsftAAFAVRDPGAET 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 653678460 924 LRLV-----AYVIPDGPVAP-DALRTELSRTL---PDYMIPaviVPVPDFPTTPNGKLDRAAL 977
Cdd:cd05906 474 EELAiffvpEYDLQDALSETlRAIRSVVSREVgvsPAYLIP---LPKEEIPKTSLGKIQRSKL 533
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
517-990 |
1.24e-33 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 140.94 E-value: 1.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 517 LSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARPVLVVTDA 596
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 597 ATADRLGPDDITGLVVLEETDTGGYPATEPPaVPAGHSAYVIYTSGSTGRPKGVVITRAALDNFLAAMAER-FPLTAEDR 675
Cdd:PRK06060 111 ALRDRFQPSRVAEAAELMSEAARVAPGGYEP-MGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKaLRLTPEDT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 676 VLATTTVSFDIA-GLELYLPLRSGAGVVLADADTARNPAALidLAGRHRVTLAQATPTLWQALVPELSGPALAGIR-VLV 753
Cdd:PRK06060 190 GLCSARMYFAYGlGNSVWFPLATGGSAVINSAPVTPEAAAI--LSARFGPSVLYGVPNFFARVIDSCSPDSFRSLRcVVS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 754 GGEALPAELARRLGDAGAEVTNMYGPTETTIWSTSGPTSEDSIRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGE 833
Cdd:PRK06060 268 AGEALELGLAERLMEFFGGIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 834 GLARGYWNRPG--LTAEKFLpdpfgppgtrmyRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRR 911
Cdd:PRK06060 348 AIAKGYWNRPDspVANEGWL------------DTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 912 AAAVVREDRPGDLRLVAYVIP------DGPVAPDALRTELSRtLPDYMIPAVIVPVPDFPTTPNGKLDRAALPApdygtR 985
Cdd:PRK06060 416 AAVVAVRESTGASTLQAFLVAtsgatiDGSVMRDLHRGLLNR-LSAFKVPHRFAVVDRLPRTPNGKLVRGALRK-----Q 489
|
....*
gi 653678460 986 STARP 990
Cdd:PRK06060 490 SPTKP 494
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
505-973 |
1.41e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 138.48 E-value: 1.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 505 PGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLL 584
Cdd:PRK07798 17 PDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 585 SDARPVLVVTDAATADRLGP--DDITGLVVLEETDTGGYPATEPPAVP------AGHSA-----------YVIYTSGSTG 645
Cdd:PRK07798 97 DDSDAVALVYEREFAPRVAEvlPRLPKLRTLVVVEDGSGNDLLPGAVDyedalaAGSPErdfgerspddlYLLYTGGTTG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 646 RPKGVVITRAalDNFLAAMAERFPLTAE---------DRVLATT-TVSFDIAglelylPLRSGAG-------------VV 702
Cdd:PRK07798 177 MPKGVMWRQE--DIFRVLLGGRDFATGEpiedeeelaKRAAAGPgMRRFPAP------PLMHGAGqwaafaalfsgqtVV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 703 LADADTArNPAALIDLAGRHRVTL------AQATPtLWQALVPElSGPALAGIRVLV-GGEALPAELARRLGDA--GAEV 773
Cdd:PRK07798 249 LLPDVRF-DADEVWRTIEREKVNVitivgdAMARP-LLDALEAR-GPYDLSSLFAIAsGGALFSPSVKEALLELlpNVVL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 774 TNMYGPTET----TIWSTSGPTSEDSIRrgsigVPIDNTQVyVLDANLHPAPIGVLGELHIAGEG-LARGYWNRPGLTAE 848
Cdd:PRK07798 326 TDSIGSSETgfggSGTVAKGAVHTGGPR-----FTIGPRTV-VLDEDGNPVEPGSGEIGWIARRGhIPLGYYKDPEKTAE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 849 KFlpdpFGPPGTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVRED-RPGDlRLV 927
Cdd:PRK07798 400 TF----PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDeRWGQ-EVV 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 653678460 928 AYVIPDGPVAPD--ALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLD 973
Cdd:PRK07798 475 AVVQLREGARPDlaELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
491-977 |
2.60e-33 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 137.96 E-value: 2.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 491 ASLRERFQQWCRRTPGAVAVI-EGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYL 569
Cdd:PRK06087 23 ASLADYWQQTARAMPDKIAVVdNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 570 PIDPDFPVERIAYLLS--------------DARPVLVVTD----------AATADRLGPDdiTGLVVLEETDTGGYPATE 625
Cdd:PRK06087 103 PLLPSWREAELVWVLNkcqakmffaptlfkQTRPVDLILPlqnqlpqlqqIVGVDKLAPA--TSSLSLSQIIADYEPLTT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 626 PPAVPAGHSAYVIYTSGSTGRPKGVVITRaalDNFLA---AMAERFPLTAEDRVLATTTVSFDIAGLE-LYLPLRSGAGV 701
Cdd:PRK06087 181 AITTHGDELAAVLFTSGTEGLPKGVMLTH---NNILAserAYCARLNLTWQDVFMMPAPLGHATGFLHgVTAPFLIGARS 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 702 VLADadtARNPAALIDLAGRHRVTLAQ-ATPTLWQALVP-ELSGPALAGIRV-LVGGEALPAELARRLGDAGAEVTNMYG 778
Cdd:PRK06087 258 VLLD---IFTPDACLALLEQQRCTCMLgATPFIYDLLNLlEKQPADLSALRFfLCGGTTIPKKVARECQQRGIKLLSVYG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 779 PTETTIWSTSGPtsEDSIRR--GSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFg 856
Cdd:PRK06087 335 STESSPHAVVNL--DDPLSRfmHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGW- 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 857 ppgtrmYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVRED-RPGDlRLVAYVIPDGP 935
Cdd:PRK06087 412 ------YYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDeRLGE-RSCAYVVLKAP 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 653678460 936 VAPDALRTELS----RTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:PRK06087 485 HHSLTLEEVVAffsrKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
502-977 |
4.33e-33 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 137.11 E-value: 4.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 502 RRTPGAVAVIE------GDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDF 575
Cdd:PRK13295 35 ASCPDKTAVTAvrlgtgAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 576 PVERIAYLLSDARP-VLVVTD-------AATADRLGPD--DITGLVVLEETDTGGYPA--TEP--------PAVPAGHS- 634
Cdd:PRK13295 115 RERELSFMLKHAESkVLVVPKtfrgfdhAAMARRLRPElpALRHVVVVGGDGADSFEAllITPaweqepdaPAILARLRp 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 635 -----AYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDRVLATTTVSFD---IAGLElyLPLRSGAGVVLADa 706
Cdd:PRK13295 195 gpddvTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQtgfMYGLM--MPVMLGATAVLQD- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 707 dtARNPAALIDLAGRHRVTLAQA-TPTLWQ-ALVPELSGPALAGIRV-LVGGEALPAELARRLGDA-GAEVTNMYGPTET 782
Cdd:PRK13295 272 --IWDPARAAELIRTEGVTFTMAsTPFLTDlTRAVKESGRPVSSLRTfLCAGAPIPGALVERARAAlGAKIVSAWGMTEN 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 783 TIWSTSGPTSEDSIRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEkflpDPFGppgtrM 862
Cdd:PRK13295 350 GAVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGT----DADG-----W 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 863 YRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIP------DGPV 936
Cdd:PRK13295 421 FDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPrpgqslDFEE 500
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 653678460 937 APDALRtelSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:PRK13295 501 MVEFLK---AQKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
498-974 |
5.40e-33 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 135.86 E-value: 5.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 498 QQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPV 577
Cdd:PRK03640 9 KQRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 578 ERIAYLLSDARPVLVVTDAATADRLGPDditGLVVLEETDTGGYPATEP-PAVPAGHSAYVIYTSGSTGRPKGVVITRAa 656
Cdd:PRK03640 89 EELLWQLDDAEVKCLITDDDFEAKLIPG---ISVKFAELMNGPKEEAEIqEEFDLDEVATIMYTSGTTGKPKGVIQTYG- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 657 lDNFLAAM--AERFPLTAEDRVLATTTVsFDIAGLELYlpLRS---GAGVVLADadtARNPAALIDLAGRHRVTLAQATP 731
Cdd:PRK03640 165 -NHWWSAVgsALNLGLTEDDCWLAAVPI-FHISGLSIL--MRSviyGMRVVLVE---KFDAEKINKLLQTGGVTIISVVS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 732 TLWQALVPEL-SGPALAGIR-VLVGGEALPAELARRLGDAGAEVTNMYGPTET-----TIwstsgpTSEDSIRR-GSIGV 803
Cdd:PRK03640 238 TMLQRLLERLgEGTYPSSFRcMLLGGGPAPKPLLEQCKEKGIPVYQSYGMTETasqivTL------SPEDALTKlGSAGK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 804 PIDNTQVYVLDaNLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgppgtrmyRTGDLVRWSAAGDLEYLGRT 883
Cdd:PRK03640 312 PLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF--------KTGDIGYLDEEGFLYVLDRR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 884 DHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDR-----PgdlrlVAYVIPDGPVAPDALRTELSRTLPDYMIPAVI 958
Cdd:PRK03640 383 SDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDkwgqvP-----VAFVVKSGEVTEEELRHFCEEKLAKYKVPKRF 457
|
490
....*....|....*.
gi 653678460 959 VPVPDFPTTPNGKLDR 974
Cdd:PRK03640 458 YFVEELPRNASGKLLR 473
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
488-972 |
6.33e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 136.63 E-value: 6.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 488 LPAASLRERFQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLM-ERGAGAETFVAVLLPRSADLLVTLLAVIKAGA 566
Cdd:PRK08314 7 LPETSLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQqECGVRKGDRVLLYMQNSPQFVIAYYAILRANA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 567 AYLPIDPDFPVERIAYLLSDARPVLVVTDAATADRL----GPDDITGLVVLEETDT----GGYP-----ATEPPAVPAGH 633
Cdd:PRK08314 87 VVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVapavGNLRLRHVIVAQYSDYlpaePEIAvpawlRAEPPLQALAP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 634 SAYVI-------------------------YTSGSTGRPKGVVIT-RAALDNFLAAmAERFPLTAEDRVLATTTVsFDIA 687
Cdd:PRK08314 167 GGVVAwkealaaglappphtagpddlavlpYTSGTTGVPKGCMHThRTVMANAVGS-VLWSNSTPESVVLAVLPL-FHVT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 688 GLE--LYLPLRSGAGVVLA---DADTARnpaaliDLAGRHRVTLAQATPTLwqaLVPELSGPALAG-----IRVLVGG-E 756
Cdd:PRK08314 245 GMVhsMNAPIYAGATVVLMprwDREAAA------RLIERYRVTHWTNIPTM---VVDFLASPGLAErdlssLRYIGGGgA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 757 ALPAELARRLGDA-GAEVTNMYGPTETTIWSTSGPTseDSIRRGSIGVPIDNTQVYVLD-ANLHPAPIGVLGELHIAGEG 834
Cdd:PRK08314 316 AMPEAVAERLKELtGLDYVEGYGLTETMAQTHSNPP--DRPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 835 LARGYWNRPGLTAEKFLP-DpfgppGTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAA 913
Cdd:PRK08314 394 VFKGYWNRPEATAEAFIEiD-----GKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEAC 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 653678460 914 AV-VREDRPGDlRLVAYVIPD----GPVAPDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKL 972
Cdd:PRK08314 469 VIaTPDPRRGE-TVKAVVVLRpearGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
507-972 |
1.13e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 135.03 E-value: 1.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 507 AVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSD 586
Cdd:PRK08276 2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 587 ARPVLVVTDAATAD------RLGPDDITGLVVLEETDTG---------GYPATEPPAVPAGhsAYVIYTSGSTGRPKGVV 651
Cdd:PRK08276 82 SGAKVLIVSAALADtaaelaAELPAGVPLLLVVAGPVPGfrsyeealaAQPDTPIADETAG--ADMLYSSGTTGRPKGIK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 652 ITR------AALDNFLAAMAERFPLTAEDRVLATTTvsfdiagleLY--LPLRSGAG-------VVLADADTARNPAALI 716
Cdd:PRK08276 160 RPLpgldpdEAPGMMLALLGFGMYGGPDSVYLSPAP---------LYhtAPLRFGMSalalggtVVVMEKFDAEEALALI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 717 DlagRHRVTLAQATPTLWQ---ALVPEL-SGPALAGIRVLVGGEA-LPAELARRLGD-AGAEVTNMYGPTE----TTIws 786
Cdd:PRK08276 231 E---RYRVTHSQLVPTMFVrmlKLPEEVrARYDVSSLRVAIHAAApCPVEVKRAMIDwWGPIIHEYYASSEgggvTVI-- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 787 tsgpTSEDSIRR-GSIGVPIDnTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDpfgppgtrmyrt 865
Cdd:PRK08276 306 ----TSEDWLAHpGSVGKAVL-GEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPH------------ 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 866 gdlvRWSAAGDLEYL---------GRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAV-VREDRPGDlRLVAYVIP-DG 934
Cdd:PRK08276 369 ----GWVTVGDVGYLdedgylyltDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFgVPDEEMGE-RVKAVVQPaDG 443
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 653678460 935 PVAPDALRTELSRTLPD----YMIPAVIVPVPDFPTTPNGKL 972
Cdd:PRK08276 444 ADAGDALAAELIAWLRGrlahYKCPRSIDFEDELPRTPTGKL 485
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1552-2029 |
4.42e-32 |
|
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: 133.11 E-value: 4.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1552 TGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMARLTRIADT 1631
Cdd:cd05911 6 DTGKELTYAQLRTLSRRLAAGLR--KLG---LKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1632 VTPALVLT--------RTGQGGCLPGAEVF-------GDVPVVALDRVADrLTAMPDQRPEVTVDPRGLAYSIFTSGSTG 1696
Cdd:cd05911 81 SKPKVIFTdpdglekvKEAAKELGPKDKIIvlddkpdGVLSIEDLLSPTL-GEEDEDLPPPLKDGKDDTAAILYSSGTTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1697 QPKGVAVEHIGIVRYLSWAAASYPTAGRRG-------TLAHSSvGFDLTMSALFeplvsgRGVTL--MPA--DATLADLA 1765
Cdd:cd05911 160 LPKGVCLSHRNLIANLSQVQTFLYGNDGSNdvilgflPLYHIY-GLFTTLASLL------NGATViiMPKfdSELFLDLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1766 EELSGPLAYdyirLTPSHLRHLVGHwtgqELPPAA-----RGWVVGGETLDPALVKQLLELRPDAEVINHYGPTETVIGR 1840
Cdd:cd05911 233 EKYKITFLY----LVPPIAAALAKS----PLLDKYdlsslRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGIL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1841 VVHPVREAGELAVDSPLPLgrplgeTRLQVLDaWL--EAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDpagepga 1918
Cdd:cd05911 305 TVNPDGDDKPGSVGRLLPN------VEAKIVD-DDgkDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDED------- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1919 RMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVV----LVRDQQLVGWFIPAEDHPPVTV 1994
Cdd:cd05911 371 GWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVigipDEVSGELPRAYVVRKPGEKLTE 450
|
490 500 510
....*....|....*....|....*....|....*....
gi 653678460 1995 SALRRFCAEQLPEFmvpNQW----VALDAFPLTPHGKVN 2029
Cdd:cd05911 451 KEVKDYVAKKVASY---KQLrggvVFVDEIPKSASGKIL 486
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
503-977 |
6.17e-32 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 133.58 E-value: 6.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 503 RTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAylPIDPDFPVERIAy 582
Cdd:PRK10946 35 AASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNALFSHQRSE- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 583 LLSDAR---PVLVVTDAATA--------DRLGPDDITGLVVLEETDTGGY--------PATEPPA--VPAGHSAYVIYTS 641
Cdd:PRK10946 112 LNAYASqiePALLIADRQHAlfsdddflNTLVAEHSSLRVVLLLNDDGEHslddainhPAEDFTAtpSPADEVAFFQLSG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 642 GSTGRPKgvVITRAALDNFLA--AMAERFPLTAEDRVLATTTVSFDiaglelyLPLRS-GA-GVVLADADT--ARNPAAL 715
Cdd:PRK10946 192 GSTGTPK--LIPRTHNDYYYSvrRSVEICGFTPQTRYLCALPAAHN-------YPMSSpGAlGVFLAGGTVvlAPDPSAT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 716 I--DLAGRHRVTLAQATP---TLW-QALVPELSGPALAGIRVL-VGGEALPAELARRLGDA-GAEVTNMYGPTETTIWST 787
Cdd:PRK10946 263 LcfPLIEKHQVNVTALVPpavSLWlQAIAEGGSRAQLASLKLLqVGGARLSETLARRIPAElGCQLQQVFGMAEGLVNYT 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 788 SGPTSEDSIrRGSIGVPI-DNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgppgtrmYRTG 866
Cdd:PRK10946 343 RLDDSDERI-FTTQGRPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF-------YCSG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 867 DLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIPDGPVAPDALRTEL- 945
Cdd:PRK10946 415 DLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKAVQLRRFLr 494
|
490 500 510
....*....|....*....|....*....|..
gi 653678460 946 SRTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:PRK10946 495 EQGIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
491-977 |
6.94e-31 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 129.61 E-value: 6.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 491 ASLRERFQqwcrrTPGAVAVIEGD-TTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYL 569
Cdd:PRK07514 7 DALRAAFA-----DRDAPFIETPDgLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 570 PIDPDFPVERIAYLLSDARPVLVVTDAATADRLGP--------------DDITGlvVLEETDTGGYPATEPPAVPAGHSA 635
Cdd:PRK07514 82 PLNTAYTLAELDYFIGDAEPALVVCDPANFAWLSKiaaaagaphvetldADGTG--SLLEAAAAAPDDFETVPRGADDLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 636 YVIYTSGSTGRPKGVVITRaalDNFLA---AMAERFPLTAEDRVLATTTVsFDIAGL--ELYLPLRSGAGVV-LADADta 709
Cdd:PRK07514 160 AILYTSGTTGRSKGAMLSH---GNLLSnalTLVDYWRFTPDDVLIHALPI-FHTHGLfvATNVALLAGASMIfLPKFD-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 710 rnPAALIDLagrhrvtLAQAT-----PTLWQALV--PELSGPALAGIRVLVGGEA-LPAELAR----RLGDAGAEvtnMY 777
Cdd:PRK07514 234 --PDAVLAL-------MPRATvmmgvPTFYTRLLqePRLTREAAAHMRLFISGSApLLAETHRefqeRTGHAILE---RY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 778 GPTETTIwSTSGPTseDSIRR-GSIGVPIDNTQVYVLD-ANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPF 855
Cdd:PRK07514 302 GMTETNM-NTSNPY--DGERRaGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 856 gppgtrmYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIEtTLINAGPVRRAAAVVREDRPgDL--RLVAYVI-- 931
Cdd:PRK07514 379 -------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVE-GEIDELPGVVESAVIGVPHP-DFgeGVTAVVVpk 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 653678460 932 PDGPVAPDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:PRK07514 450 PGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
1684-2033 |
9.25e-31 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 125.52 E-value: 9.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1684 GLAYSIFTSGSTGQPKGVAvehigivryLSWAAAsypTAGRRGTlaHSSVGFDLTMSALFE-PL--VSGRGVTL------ 1754
Cdd:cd17630 1 RLATVILTSGSTGTPKAVV---------HTAANL---LASAAGL--HSRLGFGGGDSWLLSlPLyhVGGLAILVrsllag 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1755 -MPADATLADLAEELSGPLAYDYIRLTPSHLRHLVGHWTGQELPPAARGWVVGGETLDPALVKQLLELRpdAEVINHYGP 1833
Cdd:cd17630 67 aELVLLERNQALAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADRG--IPLYTTYGM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1834 TETVIGRVVHPVREAGELAVdsplplGRPLGETRLQVLDAwleavpvgavGELFIGGDGIARGYLGRPaltaekfLPDPA 1913
Cdd:cd17630 145 TETASQVATKRPDGFGRGGV------GVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQ-------LVPEF 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1914 GEPGarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVL-VRD----QQLVGWFipaED 1988
Cdd:cd17630 202 NEDG--WFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVgVPDeelgQRPVAVI---VG 276
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 653678460 1989 HPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:cd17630 277 RGPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
1556-2028 |
2.02e-30 |
|
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: 127.11 E-value: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1556 SLTFAGLDAQANRLAHALhtGALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMARLTRIADTVTPA 1635
Cdd:cd05903 1 RLTYSELDTRADRLAAGL--AALG---VGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1636 LVLTrtgqggclpgAEVFGdvpvvaldrvADRLTAMPDQrpevtvdprgLAYSIFTSGSTGQPKGVAVEHIGIVRYLSWA 1715
Cdd:cd05903 76 VFVV----------PERFR----------QFDPAAMPDA----------VALLLFTSGTTGEPKGVMHSHNTLSASIRQY 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1716 AASYPTAGRRGTLAHSSVG-FDLTMSALFEPLVSGRGVTLMP---ADATLADLAEE------LSGPLAYDYIRL---TPS 1782
Cdd:cd05903 126 AERLGLGPGDVFLVASPMAhQTGFVYGFTLPLLLGAPVVLQDiwdPDKALALMREHgvtfmmGATPFLTDLLNAveeAGE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1783 HLRHLvghwtgqelppaaRGWVVGGETLDPALVKQLLELRpDAEVINHYGPTETV-IGRVVHPVREAGELAVDsplplGR 1861
Cdd:cd05903 206 PLSRL-------------RTFVCGGATVPRSLARRAAELL-GAKVCSAYGSTECPgAVTSITPAPEDRRLYTD-----GR 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1862 PLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFlpdPAGepgarMYRTGDLVRWRGDGLLDFVGRV 1941
Cdd:cd05903 267 PLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAA---PEG-----WFRTGDLARLDEDGYLRITGRS 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1942 DDQVKLRGYRIELGEIEARMAEHPGV-EQAVVLVRDQQL---VGWFIPAEDHPPVTVSALRRFC-AEQLPEFMVPNQWVA 2016
Cdd:cd05903 339 KDIIIRGGENIPVLEVEDLLLGHPGViEAAVVALPDERLgerACAVVVTKSGALLTFDELVAYLdRQGVAKQYWPERLVH 418
|
490
....*....|..
gi 653678460 2017 LDAFPLTPHGKV 2028
Cdd:cd05903 419 VDDLPRTPSGKV 430
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1530-2033 |
6.32e-30 |
|
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: 127.18 E-value: 6.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1530 DRTVHQLVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKA 1609
Cdd:COG1021 24 GETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLL--ALG---LRPGDRVVVQLPNVAEFVIVFFALFRA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1610 GgyFIPVD--PGYPMARLTRIADTVTPALVLTRTGQGG------------CLPGAE---VFGDV-PVVALDRvadrLTAM 1671
Cdd:COG1021 99 G--AIPVFalPAHRRAEISHFAEQSEAVAYIIPDRHRGfdyralarelqaEVPSLRhvlVVGDAgEFTSLDA----LLAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1672 PDQRPEVTVDPRGLAYSIFTSGSTGQPKGVAVEH---IGIVRYLswAAASYPTAGRRgTLAHSSVGFDLTMS---ALFEP 1745
Cdd:COG1021 173 PADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHddyLYSVRAS--AEICGLDADTV-YLAALPAAHNFPLSspgVLGVL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1746 LVSGRGVtlmpadatladLAEELSGPLAYDYIRltpshlRH------LVghwtgqelPPAARGWV--------------- 1804
Cdd:COG1021 250 YAGGTVV-----------LAPDPSPDTAFPLIE------RErvtvtaLV--------PPLALLWLdaaersrydlsslrv 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1805 --VGGETLDPALVKQLLEL-------------------RPDAevinhygPTETVIGRVVHPVREAGE-LAVDsplPLGRP 1862
Cdd:COG1021 305 lqVGGAKLSPELARRVRPAlgctlqqvfgmaeglvnytRLDD-------PEEVILTTQGRPISPDDEvRIVD---EDGNP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1863 lgetrlqvldawleaVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDpagepGarMYRTGDLVRWRGDGLLDFVGRVD 1942
Cdd:COG1021 375 ---------------VPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPD-----G--FYRTGDLVRRTPDGYLVVEGRAK 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1943 DQVKLRGYRIELGEIEARMAEHPGVEQ-AVVLVRDQQL---VGWFIPAEDHPPvTVSALRRFCAEQ-LPEFMVPNQWVAL 2017
Cdd:COG1021 433 DQINRGGEKIAAEEVENLLLAHPAVHDaAVVAMPDEYLgerSCAFVVPRGEPL-TLAELRRFLRERgLAAFKLPDRLEFV 511
|
570
....*....|....*.
gi 653678460 2018 DAFPLTPHGKVNHRAL 2033
Cdd:COG1021 512 DALPLTAVGKIDKKAL 527
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
81-370 |
6.71e-30 |
|
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: 125.29 E-value: 6.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 81 LDVDALRAALDAVTARHEALRTVFrlGPDGEpvQQTAPAAP-VALPVIDVTEADLPQALRTAAE-------QPFDLERGP 152
Cdd:cd19535 37 LDPDRLERAWNKLIARHPMLRAVF--LDDGT--QQILPEVPwYGITVHDLRGLSEEEAEAALEElrerlshRVLDVERGP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 153 LLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLLLADLARAYAG---ELPAgvAAPAFRD-VAAWQHGRLAAGELDdqLRY 228
Cdd:cd19535 113 LFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYEDpgePLPP--LELSFRDyLLAEQALRETAYERA--RAY 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 229 WRQRLAGL---PDLEIpgdRQRPADRDwRAHSVRRE--LPAATEAAVRRLAAAHDTTPFTVLLAAYGTFLHRLTGQDDFA 303
Cdd:cd19535 189 WQERLPTLppaPQLPL---AKDPEEIK-EPRFTRREhrLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRFL 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 653678460 304 VGVPVAGR--GRTDLESVVGLFAGMVPVRLDLTGRPSFDEVLSRTVAGSRNDFAHPQIPFDRLVRELRR 370
Cdd:cd19535 265 LNLTLFNRlpLHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQLWEDLDHSSYSGVVVVRRLLR 333
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1548-2033 |
1.12e-29 |
|
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: 124.88 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1548 TALRTGDRSLTFAGLDAQANRLAHALHTgaLGappVGPETPVLLLLDRSPELVVAMLAVLKAGGyfipvdpgypmarltr 1627
Cdd:cd05919 2 TAFYAADRSVTYGQLHDGANRLGSALRN--LG---VSSGDRVLLLMLDSPELVQLFLGCLARGA---------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1628 iadtvtpalvltrtgqggclpgaevfgdVPVVA--LDRVADRLTAMPDQRPE-VTVDPRGLAYSIFTSGSTGQPKGVAVE 1704
Cdd:cd05919 61 ----------------------------IAVVInpLLHPDDYAYIARDCEARlVVTSADDIAYLLYSSGTTGPPKGVMHA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1705 H---IGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMSALFePLVSGRGVTLMP----ADATLADLAEE-----LSGPL 1772
Cdd:cd05919 113 HrdpLLFADAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWF-PLAVGASAVLNPgwptAERVLATLARFrptvlYGVPT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1773 AYDYIRLTPSHLRHLVGhwtgqelppAARGWVVGGETLDPALVKQLLELRpDAEVINHYGPTETVIgrvVHPVREAGELA 1852
Cdd:cd05919 192 FYANLLDSCAGSPDALR---------SLRLCVSAGEALPRGLGERWMEHF-GGPILDGIGATEVGH---IFLSNRPGAWR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1853 VDSplpLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFlpdpAGEpgarMYRTGDLVRWRGD 1932
Cdd:cd05919 259 LGS---TGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF----NGG----WYRTGDKFCRDAD 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1933 GLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGV-EQAVVLVRDQ----QLVGWFIPAEDHPP--VTVSALRRFCAEQL 2005
Cdd:cd05919 328 GWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVaEAAVVAVPEStglsRLTAFVVLKSPAAPqeSLARDIHRHLLERL 407
|
490 500
....*....|....*....|....*...
gi 653678460 2006 PEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:cd05919 408 SAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
45-331 |
1.55e-29 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 129.90 E-value: 1.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 45 GPVPLAPGQAgiWFSEQLRPGTPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVFRLGPDGEPVQQTAPAAPVAL 124
Cdd:PRK05691 2790 GASGLTPIQH--WFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGRWQAEYRAVTAQELL 2867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 125 PVIDVTEADLPQALRTAAEQPFDLERGPLLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLLLADLARAY-AGELPAGVAA 203
Cdd:PRK05691 2868 WQVTVADFAECAALFADAQRSLDLQQGPLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYrQLSAGAEPAL 2947
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 204 PA----FRDVAAWQHGRLAAGELDDQLRYWRQRLAGlPDLEIPGDRQRPADRDWRAHSVRREL-PAATEAAVRRLAAAHD 278
Cdd:PRK05691 2948 PAktsaFRDWAARLQAYAGSESLREELGWWQAQLGG-PRAELPCDRPQGGNLNRHAQTVSVRLdAERTRQLLQQAPAAYR 3026
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 653678460 279 TTPFTVLLAAYGTFLHRLTGQDdfAVGVPVAGRGR------TDLESVVGLFAGMVPVRL 331
Cdd:PRK05691 3027 TQVNDLLLTALARVLCRWSGQP--SVLVQLEGHGRealfddIDLTRSVGWFTSAYPLRL 3083
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
516-977 |
1.77e-29 |
|
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: 123.61 E-value: 1.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 516 TLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARPVLvvtd 595
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 596 aatadrlgpDDItglvvleetdtggypateppavpaghsAYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDR 675
Cdd:cd05912 77 ---------DDI---------------------------ATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDN 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 676 VLATTTVsFDIAGLELYlpLRS---GAGVVLADADTARNPAALIDlagRHRVTLAQATPTLWQALVPELSGPALAGIR-V 751
Cdd:cd05912 121 WLCALPL-FHISGLSIL--MRSviyGMTVYLVDKFDAEQVLHLIN---SGKVTIISVVPTMLQRLLEILGEGYPNNLRcI 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 752 LVGGEALPAELARRLGDAGAEVTNMYGPTETTIWSTSGPTSEDSIRRGSIGVPIDNTQVYVLDANLHPAPIgvlGELHIA 831
Cdd:cd05912 195 LLGGGPAPKPLLEQCKEKGIPVYQSYGMTETCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPPYEV---GEILLK 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 832 GEGLARGYWNRPGLTAEKFLPDPFgppgtrmyRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRR 911
Cdd:cd05912 272 GPNVTKGYLNRPDATEESFENGWF--------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKE 343
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 653678460 912 AAAVVREDRPGDLRLVAYVIPDGPVAPDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:cd05912 344 AGVVGIPDDKWGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
1557-2033 |
2.42e-29 |
|
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: 123.60 E-value: 2.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1557 LTFAGLDAQANRLAHALHTGALGAPPVgpetpVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGY-PMARLTRIADTVTPA 1635
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDR-----VAVLLPRVPELWAVILAVIKLGAVYVPLTTLLgPKDIEYRLEAAGAKA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1636 LVltrtgqggclpgaevfgdvpvvaldrvadrltampdqrpevtVDPRGLAYSIFTSGSTGQPKGVAVEHigivrylSWA 1715
Cdd:cd05972 76 IV------------------------------------------TDAEDPALIYFTSGTTGLPKGVLHTH-------SYP 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1716 AASYPTAGRRGTLAHSSVGFDL--------TMSALFEPLVSGRGVTLMPADATLADLAEELSGPLAYDYIRLTPSHLRHL 1787
Cdd:cd05972 107 LGHIPTAAYWLGLRPDDIHWNIadpgwakgAWSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRML 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1788 VGHWTGQELPPAARGWVVGGETLDPALVKQLLElRPDAEVINHYGPTETVIGRVVHPVREAgelavdSPLPLGRPLGETR 1867
Cdd:cd05972 187 IKQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRA-ATGLPIRDGYGQTETGLTVGNFPDMPV------KPGSMGRPTPGYD 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1868 LQVLDAWLEAVPVGAVGELFI--GGDGIARGYLGRPALTAEKFLPDpagepgarMYRTGDLVRWRGDGLLDFVGRVDDQV 1945
Cdd:cd05972 260 VAIIDDDGRELPPGEEGDIAIklPPPGLFLGYVGDPEKTEASIRGD--------YYLTGDRAYRDEDGYFWFVGRADDII 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1946 KLRGYRIELGEIEARMAEHPGV-EQAVVLVRDQ---QLVGWFI---PAEDHPPVTVSALRRFCAEQLPEFMVPNQWVALD 2018
Cdd:cd05972 332 KSSGYRIGPFEVESALLEHPAVaEAAVVGSPDPvrgEVVKAFVvltSGYEPSEELAEELQGHVKKVLAPYKYPREIEFVE 411
|
490
....*....|....*
gi 653678460 2019 AFPLTPHGKVNHRAL 2033
Cdd:cd05972 412 ELPKTISGKIRRVEL 426
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
505-971 |
2.96e-29 |
|
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: 124.33 E-value: 2.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 505 PGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLL 584
Cdd:cd12118 18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 585 SDARPVLVVTDAATAdrlgpdditglvvLEETDTGGYPatEPPAVPAGHSAYVI---YTSGSTGRPKGVVIT-RAAldnF 660
Cdd:cd12118 98 RHSEAKVLFVDREFE-------------YEDLLAEGDP--DFEWIPPADEWDPIalnYTSGTTGRPKGVVYHhRGA---Y 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 661 LAAMAerfpltaedrvlatTTVSFDIAGLELYL---PL--------------RSGAGVVLADADtarnPAALIDLAGRHR 723
Cdd:cd12118 160 LNALA--------------NILEWEMKQHPVYLwtlPMfhcngwcfpwtvaaVGGTNVCLRKVD----AKAIYDLIEKHK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 724 VTLAQATPTLWQALV---PELSGPALAGIRVLVGGEALPAELARRLGDAGAEVTNMYGPTETT------IWS---TSGPT 791
Cdd:cd12118 222 VTHFCGAPTVLNMLAnapPSDARPLPHRVHVMTAGAPPPAAVLAKMEELGFDVTHVYGLTETYgpatvcAWKpewDELPT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 792 SEDSIRRGSIGVP-IDNTQVYVLDANLH---PAPIGVLGELHIAGEGLARGYWNRPGLTAEKFlpdpfgppgtR--MYRT 865
Cdd:cd12118 302 EERARLKARQGVRyVGLEEVDVLDPETMkpvPRDGKTIGEIVFRGNIVMKGYLKNPEATAEAF----------RggWFHS 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 866 GDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVI--PDGPVAPDALRT 943
Cdd:cd12118 372 GDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVElkEGAKVTEEEIIA 451
|
490 500
....*....|....*....|....*...
gi 653678460 944 ELSRTLPDYMIPAVIVpVPDFPTTPNGK 971
Cdd:cd12118 452 FCREHLAGFMVPKTVV-FGELPKTSTGK 478
|
|
| Thioesterase |
pfam00975 |
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ... |
2157-2311 |
4.40e-29 |
|
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Pssm-ID: 395776 [Multi-domain] Cd Length: 223 Bit Score: 117.49 E-value: 4.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 2157 RPVFCVHPSGGGVAWYLPLARALPAGHPVHAFQPLGMDGREAPAETIEDMAAGYLADLRLVQPEGPYVVVGWSLGGTIAF 2236
Cdd:pfam00975 1 RPLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEPPLNSIEALADEYAEALRQIQPEGPYALFGHSMGGMLAF 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 653678460 2237 EMARQLDRLGEPVQ-LILLEPTLPEVARTIDLHRPARDSYLrgaDLAERILRLPAGDPEGDRLRAELTRLLEDAGY 2311
Cdd:pfam00975 81 EVARRLERQGEAVRsLFLSDASAPHTVRYEASRAPDDDEVV---AEFTDEGGTPEELLEDEELLSMLLPALRADYR 153
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1529-1988 |
6.66e-29 |
|
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: 123.88 E-value: 6.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1529 DDRTVHQLVEAQADRTPGWTAL---RTGdRSLTFAGLDAQANRLAHALHTGALGAPPVgpetpVLLLLDRSPELVVAMLA 1605
Cdd:cd05904 3 TDLPLDSVSFLFASAHPSRPALidaATG-RALTYAELERRVRRLAAGLAKRGGRKGDV-----VLLLSPNSIEFPVAFLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1606 VLKAGGYFIPVDPGYPMARLTRIADTVTPALVLTRTGQGGCLPGAevfgDVPVVALDRVADRLTAM--------PDQRPE 1677
Cdd:cd05904 77 VLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLASL----ALPVVLLDSAEFDSLSFsdllfeadEAEPPV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1678 VTVDPRGLAYSIFTSGSTGQPKGVAVEHIGIVrylswAAASYPTAGRRGTLAHSSV-----------GFDLTMSALfepL 1746
Cdd:cd05904 153 VVIKQDDVAALLYSSGTTGRSKGVMLTHRNLI-----AMVAQFVAGEGSNSDSEDVflcvlpmfhiyGLSSFALGL---L 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1747 VSGRGVTLMPAdatlADLAEELSGPLAYD--YIRLTPSHLRHLVGHWTGQELP-PAARGWVVGGETLDPALVKQLLELRP 1823
Cdd:cd05904 225 RLGATVVVMPR----FDLEELLAAIERYKvtHLPVVPPIVLALVKSPIVDKYDlSSLRQIMSGAAPLGKELIEAFRAKFP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1824 DAEVINHYGPTETVIGRVVHPVREAGELAVDSplpLGRPLGETRLQVLD-AWLEAVPVGAVGELFIGGDGIARGYLGRPA 1902
Cdd:cd05904 301 NVDLGQGYGMTESTGVVAMCFAPEKDRAKYGS---VGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1903 LTAEKFLPDpagepgaRMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVlvrdqqlvgw 1982
Cdd:cd05904 378 ATAATIDKE-------GWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAV---------- 440
|
....*.
gi 653678460 1983 fIPAED 1988
Cdd:cd05904 441 -IPYPD 445
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
516-977 |
8.33e-29 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 122.57 E-value: 8.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 516 TLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARPVLVVtd 595
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 596 aatadrlgpdditglvvleetdtgGYPATEPPAVpaghsayVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDR 675
Cdd:cd05910 80 ------------------------GIPKADEPAA-------ILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 676 VLATttvsFDIAGleLYLPLRsGAGVVLADADTAR----NPAALIDLAGRHRVTLAQATPTLWQALVP--ELSGPALAGI 749
Cdd:cd05910 129 DLAT----FPLFA--LFGPAL-GLTSVIPDMDPTRparaDPQKLVGAIRQYGVSIVFGSPALLERVARycAQHGITLPSL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 750 R-VLVGGEALPAELARRLGDA---GAEVTNMYGPTET----------TIWSTSGPTSEDsirRGS-IGVPIDNTQVYVLD 814
Cdd:cd05910 202 RrVLSAGAPVPIALAARLRKMlsdEAEILTPYGATEAlpvssigsreLLATTTAATSGG---AGTcVGRPIPGVRVRIIE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 815 ANLHP---------APIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDpfgPPGTRMYRTGDLVRWSAAGDLEYLGRTDH 885
Cdd:cd05910 279 IDDEPiaewddtleLPRGEIGEITVTGPTVTPTYVNRPVATALAKIDD---NSEGFWHRMGDLGYLDDEGRLWFCGRKAH 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 886 QVKLRGFRIELGEIEtTLINAGPVRRAAAVVREDRPGDLRLVAYVIPDGPVAPDA--LRTELSRTLPDYMIPAVIVPV-- 961
Cdd:cd05910 356 RVITTGGTLYTEPVE-RVFNTHPGVRRSALVGVGKPGCQLPVLCVEPLPGTITPRarLEQELRALAKDYPHTQRIGRFli 434
|
490
....*....|....*....
gi 653678460 962 -PDFPTTP--NGKLDRAAL 977
Cdd:cd05910 435 hPSFPVDIrhNAKIFREKL 453
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
487-974 |
8.51e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 124.34 E-value: 8.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 487 PLPAASLRERFQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGA 566
Cdd:PRK05605 28 DYGDTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 567 AYLPIDPDFPVERIAYLLSD--ARpVLVVTD--AATADRLGPDdiTGL---VVLEETD---------------------- 617
Cdd:PRK05605 108 VVVEHNPLYTAHELEHPFEDhgAR-VAIVWDkvAPTVERLRRT--TPLetiVSVNMIAampllqrlalrlpipalrkara 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 618 --TGGYPATEP------------------PAVPAGHSAYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAED--R 675
Cdd:PRK05605 185 alTGPAPGTVPwetlvdaaiggdgsdvshPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVPGLGDGpeR 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 676 VLATTTVsFDIAGLELYLPLRS--GAGVVLAdadtarnPAALIDL----AGRHRVTLAQATPTLWQALV--PELSGPALA 747
Cdd:PRK05605 265 VLAALPM-FHAYGLTLCLTLAVsiGGELVLL-------PAPDIDLildaMKKHPPTWLPGVPPLYEKIAeaAEERGVDLS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 748 GIRV-LVGGEALPAELARRLGDA-GAEVTNMYGPTETTIWSTSGPTSEDSiRRGSIGVPIDNTQVYVLDANlHPA---PI 822
Cdd:PRK05605 337 GVRNaFSGAMALPVSTVELWEKLtGGLLVEGYGLTETSPIIVGNPMSDDR-RPGYVGVPFPDTEVRIVDPE-DPDetmPD 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 823 GVLGELHIAGEGLARGYWNRPGLTAEKFLPDpfgppgtrMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETT 902
Cdd:PRK05605 415 GEEGELLVRGPQVFKGYWNRPEETAKSFLDG--------WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEV 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 653678460 903 LINAGPVRRAAAVVREDRPGDLRLVAYVIPDGPVA--PDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDR 974
Cdd:PRK05605 487 LREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAAldPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRR 560
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
1552-2028 |
8.87e-29 |
|
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: 124.61 E-value: 8.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1552 TGDRSLTFAGLDAQANRLAhalhtGALGAPPVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGY-PMARLTRIAD 1630
Cdd:cd17634 80 SQSRTISYRELHREVCRFA-----GTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFaPEAVAGRIID 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1631 TVTPALVltrTGQGGCLPG------------AEVFGDVP--VVALDRVA--------------DRLTAMPDQRPEVTVDP 1682
Cdd:cd17634 155 SSSRLLI---TADGGVRAGrsvplkknvddaLNPNVTSVehVIVLKRTGsdidwqegrdlwwrDLIAKASPEHQPEAMNA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1683 RGLAYSIFTSGSTGQPKGVAVEHIGIVRYLSWAAAS-YPTAGRRGTLAHSSVGFDLTMSAL-FEPLVSG------RGVTL 1754
Cdd:cd17634 232 EDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYvFDYGPGDIYWCTADVGWVTGHSYLlYGPLACGattllyEGVPN 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1755 MPADATLADLAEE------LSGPLAY--------DYI-RLTPSHLRHLVGhwTGQELPPAARGW---VVGGETldpalvk 1816
Cdd:cd17634 312 WPTPARMWQVVDKhgvnilYTAPTAIralmaagdDAIeGTDRSSLRILGS--VGEPINPEAYEWywkKIGKEK------- 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1817 qllelRPdaeVINHYGPTETViGRVVHPVREAGELAVDSPLplgRPLGETRLQVLDAWLEAVPVGAVGELFIGGD--GIA 1894
Cdd:cd17634 383 -----CP---VVDTWWQTETG-GFMITPLPGAIELKAGSAT---RPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQT 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1895 RGYLGRPALTAEKFLPDPAGepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGV-EQAVVL 1973
Cdd:cd17634 451 RTLFGDHERFEQTYFSTFKG-----MYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVaEAAVVG 525
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 653678460 1974 VRD----QQLVGWFI--PAEDHPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKV 2028
Cdd:cd17634 526 IPHaikgQAPYAYVVlnHGVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
485-977 |
3.33e-28 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 122.31 E-value: 3.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 485 ARPLPAASlrerfqqwcRRTPGAVAVIEGDT----------TLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADL 554
Cdd:PRK09274 9 ARHLPRAA---------QERPDQLAVAVPGGrgadgklaydELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 555 LVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARP--VLVVTDAATADRL---GPDDITGLVVLEETD-TGGYPATEPPA 628
Cdd:PRK09274 80 FALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPdaFIGIPKAHLARRLfgwGKPSVRRLVTVGGRLlWGGTTLATLLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 629 VPAGHS-----------AYVIYTSGSTGRPKGVVITRaalDNFLA---AMAERFPLTAEDRVLATttvsfdiaglelyLP 694
Cdd:PRK09274 160 DGAAAPfpmadlapddmAAILFTSGSTGTPKGVVYTH---GMFEAqieALREDYGIEPGEIDLPT-------------FP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 695 LRS------GAGVVLADADTAR----NPAALIDLAGRHRVTLAQATPTLWQALVP--ELSGPALAGI-RVLVGGEALPAE 761
Cdd:PRK09274 224 LFAlfgpalGMTSVIPDMDPTRpatvDPAKLFAAIERYGVTNLFGSPALLERLGRygEANGIKLPSLrRVISAGAPVPIA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 762 LARRLGD---AGAEVTNMYGPTE----TTIWSTS--GPTSEDSIRRGSI--GVPIDNTQVYVLD---------ANLHPAP 821
Cdd:PRK09274 304 VIERFRAmlpPDAEILTPYGATEalpiSSIESREilFATRAATDNGAGIcvGRPVDGVEVRIIAisdapipewDDALRLA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 822 IGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFGppGTRmYRTGDLVRWSAAGDLEYLGRTDHQVKLRG---FRIELGE 898
Cdd:PRK09274 384 TGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDGQG--DVW-HRMGDLGYLDAQGRLWFCGRKAHRVETAGgtlYTIPCER 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 899 IettlINAGP-VRRAAAV-VREdrPGDLR--LVAYVIPDGPVAPDALRTELSRTLPDYMIPAVIVPV---PDFPTTP--N 969
Cdd:PRK09274 461 I----FNTHPgVKRSALVgVGV--PGAQRpvLCVELEPGVACSKSALYQELRALAAAHPHTAGIERFlihPSFPVDIrhN 534
|
....*...
gi 653678460 970 GKLDRAAL 977
Cdd:PRK09274 535 AKIFREKL 542
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
48-379 |
4.80e-28 |
|
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: 119.72 E-value: 4.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 48 PLAPGQAGIWFSEQLRPGTPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVFRLGPDGEPVQQTAPAAPVALPVI 127
Cdd:cd19547 3 PLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDLAPPWALL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 128 DVTEAD-------LPQALRTAAEQPFDLERGPLLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLLLADLARAYA----GE 196
Cdd:cd19547 83 DWSGEDpdrraelLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEelahGR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 197 LPAGVAAPAFRDVAAWQHGRLAAGelDDQLRYWRQRLAglpDLEIPGDRQRPADRDWRAHSVRRELPAATEAAVRRLAAA 276
Cdd:cd19547 163 EPQLSPCRPYRDYVRWIRARTAQS--EESERFWREYLR---DLTPSPFSTAPADREGEFDTVVHEFPEQLTRLVNEAARG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 277 HDTTPFTVLLAAYGTFLHRLTGQDDFAVGVPVAGRGR--TDLESVVGLFAGMVPVRLDLTGRPSFDEVLSRTVAGSRNDF 354
Cdd:cd19547 238 YGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPelEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDLATTA 317
|
330 340
....*....|....*....|....*
gi 653678460 355 AHPQIPFDRLVRELRRDRIAGSQLL 379
Cdd:cd19547 318 AHGHVPLAQIKSWASGERLSGGRVF 342
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
31-331 |
7.08e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 124.68 E-value: 7.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 31 QGPAhggglpvqpPGPVPLAPGQAgiWFSEQLRPGTPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVFRlGPDG 110
Cdd:PRK12316 1094 QGPA---------SGEVALAPVQR--WFFEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFR-EEDG 1161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 111 EpvQQTAPAAPVALPVI---DVTEADLPQALRTAAEQPFDLERGPLLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLLLA 187
Cdd:PRK12316 1162 G--WQQAYAAPQAGEVLwqrQAASEEELLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLE 1239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 188 DLARAYAGELPA-GVAAPAFRDVAAWQHGRlaAGELDDQLRYWRQRLAGLPDlEIPGDRQRPADRDWRAHSVRRELPAAT 266
Cdd:PRK12316 1240 DLQRAYADLDADlPARTSSYQAWARRLHEH--AGARAEELDYWQAQLEDAPH-ELPCENPDGALENRHERKLELRLDAER 1316
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 653678460 267 EAAVRRLA-AAHDTTPFTVLLAAYGTFLHRLTGQDdfAVGVPVAGRGR------TDLESVVGLFAGMVPVRL 331
Cdd:PRK12316 1317 TRQLLQEApAAYRTQVNDLLLTALARVTCRWSGQA--SVLVQLEGHGRedlfedIDLSRTVGWFTSLFPVRL 1386
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
1531-2033 |
1.27e-27 |
|
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: 119.54 E-value: 1.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1531 RTVHQLVEAQADRTPGWTALRTGDRS--LTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLK 1608
Cdd:cd05923 1 QTVFEMLRRAASRAPDACAIADPARGlrLTYSELRARIEAVAARLH--ARG---LRPGQRVAVVLPNSVEAVIALLALHR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1609 AGGYFIPVDPgypMARLTRIADTVTPALVLTRTGQGGCLPGAEVF-GDVPVVAL-DRVADR-------LTAMPDQRPEVT 1679
Cdd:cd05923 76 LGAVPALINP---RLKAAELAELIERGEMTAAVIAVDAQVMDAIFqSGVRVLALsDLVGLGepesagpLIEDPPREPEQP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1680 vdprglAYSIFTSGSTGQPKGVAVEHIGIV-RYLSWAAASYPTAGRRGTLA-----HSSVGFdltmSALFEPLVSGRGVT 1753
Cdd:cd05923 153 ------AFVFYTSGTTGLPKGAVIPQRAAEsRVLFMSTQAGLRHGRHNVVLglmplYHVIGF----FAVLVAALALDGTY 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1754 LMPADATLADlAEELSGPLAYDYIRLTPSHLRHLVGHWTGQELP-PAARGWVVGGETLDPALVKQLLELRPdAEVINHYG 1832
Cdd:cd05923 223 VVVEEFDPAD-ALKLIEQERVTSLFATPTHLDALAAAAEFAGLKlSSLRHVTFAGATMPDAVLERVNQHLP-GEKVNIYG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1833 PTETVIGRVVHPVREAGELavdsplplgRPLGETRLQ---VLDAWLEAVPVGAVGELFI--GGDGIARGYLGRPALTAEK 1907
Cdd:cd05923 301 TTEAMNSLYMRDARTGTEM---------RPGFFSEVRivrIGGSPDEALANGEEGELIVaaAADAAFTGYLNQPEATAKK 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1908 fLPDpagepgaRMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVL-VRDQ---QLVGWF 1983
Cdd:cd05923 372 -LQD-------GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIgVADErwgQSVTAC 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 653678460 1984 IPAEDHPPvTVSALRRFC-AEQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:cd05923 444 VVPREGTL-SADELDQFCrASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
1082-1494 |
1.41e-27 |
|
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: 117.67 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1082 PLPLSPMQESIWLADQVSAGDSVYNVPLALRLIGPLDRGALRRTLNRVVDRHEMLRTRIHPGPDGM-------PVQVADP 1154
Cdd:cd19537 1 DTALSPIEREWWHKYQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLrrsysssPPRVQRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1155 agGGAALTERDAAPgtdlaqlllaeaalgFTLATEHPLRAVLwrldEREHvLLLTAHHVAVDAWSMDLIQRDLTELYAAD 1234
Cdd:cd19537 81 --DTLDVWKEINRP---------------FDLEREDPIRVFI----SPDT-LLVVMSHIICDLTTLQLLLREVSAAYNGK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1235 TghrepeLDEPALAQADYAVWQRQSAQRgryaaELDFWRTELTGAVATevagDLPRPATPGGGG-GAVEFALAPRQIQGI 1313
Cdd:cd19537 139 L------LPPVRREYLDSTAWSRPASPE-----DLDFWSEYLSGLPLL----NLPRRTSSKSYRgTSRVFQLPGSLYRSL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1314 RELARRCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGRGNPRLDNLVGCLVNTVVLR--GDLSGAPTFHELLRRTHA 1391
Cdd:cd19537 204 LQFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRirFPSSSDASAADFLRAVRR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1392 RTADALAHQeLPF----EHLVADRGAGNGPLFRIMYSFSSQEpAGRSAGDVD-LEPVPVPVTTCKFDLVL--TVVDGGS- 1463
Cdd:cd19537 284 SSQAALAHA-IPWhqllEHLGLPPDSPNHPLFDVMVTFHDDR-GVSLALPIPgVEPLYTWAEGAKFPLMFefTALSDDSl 361
|
410 420 430
....*....|....*....|....*....|.
gi 653678460 1464 TLEgvLEYADDLYLPGTAERLVTSLTNLLAA 1494
Cdd:cd19537 362 LLR--LEYDTDCFSEEEIDRIESLILAALEL 390
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
515-973 |
4.33e-27 |
|
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: 117.82 E-value: 4.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 515 TTLSYRELDERANRLARLLmERGAGAETFVAVLLPRSADLLVTLLAVIKAGaaYLPIDPDFP--VERIAYLLSDARPVLV 592
Cdd:cd05909 6 TSLTYRKLLTGAIALARKL-AKMTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTagLRELRACIKLAGIKTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 593 VTDAATADRLGPDDIT------GLVVLEETDTG---------GYPATEPPA----------VPAGHSAYVIYTSGSTGRP 647
Cdd:cd05909 83 LTSKQFIEKLKLHHLFdveydaRIVYLEDLRAKiskadkckaFLAGKFPPKwllrifgvapVQPDDPAVILFTSGSEGLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 648 KGVVITRAALDNFLAAMAERFPLTAEDRVLATTTV--SFDIAGlELYLPLRSGAGVVLA-DADTARNPAALIDLAGrhrV 724
Cdd:cd05909 163 KGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFfhSFGLTG-CLWLPLLSGIKVVFHpNPLDYKKIPELIYDKK---A 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 725 TLAQATPTLWQALVPELSGPALAGIR-VLVGGEALPAELARRLGDA-GAEVTNMYGPTETT-IWSTSGPTSEDsiRRGSI 801
Cdd:cd05909 239 TILLGTPTFLRGYARAAHPEDFSSLRlVVAGAEKLKDTLRQEFQEKfGIRILEGYGTTECSpVISVNTPQSPN--KEGTV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 802 GVPIDNTQVYVLD-ANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFlpdpfgppGTRMYRTGDLVRWSAAGDLEYL 880
Cdd:cd05909 317 GRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF--------GDGWYDTGDIGKIDGEGFLTIT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 881 GRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAV--VREDRPGDLRLVAYVIPDGpvAPDALRTELSRT-LPDYMIPAV 957
Cdd:cd05909 389 GRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAVvsVPDGRKGEKIVLLTTTTDT--DPSSLNDILKNAgISNLAKPSY 466
|
490
....*....|....*.
gi 653678460 958 IVPVPDFPTTPNGKLD 973
Cdd:cd05909 467 IHQVEEIPLLGTGKPD 482
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
1558-2033 |
5.01e-27 |
|
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: 116.78 E-value: 5.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1558 TFAGLDAQANRLAHALHtgalgAPPVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMARLTRIADTVTPALV 1637
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALK-----AQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1638 LTrtgqggclpgAEVFGDVPVVALDrvADRLTAmPDQRP-EVTVDPRG--LAYSIFTSGSTGQPKGVAVEH--------- 1705
Cdd:TIGR01923 76 LT----------DSLLEEKDFQADS--LDRIEA-AGRYEtSLSASFNMdqIATLMFTSGTTGKPKAVPHTFrnhyasavg 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1706 ----IGIVRYLSWAAaSYPtagrrgtLAHSSvgfdlTMSALFEPLVSGRGVTLMPADAtlaDLAEELSGPlAYDYIRLTP 1781
Cdd:TIGR01923 143 skenLGFTEDDNWLL-SLP-------LYHIS-----GLSILFRWLIEGATLRIVDKFN---QLLEMIANE-RVTHISLVP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1782 SHLRHLVGHWTGQELppaARGWVVGGETLDPALVKQLLELRPDaeVINHYGPTETVIGRVVHPVR-EAGELAVDSPLPlG 1860
Cdd:TIGR01923 206 TQLNRLLDEGGHNEN---LRKILLGGSAIPAPLIEEAQQYGLP--IYLSYGMTETCSQVTTATPEmLHARPDVGRPLA-G 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1861 RplgETRLQVLDAwleavpvGAVGELFIGGDGIARGYLGRPALTaekflpdPAGEPGArMYRTGDLVRWRGDGLLDFVGR 1940
Cdd:TIGR01923 280 R---EIKIKVDNK-------EGHGEIMVKGANLMKGYLYQGELT-------PAFEQQG-WFNTGDIGELDGEGFLYVLGR 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1941 VDDQVKLRGYRIELGEIEARMAEHPGVEQAVVlvrdqqlvgwfIPAED-------------HPPVTVSALRRFCAEQLPE 2007
Cdd:TIGR01923 342 RDDLIISGGENIYPEEIETVLYQHPGIQEAVV-----------VPKPDaewgqvpvayivsESDISQAKLIAYLTEKLAK 410
|
490 500
....*....|....*....|....*.
gi 653678460 2008 FMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:TIGR01923 411 YKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1541-2039 |
5.80e-27 |
|
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: 118.50 E-value: 5.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1541 ADRTPGWTALR------TGDRSLTFAGLDAQANRLAHALHtgALGAPPvgpeTPVLLLLDRSPELVVAMLAVLKAGGYFI 1614
Cdd:cd05931 3 AAARPDRPAYTflddegGREETLTYAELDRRARAIAARLQ--AVGKPG----DRVLLLAPPGLDFVAAFLGCLYAGAIAV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1615 PV---DPGYPMARLTRIADTVTPALVLTRTGQGGCLPG----AEVFGDVPVVALDRVADRLtamPDQRPEVTVDPRGLAY 1687
Cdd:cd05931 77 PLpppTPGRHAERLAAILADAGPRVVLTTAAALAAVRAfaasRPAAGTPRLLVVDLLPDTS---AADWPPPSPDPDDIAY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1688 SIFTSGSTGQPKGVAVEHIGIVRYLSWAAASY-PTAGRRGT----LAHssvgfDLTM-SALFEPLVSGRGVTLMPADATL 1761
Cdd:cd05931 154 LQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYgLDPGDVVVswlpLYH-----DMGLiGGLLTPLYSGGPSVLMSPAAFL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1762 ADLA---EELS--------GP-LAYDYI--RLTPSHLRHL-VGHWtgqelppaaRGWVVGGETLDPALVKQLLE------ 1820
Cdd:cd05931 229 RRPLrwlRLISryratisaAPnFAYDLCvrRVRDEDLEGLdLSSW---------RVALNGAEPVRPATLRRFAEafapfg 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1821 LRPDAeVINHYGPTETVI---------GRVVHPVR----EAGELAVDSP-------LPLGRPLGETRLQVLDA-WLEAVP 1879
Cdd:cd05931 300 FRPEA-FRPSYGLAEATLfvsggppgtGPVVLRVDrdalAGRAVAVAADdpaarelVSCGRPLPDQEVRIVDPeTGRELP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1880 VGAVGELFIGGDGIARGYLGRPALTAEKFLPDpAGEPGARMYRTGDLvRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEA 1959
Cdd:cd05931 379 DGEVGEIWVRGPSVASGYWGRPEATAETFGAL-AATDEGGWLRTGDL-GFLHDGELYITGRLKDLIIVRGRNHYPQDIEA 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1960 RMAEHPGVEQ----AVVLVRDQQLVGWFIPAEDHPPVTVSALRRFCAEqlpefMVpnQWVAlDAFPLTPHGK--VNHRAL 2033
Cdd:cd05931 457 TAEEAHPALRpgcvAAFSVPDDGEERLVVVAEVERGADPADLAAIAAA-----IR--AAVA-REHGVAPADVvlVRPGSI 528
|
....*.
gi 653678460 2034 PGPTSG 2039
Cdd:cd05931 529 PRTSSG 534
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
1084-1499 |
6.82e-27 |
|
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: 115.47 E-value: 6.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1084 PLSPMQESiwLADQVSAGDSVYNVPLALRLIGPLDRGALRRTLNRVVDRHEMLRTRIHPGPDGMPVQVAdpagggaalte 1163
Cdd:cd19545 3 PCTPLQEG--LMALTARQPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVV----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1164 RDAAP-----GTDLAQLLLAEAALGFTLATehPL-RAVLWRLDEREHVLLLTAHHVAVDAWSMDLIQRDLTELYAadtgh 1237
Cdd:cd19545 70 VKESPiswteSTSLDEYLEEDRAAPMGLGG--PLvRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQ----- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1238 repelDEPALAQADYAVWQRQSAQRGRYAAElDFWRTELTGAVATEVagdlprPATPGGGGGAVEFALAPRQIQgIRELA 1317
Cdd:cd19545 143 -----GEPVPQPPPFSRFVKYLRQLDDEAAA-EFWRSYLAGLDPAVF------PPLPSSRYQPRPDATLEHSIS-LPSSA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1318 RRcGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGRGNP--RLDNLVGCLVNTVVLRGDLSGAPTFHELLRRTHARTAD 1395
Cdd:cd19545 210 SS-GVTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPvpGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLD 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1396 AlahqeLPFEHLVADR------GAGNGPLFRIMYSFSSQEPAGrSAGDVDLEPVPVPVTTCKFD---LVLTVVDGGSTLE 1466
Cdd:cd19545 289 M-----IPFEHTGLQNirrlgpDARAACNFQTLLVVQPALPSS-TSESLELGIEEESEDLEDFSsygLTLECQLSGSGLR 362
|
410 420 430
....*....|....*....|....*....|...
gi 653678460 1467 GVLEYADDLYLPGTAERLVTSLTNLLAAAVRTP 1499
Cdd:cd19545 363 VRARYDSSVISEEQVERLLDQFEHVLQQLASAP 395
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1545-2033 |
1.14e-26 |
|
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: 117.08 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1545 PGWTALRTGDRSLTFAGLDAQANRLAHALHTgaLGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPV-------D 1617
Cdd:cd05959 18 GDKTAFIDDAGSLTYAELEAEARRVAGALRA--LG---VKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVntlltpdD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1618 PGYPM----ARL----TRIADTVTPAL--------VLTRTGQGGCLPGAEVFGDVpvvaLDRVADRLTAMPDQRPEVtvd 1681
Cdd:cd05959 93 YAYYLedsrARVvvvsGELAPVLAAALtksehtlvVLIVSGGAGPEAGALLLAEL----VAAEAEQLKPAATHADDP--- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1682 prglAYSIFTSGSTGQPKGVAVEHigivRYLSWAAASYptAGRRGTLAHSSVGFDLTM--------SALFEPLVSGRGVT 1753
Cdd:cd05959 166 ----AFWLYSSGSTGRPKGVVHLH----ADIYWTAELY--ARNVLGIREDDVCFSAAKlffayglgNSLTFPLSVGATTV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1754 LM---PADATLADLAEELSGPLAYDYIRLTPSHLRHLVghwTGQELPPAARGWVVGGETLdPALVKQLLELRPDAEVINH 1830
Cdd:cd05959 236 LMperPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPN---LPSRDLSSLRLCVSAGEAL-PAEVGERWKARFGLDILDG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1831 YGPTETV---IGRVVHPVReagelavdsPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEK 1907
Cdd:cd05959 312 IGSTEMLhifLSNRPGRVR---------YGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1908 FLpdpaGEpgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGV-EQAVVLVRDQ----QLVGW 1982
Cdd:cd05959 383 FQ----GE----WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVlEAAVVGVEDEdgltKPKAF 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 653678460 1983 FIPAEDHPPVTVSA--LRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:cd05959 455 VVLRPGYEDSEALEeeLKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
64-459 |
1.29e-26 |
|
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: 114.70 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 64 PGTPL--------------YSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVFRLGPDGEPVQqtAPAAPVALPVIDV 129
Cdd:cd19545 3 PCTPLqeglmaltarqpgaYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQ--VVVKESPISWTES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 130 TeaDLPQALRTAAEQPFDLErGPLLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLLLADLARAYAGELPAGVaaPAFRDV 209
Cdd:cd19545 81 T--SLDEYLEEDRAAPMGLG-GPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQP--PPFSRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 210 AAWqhgrLAAGELDDQLRYWRQRLAGLpdleipgdrqrpADRDWRAHSVRRELPAATEAAVRRLA----AAHDTTPFTVL 285
Cdd:cd19545 156 VKY----LRQLDDEAAAEFWRSYLAGL------------DPAVFPPLPSSRYQPRPDATLEHSISlpssASSGVTLATVL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 286 LAAYGTFLHRLTGQDDFAVGVPVAGRG--RTDLESVVG-LFAGmVPVRLDLTGRPSFDEVLSRTvagsrNDFAHPQIPFD 362
Cdd:cd19545 220 RAAWALVLSRYTGSDDVVFGVTLSGRNapVPGIEQIVGpTIAT-VPLRVRIDPEQSVEDFLQTV-----QKDLLDMIPFE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 363 --------RLVRELRRDRIAGSQLLVQamAGTESTAVALTFGEaagtEQPVDVALAKCD---LDLSVLDDGDRLAVTLVA 431
Cdd:cd19545 294 htglqnirRLGPDARAACNFQTLLVVQ--PALPSSTSESLELG----IEEESEDLEDFSsygLTLECQLSGSGLRVRARY 367
|
410 420
....*....|....*....|....*...
gi 653678460 432 AADLFTPAAAEQLAGQFLSLLAGLTGAP 459
Cdd:cd19545 368 DSSVISEEQVERLLDQFEHVLQQLASAP 395
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
1532-2033 |
2.87e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 116.21 E-value: 2.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1532 TVHQLVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHtGALGappVGPETPVLLLLDRSPELVVAMLAVLKAGG 1611
Cdd:PRK08314 11 SLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQ-QECG---VRKGDRVLLYMQNSPQFVIAYYAILRANA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1612 YFIPVDPGYPMARLTRI---------------ADTVTPALVLTRTGQ------GGCLPGAevfGDVPVVALDRVADRLTA 1670
Cdd:PRK08314 87 VVVPVNPMNREEELAHYvtdsgarvaivgselAPKVAPAVGNLRLRHvivaqySDYLPAE---PEIAVPAWLRAEPPLQA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1671 MPDQR--------------PEVTVDPRGLAYSIFTSGSTGQPKGVAVEHigivRYLSWAAASyptAGRRGTLAHSSVG-- 1734
Cdd:PRK08314 164 LAPGGvvawkealaaglapPPHTAGPDDLAVLPYTSGTTGVPKGCMHTH----RTVMANAVG---SVLWSNSTPESVVla 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1735 ----FDLT--MSALFEPLVSGRGVTLMPA--DATLADLAEelsgplaydyirltpshlRHLVGHWTGqelPP-------- 1798
Cdd:PRK08314 237 vlplFHVTgmVHSMNAPIYAGATVVLMPRwdREAAARLIE------------------RYRVTHWTN---IPtmvvdfla 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1799 ----AARG-----WVVGGETLDPALVKQLLELRPDAEVINHYGPTETVIGRVVHPVreagelavDSPLP--LGRPLGETR 1867
Cdd:PRK08314 296 spglAERDlsslrYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTETMAQTHSNPP--------DRPKLqcLGIPTFGVD 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1868 LQVLD-AWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLP-DpagepGARMYRTGDLVRWRGDGLLDFVGRVDDQV 1945
Cdd:PRK08314 368 ARVIDpETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFIEiD-----GKRFFRTGDLGRMDEEGYFFITDRLKRMI 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1946 KLRGYRIELGEIEARMAEHPGVEQA-VVLVRDQ---QLVGWFIPAEDHPPVTVSA--LRRFCAEQLPEFMVPNQWVALDA 2019
Cdd:PRK08314 443 NASGFKVWPAEVENLLYKHPAIQEAcVIATPDPrrgETVKAVVVLRPEARGKTTEeeIIAWAREHMAAYKYPRIVEFVDS 522
|
570
....*....|....
gi 653678460 2020 FPLTPHGKVNHRAL 2033
Cdd:PRK08314 523 LPKSGSGKILWRQL 536
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
499-979 |
3.73e-26 |
|
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: 116.44 E-value: 3.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 499 QWCRRTPGAVAVI----EGDT-TLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDP 573
Cdd:cd05968 69 KWLADTRTRPALRwegeDGTSrTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 574 DFPVERIAYLLSDARPVLVVTDAATADRLGPDDIT--------------GLVVLEETDTGGYPAT----EPPAVPAGHSA 635
Cdd:cd05968 149 GFGKEAAATRLQDAEAKALITADGFTRRGREVNLKeeadkacaqcptveKVVVVRHLGNDFTPAKgrdlSYDEEKETAGD 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 636 Y-----------VIYTSGSTGRPKGVVIT------RAALDnflaaMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSG 698
Cdd:cd05968 229 GaertesedplmIIYTSGTTGKPKGTVHVhagfplKAAQD-----MYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 699 AGVVLAD-ADTARNPAALIDLAGRHRVTLAQATPTLWQALVPELSGPA----LAGIRVLVG-GEALPAE----LARRLGD 768
Cdd:cd05968 304 ATMVLYDgAPDHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVnahdLSSLRVLGStGEPWNPEpwnwLFETVGK 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 769 AGAEVTNMYGPTETTiWSTSGPTSEDSIRRGSIGVPIDNTQVYVLDANLHPAPiGVLGELHIAGE--GLARGYWNRPGLT 846
Cdd:cd05968 384 GRNPIINYSGGTEIS-GGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPAR-PEVGELVLLAPwpGMTRGFWRDEDRY 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 847 AEKF---LPDpfgppgtrMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAV-VREDRPG 922
Cdd:cd05968 462 LETYwsrFDN--------VWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIgVPHPVKG 533
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 653678460 923 DLRLVAYVIPDGPVAPDALRTELSRTLPDYM----IPAVIVPVPDFPTTPNGKLDRAALPA 979
Cdd:cd05968 534 EAIVCFVVLKPGVTPTEALAEELMERVADELgkplSPERILFVKDLPKTRNAKVMRRVIRA 594
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
1536-2036 |
5.00e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 114.32 E-value: 5.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1536 LVEAQADRTPgwtALRTGDRSLTFAGLDAQANRLAHALHtgalGAPPVGPE-TPvlllldrSPELVVAMLAVLKAGGYFI 1614
Cdd:PRK07787 8 AVAAAADIAD---AVRIGGRVLSRSDLAGAATAVAERVA----GARRVAVLaTP-------TLATVLAVVGALIAGVPVV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1615 PVDPGYPMARLTRIADTVTPALVLTRTGQGGclpgaevfGDVPVVALDRVADRLTAMPDqrpevtVDPRGLAYSIFTSGS 1694
Cdd:PRK07787 74 PVPPDSGVAERRHILADSGAQAWLGPAPDDP--------AGLPHVPVRLHARSWHRYPE------PDPDAPALIVYTSGT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1695 TGQPKGVAVEHIGIVRYLSWAAASYPTAGRrGTLAHSSVGFD---LTMSALFEPLVSGRGVTLmpADATLADLAEELSG- 1770
Cdd:PRK07787 140 TGPPKGVVLSRRAIAADLDALAEAWQWTAD-DVLVHGLPLFHvhgLVLGVLGPLRIGNRFVHT--GRPTPEAYAQALSEg 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1771 -------PLAYDYIRLTPSHLRHLVGhwtgqelppaARGWVVGGETLdPALVKQLLELRPDAEVINHYGPTETVIgrvVH 1843
Cdd:PRK07787 217 gtlyfgvPTVWSRIAADPEAARALRG----------ARLLVSGSAAL-PVPVFDRLAALTGHRPVERYGMTETLI---TL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1844 PVREAGElavDSPLPLGRPLGETRLQVLDAWLEAVPVG--AVGELFIGGDGIARGYLGRPALTAEKFLPDPagepgarMY 1921
Cdd:PRK07787 283 STRADGE---RRPGWVGLPLAGVETRLVDEDGGPVPHDgeTVGELQVRGPTLFDGYLNRPDATAAAFTADG-------WF 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1922 RTGDLVRWRGDGLLDFVGRVD-DQVKLRGYRIELGEIEARMAEHPGV-EQAVVLVRD----QQLVGWFIPAEdhpPVTVS 1995
Cdd:PRK07787 353 RTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVrEAAVVGVPDddlgQRIVAYVVGAD---DVAAD 429
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 653678460 1996 ALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRALPGP 2036
Cdd:PRK07787 430 ELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSE 470
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
515-933 |
5.07e-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: 114.38 E-value: 5.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 515 TTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARPVLVVT 594
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 595 DAatadrlGPDDItglvvleetdtggypateppavpaghsAYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAED 674
Cdd:cd17640 84 EN------DSDDL---------------------------ATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 675 RVLAtttvsfdiaglelYLPL-----RSGAGVVLAD--ADTARNPAALIDLAGRHRVTLAQATPTLWQALVP-------- 739
Cdd:cd17640 131 RFLS-------------ILPIwhsyeRSAEYFIFACgcSQAYTSIRTLKDDLKRVKPHYIVSVPRLWESLYSgiqkqvsk 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 740 ------ELSGPALAG--IRVLV-GGEALPAELARRLGDAGAEVTNMYGPTETTIWSTSGPTSEdsIRRGSIGVPIDNTQV 810
Cdd:cd17640 198 sspikqFLFLFFLSGgiFKFGIsGGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKC--NVRGSVGRPLPGTEI 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 811 YVLDANLH-PAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgppgtrmYRTGDLVRWSAAGDLEYLGRT-DHQVK 888
Cdd:cd17640 276 KIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW-------FNTGDLGWLTCGGELVLTGRAkDTIVL 348
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 653678460 889 LRGFRIELGEIETTLINAgPVRRAAAVVREDRPgdlRLVAYVIPD 933
Cdd:cd17640 349 SNGENVEPQPIEEALMRS-PFIEQIMVVGQDQK---RLGALIVPN 389
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
1540-2028 |
5.43e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 114.52 E-value: 5.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1540 QADRTPGWTALR--TGDRSLTFAGLDAQANRLAHALHTGAlgappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVD 1617
Cdd:PRK09088 4 HARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRG-----CVDGERLAVLARNSVWLVALHFACARVGAIYVPLN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1618 PGYPMARLTRIADTVTPALVLtrtgqGGCLPGAevfGDVPVVALDRVADRLTAM-PDQRPevTVDPRGLAYSIFTSGSTG 1696
Cdd:PRK09088 79 WRLSASELDALLQDAEPRLLL-----GDDAVAA---GRTDVEDLAAFIASADALePADTP--SIPPERVSLILFTSGTSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1697 QPKGVAVEHigivRYLSWAAASYPTAGRRGtlAHSSVGFDLTMSALFEPLVSGRGVTLM----------PADATLADLAE 1766
Cdd:PRK09088 149 QPKGVMLSE----RNLQQTAHNFGVLGRVD--AHSSFLCDAPMFHIIGLITSVRPVLAVggsilvsngfEPKRTLGRLGD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1767 ELSG-------PLAYDYIRLTP----SHLRHLVGHWTGQELPPAA--RGWVVGGetldpalvkqllelrpdAEVINHYGP 1833
Cdd:PRK09088 223 PALGithyfcvPQMAQAFRAQPgfdaAALRHLTALFTGGAPHAAEdiLGWLDDG-----------------IPMVDGFGM 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1834 TE--TVIGRVVHPVREAGELAVdsplpLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFlpd 1911
Cdd:PRK09088 286 SEagTVFGMSVDCDVIRAKAGA-----AGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF--- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1912 pagePGARMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGV-EQAVVLVRDQQL--VGW-FIPAE 1987
Cdd:PRK09088 358 ----TGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIrECAVVGMADAQWgeVGYlAIVPA 433
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 653678460 1988 DHPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKV 2028
Cdd:PRK09088 434 DGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKL 474
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
48-337 |
6.77e-26 |
|
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: 112.92 E-value: 6.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 48 PLAPGQAGIWFSEQLRPGTPLYSVPLAVRLTGPLDVDALRAALDAVTARHEALRTVFRLgpDG--EPVQ---QTAPaapv 122
Cdd:cd19544 3 PLAPLQEGILFHHLLAEEGDPYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAILW--EGlsEPVQvvwRQAE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 123 aLPVIDVT---EADLPQALRTAAE---QPFDLERGPLLRACL-HRIGAKQHVLLVTVHHIVLDGWSCGLLLADLARAYAG 195
Cdd:cd19544 77 -LPVEELTldpGDDALAQLRARFDprrYRLDLRQAPLLRAHVaEDPANGRWLLLLLFHHLISDHTSLELLLEEIQAILAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 196 E---LPAgvaAPAFRDVAAwqHGRLAAGELDDQlRYWRQRLA---------GLPDleIPGDrqrpadrDWRAHSVRRELP 263
Cdd:cd19544 156 RaaaLPP---PVPYRNFVA--QARLGASQAEHE-AFFREMLGdvdeptapfGLLD--VQGD-------GSDITEARLALD 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 653678460 264 AATEAAVRRLAAAHDTTPFTVLLAAYGTFLHRLTGQDDFAVGVPVAGR--GRTDLESVVGLFAGMVPVRLDLTGRP 337
Cdd:cd19544 221 AELAQRLRAQARRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRmqGGAGADRALGMFINTLPLRVRLGGRS 296
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
481-977 |
7.35e-26 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 114.86 E-value: 7.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 481 WNDTARPLPAA--SLRERFQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTL 558
Cdd:PRK06155 9 AARAVDPLPPSerTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 559 LAVIKAGAAYLPIDPDFPVERIAYLLSDARPVLVVTDAATADRL-----GPDDITGLVVLEET---------DTGGYPAT 624
Cdd:PRK06155 89 LGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALeaadpGDLPLPAVWLLDAPasvsvpagwSTAPLPPL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 625 EPPAVPA----GHSAYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDrVLATTTVSFDIAGLELYLP-LRSGA 699
Cdd:PRK06155 169 DAPAPAAavqpGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADD-VLYTTLPLFHTNALNAFFQaLLAGA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 700 GVVLADADTArnpAALIDLAGRHrvtlaQATPT-LWQALVPEL----SGPALAGIRVLVG-GEALPAELARRLGDA-GAE 772
Cdd:PRK06155 248 TYVLEPRFSA---SGFWPAVRRH-----GATVTyLLGAMVSILlsqpARESDRAHRVRVAlGPGVPAALHAAFRERfGVD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 773 VTNMYGPTETTIwSTSGPTSEDsiRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGE---GLARGYWNRPGLTAEK 849
Cdd:PRK06155 320 LLDGYGSTETNF-VIAVTHGSQ--RPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPEKTVEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 850 FlpdpfgppGTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAV-VREDRPGDLRLVA 928
Cdd:PRK06155 397 W--------RNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFpVPSELGEDEVMAA 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 653678460 929 YVIPDGPVA-PDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:PRK06155 469 VVLRDGTALePVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
505-977 |
1.05e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 113.72 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 505 PGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETfVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLL 584
Cdd:PRK07638 15 PNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKT-IAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 585 SDARPVLVVTDAATADRLgpDDITGLVVLEET---DTGGYPATEPPAVPAGHSA-YVIYTSGSTGRPKGVVIT-RAALDN 659
Cdd:PRK07638 94 AISNADMIVTERYKLNDL--PDEEGRVIEIDEwkrMIEKYLPTYAPIENVQNAPfYMGFTSGSTGKPKAFLRAqQSWLHS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 660 FLAAmAERFPLTAEDRVL-ATTTVSfdiaGLELY---LPLRSGAGVVLADAdtaRNPAALIDLAGRHRVTLAQATPTLWQ 735
Cdd:PRK07638 172 FDCN-VHDFHMKREDSVLiAGTLVH----SLFLYgaiSTLYVGQTVHLMRK---FIPNQVLDKLETENISVMYTVPTMLE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 736 ALVPELSGPAlAGIRVLVGGEALPAELARRLGDA--GAEVTNMYGPTETTIWSTSgpTSEDSIRR-GSIGVPIDNTQVYV 812
Cdd:PRK07638 244 SLYKENRVIE-NKMKIISSGAKWEAEAKEKIKNIfpYAKLYEFYGASELSFVTAL--VDEESERRpNSVGRPFHNVQVRI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 813 LDANLHPAPIGVLGELHIAGEGLARGYWNrpgltaekflpdpfgppGTRMYRTGDLVRWSAAGDLEYL---------GRT 883
Cdd:PRK07638 321 CNEAGEEVQKGEIGTVYVKSPQFFMGYII-----------------GGVLARELNADGWMTVRDVGYEdeegfiyivGRE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 884 DHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVipDGPVAPDALRTELSRTLPDYMIPAVIVPVPD 963
Cdd:PRK07638 384 KNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII--KGSATKQQLKSFCLQRLSSFKIPKEWHFVDE 461
|
490
....*....|....
gi 653678460 964 FPTTPNGKLDRAAL 977
Cdd:PRK07638 462 IPYTNSGKIARMEA 475
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
483-974 |
1.48e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 114.10 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 483 DTARPLPAASLRERFQQWCRRTPG--AVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLA 560
Cdd:PRK12583 10 GGDKPLLTQTIGDAFDATVARFPDreALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 561 VIKAGAAYLPIDPDFPVERIAYLL--SDARPVLVVtDA-------ATADRLGPD---------------DITGLVVLEET 616
Cdd:PRK12583 90 TARIGAILVNINPAYRASELEYALgqSGVRWVICA-DAfktsdyhAMLQELLPGlaegqpgalacerlpELRGVVSLAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 617 DTGGYPA-TEPPAVPAGHSAY----------------VIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDRVLAT 679
Cdd:PRK12583 169 PPPGFLAwHELQARGETVSREalaerqasldrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 680 TTVsFDIAGLEL--YLPLRSGAGVVLadADTARNPAALIDLAGRHRVTLAQATPTLWQALV--PELSGPALAGIRV-LVG 754
Cdd:PRK12583 249 VPL-YHCFGMVLanLGCMTVGACLVY--PNEAFDPLATLQAVEEERCTALYGVPTMFIAELdhPQRGNFDLSSLRTgIMA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 755 GEALPAELARRLGDA--GAEVTNMYGPTETTIWST-SGPTSEDSIRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIA 831
Cdd:PRK12583 326 GAPCPIEVMRRVMDEmhMAEVQIAYGMTETSPVSLqTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 832 GEGLARGYWNRPGLTAEKFLPDPFgppgtrMYrTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRR 911
Cdd:PRK12583 406 GYSVMKGYWNNPEATAESIDEDGW------MH-TGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVAD 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 653678460 912 AAAVVREDRPGDLRLVAYVI--PDGPVAPDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDR 974
Cdd:PRK12583 479 VQVFGVPDEKYGEEIVAWVRlhPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
502-972 |
1.50e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 113.63 E-value: 1.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 502 RRTPGAVAVIEG--DTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVER 579
Cdd:PRK13391 8 QTTPDKPAVIMAstGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 580 IAYLLSDARPVLVVTDAATAD--------------RL---GPDDITGLVVLEETdTGGYPATEPPAVPAGhsAYVIYTSG 642
Cdd:PRK13391 88 AAYIVDDSGARALITSAAKLDvarallkqcpgvrhRLvldGDGELEGFVGYAEA-VAGLPATPIADESLG--TDMLYSSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 643 STGRPKGVV--ITRAALD---NFLAAMAERFPLTAEDRVLATttvsfdiAGLELYLPLRSgAGVVLADADTA-----RNP 712
Cdd:PRK13391 165 TTGRPKGIKrpLPEQPPDtplPLTAFLQRLWGFRSDMVYLSP-------APLYHSAPQRA-VMLVIRLGGTVivmehFDA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 713 AALIDLAGRHRVTLAQATPTLWQAL--VPELSGPA--LAGIRVLVGGEA-LPAELARRLGD-AGAEVTNMYGPTEttiws 786
Cdd:PRK13391 237 EQYLALIEEYGVTHTQLVPTMFSRMlkLPEEVRDKydLSSLEVAIHAAApCPPQVKEQMIDwWGPIIHEYYAATE----- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 787 TSGPTSEDS----IRRGSIGVPIDNTqVYVLDANLHPAPIGVLGELHIAGeGLARGYWNRPGLTAEKFLPDPfgppgtrm 862
Cdd:PRK13391 312 GLGFTACDSeewlAHPGTVGRAMFGD-LHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEARHPDG-------- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 863 yrtgdlvRWSAAGDLEYLG---------RTDHQVKLRGFRIELGEIETTLINAGPVRRAAAV-VREDRPGDlRLVAYVIP 932
Cdd:PRK13391 382 -------TWSTVGDIGYVDedgylyltdRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFgVPNEDLGE-EVKAVVQP 453
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 653678460 933 DGPVAPDA---------LRTELSRtlpdYMIPAVIVPVPDFPTTPNGKL 972
Cdd:PRK13391 454 VDGVDPGPalaaeliafCRQRLSR----QKCPRSIDFEDELPRLPTGKL 498
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
492-973 |
1.97e-25 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 115.79 E-value: 1.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 492 SLRERFQQWCRRTPGAVAVIE-GDTTLSYRELDERANRLARLLmERGAGAETFVAVLLPRS-----ADLLVTLL------ 559
Cdd:PRK08633 616 PLAEAWIDTAKRNWSRLAVADsTGGELSYGKALTGALALARLL-KRELKDEENVGILLPPSvagalANLALLLAgkvpvn 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 560 ------------AVIKAG-------------AAYLPIDPDFPVERIAYLLSDARPVLVVTD---AATADRLGPdditgLV 611
Cdd:PRK08633 695 lnytaseaalksAIEQAQiktvitsrkflekLKNKGFDLELPENVKVIYLEDLKAKISKVDkltALLAARLLP-----AR 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 612 VLEETDTGGYPATEPpavpaghsAYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDRVLATTTV--SFDIAGl 689
Cdd:PRK08633 770 LLKRLYGPTFKPDDT--------ATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFfhSFGLTV- 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 690 ELYLPLRSGAGVVladadTARNP---AALIDLAGRHRVTLAQATPTLWQA------LVPELsgpaLAGIR-VLVGGEALP 759
Cdd:PRK08633 841 TLWLPLLEGIKVV-----YHPDPtdaLGIAKLVAKHRATILLGTPTFLRLylrnkkLHPLM----FASLRlVVAGAEKLK 911
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 760 AELArrlgDA-----GAEVTNMYGPTETT-IWSTSGPTSEDS-------IRRGSIGVPIDNTQVYVLDA-NLHPAPIGVL 825
Cdd:PRK08633 912 PEVA----DAfeekfGIRILEGYGATETSpVASVNLPDVLAAdfkrqtgSKEGSVGMPLPGVAVRIVDPeTFEELPPGED 987
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 826 GELHIAGEGLARGYWNRPGLTAEkFLPDpfgPPGTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIE---TT 902
Cdd:PRK08633 988 GLILIGGPQVMKGYLGDPEKTAE-VIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEeelAK 1063
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 653678460 903 LINAGPVRRAAAVVREDRPGDlRLVAyVIPDGPVAPDALRTELSRT-LPDYMIPAVIVPVPDFPTTPNGKLD 973
Cdd:PRK08633 1064 ALGGEEVVFAVTAVPDEKKGE-KLVV-LHTCGAEDVEELKRAIKESgLPNLWKPSRYFKVEALPLLGSGKLD 1133
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1557-2028 |
2.21e-25 |
|
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: 111.84 E-value: 2.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1557 LTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMARLTRIADTVTPAL 1636
Cdd:cd05973 1 LTFGELRALSARFANALQ--ELG---VGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1637 VLTRTgqggclpgaevfgdvpvvaldrvadrltampDQRPEVTVDPrglAYSIFTSGSTGQPKGVAVEhigiVRYL-SWA 1715
Cdd:cd05973 76 VVTDA-------------------------------ANRHKLDSDP---FVMMFTSGTTGLPKGVPVP----LRALaAFG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1716 AASYPTAGRRG-----TLAHSSVGFDLtMSALFEPLVSGRGVTLmpadatladLAEELSGPLAYDYIR--------LTPS 1782
Cdd:cd05973 118 AYLRDAVDLRPedsfwNAADPGWAYGL-YYAITGPLALGHPTIL---------LEGGFSVESTWRVIErlgvtnlaGSPT 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1783 HLRHLVGHWTGQELPPAARGWVV--GGETLDPALVKqLLELRPDAEVINHYGPTEtvIGRVV-------HPVREAGelav 1853
Cdd:cd05973 188 AYRLLMAAGAEVPARPKGRLRRVssAGEPLTPEVIR-WFDAALGVPIHDHYGQTE--LGMVLanhhaleHPVHAGS---- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1854 dsplpLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIA----RGYLGRPAltaekflPDPAGepgaRMYRTGDLVRW 1929
Cdd:cd05973 261 -----AGRAMPGWRVAVLDDDGDELGPGEPGRLAIDIANSPlmwfRGYQLPDT-------PAIDG----GYYLTGDTVEF 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1930 RGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGV-EQAVVLVRDQQ---LVGWFI---PAEDHPPVTVSALRRFCA 2002
Cdd:cd05973 325 DPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVaEAAVIGVPDPErteVVKAFVvlrGGHEGTPALADELQLHVK 404
|
490 500
....*....|....*....|....*.
gi 653678460 2003 EQLPEFMVPNQWVALDAFPLTPHGKV 2028
Cdd:cd05973 405 KRLSAHAYPRTIHFVDELPKTPSGKI 430
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
500-977 |
2.22e-25 |
|
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: 113.36 E-value: 2.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 500 WCRRTPGAVAVIEGDTT-----LSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPD 574
Cdd:cd05970 26 MAKEYPDKLALVWCDDAgeeriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 575 FPVERIAYLLSDARPVLVVTDA----------ATAD--------RLGPDDITGLVVLEETDTGGYPATEPP---AVPAGH 633
Cdd:cd05970 106 LTAKDIVYRIESADIKMIVAIAednipeeiekAAPEcpskpklvWVGDPVPEGWIDFRKLIKNASPDFERPtanSYPCGE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 634 SAYVIY-TSGSTGRPKGVVitraalDNFLaamaerFPL----TA-------EDRV---LATTTVSFDIAGlELYLPLRSG 698
Cdd:cd05970 186 DILLVYfSSGTTGMPKMVE------HDFT------YPLghivTAkywqnvrEGGLhltVADTGWGKAVWG-KIYGQWIAG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 699 AGVVLADADTArNPAALIDLAGRHRVTLAQATPTLWQALVPE-LSGPALAGIR-VLVGGEALPAELARRLGDA-GAEVTN 775
Cdd:cd05970 253 AAVFVYDYDKF-DPKALLEKLSKYGVTTFCAPPTIYRFLIREdLSRYDLSSLRyCTTAGEALNPEVFNTFKEKtGIKLME 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 776 MYGPTETTIWSTSGPTSEdsIRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGE-----GLARGYWNRPGLTAEKF 850
Cdd:cd05970 332 GFGQTETTLTIATFPWME--PKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTAEVW 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 851 LPDpfgppgtrMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAV-VREDRPGDLRLVAY 929
Cdd:cd05970 410 HDG--------YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTgVPDPIRGQVVKATI 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 653678460 930 VIPDGPVAPDALRTEL----SRTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:cd05970 482 VLAKGYEPSEELKKELqdhvKKVTAPYKYPRIVEFVDELPKTISGKIRRVEI 533
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
1530-2033 |
2.85e-25 |
|
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: 112.42 E-value: 2.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1530 DRTVHQLVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKA 1609
Cdd:cd05920 14 DEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLR--GLG---IRPGDRVVVQLPNVAEFVVLFFALLRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1610 GGYFIPVDPGYPMARLTRIADTVTPALVLtrtgqggclpGAEVFGDVPVVALDRvadrltampdqrpEVTVDPRGLAYSI 1689
Cdd:cd05920 89 GAVPVLALPSHRRSELSAFCAHAEAVAYI----------VPDRHAGFDHRALAR-------------ELAESIPEVALFL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1690 FTSGSTGQPKGVAVEHIGivrYLSWAAASYPTAGrrgtLAHSSV---------GFDLTMSALFEPLVSGRGVTLMP---A 1757
Cdd:cd05920 146 LSGGTTGTPKLIPRTHND---YAYNVRASAEVCG----LDQDTVylavlpaahNFPLACPGVLGTLLAGGRVVLAPdpsP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1758 DATLADLAEELSGPLAydyirLTPSHLRHLVGHWTGQELPPAARGWV-VGGETLDPALVKQLLELRpDAEVINHYGPTET 1836
Cdd:cd05920 219 DAAFPLIEREGVTVTA-----LVPALVSLWLDAAASRRADLSSLRLLqVGGARLSPALARRVPPVL-GCTLQQVFGMAEG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1837 VIG--RVVHPvreaGELAVDSPlplGRPLG-ETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDpa 1913
Cdd:cd05920 293 LLNytRLDDP----DEVIIHTQ---GRPMSpDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPD-- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1914 gepgaRMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRDQQLVG----WFIPAEDh 1989
Cdd:cd05920 364 -----GFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGerscAFVVLRD- 437
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 653678460 1990 PPVTVSALRRFCAEQ-LPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:cd05920 438 PPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1690-2028 |
5.20e-25 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 108.90 E-value: 5.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1690 FTSGSTGQPKGVAVEHIGIVRylswaaASYPTAGRRGTLAHSSV--------GFDLTMSALfepLVSGRGVTL-MPAD-- 1758
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVN------NGYFIGERLGLTEQDRLcipvplfhCFGSVLGVL---ACLTHGATMvFPSPsf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1759 ---ATLADLAEE----LSG-PLAY-------DYIRLTPSHLRhlvghwTGqelppaargwVVGGETLDPALVKQLLELRP 1823
Cdd:cd05917 80 dplAVLEAIEKEkctaLHGvPTMFiaelehpDFDKFDLSSLR------TG----------IMAGAPCPPELMKRVIEVMN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1824 DAEVINHYGPTETvigrvvHPVREAGElaVDSPLPL-----GRPLGETRLQVLDAWLEAVP-VGAVGELFIGGDGIARGY 1897
Cdd:cd05917 144 MKDVTIAYGMTET------SPVSTQTR--TDDSIEKrvntvGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGY 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1898 LGRPALTAEKFLPDpagepgaRMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQA-VVLVRD 1976
Cdd:cd05917 216 WNDPEKTAEAIDGD-------GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVqVVGVPD 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 653678460 1977 QQL---VGWFIPAEDHPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKV 2028
Cdd:cd05917 289 ERYgeeVCAWIRLKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKI 343
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
499-974 |
5.48e-25 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 113.11 E-value: 5.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 499 QWCRRTPGAVAVI-EGDT-----TLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPID 572
Cdd:TIGR02188 65 RHLEARPDKVAIIwEGDEpgevrKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 573 PDFPVERIAYLLSDARPVLVVT-----------------DAATADrlGPDDITGLVVLEETD-----------------T 618
Cdd:TIGR02188 145 GGFSAEALADRINDAGAKLVITadeglrggkviplkaivDEALEK--CPVSVEHVLVVRRTGnpvvpwvegrdvwwhdlM 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 619 GGYPAT-EPPAVPAGHSAYVIYTSGSTGRPKGVVITRAALdNFLAAMAER--FPLTAEDRVLATTTVSFdIAGLE--LYL 693
Cdd:TIGR02188 223 AKASAYcEPEPMDSEDPLFILYTSGSTGKPKGVLHTTGGY-LLYAAMTMKyvFDIKDGDIFWCTADVGW-ITGHSyiVYG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 694 PLRSGAGVVLAD-ADTARNPAALIDLAGRHRVTLAQATPTLWQALVPElsGPA------LAGIRVL--VgGEALPAE--- 761
Cdd:TIGR02188 301 PLANGATTVMFEgVPTYPDPGRFWEIIEKHKVTIFYTAPTAIRALMRL--GDEwvkkhdLSSLRLLgsV-GEPINPEawm 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 762 -LARRLGDAGAEVTNMYGPTET---TIWSTSGPTsedSIRRGSIGVPIDNTQVYVLDANLHPAPI-GVLGELHIAGE--G 834
Cdd:TIGR02188 378 wYYKVVGKERCPIVDTWWQTETggiMITPLPGAT---PTKPGSATLPFFGIEPAVVDEEGNPVEGpGEGGYLVIKQPwpG 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 835 LARGYWNRPgltaEKFLPDPFGP-PGtrMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAA 913
Cdd:TIGR02188 455 MLRTIYGDH----ERFVDTYFSPfPG--YYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAA 528
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 653678460 914 AVvreDRPGDLR---LVAYVIPDGPVAPDA-----LRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDR 974
Cdd:TIGR02188 529 VV---GIPDDIKgqaIYAFVTLKDGYEPDDelrkeLRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMR 594
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
485-977 |
1.11e-24 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 111.97 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 485 ARPLPAaSLRERFQQWCRRTPGAVAV---IEGD-----TTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLV 556
Cdd:PRK07529 20 ARDLPA-STYELLSRAAARHPDAPALsflLDADpldrpETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 557 TLLAVIKAGAAYlPIDPDFPVERIAYLLSDARPVLVVT-----DAATADRLGP--DDITGLVVLEETDTGGY-PATEPPA 628
Cdd:PRK07529 99 ALWGGEAAGIAN-PINPLLEPEQIAELLRAAGAKVLVTlgpfpGTDIWQKVAEvlAALPELRTVVEVDLARYlPGPKRLA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 629 VPAGH---------------------------------SAYViYTSGSTGRPKgVVITRAALDNFLAAMAERFPLTAEDR 675
Cdd:PRK07529 178 VPLIRrkaharildfdaelarqpgdrlfsgrpigpddvAAYF-HTGGTTGMPK-LAQHTHGNEVANAWLGALLLGLGPGD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 676 VLATTTVSFDIAGL--ELYLPLRSGAGVVLADADTARNPAALID---LAGRHRVTLAQATPTLWQAL--VPeLSGPALAG 748
Cdd:PRK07529 256 TVFCGLPLFHVNALlvTGLAPLARGAHVVLATPQGYRGPGVIANfwkIVERYRINFLSGVPTVYAALlqVP-VDGHDISS 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 749 IR-VLVGGEALPAELARRLGDA-GAEVTNMYGPTETTIWSTSGPtSEDSIRRGSIGVPIDNTQVYVL-----DANLHPAP 821
Cdd:PRK07529 335 LRyALCGAAPLPVEVFRRFEAAtGVRIVEGYGLTEATCVSSVNP-PDGERRIGSVGLRLPYQRVRVVilddaGRYLRDCA 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 822 IGVLGELHIAGEGLARGYwnrpgLTAEK----FLPDpfgppgtRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELG 897
Cdd:PRK07529 414 VDEVGVLCIAGPNVFSGY-----LEAAHnkglWLED-------GWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPA 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 898 EIETTLINAGPVRRAAAVVRED-RPGDLRlVAYV--IPDGPVAPDALRTELSRTLPD-YMIPAVIVPVPDFPTTPNGKLD 973
Cdd:PRK07529 482 AIEEALLRHPAVALAAAVGRPDaHAGELP-VAYVqlKPGASATEAELLAFARDHIAErAAVPKHVRILDALPKTAVGKIF 560
|
....
gi 653678460 974 RAAL 977
Cdd:PRK07529 561 KPAL 564
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
499-972 |
2.19e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 110.13 E-value: 2.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 499 QWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVE 578
Cdd:PRK07470 15 QAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 579 RIAYLLSDARPVLVVTDAATAD-----RLGPDDITGLVVLEETDTG-GYPA---------TEPPAVPAGHSAYVIYTSGS 643
Cdd:PRK07470 95 EVAYLAEASGARAMICHADFPEhaaavRAASPDLTHVVAIGGARAGlDYEAlvarhlgarVANAAVDHDDPCWFFFTSGT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 644 TGRPKGVVITRAAL----DNFLAAMaerFP-LTAEDRVLATTTVSFDiAGLELYLPLRSGAGVVLADADTArNPAALIDL 718
Cdd:PRK07470 175 TGRPKAAVLTHGQMafviTNHLADL---MPgTTEQDASLVVAPLSHG-AGIHQLCQVARGAATVLLPSERF-DPAEVWAL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 719 AGRHRVTLAQATPTLWQALV--PELSGPALAGIRVLV--GGEALPAELARRLGDAGAEVTNMYGPTETTIWSTSGP---- 790
Cdd:PRK07470 250 VERHRVTNLFTVPTILKMLVehPAVDRYDHSSLRYVIyaGAPMYRADQKRALAKLGKVLVQYFGLGEVTGNITVLPpalh 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 791 TSED--SIRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgppgtrmyRTGDL 868
Cdd:PRK07470 330 DAEDgpDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF--------RTGDL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 869 VRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAV-VREDRPGDLRLVAYVIPDG-PVAPDALRTELS 946
Cdd:PRK07470 402 GHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLgVPDPVWGEVGVAVCVARDGaPVDEAELLAWLD 481
|
490 500
....*....|....*....|....*.
gi 653678460 947 RTLPDYMIPAVIVPVPDFPTTPNGKL 972
Cdd:PRK07470 482 GKVARYKLPKRFFFWDALPKSGYGKI 507
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
509-980 |
2.31e-24 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 109.79 E-value: 2.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 509 AVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDAR 588
Cdd:PRK12406 4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 589 ----------------------PVLVV---TDAATADRLGPDDIT---GLVVLEETDTGGYPATePPAVPAGHSayVIYT 640
Cdd:PRK12406 84 arvliahadllhglasalpagvTVLSVptpPEIAAAYRISPALLTppaGAIDWEGWLAQQEPYD-GPPVPQPQS--MIYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 641 SGSTGRPKGVviTRAALDNFLAAMAER-----FPLTAEDRVLATTTV------SFDIAGLELylplrsGAGVVLadaDTA 709
Cdd:PRK12406 161 SGTTGHPKGV--RRAAPTPEQAAAAEQmraliYGLKPGIRALLTGPLyhsapnAYGLRAGRL------GGVLVL---QPR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 710 RNPAALIDLAGRHRVTLAQATPTLWQALvpeLSGPA-------LAGIRVLVGGEA-LPAELARRLGDAGAEVTN-MYGPT 780
Cdd:PRK12406 230 FDPEELLQLIERHRITHMHMVPTMFIRL---LKLPEevrakydVSSLRHVIHAAApCPADVKRAMIEWWGPVIYeYYGST 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 781 ETTIWSTSgpTSEDSIRR-GSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLAR-GYWNRPGLTAEkflpdpfgpp 858
Cdd:PRK12406 307 ESGAVTFA--TSEDALSHpGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAE---------- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 859 gtrMYRTGdlvrWSAAGDLEYLG---------RTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAY 929
Cdd:PRK12406 375 ---IDRGG----FITSGDVGYLDadgylflcdRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAV 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 653678460 930 VIPDGPVAPDA--LRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAALPAP 980
Cdd:PRK12406 448 VEPQPGATLDEadIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
502-980 |
2.72e-24 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 109.85 E-value: 2.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 502 RRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIA 581
Cdd:PRK13382 54 QRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 582 YLLSDARPVLVVTD---AATADR------------LGPDDITGLVVLEETDTggyPATEPPAVPAGHSAYVIYTSGSTGR 646
Cdd:PRK13382 134 EVVTREGVDTVIYDeefSATVDRaladcpqatrivAWTDEDHDLTVEVLIAA---HAGQRPEPTGRKGRVILLTSGTTGT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 647 PKGVVITRAALDNFLAAMAERFPLTAEDRVL--ATTTVSFDIAGLELYLPLRSgaGVVladadTAR--NPAALIDLAGRH 722
Cdd:PRK13382 211 PKGARRSGPGGIGTLKAILDRTPWRAEEPTVivAPMFHAWGFSQLVLAASLAC--TIV-----TRRrfDPEATLDLIDRH 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 723 RVTLAQATPTLWQ---ALVPE-LSGPALAGIRVLVG-GEALPAELAR----RLGDAgaeVTNMYGPTETTIWSTSGPtse 793
Cdd:PRK13382 284 RATGLAVVPVMFDrimDLPAEvRNRYSGRSLRFAAAsGSRMRPDVVIafmdQFGDV---IYNNYNATEAGMIATATP--- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 794 DSIRRG--SIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYwnRPGLTAEKFlpdpfgppgTRMYRTGDLVRW 871
Cdd:PRK13382 358 ADLRAApdTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKDFH---------DGFMASGDVGYL 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 872 SAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIPDGPVA--PDALRTELSRTL 949
Cdd:PRK13382 427 DENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASatPETLKQHVRDNL 506
|
490 500 510
....*....|....*....|....*....|.
gi 653678460 950 PDYMIPAVIVPVPDFPTTPNGKLDRAALPAP 980
Cdd:PRK13382 507 ANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1558-2033 |
2.92e-24 |
|
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: 108.67 E-value: 2.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1558 TFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGY-PMARLTRIADTVTPAL 1636
Cdd:cd05971 8 TFKELKTASNRFANVLK--EIG---LEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFgPEALEYRLSNSGASAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1637 VltrtgqggclpgaevfgdvpvvaldrvadrlTAMPDqrpevtvDPrglAYSIFTSGSTGQPKGVAVEHIGIVRYLSWAA 1716
Cdd:cd05971 83 V-------------------------------TDGSD-------DP---ALIIYTSGTTGPPKGALHAHRVLLGHLPGVQ 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1717 ASYPTAGRRGTLAHSS-----VG--FDLTMSALFE--PLVSGRgVTLMPADATLaDLAEELSGPLAYdyirLTPSHLRHL 1787
Cdd:cd05971 122 FPFNLFPRDGDLYWTPadwawIGglLDVLLPSLYFgvPVLAHR-MTKFDPKAAL-DLMSRYGVTTAF----LPPTALKMM 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1788 VGHWTGQELPPAA-RGWVVGGETLDPALVKQLLElRPDAEVINHYGPTET--VIGR--VVHPVReagelavdsPLPLGRP 1862
Cdd:cd05971 196 RQQGEQLKHAQVKlRAIATGGESLGEELLGWARE-QFGVEVNEFYGQTECnlVIGNcsALFPIK---------PGSMGKP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1863 LGETRLQVLDAWLEAVPVGAVGELFIG-GDGIAR-GYLGRPALTAEKFLPDpagepgarMYRTGDLVRWRGDGLLDFVGR 1940
Cdd:cd05971 266 IPGHRVAIVDDNGTPLPPGEVGEIAVElPDPVAFlGYWNNPSATEKKMAGD--------WLLTGDLGRKDSDGYFWYVGR 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1941 VDDQVKLRGYRIELGEIEARMAEHPGVEQAVVL-----VRDQQLVGWFIPAEDHPP--VTVSALRRFCAEQLPEFMVPNQ 2013
Cdd:cd05971 338 DDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVgipdpIRGEIVKAFVVLNPGETPsdALAREIQELVKTRLAAHEYPRE 417
|
490 500
....*....|....*....|
gi 653678460 2014 WVALDAFPLTPHGKVNHRAL 2033
Cdd:cd05971 418 IEFVNELPRTATGKIRRREL 437
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
1084-1407 |
3.17e-24 |
|
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: 108.17 E-value: 3.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1084 PLSPMQESIWLADQVSAGDSVYNVPLALRLIGPLDRGALRRTLNRVVDRHEMLRTRIHPGPDGMPVQV--ADPAGGGAAL 1161
Cdd:cd19547 3 PLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYvrDDLAPPWALL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1162 TERDAAPGTDLAQLLLAEA---ALGFTLATEHPLRAVLWRLDEREHVLLLTAHHVAVDAWSMDLIQRDLTELYAADTGHR 1238
Cdd:cd19547 83 DWSGEDPDRRAELLERLLAddrAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAHGR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1239 EPELdEPALAQADYAVWQRQSAQRGRYAAEldFWRTELTGAVATEVAgdlPRPATPGGGGGAVEFALAPRQIQGIRELAR 1318
Cdd:cd19547 163 EPQL-SPCRPYRDYVRWIRARTAQSEESER--FWREYLRDLTPSPFS---TAPADREGEFDTVVHEFPEQLTRLVNEAAR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1319 RCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGRgNPRL---DNLVGCLVNTVVLRGDLSGAPTFHELLRRTHARTAD 1395
Cdd:cd19547 237 GYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGR-PPELegsEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDLAT 315
|
330
....*....|..
gi 653678460 1396 ALAHQELPFEHL 1407
Cdd:cd19547 316 TAAHGHVPLAQI 327
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1536-2033 |
3.35e-24 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 109.59 E-value: 3.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1536 LVEAQADRTPGWTALR-TGDR-SLTFAGLDAQANRLAHALHTGALGappvgPETPVLLLLDRSPELVVAMLAVLKAGGYF 1613
Cdd:PRK05852 21 LVEVAATRLPEAPALVvTADRiAISYRDLARLVDDLAGQLTRSGLL-----PGDRVALRMGSNAEFVVALLAASRADLVV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1614 IPVDPGYPMARLT-RIADTVTPALVLTRTGQGGCLPGAEVFGDVPV-VALDRVADRLTAMP--DQRPEVTVD---PRGL- 1685
Cdd:PRK05852 96 VPLDPALPIAEQRvRSQAAGARVVLIDADGPHDRAEPTTRWWPLTVnVGGDSGPSGGTLSVhlDAATEPTPAtstPEGLr 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1686 ---AYSIFTSGSTGQPKGVAVEHIGIVRYLSWAAASYPTAGRRGTLAHSSV--GFDLtMSALFEPLVSGrGVTLMPADAT 1760
Cdd:PRK05852 176 pddAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLyhGHGL-IAALLATLASG-GAVLLPARGR 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1761 LA--DLAEELSGPLAYDYIRLTPSH--LRHLVGHWTGQELPPAARGWVVGGETLDPAlVKQLLELRPDAEVINHYGPTET 1836
Cdd:PRK05852 254 FSahTFWDDIKAVGATWYTAVPTIHqiLLERAATEPSGRKPAALRFIRSCSAPLTAE-TAQALQTEFAAPVVCAFGMTEA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1837 VIGRVVHPVREAG--ELAVDSPLPLGRPLGeTRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDpag 1914
Cdd:PRK05852 333 THQVTTTQIEGIGqtENPVVSTGLVGRSTG-AQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDG--- 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1915 epgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRDQQLVGWFIPAEDHP---- 1990
Cdd:PRK05852 409 -----WLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPresa 483
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 653678460 1991 PVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:PRK05852 484 PPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
485-704 |
4.87e-24 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 109.58 E-value: 4.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 485 ARPLPAASLRERFQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKA 564
Cdd:PRK08279 31 ITPDSKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 565 GAA-----------------------YLPIDPDF--PVERIAYLLSDARPVLVVTDAATADRLGPDDITGLVvleetdtG 619
Cdd:PRK08279 111 GAVvallntqqrgavlahslnlvdakHLIVGEELveAFEEARADLARPPRLWVAGGDTLDDPEGYEDLAAAA-------A 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 620 GYPATEPPA---VPAGHSAYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDRVLATttvsfdiaglelyLPLR 696
Cdd:PRK08279 184 GAPTTNPASrsgVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCC-------------LPLY 250
|
....*...
gi 653678460 697 SGAGVVLA 704
Cdd:PRK08279 251 HNTGGTVA 258
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
517-915 |
7.42e-24 |
|
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: 107.27 E-value: 7.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 517 LSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPidpdfpveriayllsdarpvlvvtda 596
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 597 ATAdRLGPDDITglvvlEETDTGGYPATEPPAVPAGHSAYVIY-TSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDR 675
Cdd:cd05974 55 ATT-LLTPDDLR-----DRVDRGGAVYAAVDENTHADDPMLLYfTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGDV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 676 VLATTTVSF-DIAGLELYLPLRSGAGVVLADaDTARNPAALIDLAGRHRVTLAQATPTLWQALVPELSGPALAGIRVLVG 754
Cdd:cd05974 129 HWNISSPGWaKHAWSCFFAPWNAGATVFLFN-YARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVKLREVVG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 755 -GEALPAELARRLGDA-GAEVTNMYGPTETTIWSTSGPTSedSIRRGSIGVPIDNTQVYVLDANLHPAPIG----VLGEL 828
Cdd:cd05974 208 aGEPLNPEVIEQVRRAwGLTIRDGYGQTETTALVGNSPGQ--PVKAGSMGRPLPGYRVALLDPDGAPATEGevalDLGDT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 829 HIAGegLARGYWNRPGLTAEKFlpdpfgppGTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGP 908
Cdd:cd05974 286 RPVG--LMKGYAGDPDKTAHAM--------RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPA 355
|
....*..
gi 653678460 909 VRRAAAV 915
Cdd:cd05974 356 VAEAAVV 362
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
1522-2028 |
7.78e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 108.98 E-value: 7.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1522 RSEQHVGDDRTVHQLVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAhalhtGALGAPPVGPETPVLLLLDRSPELVV 1601
Cdd:PRK06178 24 REPEYPHGERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFA-----ALLRQRGVGAGDRVAVFLPNCPQFHI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1602 AMLAVLKAGGYFIPVDPG------------------------YPMARLTRIADTVTPALVltrTGQGGCLPGAEVFG--- 1654
Cdd:PRK06178 99 VFFGILKLGAVHVPVSPLfrehelsyelndagaevllaldqlAPVVEQVRAETSLRHVIV---TSLADVLPAEPTLPlpd 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1655 --DVPVVALDRVADRLTAMPDQR---PEVTVDPRGLAYSIFTSGSTGQPKGVAVEHIGIVrYLswAAASYPTAGRRGTla 1729
Cdd:PRK06178 176 slRAPRLAAAGAIDLLPALRACTapvPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMV-YT--AAAAYAVAVVGGE-- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1730 hSSV-----------GFDLTMsaLFePLVSGRGVTLMP---ADATLA--------------DLAEEL---SGPLAYDYir 1778
Cdd:PRK06178 251 -DSVflsflpefwiaGENFGL--LF-PLFSGATLVLLArwdAVAFMAaveryrvtrtvmlvDNAVELmdhPRFAEYDL-- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1779 ltpSHLRHlvghwtgqelpPAARGWVvggETLDPALVKQLLELRPDAEVINHYGPTETVIGRVVHPVREAGELAVDS-PL 1857
Cdd:PRK06178 325 ---SSLRQ-----------VRVVSFV---KKLNPDYRQRWRALTGSVLAEAAWGMTETHTCDTFTAGFQDDDFDLLSqPV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1858 PLGRPLGETRLQVLD-AWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFlpdpagEPGarMYRTGDLVRWRGDGLLD 1936
Cdd:PRK06178 388 FVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL------RDG--WLHTGDIGKIDEQGFLH 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1937 FVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRD-----QQLVGWFIPAEDHpPVTVSALRRFCAEQLPEFMVP 2011
Cdd:PRK06178 460 YLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPdpdkgQVPVAFVQLKPGA-DLTAAALQAWCRENMAVYKVP 538
|
570
....*....|....*..
gi 653678460 2012 NQWVaLDAFPLTPHGKV 2028
Cdd:PRK06178 539 EIRI-VDALPMTATGKV 554
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
502-979 |
8.25e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 108.58 E-value: 8.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 502 RRTPGAVAVIEGDTTLSYRE-LDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPdfpVERI 580
Cdd:PRK13388 12 RAGDDTIAVRYGDRTWTWREvLAEAAARAAALIALADPDRPLHVGVLLGNTPEMLFWLAAAALGGYVLVGLNT---TRRG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 581 AYLLSDARPV---LVVTDAATADRLGPDDITGLVVLEeTDTGGY-------PATEP-PAVPAGHSAYVIYTSGSTGRPKG 649
Cdd:PRK13388 89 AALAADIRRAdcqLLVTDAEHRPLLDGLDLPGVRVLD-VDTPAYaelvaaaGALTPhREVDAMDPFMLIFTSGTTGAPKA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 650 VVITRAALDNFLAAMAERFPLTAEDRVLATTTVSFDIAGLELYLP-LRSGAGVVLAD--------ADTARNPAALIDLAG 720
Cdd:PRK13388 168 VRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPaVASGAAVALPAkfsasgflDDVRRYGATYFNYVG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 721 RhrvTLAQATPTlwqalvPELSGPALAGIRVLVGGEALP---AELARRLGdagAEVTNMYGPTETTIWSTSGPTSEdsir 797
Cdd:PRK13388 248 K---PLAYILAT------PERPDDADNPLRVAFGNEASPrdiAEFSRRFG---CQVEDGYGSSEGAVIVVREPGTP---- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 798 RGSIGVPIDNTQVY-----------VLDANLHPA-PIGVLGEL-HIAGEGLARGYWNRPGLTAEKFlpdpfgppgtR--M 862
Cdd:PRK13388 312 PGSIGRGAPGVAIYnpetltecavaRFDAHGALLnADEAIGELvNTAGAGFFEGYYNNPEATAERM----------RhgM 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 863 YRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAA-VVREDRPGDLRLVAYVIPDG-PVAPDA 940
Cdd:PRK13388 382 YWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVyAVPDERVGDQVMAALVLRDGaTFDPDA 461
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 653678460 941 LRTELS--RTLPDYMIPAVIVPVPDFPTTPNGKLDRAALPA 979
Cdd:PRK13388 462 FAAFLAaqPDLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
1548-2033 |
9.52e-24 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 107.18 E-value: 9.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1548 TALRTGDRSLTFAGLDAQANRLAHALhTGALGAPPVGPetpVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMARLTR 1627
Cdd:cd05958 2 TCLRSPEREWTYRDLLALANRIANVL-VGELGIVPGNR---VLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1628 IADTVTPALVLtrtgqggclpgaevfgdvpvvaldrVADRLTAMPDqrpevtvdprgLAYSIFTSGSTGQPKGVAVEHig 1707
Cdd:cd05958 78 ILDKARITVAL-------------------------CAHALTASDD-----------ICILAFTSGTTGAPKATMHFH-- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1708 ivRYLSWAAASYPTAGRRGT-------LAHSSVGFDLTMSALFePLVSGRGVTLMPadATLADLAEELSGPLAYDYIRLT 1780
Cdd:cd05958 120 --RDPLASADRYAVNVLRLReddrfvgSPPLAFTFGLGGVLLF-PFGVGASGVLLE--EATPDLLLSAIARYKPTVLFTA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1781 PSHLRHLVGH--WTGQELPPaARGWVVGGETLDPALVKQLLELRpDAEVINHYGPTEtvigrVVHPVREAGELAVdSPLP 1858
Cdd:cd05958 195 PTAYRAMLAHpdAAGPDLSS-LRKCVSAGEALPAALHRAWKEAT-GIPIIDGIGSTE-----MFHIFISARPGDA-RPGA 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1859 LGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGylgrpaltaekflpdpAGEPGARMY------RTGDLVRWRGD 1932
Cdd:cd05958 267 TGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGPTGCRY----------------LADKRQRTYvqggwnITGDTYSRDPD 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1933 GLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQ-AVVLVRDQ---QLVGWFI---PAEDHPPVTVSALRRFCAEQL 2005
Cdd:cd05958 331 GYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAEcAVVGHPDEsrgVVVKAFVvlrPGVIPGPVLARELQDHAKAHI 410
|
490 500
....*....|....*....|....*...
gi 653678460 2006 PEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:cd05958 411 APYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
1536-2023 |
1.17e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 107.91 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1536 LVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAhalhtGALGAPPVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIP 1615
Cdd:PRK06164 15 LLDAHARARPDAVALIDEDRPLSRAELRALVDRLA-----AWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1616 VDPGYPMARLTRIADTVTPALVLTRTGQGGcLPGAEVFGDVP---------VVALDRVAD--------RLTAMPDQRPEV 1678
Cdd:PRK06164 90 VNTRYRSHEVAHILGRGRARWLVVWPGFKG-IDFAAILAAVPpdalpplraIAVVDDAADatpapapgARVQLFALPDPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1679 TV--------DPRGLAYSIFTSGSTGQPKGVAVEHIGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMSALFEPLVSGR 1750
Cdd:PRK06164 169 PPaaageraaDPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1751 GVTLMP---ADATLADLAEElsgplaydyiRLTpshlrHLVG--------HWTGQELPPAARGWVVGGETLDPALVKQLL 1819
Cdd:PRK06164 249 PLVCEPvfdAARTARALRRH----------RVT-----HTFGndemlrriLDTAGERADFPSARLFGFASFAPALGELAA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1820 ELRP-DAEVINHYGPTETVIGRVVHPVREAgelAVDSPLPLGRPL-GETRLQVLDAWLEAV-PVGAVGELFIGGDGIARG 1896
Cdd:PRK06164 314 LARArGVPLTGLYGSSEVQALVALQPATDP---VSVRIEGGGRPAsPEARVRARDPQDGALlPDGESGEIEIRAPSLMRG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1897 YLGRPALTAEKFLPDPagepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVE--QAVVLV 1974
Cdd:PRK06164 391 YLDNPDATARALTDDG-------YFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAaaQVVGAT 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 653678460 1975 RDQQLVGW-FIPAEDHPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLT 2023
Cdd:PRK06164 464 RDGKTVPVaFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVT 513
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
487-977 |
1.22e-23 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 108.18 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 487 PLPAASLRERFQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGA 566
Cdd:PRK07059 19 ASQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 567 AYLPIDPDFPVERIAYLLSDA---------------------RPVLVVTDAATADRLGPDD-ITGLVV------------ 612
Cdd:PRK07059 99 VVVNVNPLYTPRELEHQLKDSgaeaivvlenfattvqqvlakTAVKHVVVASMGDLLGFKGhIVNFVVrrvkkmvpawsl 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 613 ---------LEEtdtGGYPATEPPAVPAGHSAYVIYTSGSTGRPKGVVITRAaldNFLAAMAE-----RFPLTAEDRVLA 678
Cdd:PRK07059 179 pghvrfndaLAE---GARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHR---NIVANVLQmeawlQPAFEKKPRPDQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 679 TTTVsfdiAGLELY----------LPLRSGA-GVVLADAdtaRNPAALIDLAGRHRVTLAQATPTLWQALV--PELSGPA 745
Cdd:PRK07059 253 LNFV----CALPLYhifaltvcglLGMRTGGrNILIPNP---RDIPGFIKELKKYQVHIFPAVNTLYNALLnnPDFDKLD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 746 LAGIRV-LVGGEALPAELARR-LGDAGAEVTNMYGPTETTIWSTSGPTSEDSIRrGSIGVPIDNTQVYVLDANLHPAPIG 823
Cdd:PRK07059 326 FSKLIVaNGGGMAVQRPVAERwLEMTGCPITEGYGLSETSPVATCNPVDATEFS-GTIGLPLPSTEVSIRDDDGNDLPLG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 824 VLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgppgtrmYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTL 903
Cdd:PRK07059 405 EPGEICIRGPQVMAGYWNRPDETAKVMTADGF-------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVV 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 653678460 904 INAGPVRRAAAV-VREDRPGDLrLVAYVIPDGPVAPDALRTELSRT-LPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:PRK07059 478 ASHPGVLEVAAVgVPDEHSGEA-VKLFVVKKDPALTEEDVKAFCKErLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
503-979 |
1.73e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 107.39 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 503 RTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAY 582
Cdd:PRK13383 47 RWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 583 LLSDARPVLVVTDAATADRLGPDDITGLVVLEET----DTGGYPATEPPAvpaghsAYVIYTSGSTGRPKGV---VITRA 655
Cdd:PRK13383 127 ALRAHHISTVVADNEFAERIAGADDAVAVIDPATagaeESGGRPAVAAPG------RIVLLTSGTTGKPKGVpraPQLRS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 656 ALDNFLAAMaERFPLTAEDRVLATTTVsFDIAGLELYLPLRSGAGVVLA----DADTARNPAALidlagrHRVTLAQATP 731
Cdd:PRK13383 201 AVGVWVTIL-DRTRLRTGSRISVAMPM-FHGLGLGMLMLTIALGGTVLThrhfDAEAALAQASL------HRADAFTAVP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 732 TLWqALVPEL-----SGPALAGIRVLV-GGEALPAELARRLGDAGAEVT-NMYGPTETTIWSTSGPtSEDSIRRGSIGVP 804
Cdd:PRK13383 273 VVL-ARILELpprvrARNPLPQLRVVMsSGDRLDPTLGQRFMDTYGDILyNGYGSTEVGIGALATP-ADLRDAPETVGKP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 805 IDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGltaeKFLPDPfgppgtrMYRTGDLVRWSAAGDLEYLGRTD 884
Cdd:PRK13383 351 VAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDGGG----KAVVDG-------MTSTGDMGYLDNAGRLFIVGRED 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 885 HQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVI--PDGPVAPDALRTELSRTLPDYMIPAVIVPVP 962
Cdd:PRK13383 420 DMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVlhPGSGVDAAQLRDYLKDRVSRFEQPRDINIVS 499
|
490
....*....|....*..
gi 653678460 963 DFPTTPNGKLDRAALPA 979
Cdd:PRK13383 500 SIPRNPTGKVLRKELPG 516
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
637-974 |
2.02e-23 |
|
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: 104.26 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 637 VIYTSGSTGRPKGVVITR----AALDNFlaaMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNp 712
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANktffAVPDIL---QKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYK- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 713 aALIDLAGRHRVTLAQATPTLWQALVPELSGpALAGIR----VLVGGE-ALPAELARRLGDAGAEVTNMYGPTETTIwST 787
Cdd:cd17635 82 -SLFKILTTNAVTTTCLVPTLLSKLVSELKS-ANATVPslrlIGYGGSrAIAADVRFIEATGLTNTAQVYGLSETGT-AL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 788 SGPTSEDSIRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgppgtrmyRTGD 867
Cdd:cd17635 159 CLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV--------NTGD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 868 LVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAA-AVVREDRPGDLRLVAYVIP--DGPVAPDALRTE 944
Cdd:cd17635 231 LGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECAcYEISDEEFGELVGLAVVASaeLDENAIRALKHT 310
|
330 340 350
....*....|....*....|....*....|
gi 653678460 945 LSRTLPDYMIPAVIVPVPDFPTTPNGKLDR 974
Cdd:cd17635 311 IRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
512-977 |
3.42e-23 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 106.31 E-value: 3.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 512 EGDT-TLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARPV 590
Cdd:PRK08008 32 GGVVrRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQAS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 591 LVVTDAA---TADRLGPDD---ITGLVVL---EETDTGGY---------PAT--EPPAVPAGHSAYVIYTSGSTGRPKGV 650
Cdd:PRK08008 112 LLVTSAQfypMYRQIQQEDatpLRHICLTrvaLPADDGVSsftqlkaqqPATlcYAPPLSTDDTAEILFTSGTTSRPKGV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 651 VITRAaldNFLAA---MAERFPLTAEDRVLaTTTVSFDI-----AGLELylpLRSGAGVVLADADTARnpaALIDLAGRH 722
Cdd:PRK08008 192 VITHY---NLRFAgyySAWQCALRDDDVYL-TVMPAFHIdcqctAAMAA---FSAGATFVLLEKYSAR---AFWGQVCKY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 723 RVTLAQATPTLwqalvpelsgpalagIRVLVGGEALPAELARRLGDA------------------GAEVTNMYGPTETTI 784
Cdd:PRK08008 262 RATITECIPMM---------------IRTLMVQPPSANDRQHCLREVmfylnlsdqekdafeerfGVRLLTSYGMTETIV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 785 WSTsGPTSEDSIRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELHI---AGEGLARGYWNRPGLTAEKFLPDPFgppgtr 861
Cdd:PRK08008 327 GII-GDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIkgvPGKTIFKEYYLDPKATAKVLEADGW------ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 862 mYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIP-DG-PVAPD 939
Cdd:PRK08008 400 -LHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLnEGeTLSEE 478
|
490 500 510
....*....|....*....|....*....|....*...
gi 653678460 940 ALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:PRK08008 479 EFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
639-974 |
4.14e-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: 4.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 639 YTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDRVLATTTVsFDIAGLEL--YLPLRSGAGVVLADAdtARNPAALI 716
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPL-FHCFGSVLgvLACLTHGATMVFPSP--SFDPLAVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 717 DLAGRHRVTLAQATPTLWQALV--PELSGPALAGIRV-LVGGEALPAELARRL-GDAG-AEVTNMYGPTETTIWSTSGpT 791
Cdd:cd05917 86 EAIEKEKCTALHGVPTMFIAELehPDFDKFDLSSLRTgIMAGAPCPPELMKRViEVMNmKDVTIAYGMTETSPVSTQT-R 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 792 SEDSI--RRGSIGVPIDNTQVYVLDANLHP-APIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDpfgppgtRMYRTGDL 868
Cdd:cd05917 165 TDDSIekRVNTVGRIMPHTEAKIVDPEGGIvPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGD-------GWLHTGDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 869 VRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAV-VREDRPGDlRLVAYVI--PDGPVAPDALRTEL 945
Cdd:cd05917 238 AVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVgVPDERYGE-EVCAWIRlkEGAELTEEDIKAYC 316
|
330 340
....*....|....*....|....*....
gi 653678460 946 SRTLPDYMIPAVIVPVPDFPTTPNGKLDR 974
Cdd:cd05917 317 KGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1557-2033 |
4.23e-23 |
|
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: 106.21 E-value: 4.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1557 LTFAGLDAQANRLAHALhtGALGAPPvgPETpVLLLLDRSPELVVAMLAVLKAGgyFIPVDPGYPMA---------RLTR 1627
Cdd:cd05906 40 QSYQDLLEDARRLAAGL--RQLGLRP--GDS-VILQFDDNEDFIPAFWACVLAG--FVPAPLTVPPTydepnarlrKLRH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1628 IADTVTPALVLTRTGQGGCLPGAEVFGDVPVVALDRVADRLTAMPDQrPEVTVDPRGLAYSIFTSGSTGQPKGVAVEHIG 1707
Cdd:cd05906 113 IWQLLGSPVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADH-DLPQSRPDDLALLMLTSGSTGFPKAVPLTHRN 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1708 IVRYLSWAAASYPTAGRRGTLahSSVGFD----LTMSALFePLVSGRGVTLMPADATLADlaeelsgPLAY-DYI---RL 1779
Cdd:cd05906 192 ILARSAGKIQHNGLTPQDVFL--NWVPLDhvggLVELHLR-AVYLGCQQVHVPTEEILAD-------PLRWlDLIdryRV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1780 T----P----SHLRHLV-----GHWTGQELppaaRGWVVGGETLDPALVKQLLE------LRPDAeVINHYGPTETVIGR 1840
Cdd:cd05906 262 TitwaPnfafALLNDLLeeiedGTWDLSSL----RYLVNAGEAVVAKTIRRLLRllepygLPPDA-IRPAFGMTETCSGV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1841 VVHPVREAGELAVDSPL-PLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDpagepgaR 1919
Cdd:cd05906 337 IYSRSFPTYDHSQALEFvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTED-------G 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1920 MYRTGDLVrWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQ---AVVLVRDQ-----QLVGWFIPAEDHPP 1991
Cdd:cd05906 410 WFRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsftAAFAVRDPgaeteELAIFFVPEYDLQD 488
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 653678460 1992 V---TVSALRRFCAEQL---PEFMVPnqwVALDAFPLTPHGKVNHRAL 2033
Cdd:cd05906 489 AlseTLRAIRSVVSREVgvsPAYLIP---LPKEEIPKTSLGKIQRSKL 533
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
498-977 |
6.17e-23 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 104.95 E-value: 6.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 498 QQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPV 577
Cdd:PRK09029 10 RHWAQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 578 ERIAYLLsdarPVLVVTDAATADRLG-PDDITGLVVLEetdtggYPATEPPAVPAGHSAYVIYTSGSTGRPKGVVIT-RA 655
Cdd:PRK09029 90 PLLEELL----PSLTLDFALVLEGENtFSALTSLHLQL------VEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTaQA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 656 ALDN---FLAAMaerfPLTAEDRVLatttvsfdiagleLYLPLR--SGAGVV----LADAD-TARNPAALI-DLAGrhrV 724
Cdd:PRK09029 160 HLASaegVLSLM----PFTAQDSWL-------------LSLPLFhvSGQGIVwrwlYAGATlVVRDKQPLEqALAG---C 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 725 TLAQATPT-LWQALvpELSGPALAGIRVLVGGEALPAELARRLGDAGAEVTNMYGPTETTiwSTSGPTSEDSirRGSIGV 803
Cdd:PRK09029 220 THASLVPTqLWRLL--DNRSEPLSLKAVLLGGAAIPVELTEQAEQQGIRCWCGYGLTEMA--STVCAKRADG--LAGVGS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 804 PIDNTQVYVLDanlhpapigvlGELHIAGEGLARGYWNRPGLTAekfLPDPFGppgtrMYRTGDLVRWsAAGDLEYLGRT 883
Cdd:PRK09029 294 PLPGREVKLVD-----------GEIWLRGASLALGYWRQGQLVP---LVNDEG-----WFATRDRGEW-QNGELTILGRL 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 884 DHQVKLRGFRIELGEIEtTLINAGP-VRRAAAVVRED-----RPgdlrlVAYVIPDGPVAPDALRTELSRTLPDYMIPAV 957
Cdd:PRK09029 354 DNLFFSGGEGIQPEEIE-RVINQHPlVQQVFVVPVADaefgqRP-----VAVVESDSEAAVVNLAEWLQDKLARFQQPVA 427
|
490 500
....*....|....*....|..
gi 653678460 958 IVPVPDfpTTPNG--KLDRAAL 977
Cdd:PRK09029 428 YYLLPP--ELKNGgiKISRQAL 447
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
488-985 |
9.18e-23 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 105.09 E-value: 9.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 488 LPAASLrERFQQWCRRTPGAVAV--IEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAG 565
Cdd:PRK05857 12 LPSTVL-DRVFEQARQQPEAIALrrCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 566 AAYLPIDPDFPVERIAYLLSDARPVLVVTD-----AATADRLGPDDITGLVVLEETDTG--------GYPATEpPAVPAG 632
Cdd:PRK05857 91 AIAVMADGNLPIAAIERFCQITDPAAALVApgskmASSAVPEALHSIPVIAVDIAAVTResehsldaASLAGN-ADQGSE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 633 HSAYVIYTSGSTGRPKGVVI---TRAALDNFLAAMAERFPltaeDRVLATTTVS----FDIAGLELYLPLRSGAGVVLAD 705
Cdd:PRK05857 170 DPLAMIFTSGTTGEPKAVLLanrTFFAVPDILQKEGLNWV----TWVVGETTYSplpaTHIGGLWWILTCLMHGGLCVTG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 706 ADtarNPAALIDLAGRHRVTLAQATPTLWQALVPEL--SGPALAGIRVLV-GGEALPAELARRLGDAGAEVTNMYGPTET 782
Cdd:PRK05857 246 GE---NTTSLLEILTTNAVATTCLVPTLLSKLVSELksANATVPSLRLVGyGGSRAIAADVRFIEATGVRTAQVYGLSET 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 783 TIWSTSGPTSEDSIRR---GSIGVPIDNTQVYVLDAN------LHPAPIGVLGELHIAGEGLARGYWNRPGLTAEkFLPD 853
Cdd:PRK05857 323 GCTALCLPTDDGSIVKieaGAVGRPYPGVDVYLAATDgigptaPGAGPSASFGTLWIKSPANMLGYWNNPERTAE-VLID 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 854 PFgppgtrmYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAV-VREDRPGDLRLVAyVIP 932
Cdd:PRK05857 402 GW-------VNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYeIPDEEFGALVGLA-VVA 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 933 DGPVAPDALRTELSRTLPDY-------MIPAVIVPVPDFPTTPNGKLDRAALPAPDYGTR 985
Cdd:PRK05857 474 SAELDESAARALKHTIAARFrresepmARPSTIVIVTDIPRTQSGKVMRASLAAAATADK 533
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
1557-2033 |
9.52e-23 |
|
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: 104.12 E-value: 9.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1557 LTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPvdpgypmarltrIADTVTPAL 1636
Cdd:cd05969 1 YTFAQLKVLSARFANVLK--SLG---VGKGDRVFVLSPRSPELYFSMLGIGKIGAVICP------------LFSAFGPEA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1637 VLTRTGQGGclpgAEVfgdvpVVALDRVADRLtampdqrpevtvDPRGLAYSIFTSGSTGQPKGVAVEHIGIVRYlsWAA 1716
Cdd:cd05969 64 IRDRLENSE----AKV-----LITTEELYERT------------DPEDPTLLHYTSGTTGTPKGVLHVHDAMIFY--YFT 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1717 ASYPtagrrgtlahssvgFDL-----------------TMSALFEPLVSGRGVTLMPADATladlAEELSGPLAYDYIRL 1779
Cdd:cd05969 121 GKYV--------------LDLhpddiywctadpgwvtgTVYGIWAPWLNGVTNVVYEGRFD----AESWYGIIERVKVTV 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1780 ---TPSHLRHLVGHwtGQELPPA-----ARGWVVGGETLDPALVKQLLELRpDAEVINHYGPTET---VIGRVV-HPVRe 1847
Cdd:cd05969 183 wytAPTAIRMLMKE--GDELARKydlssLRFIHSVGEPLNPEAIRWGMEVF-GVPIHDTWWQTETgsiMIANYPcMPIK- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1848 agelavdsPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGD--GIARGYLGRPALTAEKFlpdPAGepgarMYRTGD 1925
Cdd:cd05969 259 --------PGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPGwpSMFRGIWNDEERYKNSF---IDG-----WYLTGD 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1926 LVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRDQQLVGWFIPA-----EDHPPvtVSALRR- 1999
Cdd:cd05969 323 LAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAfislkEGFEP--SDELKEe 400
|
490 500 510
....*....|....*....|....*....|....*..
gi 653678460 2000 ---FCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:cd05969 401 iinFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVL 437
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
485-1085 |
2.89e-22 |
|
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: 105.17 E-value: 2.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 485 ARPLPAASLRERFQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKA 564
Cdd:COG3319 2 AAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 565 GAAYLPIDPDFPVERIAYLLSDARPVLVVTDAATADRLGPDDITGLVVLEETDTGGYPATEPPAVPAGHSAYVIYTSGST 644
Cdd:COG3319 82 AALALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 645 GRPKGVVITRAALDNFLAAMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADADTARNPAALIDLAGRHRV 724
Cdd:COG3319 162 GVLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 725 TLAQATPTLWQALVPELSGPALAGIRVLVGGEALPAELARRLGDAGAEVTNMYGPTETTIWSTSGPTSEDSIRRGSIGVP 804
Cdd:COG3319 242 LLLAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGGG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 805 IDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFGPPGTRMYRTGDLVRWSAAGDLEYLGRTD 884
Cdd:COG3319 322 PGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 885 HQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAY--VIPDGPVAPDALRTELSRTLPDYMIPAVIVPVP 962
Cdd:COG3319 402 RLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAavVAAAALAAAALLLLLLLLLLPPPLPPALLLLLL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 963 DFPTTPNGKLDRAALPAPDYGTRSTARPPRDDRERFLCTAFAEVLGLPEVAVSDNFFELGGHSLLAFRLLARIRDEFGAG 1042
Cdd:COG3319 482 LLLLLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRL 561
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 653678460 1043 FSLRRLLAAPTVAAVAAELAAETSTGDDAVHLAPVPRDEPLPL 1085
Cdd:COG3319 562 LLLLALLLAPTLAALAAALAAAAAAAALSPLVPLRAGGSGPPL 604
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
505-977 |
9.82e-22 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 102.23 E-value: 9.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 505 PGAVAVIEGDT--TLSYRELDERANRLARLLMER-GAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIA 581
Cdd:PLN02574 53 NGDTALIDSSTgfSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 582 YLLSDARPVLVVTDAATADRLGPDDITGLVVLEETD-TGGYPATEP--------------PAVPAGHSAYVIYTSGSTGR 646
Cdd:PLN02574 133 KRVVDCSVGLAFTSPENVEKLSPLGVPVIGVPENYDfDSKRIEFPKfyelikedfdfvpkPVIKQDDVAAIMYSSGTTGA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 647 PKGVVITR----AALDNFLAAMAERFPLTAEDRVLATTTVSFDIAGLELYLP--LRSGAGVVLADADTARNPAALIDlag 720
Cdd:PLN02574 213 SKGVVLTHrnliAMVELFVRFEASQYEYPGSDNVYLAALPMFHIYGLSLFVVglLSLGSTIVVMRRFDASDMVKVID--- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 721 RHRVTLAQATPTLWQALVPELSGPALAGIRVLVGGEALPAELARRLGDAGAEV------TNMYGPTETTIWSTSGPTSED 794
Cdd:PLN02574 290 RFKVTHFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTlphvdfIQGYGMTESTAVGTRGFNTEK 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 795 SIRRGSIGVPIDNTQVYVLDANLHPA-PIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgppgtrmYRTGDLVRWSA 873
Cdd:PLN02574 370 LSKYSSVGLLAPNMQAKVVDWSTGCLlPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW-------LRTGDIAYFDE 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 874 AGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVI--PDGPVAPDALRTELSRTLPD 951
Cdd:PLN02574 443 DGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVrrQGSTLSQEAVINYVAKQVAP 522
|
490 500
....*....|....*....|....*.
gi 653678460 952 YMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:PLN02574 523 YKKVRKVVFVQSIPKSPAGKILRREL 548
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
635-977 |
1.21e-21 |
|
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: 99.09 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 635 AYVIYTSGSTGRPKgVVITRAALDNFLAAMAERFPLTAEDRVLATTTVSFDIAGL--ELYLPLRSGAGVVLADADTARNP 712
Cdd:cd05944 5 AAYFHTGGTTGTPK-LAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSvvTLLTPLASGAHVVLAGPAGYRNP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 713 AALID---LAGRHRVTLAQATPTLWQALVPELSGPALAGIR-VLVGGEALPAELARRLGDA-GAEVTNMYGPTETTIWST 787
Cdd:cd05944 84 GLFDNfwkLVERYRITSLSTVPTVYAALLQVPVNADISSLRfAMSGAAPLPVELRARFEDAtGLPVVEGYGLTEATCLVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 788 SGPtSEDSIRRGSIGVPIDNTQV--YVLDANLH---PAPIGVLGELHIAGEGLARGYWNRPGLTaekflpDPFGPPGtrM 862
Cdd:cd05944 164 VNP-PDGPKRPGSVGLRLPYARVriKVLDGVGRllrDCAPDEVGEICVAGPGVFGGYLYTEGNK------NAFVADG--W 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 863 YRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYV--IPDGPVAPDA 940
Cdd:cd05944 235 LNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVqlKPGAVVEEEE 314
|
330 340 350
....*....|....*....|....*....|....*...
gi 653678460 941 LRTELSRTLPDY-MIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:cd05944 315 LLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
1536-2031 |
1.25e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 101.50 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1536 LVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIP 1615
Cdd:PRK07798 8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLI--AQG---LGPGDHVGIYARNRIEYVEAMLGAFKARAVPVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1616 VDPGYPMARLTRIADTVTPALVLTRTGQGGCLpgAEVFGDVP----VVALD------------RVADRLTAMPDQRPEVT 1679
Cdd:PRK07798 83 VNYRYVEDELRYLLDDSDAVALVYEREFAPRV--AEVLPRLPklrtLVVVEdgsgndllpgavDYEDALAAGSPERDFGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1680 VDPRGLaYSIFTSGSTGQPKGVAVEH--------IGIVRYLSWAAASYPTAGRRGTLAHSSVGFDL-----------TMS 1740
Cdd:PRK07798 161 RSPDDL-YLLYTGGTTGMPKGVMWRQedifrvllGGRDFATGEPIEDEEELAKRAAAGPGMRRFPApplmhgagqwaAFA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1741 AL-------------FEP-----LVSGRGVTLMP--ADATLADLAEELSGPLAYDYirltpSHLRHLVGhwtgqelppaa 1800
Cdd:PRK07798 240 ALfsgqtvvllpdvrFDAdevwrTIEREKVNVITivGDAMARPLLDALEARGPYDL-----SSLFAIAS----------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1801 rgwvvGGETLDPALVKQLLELRPDAEVINHYGPTETVIGRVVHPvrEAGELAVDSPLPLGRPlgetRLQVLDAWLEAVPV 1880
Cdd:PRK07798 304 -----GGALFSPSVKEALLELLPNVVLTDSIGSSETGFGGSGTV--AKGAVHTGGPRFTIGP----RTVVLDEDGNPVEP 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1881 GAVGELFIGGDG-IARGYLGRPALTAEKFlpdPAGEpGARMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEA 1959
Cdd:PRK07798 373 GSGEIGWIARRGhIPLGYYKDPEKTAETF---PTID-GVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEE 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 653678460 1960 RMAEHPGVEQAVVLVRD-----QQLVGWFIPAEDHPPvTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHR 2031
Cdd:PRK07798 449 ALKAHPDVADALVVGVPderwgQEVVAVVQLREGARP-DLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKADYR 524
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
502-974 |
1.60e-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: 101.87 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 502 RRTPGAVAVI-EGD-----TTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDF 575
Cdd:cd05966 64 KERGDKVAIIwEGDepdqsRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 576 PVERIAYLLSDARPVLVVT-DA-----------ATAD---RLGPDdITGLVVLEETDT----------------GGYPAT 624
Cdd:cd05966 144 SAESLADRINDAQCKLVITaDGgyrggkviplkEIVDealEKCPS-VEKVLVVKRTGGevpmtegrdlwwhdlmAKQSPE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 625 -EPPAVPAGHSAYVIYTSGSTGRPKGVVITRAAldnFL--AAMAER--FPLTAEDRVLATTTVSFdIAGLE--LYLPLRS 697
Cdd:cd05966 223 cEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGG---YLlyAATTFKyvFDYHPDDIYWCTADIGW-ITGHSyiVYGPLAN 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 698 GAGVVLAD-ADTARNPAALIDLAGRHRVTLAQATPTLWQALVPElsGPA------LAGIRVL--VGgEALPAE----LAR 764
Cdd:cd05966 299 GATTVMFEgTPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKF--GDEwvkkhdLSSLRVLgsVG-EPINPEawmwYYE 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 765 RLGDAGAEVTNMYGPTET-TIWSTSGPtSEDSIRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGE--GLARGYWN 841
Cdd:cd05966 376 VIGKERCPIVDTWWQTETgGIMITPLP-GATPLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYG 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 842 RPgltaEKFLPDPFGP-PGtrMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVvreDR 920
Cdd:cd05966 455 DH----ERYEDTYFSKfPG--YYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVV---GR 525
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 653678460 921 PGDLR---LVAYVIP-DGPVAPDALRTEL----SRTLPDYMIPAVIVPVPDFPTTPNGKLDR 974
Cdd:cd05966 526 PHDIKgeaIYAFVTLkDGEEPSDELRKELrkhvRKEIGPIATPDKIQFVPGLPKTRSGKIMR 587
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
484-977 |
1.95e-21 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 101.12 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 484 TARPLPAA---SLRERFQQWCRRTPGAVAVIEGD--TTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTL 558
Cdd:PRK05852 6 GAAPMASDfgpRIADLVEVAATRLPEAPALVVTAdrIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 559 LAVIKAGAAYLPIDPDFPV--ERIAYLLSDARPVLVVTDA------------ATADRLGPDDITGLVVLEETDTGGYPAT 624
Cdd:PRK05852 86 LAASRADLVVVPLDPALPIaeQRVRSQAAGARVVLIDADGphdraepttrwwPLTVNVGGDSGPSGGTLSVHLDAATEPT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 625 EPPAVPAG---HSAYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGV 701
Cdd:PRK05852 166 PATSTPEGlrpDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 702 VLADAD---TARNPAALIDLAGrhrVTLAQATPTLWQALV----PELSGPALAGIRVLVGGEA-LPAELARRLGDA-GAE 772
Cdd:PRK05852 246 VLLPARgrfSAHTFWDDIKAVG---ATWYTAVPTIHQILLeraaTEPSGRKPAALRFIRSCSApLTAETAQALQTEfAAP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 773 VTNMYGPTETTIWSTSgpTSEDSIRRG-----SIGVPIDNT--QVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGL 845
Cdd:PRK05852 323 VVCAFGMTEATHQVTT--TQIEGIGQTenpvvSTGLVGRSTgaQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 846 TAEKFLPDPFgppgtrmyRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLR 925
Cdd:PRK05852 401 TAANFTDGWL--------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEA 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 653678460 926 LVAYVIPDGPVAP--DALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:PRK05852 473 VAAVIVPRESAPPtaEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
1534-2036 |
2.13e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 100.83 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1534 HQLVEAQAdRTPGWTALRTGDRSLTFAGLDAQANRLAHALHtgALGAppvGPETPVLLLLDRSPELVVAMLAVLKAGGYF 1613
Cdd:PRK06188 16 HLLVSALK-RYPDRPALVLGDTRLTYGQLADRISRYIQAFE--ALGL---GTGDAVALLSLNRPEVLMAIGAAQLAGLRR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1614 IPVdpgYPMARLTR----IAD------TVTPALVLTRTG----QGGCLPGAEVFGDVPV-VALDRVADRLTAMPDQRPEV 1678
Cdd:PRK06188 90 TAL---HPLGSLDDhayvLEDagistlIVDPAPFVERALallaRVPSLKHVLTLGPVPDgVDLLAAAAKFGPAPLVAAAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1679 TVDPRGLAYsifTSGSTGQPKGVAVEHIGIVRYLSWAAASY--PTAGRRGT---LAHSSvgfdltmSALFEP-LVSGRGV 1752
Cdd:PRK06188 167 PPDIAGLAY---TGGTTGKPKGVMGTHRSIATMAQIQLAEWewPADPRFLMctpLSHAG-------GAFFLPtLLRGGTV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1753 TLMP---ADATLADLAEElsgplaydYIRLT---PSHLRHLVGHwtgqelPPAARG------WVV-GGETLDPALVKQLL 1819
Cdd:PRK06188 237 IVLAkfdPAEVLRAIEEQ--------RITATflvPTMIYALLDH------PDLRTRdlssleTVYyGASPMSPVRLAEAI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1820 ElRPDAEVINHYGPTE-----TVIGRVVHPVREAGELAvdsplPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIA 1894
Cdd:PRK06188 303 E-RFGPIFAQYYGQTEapmviTYLRKRDHDPDDPKRLT-----SCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVM 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1895 RGYLGRPALTAEKFLPDpagepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQ-AVVL 1973
Cdd:PRK06188 377 DGYWNRPEETAEAFRDG--------WLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQvAVIG 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 653678460 1974 VRDQQ---LVGWFIPAEDHPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRALPGP 2036
Cdd:PRK06188 449 VPDEKwgeAVTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRAR 514
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1529-2031 |
2.67e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 100.84 E-value: 2.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1529 DDRTVHQLVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLK 1608
Cdd:PRK05605 30 GDTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLR--ALG---VRPGDRVAIVLPNCPQHIVAFYAVLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1609 AGGYFIPVDPGYPMARLT---------------RIADTVT--------------------------------PALVLTRT 1641
Cdd:PRK05605 105 LGAVVVEHNPLYTAHELEhpfedhgarvaivwdKVAPTVErlrrttpletivsvnmiaampllqrlalrlpiPALRKARA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1642 GQGGCLPGAevfgdVPVVALdrVADRLTAMPDQRPEVTVDPRGLAYSIFTSGSTGQPKGVAVEHIGIVRYLSWAAASYPT 1721
Cdd:PRK05605 185 ALTGPAPGT-----VPWETL--VDAAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVPG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1722 AGRRGT-------LAHSsvgFDLTMSALFEPLVSGRGV-------------------TLMPADATL----ADLAEE---- 1767
Cdd:PRK05605 258 LGDGPErvlaalpMFHA---YGLTLCLTLAVSIGGELVllpapdidlildamkkhppTWLPGVPPLyekiAEAAEErgvd 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1768 LSGplaydyIRLTPShlrhlvghwtgqelppaargwvvGGETLDPALVkQLLELRPDAEVINHYGPTET---VIGRVVHP 1844
Cdd:PRK05605 335 LSG------VRNAFS-----------------------GAMALPVSTV-ELWEKLTGGLLVEGYGLTETspiIVGNPMSD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1845 VREAGELAVdsplPLgrPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDpagepgarMYRTG 1924
Cdd:PRK05605 385 DRRPGYVGV----PF--PDTEVRIVDPEDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG--------WFRTG 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1925 DLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVlvrdqqlVGwfIPAED-----------HPPVT 1993
Cdd:PRK05605 451 DVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAV-------VG--LPREDgseevvaavvlEPGAA 521
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 653678460 1994 VS--ALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHR 2031
Cdd:PRK05605 522 LDpeGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRR 561
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
1541-2044 |
4.93e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 99.58 E-value: 4.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1541 ADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHTGALGAPPVgpetpVLLLLDRSPELVVAMLAVLKAGGYFIPVDpgy 1620
Cdd:PRK06145 12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDV-----VALLMKNSAAFLELAFAASYLGAVFLPIN--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1621 pmARLTRiaDTVtpALVLTRTGQGGCLPGAEVFGDVPVVALDRVADRLTAMPDQR---------PEVTVDPRGLAYSIFT 1691
Cdd:PRK06145 84 --YRLAA--DEV--AYILGDAGAKLLLVDEEFDAIVALETPKIVIDAAAQADSRRlaqggleipPQAAVAPTDLVRLMYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1692 SGSTGQPKGVAVEHIGivryLSWAAASYP-----TAGRR----GTLAHssVG-FDLTMSALfepLVSGRGVTLM---PAD 1758
Cdd:PRK06145 158 SGTTDRPKGVMHSYGN----LHWKSIDHVialglTASERllvvGPLYH--VGaFDLPGIAV---LWVGGTLRIHrefDPE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1759 ATLADLAEE-LSG----PLAYDYIRLTPSHLRHLVGHWTgqelppaargWVVGGETLDPAL-VKQLLELRPDAEVINHYG 1832
Cdd:PRK06145 229 AVLAAIERHrLTCawmaPVMLSRVLTVPDRDRFDLDSLA----------WCIGGGEKTPESrIRDFTRVFTRARYIDAYG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1833 PTETVIGRVVhpvREAGElAVDSPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDp 1912
Cdd:PRK06145 299 LTETCSGDTL---MEAGR-EIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGD- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1913 agepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGV-EQAVVLVRD----QQLVGWFIPAE 1987
Cdd:PRK06145 374 -------WFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVaEAAVIGVHDdrwgERITAVVVLNP 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 653678460 1988 DHpPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRALpgptsgRPELE 2044
Cdd:PRK06145 447 GA-TLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL------RDELN 496
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
636-974 |
5.04e-21 |
|
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: 96.71 E-value: 5.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 636 YVIYTSGSTGRPKgvVITRAAlDNFLAAMAER---FPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLadaDTARNP 712
Cdd:cd17633 4 YIGFTSGTTGLPK--AYYRSE-RSWIESFVCNedlFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIG---QRKFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 713 AALIDLAGRHRVTLAQATPTLWQALVPELSgPALAGIRVLVGGEALPAELARRLGDA--GAEVTNMYGPTETTIWSTSGP 790
Cdd:cd17633 78 KSWIRKINQYNATVIYLVPTMLQALARTLE-PESKIKSIFSSGQKLFESTKKKLKNIfpKANLIEFYGTSELSFITYNFN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 791 tsEDSIRRGSIGVPIDNTQVYVLDANLhpapiGVLGELHIAGEGLARGYWNRPGLTAEKFlpdpfgppgtrmYRTGDLVR 870
Cdd:cd17633 157 --QESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNPDGW------------MSVGDIGY 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 871 WSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIPDGPVAPDALRTeLSRTLP 950
Cdd:cd17633 218 VDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDKLTYKQLKRF-LKQKLS 296
|
330 340
....*....|....*....|....
gi 653678460 951 DYMIPAVIVPVPDFPTTPNGKLDR 974
Cdd:cd17633 297 RYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
1556-2033 |
6.12e-21 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 98.19 E-value: 6.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1556 SLTFAGLDAQANRLAHalHTGALGAPPvgpETPVLLLLDRSPELVVAMLAVLKAGgyfipvdpgypmarltriadtvtpa 1635
Cdd:cd05912 1 SYTFAELFEEVSRLAE--HLAALGVRK---GDRVALLSKNSIEMILLIHALWLLG------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1636 lvltrtgqggclpgaevfgdVPVVALDRvadRLTA--MPDQRPEVTVDPRGLAYSIFTSGSTGQPKGV------------ 1701
Cdd:cd05912 51 --------------------AEAVLLNT---RLTPneLAFQLKDSDVKLDDIATIMYTSGTTGKPKGVqqtfgnhwwsai 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1702 -AVEHIGIVRYLSWAAAsYPtagrrgtLAHSSvgfdlTMSALFEPLVSGRGVTLMP---ADATLADLAEElsgplAYDYI 1777
Cdd:cd05912 108 gSALNLGLTEDDNWLCA-LP-------LFHIS-----GLSILMRSVIYGMTVYLVDkfdAEQVLHLINSG-----KVTII 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1778 RLTPSHLRHLVGHwTGQELPPAARGWVVGGETLDPALVKQLLELrpDAEVINHYGPTETViGRVVHPVREAGELAVDSpl 1857
Cdd:cd05912 170 SVVPTMLQRLLEI-LGEGYPNNLRCILLGGGPAPKPLLEQCKEK--GIPVYQSYGMTETC-SQIVTLSPEDALNKIGS-- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1858 pLGRPLGETRLQVLDawlEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFlpdpagEPGArmYRTGDLVRWRGDGLLDF 1937
Cdd:cd05912 244 -AGKPLFPVELKIED---DGQPPYEVGEILLKGPNVTKGYLNRPDATEESF------ENGW--FKTGDIGYLDEEGFLYV 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1938 VGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVlvrdqqlVG-----W------FIPAEDhpPVTVSALRRFCAEQLP 2006
Cdd:cd05912 312 LDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGV-------VGipddkWgqvpvaFVVSER--PISEEELIAYCSEKLA 382
|
490 500
....*....|....*....|....*..
gi 653678460 2007 EFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:cd05912 383 KYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
493-977 |
8.29e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 99.34 E-value: 8.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 493 LRERFQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPID 572
Cdd:PRK06710 26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 573 PDFPVERIAYLLSD--ARPVLV-------VTDAATADRLG-------------PDDI---------TGLVV-LEETDTGG 620
Cdd:PRK06710 106 PLYTERELEYQLHDsgAKVILCldlvfprVTNVQSATKIEhvivtriadflpfPKNLlypfvqkkqSNLVVkVSESETIH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 621 Y---------PATEPPAVPAGHSAYVIYTSGSTGRPKGVVITRAAL-DNFLAAMAERFPLTAEDRVLATTTVSFDIAGLE 690
Cdd:PRK06710 186 LwnsvekevnTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLvSNTLMGVQWLYNCKEGEEVVLGVLPFFHVYGMT 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 691 --LYLPLRSGAGVVLADADTARnpaALIDLAGRHRVTLAQATPTLWQALV--PELSGPALAGIRVLVGGEA-LPAELARR 765
Cdd:PRK06710 266 avMNLSIMQGYKMVLIPKFDMK---MVFEAIKKHKVTLFPGAPTIYIALLnsPLLKEYDISSIRACISGSApLPVEVQEK 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 766 LGD-AGAEVTNMYGPTETTIWSTSGPTSEDSIRrGSIGVPIDNTQVYVLDANLHPA-PIGVLGELHIAGEGLARGYWNRP 843
Cdd:PRK06710 343 FETvTGGKLVEGYGLTESSPVTHSNFLWEKRVP-GSIGVPWPDTEAMIMSLETGEAlPPGEIGEIVVKGPQIMKGYWNKP 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 844 GLTAeKFLPDPFgppgtrmYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAV-VREDRPG 922
Cdd:PRK06710 422 EETA-AVLQDGW-------LHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIgVPDPYRG 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 653678460 923 DLRLVAYVIPDGPVAPDALRTELSRT-LPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:PRK06710 494 ETVKAFVVLKEGTECSEEELNQFARKyLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
637-882 |
1.04e-20 |
|
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: 95.80 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 637 VIYTSGSTGRPKGVVITRAaldNFLAA---MAERFPLTAEDRVLATTTVsFDIAGLELYLPL--RSGAGVVLADADtarn 711
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHG---NLIAAnlqLIHAMGLTEADVYLNMLPL-FHIAGLNLALATfhAGGANVVMEKFD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 712 PAALIDLAGRHRVTLAQATPTLWQALVPEL--SGPALAGIRVLVGGEAlPAELARRLGDAGAEVTNMYGPTETTIWSTSG 789
Cdd:cd17637 77 PAEALELIEEEKVTLMGSFPPILSNLLDAAekSGVDLSSLRHVLGLDA-PETIQRFEETTGATFWSLYGQTETSGLVTLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 790 PTSEdsiRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDpfgppgtrMYRTGDLV 869
Cdd:cd17637 156 PYRE---RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG--------WHHTGDLG 224
|
250
....*....|...
gi 653678460 870 RWSAAGDLEYLGR 882
Cdd:cd17637 225 RFDEDGYLWYAGR 237
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
635-977 |
1.40e-20 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 95.88 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 635 AYVIYTSGSTGRPKGVVITRAALDNFLAAMAERfpLTAEDRVLATTTvSFDIAGLELYL-PLRSGAGVVLADADTARNPA 713
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTAAALTASADATHDR--LGGPGQWLLALP-AHHIAGLQVLVrSVIAGSEPVELDVSAGFDPT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 714 ALIDLAGRHRV--TLAQATPT-LWQALVPELSGPALAGI-RVLVGGEALPAELARRLGDAGAEVTNMYGPTEttiwsTSG 789
Cdd:PRK07824 115 ALPRAVAELGGgrRYTSLVPMqLAKALDDPAATAALAELdAVLVGGGPAPAPVLDAAAAAGINVVRTYGMSE-----TSG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 790 PTSEDsirrgsiGVPIDNTQVYVLDanlhpapigvlGELHIAGEGLARGYWNRPGltaekflPDPFGPPGtrMYRTGDLV 869
Cdd:PRK07824 190 GCVYD-------GVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPVD-------PDPFAEPG--WFRTDDLG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 870 RWSaAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAV-VREDRPGDlRLVAYVIPDGPVAP--DALRTELS 946
Cdd:PRK07824 243 ALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFgLPDDRLGQ-RVVAAVVGDGGPAPtlEALRAHVA 320
|
330 340 350
....*....|....*....|....*....|.
gi 653678460 947 RTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:PRK07824 321 RTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
491-977 |
1.76e-20 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 98.20 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 491 ASLRERFQQWCRRTPGAVAVIEGDTTLSYRELDERANRLARLL-----MERGagaeTFVAVLLPrsaDLL---VTLLAVI 562
Cdd:PRK08974 23 QSLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLqnglgLKKG----DRVALMMP---NLLqypIALFGIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 563 KAGAAYLPIDPDFPVERIAYLLSD--ARPVLVVTD-AATAD--------------RLG---------------------- 603
Cdd:PRK08974 96 RAGMIVVNVNPLYTPRELEHQLNDsgAKAIVIVSNfAHTLEkvvfktpvkhviltRMGdqlstakgtlvnfvvkyikrlv 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 604 -----PDDITGLVVLEEtdtGGYPATEPPAVPAGHSAYVIYTSGSTGRPKGVVIT-RAALDNFLAAMAERFPLTAEDRVL 677
Cdd:PRK08974 176 pkyhlPDAISFRSALHK---GRRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLThRNMLANLEQAKAAYGPLLHPGKEL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 678 ATTtvsfdiaGLELY----------LPLRSGAGVVLADadTARNPAALIDLAGRHRVTLAQATPTLWQALV--PELSGPA 745
Cdd:PRK08974 253 VVT-------ALPLYhifaltvnclLFIELGGQNLLIT--NPRDIPGFVKELKKYPFTAITGVNTLFNALLnnEEFQELD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 746 LAGIRVLVGG-EALPAELARRLGDA-GAEVTNMYGPTETTIWSTSGPTSEDSiRRGSIGVPIDNTQVYVLDANLHPAPIG 823
Cdd:PRK08974 324 FSSLKLSVGGgMAVQQAVAERWVKLtGQYLLEGYGLTECSPLVSVNPYDLDY-YSGSIGLPVPSTEIKLVDDDGNEVPPG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 824 VLGELHIAGEGLARGYWNRPGLTAEkFLPDPFgppgtrmYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTL 903
Cdd:PRK08974 403 EPGELWVKGPQVMLGYWQRPEATDE-VIKDGW-------LATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVV 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 653678460 904 INAGPVRRAAAV-VREDRPGDLRLVAYVIPDGPVAPDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:PRK08974 475 MLHPKVLEVAAVgVPSEVSGEAVKIFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1522-1973 |
1.93e-20 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 98.25 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1522 RSEQHVGDDRTVHQLVEAQADRTPGWTALRTGD----RSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSP 1597
Cdd:COG1022 2 SEFSDVPPADTLPDLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLL--ALG---VKPGDRVAILSDNRP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1598 ELVVAMLAVLKAGGYFIPVDPGYPMARLTRIADTVTPALVLTRTGQ--------GGCLP---------GAEVFGDVPVVA 1660
Cdd:COG1022 77 EWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEqldkllevRDELPslrhivvldPRGLRDDPRLLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1661 LDRVADRLTAMPDQ----RPEVTVDPRGLAYSIFTSGSTGQPKGVAVEHigivRYLSWAAASYPTAGRRGT--------- 1727
Cdd:COG1022 157 LDELLALGREVADPaeleARRAAVKPDDLATIIYTSGTTGRPKGVMLTH----RNLLSNARALLERLPLGPgdrtlsflp 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1728 LAHSsvgFDLTMSALFepLVSG------RGVTLMPAD--------------------ATLADLAEELSGP---------- 1771
Cdd:COG1022 233 LAHV---FERTVSYYA--LAAGatvafaESPDTLAEDlrevkptfmlavprvwekvyAGIQAKAEEAGGLkrklfrwala 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1772 LAYDYIRL-----TPS---HLRHLVGHW---------TGQELppaaRGWVVGGETLDPALVK-------QLLELrpdaev 1827
Cdd:COG1022 308 VGRRYARArlagkSPSlllRLKHALADKlvfsklreaLGGRL----RFAVSGGAALGPELARffralgiPVLEG------ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1828 inhYGPTET--VIGrvvhpVREAGELAVDSplpLGRPLGETRLQVldawleavpvGAVGELFIGGDGIARGYLGRPALTA 1905
Cdd:COG1022 378 ---YGLTETspVIT-----VNRPGDNRIGT---VGPPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATA 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 653678460 1906 EKFLPDpagepgaRMYRTGDLVRWRGDGLLDFVGRVDDQVKLR-GYRIELGEIEARMAEHPGVEQAVVL 1973
Cdd:COG1022 437 EAFDAD-------GWLHTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVV 498
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
1541-2052 |
2.33e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 97.70 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1541 ADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPV---- 1616
Cdd:PRK08316 21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALL--DLG---LKKGDRVAALGHNSDAYALLWLACARAGAVHVPVnfml 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1617 ---DPGY----PMARL----TRIADTVTPALVLTRTGQGGCLPGAEvfGDVPVVALDRVADRLTAMPDQRPEVTVDPRGL 1685
Cdd:PRK08316 96 tgeELAYildhSGARAflvdPALAPTAEAALALLPVDTLILSLVLG--GREAPGGWLDFADWAEAGSVAEPDVELADDDL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1686 AYSIFTSGSTGQPKGVAVEHIGIV-RYLSWAAASYPTAGrrgtlahssvgfDLTMSALfePL--VSGRGVTLMPADATLA 1762
Cdd:PRK08316 174 AQILYTSGTESLPKGAMLTHRALIaEYVSCIVAGDMSAD------------DIPLHAL--PLyhCAQLDVFLGPYLYVGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1763 D--LAEELSGPLAYDYI---RLT-----P----SHLRHLVghWTGQELPPAARGWVvgGETLDPALVkqLLELR---PDA 1825
Cdd:PRK08316 240 TnvILDAPDPELILRTIeaeRITsffapPtvwiSLLRHPD--FDTRDLSSLRKGYY--GASIMPVEV--LKELRerlPGL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1826 EVINHYGPTE-----TVIGRVVHPVReagelavdsPLPLGRPL--GETRlqVLDAWLEAVPVGAVGELFIGGDGIARGYL 1898
Cdd:PRK08316 314 RFYNCYGQTEiaplaTVLGPEEHLRR---------PGSAGRPVlnVETR--VVDDDGNDVAPGEVGEIVHRSPQLMLGYW 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1899 GRPALTAEKFLPDpagepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGV-EQAVVLVRDQ 1977
Cdd:PRK08316 383 DDPEKTAEAFRGG--------WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVaEVAVIGLPDP 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 653678460 1978 ---QLVGWFIPAEDHPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRalpgptsgrpELEDRYQAPRT 2052
Cdd:PRK08316 455 kwiEAVTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKR----------ELRERYAGAFT 522
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
509-979 |
2.54e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 97.44 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 509 AVIEGDTTLSYRELDERANRLARLLMER-GAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPdfpVERIAYLLSDA 587
Cdd:PRK07867 21 GLYFEDSFTSWREHIRGSAARAAALRARlDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNP---TRRGAALARDI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 588 RPV---LVVTDAATADRLgpDDITGLVVLEETDT-------GGYPATEPPAVPAGHS--AYVIYTSGSTGRPKGVVITRA 655
Cdd:PRK07867 98 AHAdcqLVLTESAHAELL--DGLDPGVRVINVDSpawadelAAHRDAEPPFRVADPDdlFMLIFTSGTSGDPKAVRCTHR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 656 ALDNFLAAMAERFPLTAEDRVLATTTVSFDIAGLELYLP-LRSGAGVVLADADTArnpAALIDLAGRHRVTLAQ--ATPT 732
Cdd:PRK07867 176 KVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVaLAAGASIALRRKFSA---SGFLPDVRRYGATYANyvGKPL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 733 LWQALVPELSGPALAGIRVLVGGEALPAELARRLGDAGAEVTNMYGPTETTIWSTSGPTSEDsirrGSIGVPIDNTQVY- 811
Cdd:PRK07867 253 SYVLATPERPDDADNPLRIVYGNEGAPGDIARFARRFGCVVVDGFGSTEGGVAITRTPDTPP----GALGPLPPGVAIVd 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 812 ----------VLDANLHPAPIGVLGEL-HIAGEGLARGYWNRPGLTAEKFLPDpfgppgtrMYRTGDLVRWSAAGDLEYL 880
Cdd:PRK07867 329 pdtgtecppaEDADGRLLNADEAIGELvNTAGPGGFEGYYNDPEADAERMRGG--------VYWSGDLAYRDADGYAYFA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 881 GRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRP-GDLRLVAYVIPDGPV-APDALRTELS--RTLPDYMIPA 956
Cdd:PRK07867 401 GRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVvGDQVMAALVLAPGAKfDPDAFAEFLAaqPDLGPKQWPS 480
|
490 500
....*....|....*....|...
gi 653678460 957 VIVPVPDFPTTPNGKLDRAALPA 979
Cdd:PRK07867 481 YVRVCAELPRTATFKVLKRQLSA 503
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
1530-2028 |
2.58e-20 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 97.43 E-value: 2.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1530 DRTVHQLVEAQADRTPGWTAL------RTGDRSLTFAGLDAQANRLAHALhtGALGappVGPETPVLLLLDRSPELVVAM 1603
Cdd:PRK13295 23 DRTINDDLDACVASCPDKTAVtavrlgTGAPRRFTYRELAALVDRVAVGL--ARLG---VGRGDVVSCQLPNWWEFTVLY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1604 LAVLKAGGYFIPVDP--------------------------GYPMARLTRIADTVTPAL--VLTRTGQGgclpgAEVFGD 1655
Cdd:PRK13295 98 LACSRIGAVLNPLMPifrerelsfmlkhaeskvlvvpktfrGFDHAAMARRLRPELPALrhVVVVGGDG-----ADSFEA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1656 V---PVVALDRVADRLTAMPdqRPevtvDPRGLAYSIFTSGSTGQPKGVAVEHIGIVrylswaAASYPTAGRRG------ 1726
Cdd:PRK13295 173 LlitPAWEQEPDAPAILARL--RP----GPDDVTQLIYTSGTTGEPKGVMHTANTLM------ANIVPYAERLGlgaddv 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1727 -----TLAHSSvGFdltMSALFEPLVSGRGVTLM----PADAtlADLAEE-------LSGPLAYDYIRlTPSHLRHLVgh 1790
Cdd:PRK13295 241 ilmasPMAHQT-GF---MYGLMMPVMLGATAVLQdiwdPARA--AELIRTegvtftmASTPFLTDLTR-AVKESGRPV-- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1791 wtgqelpPAARGWVVGGETLDPALVKQLLElRPDAEVINHYGPTETVIGRVVHPvREAGELAVDSPlplGRPLGETRLQV 1870
Cdd:PRK13295 312 -------SSLRTFLCAGAPIPGALVERARA-ALGAKIVSAWGMTENGAVTLTKL-DDPDERASTTD---GCPLPGVEVRV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1871 LDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEkflpDPAGepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGY 1950
Cdd:PRK13295 380 VDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGT----DADG-----WFDTGDLARIDADGYIRISGRSKDVIIRGGE 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1951 RIELGEIEARMAEHPGVEQ-AVVLVRDQQL---VGWFIPAEDHPPVTVSALRRFCAEQ-LPEFMVPNQWVALDAFPLTPH 2025
Cdd:PRK13295 451 NIPVVEIEALLYRHPAIAQvAIVAYPDERLgerACAFVVPRPGQSLDFEEMVEFLKAQkVAKQYIPERLVVRDALPRTPS 530
|
...
gi 653678460 2026 GKV 2028
Cdd:PRK13295 531 GKI 533
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
1541-2048 |
3.14e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 96.77 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1541 ADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHtgalgAPPVGPETpVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGY 1620
Cdd:PRK07638 11 ASLQPNKIAIKENDRVLTYKDWFESVCKVANWLN-----EKESKNKT-IAILLENRIEFLQLFAGAAMAGWTCVPLDIKW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1621 PMA-RLTRIADTvTPALVLTRTGQGGCLPGAEVfgdvPVVALDRVaDRLTAMPDQRPEVTVDPRGLA-YSIFTSGSTGQP 1698
Cdd:PRK07638 85 KQDeLKERLAIS-NADMIVTERYKLNDLPDEEG----RVIEIDEW-KRMIEKYLPTYAPIENVQNAPfYMGFTSGSTGKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1699 KGVAVEHigivryLSWAAASYPTAGR-----------RGTLAHSSVGFDlTMSALFeplvSGRGVTLMPaDATLADLAEE 1767
Cdd:PRK07638 159 KAFLRAQ------QSWLHSFDCNVHDfhmkredsvliAGTLVHSLFLYG-AISTLY----VGQTVHLMR-KFIPNQVLDK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1768 LSGPlAYDYIRLTPSHLRHLVghwTGQELPPAARGWVVGGETLDPALVKQLLELRPDAEVINHYGPTEtvIGRVVHPVRE 1847
Cdd:PRK07638 227 LETE-NISVMYTVPTMLESLY---KENRVIENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASE--LSFVTALVDE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1848 AGELAVDSplpLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEkflPDPAGepgarmYRTGDLV 1927
Cdd:PRK07638 301 ESERRPNS---VGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARE---LNADG------WMTVRDV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1928 RWRG-DGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRDQQLVGWFIPAEDHPPVTVSALRRFCAEQLP 2006
Cdd:PRK07638 369 GYEDeEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSATKQQLKSFCLQRLS 448
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 653678460 2007 EFMVPNQWVALDAFPLTPHGKVNHRALpgpTSGRPELEDRYQ 2048
Cdd:PRK07638 449 SFKIPKEWHFVDEIPYTNSGKIARMEA---KSWIENQEKIYE 487
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
1556-2033 |
3.60e-20 |
|
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: 96.01 E-value: 3.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1556 SLTFAGLDAQANRLAhalhtGALGAPPVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMARLTRIADTVtpa 1635
Cdd:cd05935 1 SLTYLELLEVVKKLA-----SFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDS--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1636 lvltrtgqggclpgaevfGDVPVVALDRVADrltampdqrpevtvdprgLAYSIFTSGSTGQPKGVAVEHIGIvrylsWA 1715
Cdd:cd05935 73 ------------------GAKVAVVGSELDD------------------LALIPYTSGTTGLPKGCMHTHFSA-----AA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1716 AASYPTAGRRGTLAHSSVG----FDLT-MSALFEPLVSGRGVTLMPA---DATLADLAEelsgplaydyirltpshlRHL 1787
Cdd:cd05935 112 NALQSAVWTGLTPSDVILAclplFHVTgFVGSLNTAVYVGGTYVLMArwdRETALELIE------------------KYK 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1788 VGHWTGqeLPPA-----------ARGW----VV--GGETLDPALVKQLLELrPDAEVINHYGPTETVIGRVVHPvreAGE 1850
Cdd:cd05935 174 VTFWTN--IPTMlvdllatpefkTRDLsslkVLtgGGAPMPPAVAEKLLKL-TGLRFVEGYGLTETMSQTHTNP---PLR 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1851 LAVDSplpLGRPLGETRLQVLDAW-LEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPagepGARMYRTGDLVRW 1929
Cdd:cd05935 248 PKLQC---LGIP*FGVDARVIDIEtGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIK----GRRFFRTGDLGYM 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1930 RGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRDQQLVGWFIPA------EDHPPVTVSALRRFCAE 2003
Cdd:cd05935 321 DEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAfivlrpEYRGKVTEEDIIEWARE 400
|
490 500 510
....*....|....*....|....*....|
gi 653678460 2004 QLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:cd05935 401 QMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
485-878 |
3.96e-20 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 97.26 E-value: 3.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 485 ARPLPAASLR--ERFQQWCRRTPGAVAVIEGDT-----TLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVT 557
Cdd:PRK08180 31 AEPLGDYPRRltDRLVHWAQEAPDRVFLAERGAdggwrRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 558 LLAVIKAGAAYLPIDP-------DFpvERIAYLLSDARPVLVVTDAATA-----DRLGPDDITglVVLEETDTGGYPAT- 624
Cdd:PRK08180 111 ALAAMYAGVPYAPVSPayslvsqDF--GKLRHVLELLTPGLVFADDGAAfaralAAVVPADVE--VVAVRGAVPGRAATp 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 625 --------EPPAVPAGHS-------AYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFP-LTAEDRVLA-------TTT 681
Cdd:PRK08180 187 faallatpPTAAVDAAHAavgpdtiAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPfLAEEPPVLVdwlpwnhTFG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 682 VSFDIaGLELY----LPLRSGAGVVLADADTARNpaaLIDLAGrhrvTLAQATPTLWQALVPELSG-PALA-----GIRV 751
Cdd:PRK08180 267 GNHNL-GIVLYnggtLYIDDGKPTPGGFDETLRN---LREISP----TVYFNVPKGWEMLVPALERdAALRrrffsRLKL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 752 LV-GGEALPAELARRLgDAGAE--------VTNMYGPTET--TIWSTSGPTSedsiRRGSIGVPIDNTQVYVldanlhpA 820
Cdd:PRK08180 339 LFyAGAALSQDVWDRL-DRVAEatcgerirMMTGLGMTETapSATFTTGPLS----RAGNIGLPAPGCEVKL-------V 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 653678460 821 PIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgppgtrmYRTGDLVRWSAAGDLE 878
Cdd:PRK08180 407 PVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY-------YRSGDAVRFVDPADPE 457
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
516-933 |
5.08e-20 |
|
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: 96.52 E-value: 5.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 516 TLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGaaylpidpdFPV---------ERIAYLLSD 586
Cdd:cd17639 5 YMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---------IPIvtvyatlgeDALIHSLNE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 587 ARPVLVVTDAatadrlGPDDItglvvleetdtggypateppavpaghsAYVIYTSGSTGRPKGVVITRAALDNFLAAMAE 666
Cdd:cd17639 76 TECSAIFTDG------KPDDL---------------------------ACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 667 RFP--LTAEDRVLAtttvsfdiaglelYLPL-----------------RSGAGVV--LADADTAR--------NPAALI- 716
Cdd:cd17639 123 RVPelLGPDDRYLA-------------YLPLahifelaaenvclyrggTIGYGSPrtLTDKSKRGckgdltefKPTLMVg 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 717 ---------------------------DLAGRHRVTLAQATP--TLWQALVPELSGPALAG-IR-VLVGGEALPAELARR 765
Cdd:cd17639 190 vpaiwdtirkgvlaklnpmgglkrtlfWTAYQSKLKALKEGPgtPLLDELVFKKVRAALGGrLRyMLSGGAPLSADTQEF 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 766 LGDAGAEVTNMYGPTETtiwSTSGPTSE-DSIRRGSIGVPIDNTQV---------YVLDAnlhPAPigvLGELHIAGEGL 835
Cdd:cd17639 270 LNIVLCPVIQGYGLTET---CAGGTVQDpGDLETGRVGPPLPCCEIklvdweeggYSTDK---PPP---RGEILIRGPNV 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 836 ARGYWNRPGLTAEKFLPDpfgppgtRMYRTGDLVRWSAAGDLEYLGRTDHQVKLR-GFRIELGEIETTLINAGPVRRAAA 914
Cdd:cd17639 341 FKGYYKNPEKTKEAFDGD-------GWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICV 413
|
490
....*....|....*....
gi 653678460 915 VVREDRPgdlRLVAYVIPD 933
Cdd:cd17639 414 YADPDKS---YPVAIVVPN 429
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
1537-2011 |
5.47e-20 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 96.87 E-value: 5.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1537 VEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHTGALGAPPVgpetpVLLLLDRSPELVVAMLAVLKAGGY--FI 1614
Cdd:PRK08279 43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDV-----VALLMENRPEYLAAWLGLAKLGAVvaLL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1615 -PVDPGYPMARLTRIADT----VTPALVLTRTGQGGCLPGAE---VFGDV---PVVALDRVADRLTAMPDQRPEVT--VD 1681
Cdd:PRK08279 118 nTQQRGAVLAHSLNLVDAkhliVGEELVEAFEEARADLARPPrlwVAGGDtldDPEGYEDLAAAAAGAPTTNPASRsgVT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1682 PRGLAYSIFTSGSTGQPKGVAVEHIGIVRYLSWAAAS---------------YPTAGrrGTLAHSSVgfdltmsalfepL 1746
Cdd:PRK08279 198 AKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLlrltpddvlycclplYHNTG--GTVAWSSV------------L 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1747 VSGRGVTLMP---ADATLADLAEElsGPLAYDYI-RLtpshLRHLVGHwtgqelPPAA-----RGWVVGGETLDPAL--- 1814
Cdd:PRK08279 264 AAGATLALRRkfsASRFWDDVRRY--RATAFQYIgEL----CRYLLNQ------PPKPtdrdhRLRLMIGNGLRPDIwde 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1815 ------VKQLLELrpdaevinhYGPTET------------VIGRVvhpvreagelavdsPLPLGRPLG------ETRLQV 1870
Cdd:PRK08279 332 fqqrfgIPRILEF---------YAASEGnvgfinvfnfdgTVGRV--------------PLWLAHPYAivkydvDTGEPV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1871 LDA--WLEAVPVGAVGELF--IGGDGIARGYlGRPALTAEKFLPDpAGEPGARMYRTGDLVRWRGDGLLDFVGRVDDQVK 1946
Cdd:PRK08279 389 RDAdgRCIKVKPGEVGLLIgrITDRGPFDGY-TDPEASEKKILRD-VFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFR 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 653678460 1947 LRGYRIELGEIEARMAEHPGVEQAVVLvrdqqlvGWFIP------------AEDHPPVTVSALRRFCAEQLPEFMVP 2011
Cdd:PRK08279 467 WKGENVATTEVENALSGFPGVEEAVVY-------GVEVPgtdgragmaaivLADGAEFDLAALAAHLYERLPAYAVP 536
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
504-994 |
7.14e-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: 7.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 504 TPGAVAVI------EGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPV 577
Cdd:cd05967 64 RGDQIALIydspvtGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 578 ERIAYLLSDARPVLVVT------------------DAATADRLGPDDIT----GLVVLEETDTGG--------YPATEPP 627
Cdd:cd05967 144 KELASRIDDAKPKLIVTascgiepgkvvpykplldKALELSGHKPHHVLvlnrPQVPADLTKPGRdldwsellAKAEPVD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 628 AVP--AGHSAYVIYTSGSTGRPKGVVITRA----ALDnflAAMAERFPLTAEDRVLATTTVSFdIAG--LELYLPLRSGA 699
Cdd:cd05967 224 CVPvaATDPLYILYTSGTTGKPKGVVRDNGghavALN---WSMRNIYGIKPGDVWWAASDVGW-VVGhsYIVYGPLLHGA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 700 GVVLADADTARNPAA-----LIDlagRHRVTLAQATPTLWQALVPE------LSGPALAGIRVL-VGGEALPAELARRLG 767
Cdd:cd05967 300 TTVLYEGKPVGTPDPgafwrVIE---KYQVNALFTAPTAIRAIRKEdpdgkyIKKYDLSSLRTLfLAGERLDPPTLEWAE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 768 DA-GAEVTNMYGPTETTiWSTSGPTS---EDSIRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAG---EGLARGYW 840
Cdd:cd05967 377 NTlGVPVIDHWWQTETG-WPITANPVglePLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLplpPGCLLTLW 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 841 NRPGLTAEKFLPDpfgPPGtrMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAV-VRED 919
Cdd:cd05967 456 KNDERFKKLYLSK---FPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVgVRDE 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 920 RPGDLRLVAYVI-PDGPVAPDALRTELSRtlpdyMIPAVIVPVPDF---------PTTPNGKLDRAALPAPDYGTRSTAR 989
Cdd:cd05967 531 LKGQVPLGLVVLkEGVKITAEELEKELVA-----LVREQIGPVAAFrlvifvkrlPKTRSGKILRRTLRKIADGEDYTIP 605
|
....*
gi 653678460 990 PPRDD 994
Cdd:cd05967 606 STIED 610
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
628-977 |
9.23e-20 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 96.04 E-value: 9.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 628 AVPAGHS--AYVIYTSGSTGRPKGVVITRAAL-DNFLAAMAERFPLTAEDRVLATTTVSFDIAGLELY----------LP 694
Cdd:PRK12492 201 PVPVGLDdiAVLQYTGGTTGLAKGAMLTHGNLvANMLQVRACLSQLGPDGQPLMKEGQEVMIAPLPLYhiyaftancmCM 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 695 LRSGAGVVLADadTARNPAALIDLAGRHRVTLAQATPTLWQALV--PELSGPALAGIRVL-VGGEALPAELARRLGD-AG 770
Cdd:PRK12492 281 MVSGNHNVLIT--NPRDIPGFIKELGKWRFSALLGLNTLFVALMdhPGFKDLDFSALKLTnSGGTALVKATAERWEQlTG 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 771 AEVTNMYGPTETTIWSTSGPTSEDSiRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKF 850
Cdd:PRK12492 359 CTIVEGYGLTETSPVASTNPYGELA-RLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEAL 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 851 lpDPFGppgtrMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAV-VREDRPGDLRLVAY 929
Cdd:PRK12492 438 --DAEG-----WFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIgVPDERSGEAVKLFV 510
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 653678460 930 VIPDGPVAPDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:PRK12492 511 VARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1082-1494 |
9.74e-20 |
|
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: 94.63 E-value: 9.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1082 PLPLSPMQEsiWLADQVSAGDSVYNVPLALRLIGPLDRGALRRTLNRVVDRHEMLRTRIHPGPDGMPVQVADPAGGGAAL 1161
Cdd:cd19534 1 EVPLTPIQR--WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEELFRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1162 TERDAAPGTDLAQLLLAEAALGFTLATEH-PL-RAVLWRLDEREHVLLLTAHHVAVDAWSMDLIQRDLTELYAADTGHRE 1239
Cdd:cd19534 79 EVVDLSSLAQAAAIEALAAEAQSSLDLEEgPLlAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1240 PELdEPALAQADYAVWQRQSAQRGRYAAELDFWRTELTGAVATEVAGDLPRPATpgggGGAVEFALAP---RQIqgIREL 1316
Cdd:cd19534 159 IPL-PSKTSFQTWAELLAEYAQSPALLEELAYWRELPAADYWGLPKDPEQTYGD----ARTVSFTLDEeetEAL--LQEA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1317 ARRCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGR--GNPRLDnlvgcLVNTV---------VLrgDLSGAPTFHEL 1385
Cdd:cd19534 232 NAAYRTEINDLLLAALALAFQDWTGRAPPAIFLEGHGReeIDPGLD-----LSRTVgwftsmypvVL--DLEASEDLGDT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1386 LRRT--------------------HARTADALAHQELP---FEHL-VADRGAGNGPLFRIMYSFSSQEPAGRSAgdvdle 1441
Cdd:cd19534 305 LKRVkeqlrripnkgigygilrylTPEGTKRLAFHPQPeisFNYLgQFDQGERDDALFVSAVGGGGSDIGPDTP------ 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 653678460 1442 pvpvpvTTCKFDLVLTVVDGgsTLEGVLEYADDLYLPGTAERLVTSLTNLLAA 1494
Cdd:cd19534 379 ------RFALLDINAVVEGG--QLVITVSYSRNMYHEETIQQLADSYKEALEA 423
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
1689-2028 |
1.09e-19 |
|
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: 92.95 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1689 IFTSGSTGQPKGVAVEHIGIVR-YLSWAAASYPTAGRRGTLAHS---SVGFDLTMSALFEplvsgRGVTLMP-----ADA 1759
Cdd:cd17638 6 MFTSGTTGRSKGVMCAHRQTLRaAAAWADCADLTEDDRYLIINPffhTFGYKAGIVACLL-----TGATVVPvavfdVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1760 TLADLAEE----LSGPlaydyirltPSHLRHLVGHWTGQELPPAA-RGWVVGGETLDPALVKQLLELRPDAEVINHYGPT 1834
Cdd:cd17638 81 ILEAIEREritvLPGP---------PTLFQSLLDHPGRKKFDLSSlRAAVTGAATVPVELVRRMRSELGFETVLTAYGLT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1835 ETVIGRVVHPvreaGELAVDSPLPLGRPLGETRLQVLDAwleavpvgavGELFIGGDGIARGYLGRPALTAEKFlpDPAG 1914
Cdd:cd17638 152 EAGVATMCRP----GDDAETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAI--DADG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1915 epgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQ-AVVLVRDQQL--VG-WFIPAEDHP 1990
Cdd:cd17638 216 -----WLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQvAVIGVPDERMgeVGkAFVVARPGV 290
|
330 340 350
....*....|....*....|....*....|....*...
gi 653678460 1991 PVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKV 2028
Cdd:cd17638 291 TLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
1537-2028 |
1.85e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 94.84 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1537 VEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAhalhtGALGAPPVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPV 1616
Cdd:PRK07786 23 LARHALMQPDAPALRFLGNTTTWRELDDRVAALA-----GALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1617 DPGYPMARLTRIADTVTPALVLTRTGQGGClpGAEVFGDVP-----VVALDRVADRLTAMPDQRPEVTVDPRGL------ 1685
Cdd:PRK07786 98 NFRLTPPEIAFLVSDCGAHVVVTEAALAPV--ATAVRDIVPllstvVVAGGSSDDSVLGYEDLLAEAGPAHAPVdipnds 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1686 -AYSIFTSGSTGQPKGVAVEHIGIVrylswAAASYPTAGRRGTLAHSsVGFdlTMSALFE---------PLVSGRGVTLM 1755
Cdd:PRK07786 176 pALIMYTSGTTGRPKGAVLTHANLT-----GQAMTCLRTNGADINSD-VGF--VGVPLFHiagigsmlpGLLLGAPTVIY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1756 PADA----TLADL--AEELSGplaydyIRLTPSHLRHLVGHWT--GQELPPAARGWvvGGETLDPALVKQLLELRPDAEV 1827
Cdd:PRK07786 248 PLGAfdpgQLLDVleAEKVTG------IFLVPAQWQAVCAEQQarPRDLALRVLSW--GAAPASDTLLRQMAATFPEAQI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1828 INHYGPTEtvigrvVHPVREA--GELAVDSPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTA 1905
Cdd:PRK07786 320 LAAFGQTE------MSPVTCMllGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1906 EKFlpdpAGEpgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRDQQL-----V 1980
Cdd:PRK07786 394 EAF----AGG----WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKwgevpV 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 653678460 1981 GWFIPAEDHPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKV 2028
Cdd:PRK07786 466 AVAAVRNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
507-977 |
2.30e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 94.31 E-value: 2.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 507 AVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSD 586
Cdd:PRK13390 15 AVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 587 ARPVLVVTDAA---TADRLGPD---------DITGLVVLEETDTG-GYPATEPPAvpaghSAYVIYTSGSTGRPKGVvit 653
Cdd:PRK13390 95 SGARVLVASAAldgLAAKVGADlplrlsfggEIDGFGSFEAALAGaGPRLTEQPC-----GAVMLYSSGTTGFPKGI--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 654 raaldnfLAAMAERFPLTAEDRVLATTTVSFDIAGLELYL---------PLR-------SGAGVVLADADTARNPAALID 717
Cdd:PRK13390 167 -------QPDLPGRDVDAPGDPIVAIARAFYDISESDIYYssapiyhaaPLRwcsmvhaLGGTVVLAKRFDAQATLGHVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 718 lagRHRVTLAQATPTLWQALV-------PELSGPALAGirVLVGGEALPAELARRLGD-AGAEVTNMYGPTEttiwsTSG 789
Cdd:PRK13390 240 ---RYRITVTQMVPTMFVRLLkldadvrTRYDVSSLRA--VIHAAAPCPVDVKHAMIDwLGPIVYEYYSSTE-----AHG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 790 PTSEDS----IRRGSIGVPIDNTqVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLP-DPFgppgtrmyr 864
Cdd:PRK13390 310 MTFIDSpdwlAHPGSVGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPaHPF--------- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 865 tgdlvrWSAAGDLEYL---------GRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAV------VREDRPGDLRLVAY 929
Cdd:PRK13390 380 ------WTTVGDLGSVdedgylylaDRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIgvpdpeMGEQVKAVIQLVEG 453
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 653678460 930 VIPDGPVAPDALRTELSRtLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:PRK13390 454 IRGSDELARELIDYTRSR-IAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
1534-2029 |
3.64e-19 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 94.04 E-value: 3.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1534 HQLVEAQADRTpgWTALRTGdRSLTFAGLDAQANRLAhalhtGALGAPPVGPETPVLLLLDRSPELVVAMLAVLKAGGYF 1613
Cdd:PRK06087 30 QQTARAMPDKI--AVVDNHG-ASYTYSALDHAASRLA-----NWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1614 IPVDPGYPMARLTRIADTV------TPALVLTRTGQGGCLPGAEvfgDVP----VVALDRVADRLTA------MPDQRP- 1676
Cdd:PRK06087 102 VPLLPSWREAELVWVLNKCqakmffAPTLFKQTRPVDLILPLQN---QLPqlqqIVGVDKLAPATSSlslsqiIADYEPl 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1677 --EVTVDPRGLAYSIFTSGSTGQPKGVAVEHIGIVrylswAAASYPTAGRRGT----------LAHSSvGFDLTMSALFe 1744
Cdd:PRK06087 179 ttAITTHGDELAAVLFTSGTEGLPKGVMLTHNNIL-----ASERAYCARLNLTwqdvfmmpapLGHAT-GFLHGVTAPF- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1745 pLVSGRGVTL--MPADATLADLAEE----LSG--PLAYDYIRLTPSHLRHLvghwtgqelpPAARGWVVGGETLDPALVK 1816
Cdd:PRK06087 252 -LIGARSVLLdiFTPDACLALLEQQrctcMLGatPFIYDLLNLLEKQPADL----------SALRFFLCGGTTIPKKVAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1817 QLLElrPDAEVINHYGPTETVIGRVVHPvreagelavDSPLPL-----GRPLGETRLQVLDAWLEAVPVGAVGELFIGGD 1891
Cdd:PRK06087 321 ECQQ--RGIKLLSVYGSTESSPHAVVNL---------DDPLSRfmhtdGYAAAGVEIKVVDEARKTLPPGCEGEEASRGP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1892 GIARGYLGRPALTAEKFlpDPAGepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGV-EQA 1970
Cdd:PRK06087 390 NVFMGYLDEPELTARAL--DEEG-----WYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIhDAC 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 653678460 1971 VVLVRDQQL----VGWFIPAEDHPPVTVSALRRFCAEQ-LPEFMVPNQWVALDAFPLTPHGKVN 2029
Cdd:PRK06087 463 VVAMPDERLgersCAYVVLKAPHHSLTLEEVVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKIQ 526
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
1554-2011 |
4.38e-19 |
|
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: 92.80 E-value: 4.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1554 DRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGgyfipvdpgypmarltriadtVT 1633
Cdd:cd05940 1 DEALTYAELDAMANRYARWLK--SLG---LKPGDVVALFMENRPEYVLLWLGLVKIG---------------------AV 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1634 PALV-LTRTGQggclpgaevfgdvpvvALDRVADRLTAMpdqrpEVTVDPrglAYSIFTSGSTGQPKGVAVEHIGIVRYL 1712
Cdd:cd05940 55 AALInYNLRGE----------------SLAHCLNVSSAK-----HLVVDA---ALYIYTSGTTGLPKAAIISHRRAWRGG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1713 SWAAASyptagrrGTLAHSSVGFDlTMsalfePLVSGRGVTLMP-----ADATLAdLAEELSGPLAYDYIRLTPSHLRHL 1787
Cdd:cd05940 111 AFFAGS-------GGALPSDVLYT-CL-----PLYHSTALIVGWsaclaSGATLV-IRKKFSASNFWDDIRKYQATIFQY 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1788 VGhwtgqEL-------PP-----AARGWVVGGETLDPALVKQLLELRPDAEVINHYGPTETV------------IGRVVH 1843
Cdd:cd05940 177 IG-----ELcryllnqPPkpterKHKVRMIFGNGLRPDIWEEFKERFGVPRIAEFYAATEGNsgfinffgkpgaIGRNPS 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1844 PVREAGELA-VDSPLPLGRPLGETrlqvlDAWLEAVPVGAVGELF--IGGDGIARGYLGrPALTAEKFLPDpAGEPGARM 1920
Cdd:cd05940 252 LLRKVAPLAlVKYDLESGEPIRDA-----EGRCIKVPRGEPGLLIsrINPLEPFDGYTD-PAATEKKILRD-VFKKGDAW 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1921 YRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLvrdqqlvGWFIPAED------------ 1988
Cdd:cd05940 325 FNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVY-------GVQVPGTDgragmaaivlqp 397
|
490 500
....*....|....*....|...
gi 653678460 1989 HPPVTVSALRRFCAEQLPEFMVP 2011
Cdd:cd05940 398 NEEFDLSALAAHLEKNLPGYARP 420
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
495-979 |
4.54e-19 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 93.51 E-value: 4.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 495 ERFQQWcrrtPGAVAVIEGDT--TLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPID 572
Cdd:PLN02246 31 ERLSEF----SDRPCLIDGATgrVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTAN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 573 PDFPVERIAYLLSDARPVLVVTDAATADRL----------------GPDDITGLVVLEETDTGGYPATE-----PPAVPa 631
Cdd:PLN02246 107 PFYTPAEIAKQAKASGAKLIITQSCYVDKLkglaeddgvtvvtiddPPEGCLHFSELTQADENELPEVEispddVVALP- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 632 ghsayviYTSGSTGRPKGVVITRAALDNFLAAMAE----RFPLTAEDRVLATTTVsFDIAGLE--LYLPLRSGAGVVL-A 704
Cdd:PLN02246 186 -------YSSGTTGLPKGVMLTHKGLVTSVAQQVDgenpNLYFHSDDVILCVLPM-FHIYSLNsvLLCGLRVGAAILImP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 705 DADTarnpAALIDLAGRHRVTLAQATPTLWQALV--PELSGPALAGIRVLVGGealPAELARRLGDA-GAEVTNM----- 776
Cdd:PLN02246 258 KFEI----GALLELIQRHKVTIAPFVPPIVLAIAksPVVEKYDLSSIRMVLSG---AAPLGKELEDAfRAKLPNAvlgqg 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 777 YGPTEttiwstSGPTSEDS---------IRRGSIGVPIDNTQVYVLD----ANLhpaPIGVLGELHIAGEGLARGYWNRP 843
Cdd:PLN02246 331 YGMTE------AGPVLAMClafakepfpVKSGSCGTVVRNAELKIVDpetgASL---PRNQPGEICIRGPQIMKGYLNDP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 844 GLTAekflpdpfgppgtrmyRTGDLVRWSAAGDLEYLGRTDHQ---------VKLRGFRIELGEIETTLINAGPVRRAAA 914
Cdd:PLN02246 402 EATA----------------NTIDKDGWLHTGDIGYIDDDDELfivdrlkelIKYKGFQVAPAELEALLISHPSIADAAV 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 653678460 915 VVREDRPGDLRLVAYVI--PDGPVAPDALRTELSRTLPDY-MIPAVIVpVPDFPTTPNGKLDRAALPA 979
Cdd:PLN02246 466 VPMKDEVAGEVPVAFVVrsNGSEITEDEIKQFVAKQVVFYkRIHKVFF-VDSIPKAPSGKILRKDLRA 532
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
1536-2035 |
7.28e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 93.07 E-value: 7.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1536 LVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALhtGALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIP 1615
Cdd:PRK07788 54 LVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGL--LALG---VRAGDGVAVLARNHRGFVLALYAAGKVGARIIL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1616 VDPGYPMARLTRIA-----------DTVTPALVLTRTGQGGCLP-GAEVFGDVPVVALDRVADRLTAMPDQRPEVTVDPR 1683
Cdd:PRK07788 129 LNTGFSGPQLAEVAaregvkalvydDEFTDLLSALPPDLGRLRAwGGNPDDDEPSGSTDETLDDLIAGSSTAPLPKPPKP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1684 GlAYSIFTSGSTGQPKGVAVEHI-------GIVRYLSW--------AAASYPTAGrrgtLAHSSVGFDL----TMSALFE 1744
Cdd:PRK07788 209 G-GIVILTSGTTGTPKGAPRPEPsplaplaGLLSRVPFragettllPAPMFHATG----WAHLTLAMALgstvVLRRRFD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1745 PlvsgrgvtlmpaDATLADLAEELSgplayDYIRLTPSHLRHLVghwtgqELPPAARG---------WVVGGETLDPALV 1815
Cdd:PRK07788 284 P------------EATLEDIAKHKA-----TALVVVPVMLSRIL------DLGPEVLAkydtsslkiIFVSGSALSPELA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1816 KQLLELRpdAEVI-NHYGPTETVIGRVVHPvreaGELAVDsPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIA 1894
Cdd:PRK07788 341 TRALEAF--GPVLyNLYGSTEVAFATIATP----EDLAEA-PGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPF 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1895 RGYLGRPaltaekflpDPAGEPGarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGV-EQAVVL 1973
Cdd:PRK07788 414 EGYTDGR---------DKQIIDG--LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVvEAAVIG 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 653678460 1974 VRD----QQLVGWFIPAEDHPpVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRALPG 2035
Cdd:PRK07788 483 VDDeefgQRLRAFVVKAPGAA-LDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
1530-2028 |
1.05e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 92.53 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1530 DRTVHQLVEAQADRTPGWTAL--RTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVL 1607
Cdd:PRK12583 17 TQTIGDAFDATVARFPDREALvvRHQALRYTWRQLADAVDRLARGLL--ALG---VQPGDRVGIWAPNCAEWLLTQFATA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1608 KAGGYFIPVDPGYPMARLT-----------------------RIADTVTPALVLTRTGQGGC-----LPGAEVFGDVP-- 1657
Cdd:PRK12583 92 RIGAILVNINPAYRASELEyalgqsgvrwvicadafktsdyhAMLQELLPGLAEGQPGALACerlpeLRGVVSLAPAPpp 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1658 -VVALDRVADRLTAMPDQR-PEVTV-----DPRGLAYsifTSGSTGQPKGVAVEHIGIVRylswaaASYPTAGRRGTLAH 1730
Cdd:PRK12583 172 gFLAWHELQARGETVSREAlAERQAsldrdDPINIQY---TSGTTGFPKGATLSHHNILN------NGYFVAESLGLTEH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1731 SSV--------GFDLTMSALFepLVSGRGVTLMPAD-----ATLADLAEELSGPLaYDYIRLTPSHLRH-LVGHWTGQEL 1796
Cdd:PRK12583 243 DRLcvpvplyhCFGMVLANLG--CMTVGACLVYPNEafdplATLQAVEEERCTAL-YGVPTMFIAELDHpQRGNFDLSSL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1797 ppaaRGWVVGGETLDPALVKQLLELRPDAEVINHYGPTETvigrvvHPVreAGELAVDSPLPL-----GRPLGETRLQVL 1871
Cdd:PRK12583 320 ----RTGIMAGAPCPIEVMRRVMDEMHMAEVQIAYGMTET------SPV--SLQTTAADDLERrvetvGRTQPHLEVKVV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1872 DAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDpagepgARMYrTGDLVRWRGDGLLDFVGRVDDQVKLRGYR 1951
Cdd:PRK12583 388 DPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDED------GWMH-TGDLATMDEQGYVRIVGRSKDMIIRGGEN 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1952 IELGEIEARMAEHPGVEQ-AVVLVRDQ----QLVGWFIPAEDHpPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHG 2026
Cdd:PRK12583 461 IYPREIEEFLFTHPAVADvQVFGVPDEkygeEIVAWVRLHPGH-AASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTG 539
|
..
gi 653678460 2027 KV 2028
Cdd:PRK12583 540 KV 541
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
1531-2033 |
1.14e-18 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 92.05 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1531 RTVHQLVEAQADRTPGWTAL----RTGD-RSLTFAGLDAQANRLAHALHTgaLGappVGPETPVLLLLDRSPELVVAMLA 1605
Cdd:PRK08008 7 QHLRQMWDDLADVYGHKTALifesSGGVvRRYSYLELNEEINRTANLFYS--LG---IRKGDKVALHLDNCPEFIFCWFG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1606 VLKAGGYFIPVDPGY------------------------PM-ARLTRIADTVTPALVLTRTGQGGclpgaevfgDVPVVA 1660
Cdd:PRK08008 82 LAKIGAIMVPINARLlreesawilqnsqasllvtsaqfyPMyRQIQQEDATPLRHICLTRVALPA---------DDGVSS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1661 LDRVADRLTAMPDQRPEVTVDprGLAYSIFTSGSTGQPKGVAVEHIGIV---RYLSWAAAsyptagrrgtLAHSSVGfdL 1737
Cdd:PRK08008 153 FTQLKAQQPATLCYAPPLSTD--DTAEILFTSGTTSRPKGVVITHYNLRfagYYSAWQCA----------LRDDDVY--L 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1738 TMSALFEplVSGRGVTLMPA---DATLAdLAEELSGPLAYDYIR-----LT---PSHLRHLVG----------------- 1789
Cdd:PRK08008 219 TVMPAFH--IDCQCTAAMAAfsaGATFV-LLEKYSARAFWGQVCkyratITeciPMMIRTLMVqppsandrqhclrevmf 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1790 --HWTGQElppaargwvvggetldpalvKQLLELRPDAEVINHYGPTETVIGrvvhpvreageLAVDSP-----LP-LGR 1861
Cdd:PRK08008 296 ylNLSDQE--------------------KDAFEERFGVRLLTSYGMTETIVG-----------IIGDRPgdkrrWPsIGR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1862 PLGETRLQVLDAWLEAVPVGAVGELFIGG---DGIARGYLGRPALTAEKFlpdpagEPGARMYrTGDLVRWRGDGLLDFV 1938
Cdd:PRK08008 345 PGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVL------EADGWLH-TGDTGYVDEEGFFYFV 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1939 GRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVL-----VRDQQLVGWFIPAEDHPpVTVSALRRFCAEQLPEFMVPNQ 2013
Cdd:PRK08008 418 DRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVgikdsIRDEAIKAFVVLNEGET-LSEEEFFAFCEQNMAKFKVPSY 496
|
570 580
....*....|....*....|
gi 653678460 2014 WVALDAFPLTPHGKVNHRAL 2033
Cdd:PRK08008 497 LEIRKDLPRNCSGKIIKKNL 516
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
501-971 |
1.28e-18 |
|
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: 92.72 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 501 CRRTPGAVAVIEGD----TTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFP 576
Cdd:cd05943 79 HADADDPAAIYAAEdgerTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 577 V-------------------------------ERIAYL---LSDARPVLVVTDAATADRLGPDDITGLVVLEE---TDTG 619
Cdd:cd05943 159 VpgvldrfgqiepkvlfavdaytyngkrhdvrEKVAELvkgLPSLLAVVVVPYTVAAGQPDLSKIAKALTLEDflaTGAA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 620 GYPATEPpaVPAGHSAYVIYTSGSTGRPKGVVitRAALDNFLAAMAE---RFPLTAEDRVLATTTVS-----FDIAGLEl 691
Cdd:cd05943 239 GELEFEP--LPFDHPLYILYSSGTTGLPKCIV--HGAGGTLLQHLKEhilHCDLRPGDRLFYYTTCGwmmwnWLVSGLA- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 692 ylplrSGAGVVLAD-ADTARNPAALIDLAGRHRVTLAQATPTLWQALvpELSG--PA----LAGIR-VLVGGEALPAELA 763
Cdd:cd05943 314 -----VGATIVLYDgSPFYPDTNALWDLADEEGITVFGTSAKYLDAL--EKAGlkPAethdLSSLRtILSTGSPLKPESF 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 764 RRLGDAGAEvtnmygptetTIW--STSGPT----------SEDSIRRGSIGVPIDNTQVYVLDANLHPApIGVLGELHIA 831
Cdd:cd05943 387 DYVYDHIKP----------DVLlaSISGGTdiiscfvggnPLLPVYRGEIQCRGLGMAVEAFDEEGKPV-WGEKGELVCT 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 832 GEGLAR--GYWNRPGltAEKFLPDPFGP-PGTrmYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGP 908
Cdd:cd05943 456 KPFPSMpvGFWNDPD--GSRYRAAYFAKyPGV--WAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPE 531
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 653678460 909 VRRAAAVVREDRPGDLRLVAYV-IPDGPVAPDALRTELSRTLPDYM----IPAVIVPVPDFPTTPNGK 971
Cdd:cd05943 532 VEDSLVVGQEWKDGDERVILFVkLREGVELDDELRKRIRSTIRSALsprhVPAKIIAVPDIPRTLSGK 599
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
1690-2028 |
1.98e-18 |
|
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: 89.00 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1690 FTSGSTGQPKGVAVEHigivryLSWAAaSYPtAGRR-------------GTLAHSsvgfdLTMSALFEPLVSGRGVTLMP 1756
Cdd:cd17633 7 FTSGTTGLPKAYYRSE------RSWIE-SFV-CNEDlfnisgedailapGPLSHS-----LFLYGAISALYLGGTFIGQR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1757 --ADATLADLAEELSGPLAYdyirLTPSHLRHLVGHwtgQELPPAARGWVVGGETLDPALVKQLLELRPDAEVINHYGPT 1834
Cdd:cd17633 74 kfNPKSWIRKINQYNATVIY----LVPTMLQALART---LEPESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1835 ET--VIGRVVhpvreaGELAvdSPLPLGRPLGETRLQVLDAwleavPVGAVGELFIGGDGIARGYLGRPALTAEKFlpdp 1912
Cdd:cd17633 147 ELsfITYNFN------QESR--PPNSVGRPFPNVEIEIRNA-----DGGEIGKIFVKSEMVFSGYVRGGFSNPDGW---- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1913 agepgarmYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVL----VRDQQLVGWFIPAED 1988
Cdd:cd17633 210 --------MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVgipdARFGEIAVALYSGDK 281
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 653678460 1989 hppVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKV 2028
Cdd:cd17633 282 ---LTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
1678-2033 |
2.05e-18 |
|
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: 91.24 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1678 VTVDPRGLAYSIFTSGSTGQPKGVAVEHIGIVRYLSWAAASYPTAGRRGTLA-----HSsvgFDLTmSALFEPLVSGRGV 1752
Cdd:cd05909 142 APVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGalpffHS---FGLT-GCLWLPLLSGIKV 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1753 TLMPADatladLAEELSGPLAYDY---IRL-TPSHLRHLVGHWTGQELPpAARGWVVGGETLDPALvKQLLELRPDAEVI 1828
Cdd:cd05909 218 VFHPNP-----LDYKKIPELIYDKkatILLgTPTFLRGYARAAHPEDFS-SLRLVVAGAEKLKDTL-RQEFQEKFGIRIL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1829 NHYGPTETVigrvvhPVreageLAVDSPLP------LGRPL--GETRLqVLDAWLEAVPVGAVGELFIGGDGIARGYLGR 1900
Cdd:cd05909 291 EGYGTTECS------PV-----ISVNTPQSpnkegtVGRPLpgMEVKI-VSVETHEEVPIGEGGLLLVRGPNVMLGYLNE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1901 PALTAEKFlpdpagepGARMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPG--VEQAVVLVRDQQ 1978
Cdd:cd05909 359 PELTSFAF--------GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPedNEVAVVSVPDGR 430
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 653678460 1979 lvgwfiPAE------DHPPVTVSALRRFCAE-QLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:cd05909 431 ------KGEkivlltTTTDTDPSSLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
1555-1973 |
2.64e-18 |
|
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: 90.35 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1555 RSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGyfIPVdPGYPmarltriadTVTP 1634
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLI--ALG---VEPGDRVAILSRNRPEWTIADLAILAIGA--VPV-PIYP---------TSSA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1635 ALVltrtgqggclpgAEVFGDVPVVALdrvadrltampdqrpeVTVDPRGLAYSIFTSGSTGQPKGVAVEHigivRYLSW 1714
Cdd:cd05907 67 EQI------------AYILNDSEAKAL----------------FVEDPDDLATIIYTSGTTGRPKGVMLSH----RNILS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1715 AAASYPTAGRRGTLAHsSVGFdLTMSALFE-------PLVSGRGVTLMPADATL-ADLAEE-----LSGPLAYDYIRLTP 1781
Cdd:cd05907 115 NALALAERLPATEGDR-HLSF-LPLAHVFErraglyvPLLAGARIYFASSAETLlDDLSEVrptvfLAVPRVWEKVYAAI 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1782 SH-----LRHLVGHWT-GQELppaaRGWVVGGETLDPALVKQLLELrpDAEVINHYGPTETviGRVVHpVREAGELAVDS 1855
Cdd:cd05907 193 KVkavpgLKRKLFDLAvGGRL----RFAASGGAPLPAELLHFFRAL--GIPVYEGYGLTET--SAVVT-LNPPGDNRIGT 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1856 PlplGRPLGETRLQvldawleavpVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPAgepgarmYRTGDLVRWRGDGLL 1935
Cdd:cd05907 264 V---GKPLPGVEVR----------IADDGEILVRGPNVMLGYYKNPEATAEALDADGW-------LHTGDLGEIDEDGFL 323
|
410 420 430
....*....|....*....|....*....|....*....
gi 653678460 1936 DFVGRVDDQVKLR-GYRIELGEIEARMAEHPGVEQAVVL 1973
Cdd:cd05907 324 HITGRKKDLIITSgGKNISPEPIENALKASPLISQAVVI 362
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
620-977 |
8.89e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 89.82 E-value: 8.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 620 GYPATEppAVPAGHSAYVI-YTSGSTGRPKGVVITRAaldNFLAAMAERFPLTAEDRVLATTTVsfdIAGLELY----LP 694
Cdd:PRK05677 196 GQPVTE--ANPQADDVAVLqYTGGTTGVAKGAMLTHR---NLVANMLQCRALMGSNLNEGCEIL---IAPLPLYhiyaFT 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 695 LRSGAGVVLADAD----TARNPAALIDLAGRHRVTLAQATPTLWQALVPELSGPAL--AGIRV-LVGGEALPAELARRLG 767
Cdd:PRK05677 268 FHCMAMMLIGNHNilisNPRDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLdfSALKLtLSGGMALQLATAERWK 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 768 D-AGAEVTNMYGPTETTIWSTSGPTseDSIRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLT 846
Cdd:PRK05677 348 EvTGCAICEGYGMTETSPVVSVNPS--QAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEAT 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 847 AEKFLPDPFgppgtrmYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAV-VREDRPGDLR 925
Cdd:PRK05677 426 DEILDSDGW-------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIgVPDEKSGEAI 498
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 653678460 926 LVAYVIPDGP-VAPDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:PRK05677 499 KVFVVVKPGEtLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
1827-2033 |
8.92e-18 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 89.50 E-value: 8.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1827 VINHYGPTETVIGRVVHPVREAGELAVdsplpLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAE 1906
Cdd:PRK12492 361 IVEGYGLTETSPVASTNPYGELARLGT-----VGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAE 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1907 KFlpDPAGepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQ-AVVLVRDQ---QLVGW 1982
Cdd:PRK12492 436 AL--DAEG-----WFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANcAAIGVPDErsgEAVKL 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 653678460 1983 FIPAEDhPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:PRK12492 509 FVVARD-PGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1540-2033 |
9.27e-18 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 89.25 E-value: 9.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1540 QADRTPGWTALRTGDRSLTFAGLDAQANRLAhalhtGALGAPPVGPETPVLLLLDRSPELVVAMLAV--LKAGGYFIPVd 1617
Cdd:PRK03640 11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVA-----GKLAALGVKKGDRVALLMKNGMEMILVIHALqqLGAVAVLLNT- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1618 pgypmaRLTR------IADT-VTpaLVLTRTGQGgclpgAEVFGDVPVVaLDRVADrlTAMPDQRPEVTVDPRGLAYSIF 1690
Cdd:PRK03640 85 ------RLSReellwqLDDAeVK--CLITDDDFE-----AKLIPGISVK-FAELMN--GPKEEAEIQEEFDLDEVATIMY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1691 TSGSTGQPKGV-------------AVEHIGIVRYLSWAAAsYPtagrrgtLAHSSvGFdltmSALFEPLVSGRGVTLMPA 1757
Cdd:PRK03640 149 TSGTTGKPKGViqtygnhwwsavgSALNLGLTEDDCWLAA-VP-------IFHIS-GL----SILMRSVIYGMRVVLVEK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1758 -DATLA-DLAEELSGPLaydyIRLTPSHLRHLVGHWTGQELPPAARGWVVGGETLDPALVKQLLElrPDAEVINHYGPTE 1835
Cdd:PRK03640 216 fDAEKInKLLQTGGVTI----ISVVSTMLQRLLERLGEGTYPSSFRCMLLGGGPAPKPLLEQCKE--KGIPVYQSYGMTE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1836 TV--IgrvvhpVREAGELAVDSPLPLGRPLGETRLQVLDAWLEAVPvGAVGELFIGGDGIARGYLGRPALTAEKFlpdpa 1913
Cdd:PRK03640 290 TAsqI------VTLSPEDALTKLGSAGKPLFPCELKIEKDGVVVPP-FEEGEIVVKGPNVTKGYLNREDATRETF----- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1914 gEPGarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVL-VRDQQlvgW------FIPA 1986
Cdd:PRK03640 358 -QDG--WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVgVPDDK---WgqvpvaFVVK 431
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 653678460 1987 EDhpPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:PRK03640 432 SG--EVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHEL 476
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1532-2122 |
1.33e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 90.61 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1532 TVHQLVEAQADRTPGWTALR------TGDRSLTFAGLDAQANRLAHALHTGAlgappvGPETPVLLLLDRSPELVVAMLA 1605
Cdd:PRK05691 10 TLVQALQRRAAQTPDRLALRfladdpGEGVVLSYRDLDLRARTIAAALQARA------SFGDRAVLLFPSGPDYVAAFFG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1606 VLKAGgyFIPVdPGYP--------MARLTRIADTVTPALVLTRTGQGGCLPGAEVFGDVPVVALDRVADRLTAMPDQRPE 1677
Cdd:PRK05691 84 CLYAG--VIAV-PAYPpesarrhhQERLLSIIADAEPRLLLTVADLRDSLLQMEELAAANAPELLCVDTLDPALAEAWQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1678 VTVDPRGLAYSIFTSGSTGQPKGVAVEHIGIVRylswaaasyptagrRGTLAHSSVGFDLT-----------------MS 1740
Cdd:PRK05691 161 PALQPDDIAFLQYTSGSTALPKGVQVSHGNLVA--------------NEQLIRHGFGIDLNpddvivswlplyhdmglIG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1741 ALFEPLVSGRGVTLMPADATLADLAEELS-----------GP-LAYDYI--RLTPSHLRHLvghwtgqELppaaRGWVV- 1805
Cdd:PRK05691 227 GLLQPIFSGVPCVLMSPAYFLERPLRWLEaiseyggtisgGPdFAYRLCseRVSESALERL-------DL----SRWRVa 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1806 --GGETLDPALVKQLLE------LRPDAeVINHYGPTETVI-------GRVVHPVR-EAGELAVDSPLP--------LGR 1861
Cdd:PRK05691 296 ysGSEPIRQDSLERFAEkfaacgFDPDS-FFASYGLAEATLfvsggrrGQGIPALElDAEALARNRAEPgtgsvlmsCGR 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1862 PLGETRLQVLD-AWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPdpagEPGARMYRTGDLVRWRgDGLLDFVGR 1940
Cdd:PRK05691 375 SQPGHAVLIVDpQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVE----HDGRTWLRTGDLGFLR-DGELFVTGR 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1941 VDDQVKLRGYRIELGEIEARMAEHPGVEQ----AVVLVRDQQLVGWFIPAEDH--------PPVTVSALRRFCAEQLPEf 2008
Cdd:PRK05691 450 LKDMLIVRGHNLYPQDIEKTVEREVEVVRkgrvAAFAVNHQGEEGIGIAAEISrsvqkilpPQALIKSIRQAVAEACQE- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 2009 mVPNQWVALD--AFPLTPHGKVNHRA---------------LPGptsGRPELEDRYQAPRTPGEQLLAELWSTVLGTDRI 2071
Cdd:PRK05691 529 -APSVVLLLNpgALPKTSSGKLQRSAcrlrladgsldsyalFPA---LQAVEAAQTAASGDELQARIAAIWCEQLKVEQV 604
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 653678460 2072 GIEDNFFDLGGTSISVIQLSGACR-RAGVEISPKDVFEQPTVRGQAMrAIAR 2122
Cdd:PRK05691 605 AADDHFFLLGGNSIAATQVVARLRdELGIDLNLRQLFEAPTLAAFSA-AVAR 655
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
1589-2055 |
1.65e-17 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 89.32 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1589 VLLLLDRSPELVVAMLAVLKAGGYFIPVDP-------GYPmARLTRIADTVTPALVLTRTGQGGCLPGAEVFGDvpvval 1661
Cdd:PRK06060 58 VLLCLPDSPDLVQLLLACLARGVMAFLANPelhrddhALA-ARNTEPALVVTSDALRDRFQPSRVAEAAELMSE------ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1662 drvADRltAMPDQRPEVTVDprGLAYSIFTSGSTGQPKGVAVEH---IGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLT 1738
Cdd:PRK06060 131 ---AAR--VAPGGYEPMGGD--ALAYATYTSGTTGPPKAAIHRHadpLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1739 MSALFePLVSGRGVTLMPADATlADLAEELSGPLAYDYIRLTPSHLRHLVGHWTGQELPpAARGWVVGGETLDPALVKQL 1818
Cdd:PRK06060 204 NSVWF-PLATGGSAVINSAPVT-PEAAAILSARFGPSVLYGVPNFFARVIDSCSPDSFR-SLRCVVSAGEALELGLAERL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1819 LELRPDAEVINHYGPTETVIGRVVHPVREAgelavdSPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYL 1898
Cdd:PRK06060 281 MEFFGGIPILDGIGSTEVGQTFVSNRVDEW------RLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYW 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1899 GRPaltaekflpDPAGEPGARMyRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGV-EQAVVLVRD- 1976
Cdd:PRK06060 355 NRP---------DSPVANEGWL-DTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVaEAAVVAVREs 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1977 ---QQLVGWFIPAEDHPpVTVSALR---RFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRALPGPTSGRP--ELEDRYQ 2048
Cdd:PRK06060 425 tgaSTLQAFLVATSGAT-IDGSVMRdlhRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQSPTKPiwELSLTEP 503
|
....*..
gi 653678460 2049 APRTPGE 2055
Cdd:PRK06060 504 GSGVRAQ 510
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
1548-2033 |
2.13e-17 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 88.41 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1548 TALR----TGDRSLTFAGLDAQANRLAHALHTgaLGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGY-PM 1622
Cdd:PRK04319 61 VALRyldaSRKEKYTYKELKELSNKFANVLKE--LG---VEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFmEE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1623 ARLTRIADT------VTPALvLTRTGQGGcLP--------GAEVFGDVPVVALDRvadRLTAMPDQRPEVTVDPRGLAYS 1688
Cdd:PRK04319 136 AVRDRLEDSeakvliTTPAL-LERKPADD-LPslkhvllvGEDVEEGPGTLDFNA---LMEQASDEFDIEWTDREDGAIL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1689 IFTSGSTGQPKGVAVEHIGIVRYlsWAAASYP-----------TAGrRGTLAHSSVGfdltmsaLFEPLVSGrgvtlmpa 1757
Cdd:PRK04319 211 HYTSGSTGKPKGVLHVHNAMLQH--YQTGKYVldlheddvywcTAD-PGWVTGTSYG-------IFAPWLNG-------- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1758 dATLADLAEELSGPLAYDYI---RLT-----PSHLRHLVGHwtGQELP-----PAARGWVVGGETLDPALV---KQLLEL 1821
Cdd:PRK04319 273 -ATNVIDGGRFSPERWYRILedyKVTvwytaPTAIRMLMGA--GDDLVkkydlSSLRHILSVGEPLNPEVVrwgMKVFGL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1822 RpdaeVINHYGPTET---VIgrvvhpvreAGELAVD-SPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFI--GGDGIAR 1895
Cdd:PRK04319 350 P----IHDNWWMTETggiMI---------ANYPAMDiKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIkkGWPSMMR 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1896 GYLGRPALTAEKFLPDpagepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVR 1975
Cdd:PRK04319 417 GIWNNPEKYESYFAGD--------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGK 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 653678460 1976 DQQLVGWFIPA-----EDHPPvtVSALRR----FCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:PRK04319 489 PDPVRGEIIKAfvalrPGYEP--SEELKEeirgFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVL 553
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
1553-2033 |
2.49e-17 |
|
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: 88.07 E-value: 2.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1553 GDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMARLTRIAD-- 1630
Cdd:cd12119 22 EVHRYTYAEVAERARRLANALR--RLG---VKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINha 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1631 -----TVTPALVLTRTGQGGCLPGAEVFgdvpVVALDRVADRLTAMP---------DQRPEVTVDPR---GLAYSI-FTS 1692
Cdd:cd12119 97 edrvvFVDRDFLPLLEAIAPRLPTVEHV----VVMTDDAAMPEPAGVgvlayeellAAESPEYDWPDfdeNTAAAIcYTS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1693 GSTGQPKGVAVEHIGIVRYlSWAAASYPTAGrrgtLAHSSVGfdLTMSALFEplVSGRGvtlMPADATLADLAEELSGPl 1772
Cdd:cd12119 173 GTTGNPKGVVYSHRSLVLH-AMAALLTDGLG----LSESDVV--LPVVPMFH--VNAWG---LPYAAAMVGAKLVLPGP- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1773 aydyiRLTPSHLRHLV---------------------GHWTGQELPPAaRGWVVGGETLDPALVKQLLELrpDAEVINHY 1831
Cdd:cd12119 240 -----YLDPASLAELIeregvtfaagvptvwqglldhLEANGRDLSSL-RRVVIGGSAVPRSLIEAFEER--GVRVIHAW 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1832 GPTETV-IGRVVHPVREAGELAVDSPLPL----GRPLGETRLQVLDAWLEAVPV--GAVGELFIGGDGIARGYLGRPALT 1904
Cdd:cd12119 312 GMTETSpLGTVARPPSEHSNLSEDEQLALrakqGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEES 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1905 AEKFlpdpagEPGarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQ-AVVLVRDQQL---- 1979
Cdd:cd12119 392 EALT------EDG--WLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEaAVIGVPHPKWgerp 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 653678460 1980 VGWFIPAEDHPpVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:cd12119 464 LAVVVLKEGAT-VTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
515-977 |
3.22e-17 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 88.01 E-value: 3.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 515 TTLSYRELDERANRLAR-LLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDA-RPVLV 592
Cdd:PRK08751 49 KTITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSgASVLV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 593 VTD----------AAT----------ADRLG------------------PD-DITGLVVLEETDTGGYPATEPPA-VPAG 632
Cdd:PRK08751 129 VIDnfgttvqqviADTpvkqvittglGDMLGfpkaalvnfvvkyvkklvPEyRINGAIRFREALALGRKHSMPTLqIEPD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 633 HSAYVIYTSGSTGRPKGVVITRAaldNFLAAMAERFP-LTAEDRVLATTTVSfdIAGLELYLPLRSGA-GVVLADA---- 706
Cdd:PRK08751 209 DIAFLQYTGGTTGVAKGAMLTHR---NLVANMQQAHQwLAGTGKLEEGCEVV--ITALPLYHIFALTAnGLVFMKIggcn 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 707 ---DTARNPAALIDLAGRHRVTLAQATPTLWQALvpeLSGPALAGIR------VLVGGEALPAELARRLGD-AGAEVTNM 776
Cdd:PRK08751 284 hliSNPRDMPGFVKELKKTRFTAFTGVNTLFNGL---LNTPGFDQIDfsslkmTLGGGMAVQRSVAERWKQvTGLTLVEA 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 777 YGPTETTIWSTSGPTSEDSiRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFg 856
Cdd:PRK08751 361 YGLTETSPAACINPLTLKE-YNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGW- 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 857 ppgtrmYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAV-VREDRPGDLRLVAYVIPDGP 935
Cdd:PRK08751 439 ------LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVgVPDEKSGEIVKVVIVKKDPA 512
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 653678460 936 VAPDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:PRK08751 513 LTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
1529-2028 |
3.72e-17 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 87.51 E-value: 3.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1529 DDRTVHQLVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALhtgalGAPPVGPETPVLLLLDRSPELVVAMLAVLK 1608
Cdd:PRK06155 19 SERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHAL-----AAAGVKRGDRVALMCGNRIEFLDVFLGCAW 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1609 AGGYFIPVDPGYPMARLTRIADTVTPALVLT--------RTGQGGCLPGAEVF--GDVPVVALDRvADRLTAMP--DQR- 1675
Cdd:PRK06155 94 LGAIAVPINTALRGPQLEHILRNSGARLLVVeaallaalEAADPGDLPLPAVWllDAPASVSVPA-GWSTAPLPplDAPa 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1676 PEVTVDPRGLAYSIFTSGSTGQPKGVAVEHigiVRYLSWAAASYPTAG-RRGTLAHSSVGFDLT--MSALFEPLVSGrgv 1752
Cdd:PRK06155 173 PAAAVQPGDTAAILYTSGTTGPSKGVCCPH---AQFYWWGRNSAEDLEiGADDVLYTTLPLFHTnaLNAFFQALLAG--- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1753 tlmpadATLAdLAEELSGPLAYDYIRLTPSHLRHLVGHWT----GQELPPAARGWVVG---GETLDPALVKQLLElRPDA 1825
Cdd:PRK06155 247 ------ATYV-LEPRFSASGFWPAVRRHGATVTYLLGAMVsillSQPARESDRAHRVRvalGPGVPAALHAAFRE-RFGV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1826 EVINHYGPTET--VIGrVVHPVREAGELavdsplplGRPLGETRLQVLDAWLEAVPVGAVGELFIGGD---GIARGYLGR 1900
Cdd:PRK06155 319 DLLDGYGSTETnfVIA-VTHGSQRPGSM--------GRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGM 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1901 PALTAEKFlpdpagepGARMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRDQQLv 1980
Cdd:PRK06155 390 PEKTVEAW--------RNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSEL- 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 653678460 1981 gwfipAEDHPPVTV----------SALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKV 2028
Cdd:PRK06155 461 -----GEDEVMAAVvlrdgtalepVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKV 513
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
1852-2127 |
4.55e-17 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 84.42 E-value: 4.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1852 AVDSPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPAGEPGARMYRTGDLVRWRG 1931
Cdd:COG3433 15 EPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLRLLLRRGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1932 DGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRDQQLVGWFIPAEDHPPVTVSALRRFCAEQLPEFMVP 2011
Cdd:COG3433 95 PGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAAALAALDKVPPDVVA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 2012 nqWVALDAFPLTPHGKVNHRALPGPTSGRPELEDRYQAPRTPGE-----QLLAELWSTVLGT--DRIGIEDNFFDLGGTS 2084
Cdd:COG3433 175 --ASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALEtalteEELRADVAELLGVdpEEIDPDDNLFDLGLDS 252
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 653678460 2085 ISVIQLSGACRRAGVEISPKDVFEQPTVRGQAMRAIARSRDDA 2127
Cdd:COG3433 253 IRLMQLVERWRKAGLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
501-977 |
4.66e-17 |
|
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: 86.66 E-value: 4.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 501 CRRTPGAVAVIegdTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIK---AGAAYLPIDPDFPV 577
Cdd:cd05929 5 DLDRAQVFHQR---RLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKcgaCPAYKSSRAPRAEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 578 ERIAYLLSDARPVLVVTDAATADRLGPDditglvvleETDTGGYPATEPPAVPAGHsaYVIYTSGSTGRPKGVvitRAAL 657
Cdd:cd05929 82 CAIIEIKAAALVCGLFTGGGALDGLEDY---------EAAEGGSPETPIEDEAAGW--KMLYSGGTTGRPKGI---KRGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 658 -----DNFLAAMAE-RFPLTAEDRVLATTTVSFDIAGLELYLPLRSGAGVVLADadtARNPAALIDLAGRHRVTLAQATP 731
Cdd:cd05929 148 pggppDNDTLMAAAlGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLME---KFDPEEFLRLIERYRVTFAQFVP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 732 TLWQAL--VPELSGPA--LAGIRVLVGGEA-LPAELARRLGDAGAEVT-NMYGPTE----TTIwstsgpTSEDSIR-RGS 800
Cdd:cd05929 225 TMFVRLlkLPEAVRNAydLSSLKRVIHAAApCPPWVKEQWIDWGGPIIwEYYGGTEgqglTII------NGEEWLThPGS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 801 IGVPIDNtQVYVLDANLHPAPIGVLGELHIAGeGLARGYWNRPGLTAEKFLPDPFgppgtrmyRT-GDLVRWSAAGDLEY 879
Cdd:cd05929 299 VGRAVLG-KVHILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAARNEGGW--------STlGDVGYLDEDGYLYL 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 880 LGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIP-----DGPVAPDALRTELSRTLPDYMI 954
Cdd:cd05929 369 TDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPapgadAGTALAEELIAFLRDRLSRYKC 448
|
490 500
....*....|....*....|...
gi 653678460 955 PAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:cd05929 449 PRSIEFVAELPRDDTGKLYRRLL 471
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1687-2031 |
4.70e-17 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 85.51 E-value: 4.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1687 YSIFTSGSTGQPKGV-------------------------------AVEHIGIVRYL---------SWAAASYPTAGrrG 1726
Cdd:cd05924 7 YILYTGGTTGMPKGVmwrqedifrmlmggadfgtgeftpsedahkaAAAAAGTVMFPapplmhgtgSWTAFGGLLGG--Q 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1727 TLAHSSVGFDltMSALFEpLVSGRGVTLMP--ADATLADLAEELSGPLAYDYirltpSHLRHLVGhwtgqelppaargwv 1804
Cdd:cd05924 85 TVVLPDDRFD--PEEVWR-TIEKHKVTSMTivGDAMARPLIDALRDAGPYDL-----SSLFAISS--------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1805 vGGETLDPALVKQLLELRPDAEVINHYGPTETVIGRVVHPVREAGELAVdsplplgRPLGETRLQVLDAWLEAVPVGAVG 1884
Cdd:cd05924 142 -GGALLSPEVKQGLLELVPNITLVDAFGSSETGFTGSGHSAGSGPETGP-------FTRANPDTVVLDDDGRVVPPGSGG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1885 ELFIGGDG-IARGYLGRPALTAEKFlpdPAGEpGARMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAE 1963
Cdd:cd05924 214 VGWIARRGhIPLGYYGDEAKTAETF---PEVD-GVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKS 289
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 653678460 1964 HPGVEQAVVL-VRDQ---QLVGWFIPAEDHPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHR 2031
Cdd:cd05924 290 HPAVYDVLVVgRPDErwgQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKADYR 361
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
513-979 |
5.37e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 85.86 E-value: 5.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 513 GDTTLSYRELDERANRLARLLMERGAGAETFvAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARPVLV 592
Cdd:PRK08308 5 NDEEYSKSDFDLRLQRYEEMEQFQEAAGNRF-AVCLKDPFDIITLVFFLKEKGASVLPIHPDTPKEAAIRMAKRAGCHGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 593 VTDaatadrlgpddiTGLVVLEETDTGgypATEPPAVpaghsayVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTA 672
Cdd:PRK08308 84 LYG------------ESDFTKLEAVNY---LAEEPSL-------LQYSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 673 EDR--VLATTTVSFD-IAGLelYLPLRSGAGVVLAdadTARNPAALIDLAGRHRVTLAQATPTLWQALVPELsgPALAGI 749
Cdd:PRK08308 142 DETpiVACPVTHSYGlICGV--LAALTRGSKPVII---TNKNPKFALNILRNTPQHILYAVPLMLHILGRLL--PGTFQF 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 750 -RVLVGGEALPAELARRLGDAGAEVTNMYGPTETTIWSTSGPTSEdsirRGSIGVPIDNTQVYvldanlhpapigvlgel 828
Cdd:PRK08308 215 hAVMTSGTPLPEAWFYKLRERTTYMMQQYGCSEAGCVSICPDMKS----HLDLGNPLPHVSVS----------------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 829 hiAGEGLargywNRPGLTAEKFlpdpfgppGTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGP 908
Cdd:PRK08308 274 --AGSDE-----NAPEEIVVKM--------GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPG 338
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 653678460 909 VRRAAAVVREDRPGDLRLVAYVIPDGPVAPDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAALPA 979
Cdd:PRK08308 339 VQEAVVYRGKDPVAGERVKAKVISHEEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLEL 409
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
517-949 |
5.71e-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: 5.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 517 LSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLL--SDARPVLV-V 593
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLehSESKALFVgK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 594 TDAATADRLGPDDITGLVVLEETDTG------------GYPATEPPAVPAGHSAYVIYTSGSTGRPKGVVITRAALDNFL 661
Cdd:cd05932 87 LDDWKAMAPGVPEGLISISLPPPSAAncqyqwddliaqHPPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 662 AAMAERFPLTAEDRVLAtttvsfdiaglelYLPL--------------RSGAGVVLADA-DTarnpaaLIDLAGRHRVTL 726
Cdd:cd05932 167 QAGIEHIGTEENDRMLS-------------YLPLahvtervfveggslYGGVLVAFAESlDT------FVEDVQRARPTL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 727 AQATPTLW-------QALVPE--------------------LSGPALAGIRVLVGGEA-LPAELARRLGDAGAEVTNMYG 778
Cdd:cd05932 228 FFSVPRLWtkfqqgvQDKIPQqklnlllkipvvnslvkrkvLKGLGLDQCRLAGCGSApVPPALLEWYRSLGLNILEAYG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 779 PTETTIWSTSGPTSEDSIrrGSIGVPIDNTQVyvldanlhpaPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgpp 858
Cdd:cd05932 308 MTENFAYSHLNYPGRDKI--GTVGNAGPGVEV----------RISEDGEILVRSPALMMGYYKDPEATAEAFTADGF--- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 859 gtrmYRTGDLVRWSAAGDLEYLGRTDHQVKL-RGFRIELGEIETTLINAGPVrRAAAVVREDRPGDLRLVayVIPDGPV- 936
Cdd:cd05932 373 ----LRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRV-EMVCVIGSGLPAPLALV--VLSEEARl 445
|
490
....*....|....
gi 653678460 937 -APDALRTELSRTL 949
Cdd:cd05932 446 rADAFARAELEASL 459
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
1536-1976 |
1.21e-16 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 86.01 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1536 LVEAQADRTPG-----WTALRTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAG 1610
Cdd:cd05970 22 VVDAMAKEYPDklalvWCDDAGEERIFTFAELADYSDKTANFFK--AMG---IGKGDTVMLTLKRRYEFWYSLLALHKLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1611 GYFIPV-------DPGYPMAR-----LTRIADTVTPALVLTRTGQGGCLPG-AEVFGDVPVVALDRVADRLTAMPD-QRP 1676
Cdd:cd05970 97 AIAIPAthqltakDIVYRIESadikmIVAIAEDNIPEEIEKAAPECPSKPKlVWVGDPVPEGWIDFRKLIKNASPDfERP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1677 EVTVDPRG----LAYsiFTSGSTGQPKGVAVEHIGIVRYLswAAASY----PTAGRRGTLAHSSVG-------------- 1734
Cdd:cd05970 177 TANSYPCGedilLVY--FSSGTTGMPKMVEHDFTYPLGHI--VTAKYwqnvREGGLHLTVADTGWGkavwgkiygqwiag 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1735 -----FDLTMsalFEP-----LVSGRGVTLMPADATLAD--LAEELSgplAYDYirltpSHLRHLVghwtgqelppaarg 1802
Cdd:cd05970 253 aavfvYDYDK---FDPkalleKLSKYGVTTFCAPPTIYRflIREDLS---RYDL-----SSLRYCT-------------- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1803 wvVGGETLDPALVKQLLELrPDAEVINHYGPTETVIGRVVHPVREAgelavdSPLPLGRPLGETRLQVLDAWLEAVPVGA 1882
Cdd:cd05970 308 --TAGEALNPEVFNTFKEK-TGIKLMEGFGQTETTLTIATFPWMEP------KPGSMGKPAPGYEIDLIDREGRSCEAGE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1883 VGELFIGGD-----GIARGYLGRPALTAEKFLPDpagepgarMYRTGDlVRWRG-DGLLDFVGRVDDQVKLRGYRIELGE 1956
Cdd:cd05970 379 EGEIVIRTSkgkpvGLFGGYYKDAEKTAEVWHDG--------YYHTGD-AAWMDeDGYLWFVGRTDDLIKSSGYRIGPFE 449
|
490 500
....*....|....*....|.
gi 653678460 1957 IEARMAEHPGV-EQAVVLVRD 1976
Cdd:cd05970 450 VESALIQHPAVlECAVTGVPD 470
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
483-971 |
1.67e-16 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 85.63 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 483 DTARPLPAASLRERFQQWCRRTPG--AVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLA 560
Cdd:PRK08315 8 PTDVPLLEQTIGQLLDRTAARYPDreALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 561 VIKAGAAYLPIDPDFPVERIAYLL--SDARpVLVVTDA-------ATADRLGPD---------------DITGLVVLEET 616
Cdd:PRK08315 88 TAKIGAILVTINPAYRLSELEYALnqSGCK-ALIAADGfkdsdyvAMLYELAPElatcepgqlqsarlpELRRVIFLGDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 617 DTGG-------------YPATEPPAVPAGHSAY-VI---YTSGSTGRPKGVVIT-RAALDN-FLAAMAERFplTAEDR-- 675
Cdd:PRK08315 167 KHPGmlnfdellalgraVDDAELAARQATLDPDdPIniqYTSGTTGFPKGATLThRNILNNgYFIGEAMKL--TEEDRlc 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 676 --------------VLATTTVsfdiaglelylplrsGAGVVL-ADadtARNPAALIDLAGRHRVTLAQATPTLWQAlvpE 740
Cdd:PRK08315 245 ipvplyhcfgmvlgNLACVTH---------------GATMVYpGE---GFDPLATLAAVEEERCTALYGVPTMFIA---E 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 741 LSGPALA---------GIrvlVGGEALPAELARRLGDA--GAEVTNMYGPTETTIWST-SGPTseDSIRR--GSIGVPID 806
Cdd:PRK08315 304 LDHPDFArfdlsslrtGI---MAGSPCPIEVMKRVIDKmhMSEVTIAYGMTETSPVSTqTRTD--DPLEKrvTTVGRALP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 807 NTQVYVLDANLH-PAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgppgtrMyRTGDLVRWSAAGDLEYLGRtdh 885
Cdd:PRK08315 379 HLEVKIVDPETGeTVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGW------M-HTGDLAVMDEEGYVNIVGR--- 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 886 qVK---LRGfrielG------EIETTLINAGPVRRAAAV-VREDRPGDlRLVAYVI--PDGPVAPDALRTELSRTLPDYM 953
Cdd:PRK08315 449 -IKdmiIRG-----GeniyprEIEEFLYTHPKIQDVQVVgVPDEKYGE-EVCAWIIlrPGATLTEEDVRDFCRGKIAHYK 521
|
570
....*....|....*...
gi 653678460 954 IPAVIVPVPDFPTTPNGK 971
Cdd:PRK08315 522 IPRYIRFVDEFPMTVTGK 539
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1536-1974 |
1.73e-16 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 85.34 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1536 LVEAqADRTPGWTALRTGD----------RSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLA 1605
Cdd:PRK09274 12 LPRA-AQERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLN--AAG---IGRGMRAVLMVTPSLEFFALTFA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1606 VLKAGGYFIPVDPGYPMARLTRIADTVTPALVLTrtgqggcLPGAEV--------FGDV-PVVALDR-------VADRLT 1669
Cdd:PRK09274 86 LFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIG-------IPKAHLarrlfgwgKPSVrRLVTVGGrllwggtTLATLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1670 AMPDQR--PEVTVDPRGLAYSIFTSGSTGQPKGVAVEHIGIVRYLSWAAASYPTagRRGtlahssvGFDLTM---SALFE 1744
Cdd:PRK09274 159 RDGAAApfPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGI--EPG-------EIDLPTfplFALFG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1745 PLVSGRGVtLMPADAT---LADLAEELSGPLAYDYIRL--TPSHLRHLVGHWTGQELP-PAARGWVVGGETLDPALVKQL 1818
Cdd:PRK09274 230 PALGMTSV-IPDMDPTrpaTVDPAKLFAAIERYGVTNLfgSPALLERLGRYGEANGIKlPSLRRVISAGAPVPIAVIERF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1819 LE-LRPDAEVINHYGPTE----TVIG-------RVVHPVREAGELavdsplpLGRPLGETRLQV-------LDAWLEA-- 1877
Cdd:PRK09274 309 RAmLPPDAEILTPYGATEalpiSSIEsreilfaTRAATDNGAGIC-------VGRPVDGVEVRIiaisdapIPEWDDAlr 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1878 VPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPAGEPGARMyrtGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEI 1957
Cdd:PRK09274 382 LATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDGQGDVWHRM---GDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPC 458
|
490
....*....|....*...
gi 653678460 1958 EARMAEHPGVEQ-AVVLV 1974
Cdd:PRK09274 459 ERIFNTHPGVKRsALVGV 476
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
1537-2033 |
1.79e-16 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 85.30 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1537 VEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHTgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPV 1616
Cdd:PRK06839 8 IEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIY-ELN---VKKGERIAILSQNSLEYIVLLFAIAKVECIAVPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1617 DpgypmARLT------RIADTVTPALVLTRTGQGGCLPGAEVFGDVPVVALDRVADRLtampDQRPEVTVDPRGLAYSI- 1689
Cdd:PRK06839 84 N-----IRLTenelifQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVISITSLKEIE----DRKIDNFVEKNESASFIi 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1690 -FTSGSTGQPKGVAVEHIGIVrylsWAAAsyptagrrgtlaHSSVGFDLTM---SALFEPLVSGRGVTLMPADATLADLA 1765
Cdd:PRK06839 155 cYTSGTTGKPKGAVLTQENMF----WNAL------------NNTFAIDLTMhdrSIVLLPLFHIGGIGLFAFPTLFAGGV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1766 EELSGPLAYDY-IRLTPSHLRHLVghwtgqelppaargwvVGGETLDPALVKQLLELRPD---------------AEVIN 1829
Cdd:PRK06839 219 IIVPRKFEPTKaLSMIEKHKVTVV----------------MGVPTIHQALINCSKFETTNlqsvrwfynggapcpEELMR 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1830 H-----------YGPTETviGRVVHPVREagELAVDSPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYL 1898
Cdd:PRK06839 283 EfidrgflfgqgFGMTET--SPTVFMLSE--EDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYW 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1899 GRPALTAEkflpdpAGEPGarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRdqQ 1978
Cdd:PRK06839 359 NRPDATEE------TIQDG--WLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGR--Q 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 653678460 1979 LVGW------FIPAEDHPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:PRK06839 429 HVKWgeipiaFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1557-1973 |
2.17e-16 |
|
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: 84.16 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1557 LTFAGLDAQANRLAHALHTGAlgappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVdpgypmarltriADTVTPAL 1636
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIG-----VGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPA------------TTLLTPDD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1637 VLTRTGQGGclpgaevfgdvpvvALDRVADRLTAMPDQRpevtvdprgLAYsiFTSGSTGQPKgvAVEHIGIVRYLSWAA 1716
Cdd:cd05974 64 LRDRVDRGG--------------AVYAAVDENTHADDPM---------LLY--FTSGTTSKPK--LVEHTHRSYPVGHLS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1717 ASYPTAGRRGT--LAHSSVGF-DLTMSALFEPLVSGRGVTLMPADATLADLAEELSGPLAYDYIRLTPSHLRHLVGH-WT 1792
Cdd:cd05974 117 TMYWIGLKPGDvhWNISSPGWaKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQdLA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1793 GQELPPaaRGWVVGGETLDPALVKQLLELRpDAEVINHYGPTETV--IGRVVHPVREAGELavdsplplGRPLGETRLQV 1870
Cdd:cd05974 197 SFDVKL--REVVGAGEPLNPEVIEQVRRAW-GLTIRDGYGQTETTalVGNSPGQPVKAGSM--------GRPLPGYRVAL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1871 LDAWLEAVPVGAVGeLFIGGD---GIARGYLGRPALTAEKFlpdpagepGARMYRTGDLVRWRGDGLLDFVGRVDDQVKL 1947
Cdd:cd05974 266 LDPDGAPATEGEVA-LDLGDTrpvGLMKGYAGDPDKTAHAM--------RGGYYRTGDIAMRDEDGYLTYVGRADDVFKS 336
|
410 420
....*....|....*....|....*.
gi 653678460 1948 RGYRIELGEIEARMAEHPGVEQAVVL 1973
Cdd:cd05974 337 SDYRISPFELESVLIEHPAVAEAAVV 362
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
637-972 |
3.13e-16 |
|
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: 82.55 E-value: 3.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 637 VIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDRVLATTTVsFDIAGLE--LYLPLRSGAGVVladADTARNPAA 714
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPF-FHTFGYKagIVACLLTGATVV---PVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 715 LIDLAGRHRVTLAQATPTLWQAL--VPELSGPALAGIRVLVGGEA-LPAELARRL-GDAGAE-VTNMYGPTETTIWSTSG 789
Cdd:cd17638 81 ILEAIERERITVLPGPPTLFQSLldHPGRKKFDLSSLRAAVTGAAtVPVELVRRMrSELGFEtVLTAYGLTEAGVATMCR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 790 PTSEDSIRRGSIGVPIDNTQVYVLDAnlhpapigvlGELHIAGEGLARGYWNRPGLTAEKFLPDPFgppgtrmYRTGDLV 869
Cdd:cd17638 161 PGDDAETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGW-------LHTGDVG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 870 RWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAV-VREDRPGDLRlVAYVI--PDGPVAPDALRTELS 946
Cdd:cd17638 224 ELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIgVPDERMGEVG-KAFVVarPGVTLTEEDVIAWCR 302
|
330 340
....*....|....*....|....*.
gi 653678460 947 RTLPDYMIPAVIVPVPDFPTTPNGKL 972
Cdd:cd17638 303 ERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
514-904 |
3.13e-16 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 84.95 E-value: 3.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 514 DTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARPVLVV 593
Cdd:PRK04319 71 KEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 594 TDAATADRLGPDDITGL--VVL---EETDTGGY-----------PATEPPAVPAGHSAYVIYTSGSTGRPKGVV------ 651
Cdd:PRK04319 151 TTPALLERKPADDLPSLkhVLLvgeDVEEGPGTldfnalmeqasDEFDIEWTDREDGAILHYTSGSTGKPKGVLhvhnam 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 652 ----IT-RAALDnflaamaerfpLTAEDRVLAT------TTVSFDIAGlelylPLRSGAGVVLADADTarNPAALIDLAG 720
Cdd:PRK04319 231 lqhyQTgKYVLD-----------LHEDDVYWCTadpgwvTGTSYGIFA-----PWLNGATNVIDGGRF--SPERWYRILE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 721 RHRVTLAQATPTLWQALV---PEL-SGPALAGIR-VLVGGEALPAELARrlgdAGAEVTNMygPTETTIWST-SG----- 789
Cdd:PRK04319 293 DYKVTVWYTAPTAIRMLMgagDDLvKKYDLSSLRhILSVGEPLNPEVVR----WGMKVFGL--PIHDNWWMTeTGgimia 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 790 --PTSEdsIRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAgEG---LARGYWNRPGLTAEKFLPDpfgppgtrMYR 864
Cdd:PRK04319 367 nyPAMD--IKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIK-KGwpsMMRGIWNNPEKYESYFAGD--------WYV 435
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 653678460 865 TGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLI 904
Cdd:PRK04319 436 SGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLM 475
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1555-1998 |
3.42e-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: 341236 [Multi-domain] Cd Length: 457 Bit Score: 84.05 E-value: 3.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1555 RSLTFAGLDAQANRLAHALHtgalgAPPVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMARLTRIADTVTP 1634
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLT-----AYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1635 alvltrtgqggclpgaEVFGDVPVvaldrvADRLTAMpdqrpevtvdprglaysIFTSGSTGQPKGVAVEHIGIVRYLSW 1714
Cdd:cd05910 76 ----------------DAFIGIPK------ADEPAAI-----------------LFTSGSTGTPKGVVYRHGTFAAQIDA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1715 AAASYPTAGRRGTLAhssvGFDLTmsALFEPLVsgrGVT--------LMPADATLADLAEELSgPLAYDYIRLTPSHLRH 1786
Cdd:cd05910 117 LRQLYGIRPGEVDLA----TFPLF--ALFGPAL---GLTsvipdmdpTRPARADPQKLVGAIR-QYGVSIVFGSPALLER 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1787 LVGHWTGQELP-PAARGWVVGGETLDPALVKQLLE-LRPDAEVINHYGPTETVigrvvhPVREAGE---LAVDSPLP--- 1858
Cdd:cd05910 187 VARYCAQHGITlPSLRRVLSAGAPVPIALAARLRKmLSDEAEILTPYGATEAL------PVSSIGSrelLATTTAATsgg 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1859 ----LGRPLGETRLQVLDA-------WLEA--VPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPAGEpgaRMYRTGD 1925
Cdd:cd05910 261 agtcVGRPIPGVRVRIIEIddepiaeWDDTleLPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNSEG---FWHRMGD 337
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 653678460 1926 LVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGveqavvlVRDQQLVGWFIPAEDHPPVTVSALR 1998
Cdd:cd05910 338 LGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPG-------VRRSALVGVGKPGCQLPVLCVEPLP 403
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
1530-2028 |
4.42e-16 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 84.09 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1530 DRTVHQLVEAQADRTPGWTAL--RTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVL 1607
Cdd:PRK08315 15 EQTIGQLLDRTAARYPDREALvyRDQGLRWTYREFNEEVDALAKGLL--ALG---IEKGDRVGIWAPNVPEWVLTQFATA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1608 KAGGYFIPVDPGYPMARLTRIADTV-TPALVLTR-------------------TGQGGCLPGAEV--------FGDVPVV 1659
Cdd:PRK08315 90 KIGAILVTINPAYRLSELEYALNQSgCKALIAADgfkdsdyvamlyelapelaTCEPGQLQSARLpelrrvifLGDEKHP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1660 ALDRVADrLTAMPDQRPEVTVDPRGLAYSI-------FTSGSTGQPKGVAVEHIGIVR--YLSWAAASYpTAGRR----- 1725
Cdd:PRK08315 170 GMLNFDE-LLALGRAVDDAELAARQATLDPddpiniqYTSGTTGFPKGATLTHRNILNngYFIGEAMKL-TEEDRlcipv 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1726 ----------GTLAHSSVGfdLTM---SALFEPLvsgrgvtlmpadATLADLAEE---------------LSGPL--AYD 1775
Cdd:PRK08315 248 plyhcfgmvlGNLACVTHG--ATMvypGEGFDPL------------ATLAAVEEErctalygvptmfiaeLDHPDfaRFD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1776 YirltpSHLRhlvghwTGqelppaargwVVGGETLDPALVKQLLELRPDAEVINHYGPTETvigrvvHPVreAGELAVDS 1855
Cdd:PRK08315 314 L-----SSLR------TG----------IMAGSPCPIEVMKRVIDKMHMSEVTIAYGMTET------SPV--STQTRTDD 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1856 PLPL-----GRPLGETRLQVLDAWL-EAVPVGAVGELFIGGDGIARGYLGRPALTAEKFlpDPAGepgarMYRTGDLVRW 1929
Cdd:PRK08315 365 PLEKrvttvGRALPHLEVKIVDPETgETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAI--DADG-----WMHTGDLAVM 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1930 RGDGLLDFVGRVDDQVkLRG----Y-RielgEIEARMAEHPGVEQA-VVLVRDQ----QLVGWFIPAEDHPpVTVSALRR 1999
Cdd:PRK08315 438 DEEGYVNIVGRIKDMI-IRGgeniYpR----EIEEFLYTHPKIQDVqVVGVPDEkygeEVCAWIILRPGAT-LTEEDVRD 511
|
570 580
....*....|....*....|....*....
gi 653678460 2000 FCAEQLPEFMVPNQWVALDAFPLTPHGKV 2028
Cdd:PRK08315 512 FCRGKIAHYKIPRYIRFVDEFPMTVTGKI 540
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
499-950 |
5.38e-16 |
|
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: 84.02 E-value: 5.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 499 QWCRRTPGAVAVIEGD-----TTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDP 573
Cdd:cd05921 3 HWARQAPDRTWLAEREgnggwRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 574 DFPV-----ERIAYLLSDARPVLVVTDAATA-----DRLGPDDITGLVV---LEETDTGGYP---ATEP-PAVPAGHS-- 634
Cdd:cd05921 83 AYSLmsqdlAKLKHLFELLKPGLVFAQDAAPfaralAAIFPLGTPLVVSrnaVAGRGAISFAelaATPPtAAVDAAFAav 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 635 -----AYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDrvlatTTVSFDIAGLELYLPLRSGAGVVLADADTa 709
Cdd:cd05921 163 gpdtvAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEE-----PPVLVDWLPWNHTFGGNHNFNLVLYNGGT- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 710 rnpaALID----LAGRHRVTLA---QATPTL-------WQALVPELSG-PAL-----AGIRVLV-GGEALPAELARRLGD 768
Cdd:cd05921 237 ----LYIDdgkpMPGGFEETLRnlrEISPTVyfnvpagWEMLVAALEKdEALrrrffKRLKLMFyAGAGLSQDVWDRLQA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 769 -AGAEV------TNMYGPTET--TIWSTSGPTSedsiRRGSIGVPIDNTQVYVldanlhpAPIGVLGELHIAGEGLARGY 839
Cdd:cd05921 313 lAVATVgeripmMAGLGATETapTATFTHWPTE----RSGLIGLPAPGTELKL-------VPSGGKYEVRVKGPNVTPGY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 840 WNRPGLTAEKFLPDPFgppgtrmYRTGDLVRWSAAGD----LEYLGRTDHQVKLR-GFRIELGEIETTLINA-GPVRRAA 913
Cdd:cd05921 382 WRQPELTAQAFDEEGF-------YCLGDAAKLADPDDpakgLVFDGRVAEDFKLAsGTWVSVGPLRARAVAAcAPLVHDA 454
|
490 500 510
....*....|....*....|....*....|....*..
gi 653678460 914 AVVREDRPGdlrLVAYVIPDgpvaPDALRtELSRTLP 950
Cdd:cd05921 455 VVAGEDRAE---VGALVFPD----LLACR-RLVGLQE 483
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
501-977 |
6.02e-16 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 84.63 E-value: 6.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 501 CRRTPGAVAVIEGDTT-LSYRELDERANRLARLLmERGAGAETFVAVLLPRSADLLVTLLAVIKAGaaYLPIDPDFPVEr 579
Cdd:PRK06814 642 KIHGFKKLAVEDPVNGpLTYRKLLTGAFVLGRKL-KKNTPPGENVGVMLPNANGAAVTFFALQSAG--RVPAMINFSAG- 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 580 IAYLLSDARPV---LVVTDAA--TADRLGPDdITGL------VVLEETD-------------TGGYPATEPPAVPAGHSA 635
Cdd:PRK06814 718 IANILSACKAAqvkTVLTSRAfiEKARLGPL-IEALefgiriIYLEDVRaqigladkikgllAGRFPLVYFCNRDPDDPA 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 636 YVIYTSGSTGRPKGVVITRAaldNFLAAMAE---RFPLTAEDRVLATTTV--SFDIAGlELYLPLRSGAGVVLAdadtar 710
Cdd:PRK06814 797 VILFTSGSEGTPKGVVLSHR---NLLANRAQvaaRIDFSPEDKVFNALPVfhSFGLTG-GLVLPLLSGVKVFLY------ 866
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 711 nPAALidlagRHRV----------TLAQATPTLwqalvpeLSGPA-------LAGIR-VLVGGEALPAElARRL--GDAG 770
Cdd:PRK06814 867 -PSPL-----HYRIipeliydtnaTILFGTDTF-------LNGYAryahpydFRSLRyVFAGAEKVKEE-TRQTwmEKFG 932
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 771 AEVTNMYGPTETT-IWSTSGPTSEdsiRRGSIG--VPIdntqvyvLDANLHPAP-IGVLGELHIAGEGLARGYwnrpgLT 846
Cdd:PRK06814 933 IRILEGYGVTETApVIALNTPMHN---KAGTVGrlLPG-------IEYRLEPVPgIDEGGRLFVRGPNVMLGY-----LR 997
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 847 AEKflPDPFGPPGTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVRED-RPGDlR 925
Cdd:PRK06814 998 AEN--PGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDaRKGE-R 1074
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 653678460 926 LVAYVipdgpVAPDALRTEL-----SRTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:PRK06814 1075 IILLT-----TASDATRAAFlahakAAGASELMVPAEIITIDEIPLLGTGKIDYVAV 1126
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
516-976 |
1.21e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 83.07 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 516 TLSYRELDERANRLARLLMERGAGAETfVAVLLPRSADLLVTLLAVIKAG--AAYLPIdPDFPV--ERIAYLLSDARPVL 591
Cdd:PRK05850 35 TLTWSQLYRRTLNVAEELRRHGSTGDR-AVILAPQGLEYIVAFLGALQAGliAVPLSV-PQGGAhdERVSAVLRDTSPSV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 592 VVTDAATADRLG------PDDITGLVVleETDTGGYPA-TEPPAVPAGHS--AYVIYTSGSTGRPKGVVIT-RAALDNFL 661
Cdd:PRK05850 113 VLTTSAVVDDVTeyvapqPGQSAPPVI--EVDLLDLDSpRGSDARPRDLPstAYLQYTSGSTRTPAGVMVShRNVIANFE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 662 AAMAERFPLTAEDRVLATTTVSFdiagLELY----------LPLRSGAGVVLADADT------------ARNPAAL---- 715
Cdd:PRK05850 191 QLMSDYFGDTGGVPPPDTTVVSW----LPFYhdmglvlgvcAPILGGCPAVLTSPVAflqrparwmqllASNPHAFsaap 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 716 ---IDLAGRhRVTLAqatptlwqalvpELSGPALAGIRVLV-GGEAL-PAELAR------RLGDAGAEVTNMYGPTETTI 784
Cdd:PRK05850 267 nfaFELAVR-KTSDD------------DMAGLDLGGVLGIIsGSERVhPATLKRfadrfaPFNLRETAIRPSYGLAEATV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 785 WSTSGPTSE---------DSIRRG--------------SIGVPiDNTQVYVLDANLH-PAPIGVLGELHIAGEGLARGYW 840
Cdd:PRK05850 334 YVATREPGQppesvrfdyEKLSAGhakrcetgggtplvSYGSP-RSPTVRIVDPDTCiECPAGTVGEIWVHGDNVAAGYW 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 841 NRPGLTAEKF---LPDPfgPPGTRM---YRTGDLVRWSaAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAA 914
Cdd:PRK05850 413 QKPEETERTFgatLVDP--SPGTPEgpwLRTGDLGFIS-EGELFIVGRIKDLLIVDGRNHYPDDIEATIQEITGGRVAAI 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 653678460 915 VVREDRPGDLRLVAYVIPDGPVAPDALR----------TELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAA 976
Cdd:PRK05850 490 SVPDDGTEKLVAIIELKKRGDSDEEAMDrlrtvkrevtSAISKSHGLSVADLVLVAPGSIPITTSGKIRRAA 561
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
1681-1984 |
1.90e-15 |
|
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: 81.64 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1681 DPRGLAYSIFTSGSTGQPKGVAVEHIGIVRYLSWAAASYPTagrrgtlahsSVGfDLTMSAL---------FEPLVSGRG 1751
Cdd:cd17640 86 DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPP----------QPG-DRFLSILpiwhsyersAEYFIFACG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1752 VTLMPAD--ATLADLAEE-----LSGPLAYDYIRL-------TPSHLRHLVGHW--TGQELPPAargwVVGGETLDPALV 1815
Cdd:cd17640 155 CSQAYTSirTLKDDLKRVkphyiVSVPRLWESLYSgiqkqvsKSSPIKQFLFLFflSGGIFKFG----ISGGGALPPHVD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1816 KQLLELrpDAEVINHYGPTET----VIGRVVHPVREAgelavdsplpLGRPLGETRLQVLDAWLEAV-PVGAVGELFIGG 1890
Cdd:cd17640 231 TFFEAI--GIEVLNGYGLTETspvvSARRLKCNVRGS----------VGRPLPGTEIKIVDPEGNVVlPPGEKGIVWVRG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1891 DGIARGYLGRPALTAEKFLPDPagepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLR-GYRIELGEIEARMAEHPGVEQ 1969
Cdd:cd17640 299 PQVMKGYYKNPEATSKVLDSDG-------WFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQ 371
|
330
....*....|....*
gi 653678460 1970 AVVLVRDQQLVGWFI 1984
Cdd:cd17640 372 IMVVGQDQKRLGALI 386
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
1541-2046 |
2.24e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 82.01 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1541 ADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVD--- 1617
Cdd:PRK07470 17 ARRFPDRIALVWGDRSWTWREIDARVDALAAALA--ARG---VRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNfrq 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1618 -PGyPMARLTR-------IADTVTP----ALVLTRTGQGGCLPGAEVFGDVPVVALdrVADRLTAMPdqrPEVTVDPRGL 1685
Cdd:PRK07470 92 tPD-EVAYLAEasgaramICHADFPehaaAVRAASPDLTHVVAIGGARAGLDYEAL--VARHLGARV---ANAAVDHDDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1686 AYSIFTSGSTGQPKGvAVehigivrylswaaasyptagrrgtLAHSSVGF-------DLT-------MSALFEPLVSGRG 1751
Cdd:PRK07470 166 CWFFFTSGTTGRPKA-AV------------------------LTHGQMAFvitnhlaDLMpgtteqdASLVVAPLSHGAG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1752 VTLM----PADATLADLAEELSGPLAYDYI---RLT-----PSHLRHLVGHwtgqelpPAA--------RGWVVGGETLD 1811
Cdd:PRK07470 221 IHQLcqvaRGAATVLLPSERFDPAEVWALVerhRVTnlftvPTILKMLVEH-------PAVdrydhsslRYVIYAGAPMY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1812 PAlvKQLLELRPDAEVI-NHYGPTE-----TVIGRVVHPVREAGELAVDSplpLGRPLGETRLQVLDAWLEAVPVGAVGE 1885
Cdd:PRK07470 294 RA--DQKRALAKLGKVLvQYFGLGEvtgniTVLPPALHDAEDGPDARIGT---CGFERTGMEVQIQDDEGRELPPGETGE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1886 LFIGGDGIARGYLGRPALTAEKFLPDpagepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHP 1965
Cdd:PRK07470 369 ICVIGPAVFAGYYNNPEANAKAFRDG--------WFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHP 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1966 GV-EQAVVLVRDQQL--VGW-FIPAEDHPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRALpgptsgRP 2041
Cdd:PRK07470 441 AVsEVAVLGVPDPVWgeVGVaVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV------RE 514
|
....*
gi 653678460 2042 ELEDR 2046
Cdd:PRK07470 515 ELEER 519
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
1534-2035 |
2.53e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 81.58 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1534 HQLVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAhalhtGALGAPPVGPETPVLLLLDRSPELVVAMLAVLKAGGYF 1613
Cdd:PRK13383 38 YTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLA-----RRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1614 IPVDPGYPmarltriADTVTPALvltRTGQGGCLPGAEVFGDVPVVALDRVA--DRLTAMPDQ---RPEVTVDPRGLays 1688
Cdd:PRK13383 113 VPISTEFR-------SDALAAAL---RAHHISTVVADNEFAERIAGADDAVAviDPATAGAEEsggRPAVAAPGRIV--- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1689 IFTSGSTGQPKGVAVE---HIGIVRYLSWAAASYPTAGRRGTLA---HSSVGFDLTMsalfepLVSGRGVTLMP-----A 1757
Cdd:PRK13383 180 LLTSGTTGKPKGVPRApqlRSAVGVWVTILDRTRLRTGSRISVAmpmFHGLGLGMLM------LTIALGGTVLThrhfdA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1758 DATLADL----AEELSG-PLAYDYIRLTPSHLRhlvghwtGQELPPAARGWVVGGETLDPALVKQLLELRPDAeVINHYG 1832
Cdd:PRK13383 254 EAALAQAslhrADAFTAvPVVLARILELPPRVR-------ARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDI-LYNGYG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1833 PTETVIGRVVHPvreaGELAvDSPLPLGRPLGETRLQVLDAwlEAVPVG--AVGELFIGGDGIARGYLGrpalTAEKFLP 1910
Cdd:PRK13383 326 STEVGIGALATP----ADLR-DAPETVGKPVAGCPVRILDR--NNRPVGprVTGRIFVGGELAGTRYTD----GGGKAVV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1911 DPagepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGV-EQAVVLVRDQQL---VGWFIPA 1986
Cdd:PRK13383 395 DG-------MTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVaDNAVIGVPDERFghrLAAFVVL 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 653678460 1987 EDHPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRALPG 2035
Cdd:PRK13383 468 HPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELPG 516
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
1539-2036 |
2.78e-15 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 81.73 E-value: 2.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1539 AQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHTGALGAPPVgpetpVLLLLDRSPELVVAMLAVLKAGGYFIPVDP 1618
Cdd:PRK13382 51 IAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRV-----VGIMCRNHRGFVEALLAANRIGADILLLNT 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1619 GYPMARLtriadtvtpALVLTRTGQGGCLPGAEVFGDVPVVALDRV-ADRLTAMPDQRPEVTVD--------------PR 1683
Cdd:PRK13382 126 SFAGPAL---------AEVVTREGVDTVIYDEEFSATVDRALADCPqATRIVAWTDEDHDLTVEvliaahagqrpeptGR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1684 GLAYSIFTSGSTGQPKGVAVEHIG-------IVRYLSWAA--ASYPTAGRRGTLAHSSVGFDLTMSAlfePLVSGRGVTl 1754
Cdd:PRK13382 197 KGRVILLTSGTTGTPKGARRSGPGgigtlkaILDRTPWRAeePTVIVAPMFHAWGFSQLVLAASLAC---TIVTRRRFD- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1755 mpADATLADLAEELSGPLAydyirLTPSHLRHLVghwtgqELPPAARGWVVG---------GETLDPALVKQLLELRPDA 1825
Cdd:PRK13382 273 --PEATLDLIDRHRATGLA-----VVPVMFDRIM------DLPAEVRNRYSGrslrfaaasGSRMRPDVVIAFMDQFGDV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1826 eVINHYGPTEtvigrvvhpvreAGELAVDSPLPL-------GRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYl 1898
Cdd:PRK13382 340 -IYNNYNATE------------AGMIATATPADLraapdtaGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY- 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1899 grpaltaekfLPDPAGEPGARMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVL-VRD- 1976
Cdd:PRK13382 406 ----------TSGSTKDFHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIgVDDe 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 653678460 1977 ---QQLVGWFIPAEDhPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRALPGP 2036
Cdd:PRK13382 476 qygQRLAAFVVLKPG-ASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
501-974 |
2.96e-15 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 81.77 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 501 CRRTpgAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERI 580
Cdd:PLN02860 19 LRGN--AVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 581 AYLLSDARPVLVVTDAAT---ADRLGPDDITGL---VVLEETDTGGYPA-----------------TEPPAVPAGHSAYV 637
Cdd:PLN02860 97 KSAMLLVRPVMLVTDETCsswYEELQNDRLPSLmwqVFLESPSSSVFIFlnsflttemlkqralgtTELDYAWAPDDAVL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 638 I-YTSGSTGRPKGVVITRAAL-DNFLAAMAerFPLTAEDRVLATTTVSFDIAGLELYLP-LRSGAGVVLA---DADTArn 711
Cdd:PLN02860 177 IcFTSGTTGRPKGVTISHSALiVQSLAKIA--IVGYGEDDVYLHTAPLCHIGGLSSALAmLMVGACHVLLpkfDAKAA-- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 712 paalIDLAGRHRVTLAQATPTLWQALVP----ELSGPALAGIR-VLVGGEALPAEL--ARRLGDAGAEVTNMYGPTET-- 782
Cdd:PLN02860 253 ----LQAIKQHNVTSMITVPAMMADLISltrkSMTWKVFPSVRkILNGGGSLSSRLlpDAKKLFPNAKLFSAYGMTEAcs 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 783 --TIWSTSGPTSEDSIRRGSIGVPIDNTQVYVLDANL--HPAP-----IGVLGELHIaGEGLARG------YWNRPGLTA 847
Cdd:PLN02860 329 slTFMTLHDPTLESPKQTLQTVNQTKSSSVHQPQGVCvgKPAPhvelkIGLDESSRV-GRILTRGphvmlgYWGQNSETA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 848 EKFLPDPFgppgtrmYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAV-VREDRPGDLrL 926
Cdd:PLN02860 408 SVLSNDGW-------LDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVgVPDSRLTEM-V 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 653678460 927 VAYV-IPDG---------------PVAPDALRTELS-RTLPDYMIPAVIVPVPD-FPTTPNGKLDR 974
Cdd:PLN02860 480 VACVrLRDGwiwsdnekenakknlTLSSETLRHHCReKNLSRFKIPKLFVQWRKpFPLTTTGKIRR 545
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
636-973 |
3.21e-15 |
|
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: 79.73 E-value: 3.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 636 YVIYTSGSTGRPKGVV-----ITRAALDNFLAAMAERFP--LTAEDRVLATTTVSFDIAglelylPLRSGAGVVLADADT 708
Cdd:cd05924 7 YILYTGGTTGMPKGVMwrqedIFRMLMGGADFGTGEFTPseDAHKAAAAAAGTVMFPAP------PLMHGTGSWTAFGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 709 AR-----------NPAALIDLAGRHRVTL------AQATPtlwqaLVPELSGPA---LAGIRVLV-GGEALPAELARRLG 767
Cdd:cd05924 81 LGgqtvvlpddrfDPEEVWRTIEKHKVTSmtivgdAMARP-----LIDALRDAGpydLSSLFAISsGGALLSPEVKQGLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 768 DA--GAEVTNMYGPTETTIWSTSGPTSEDSIRRGSIGVpidNTQVYVLDANLHPAPIGVLGELHIAGEGL-ARGYWNRPG 844
Cdd:cd05924 156 ELvpNITLVDAFGSSETGFTGSGHSAGSGPETGPFTRA---NPDTVVLDDDGRVVPPGSGGVGWIARRGHiPLGYYGDEA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 845 LTAEKFlpdpFGPPGTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDL 924
Cdd:cd05924 233 KTAETF----PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQ 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 653678460 925 RLVAYVIPDGPVAPD--ALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLD 973
Cdd:cd05924 309 EVVAVVQLREGAGVDleELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
1656-2033 |
3.96e-15 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 79.70 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1656 VPVVALDRV-ADRLTAmpDQRPEVTVDPrGLAYSIFTSGSTGQPKGVAVEHIGIVrylSWAAASYPTAGRRGTL-----A 1729
Cdd:PRK07824 10 LPVPAQDERrAALLRD--ALRVGEPIDD-DVALVVATSGTTGTPKGAMLTAAALT---ASADATHDRLGGPGQWllalpA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1730 HSSVGFDLTMSALF---EPLVSGRGVTLMPADatLADLAEELSGPLAYdyIRLTPSHLRHLVGHWTGQELPPAARGWVVG 1806
Cdd:PRK07824 84 HHIAGLQVLVRSVIagsEPVELDVSAGFDPTA--LPRAVAELGGGRRY--TSLVPMQLAKALDDPAATAALAELDAVLVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1807 GETLDPALVKQLLELRpdAEVINHYGPTETVIGRVVHpvreagelavdsplplGRPLGETRLQVLDawleavpvgavGEL 1886
Cdd:PRK07824 160 GGPAPAPVLDAAAAAG--INVVRTYGMSETSGGCVYD----------------GVPLDGVRVRVED-----------GRI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1887 FIGGDGIARGYLGRPAltaekflPDPAGEPGarMYRTGDLVRWrGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPG 1966
Cdd:PRK07824 211 ALGGPTLAKGYRNPVD-------PDPFAEPG--WFRTDDLGAL-DDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPA 280
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 653678460 1967 VEQAVVL-VRDQQL---VGWFIPAEDHPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:PRK07824 281 VADCAVFgLPDDRLgqrVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
1555-2033 |
4.55e-15 |
|
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: 81.21 E-value: 4.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1555 RSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMARL-TRIADtVT 1633
Cdd:cd05967 81 RTYTYAELLDEVSRLAGVLR--KLG---VVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELaSRIDD-AK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1634 PALVLTrtGQGGCLPGAEV------------------------FGDVPVVALDRVAD------RLTAMPdqRPEVTVDPR 1683
Cdd:cd05967 155 PKLIVT--ASCGIEPGKVVpykplldkalelsghkphhvlvlnRPQVPADLTKPGRDldwselLAKAEP--VDCVPVAAT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1684 GLAYSIFTSGSTGQPKGVAVEHIGIVRYLSWAAASYPTAGRRGTL-AHSSVGFDLTMSAL-FEPLVSGrGVTLM------ 1755
Cdd:cd05967 231 DPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWwAASDVGWVVGHSYIvYGPLLHG-ATTVLyegkpv 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1756 --PADATLADLAEE------LSGPLAYDYIRLTPSHLRHLVGHWTGqelppAARGWVVGGETLDPAlVKQLLELRPDAEV 1827
Cdd:cd05967 310 gtPDPGAFWRVIEKyqvnalFTAPTAIRAIRKEDPDGKYIKKYDLS-----SLRTLFLAGERLDPP-TLEWAENTLGVPV 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1828 INHYGPTET-------VIGRVVHPVReAGelavdSPlplGRPLGETRLQVLDAWLEAVPVGAVGELFIGGD---GIARGY 1897
Cdd:cd05967 384 IDHWWQTETgwpitanPVGLEPLPIK-AG-----SP---GKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPlppGCLLTL 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1898 LGRPALTAEKFLPDPAGepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGV-EQAVVLVRD 1976
Cdd:cd05967 455 WKNDERFKKLYLSKFPG-----YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVaECAVVGVRD 529
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 653678460 1977 ----QQLVGWFIPAEDHPPVT---VSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:cd05967 530 elkgQVPLGLVVLKEGVKITAeelEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTL 593
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
517-921 |
4.90e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 81.25 E-value: 4.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 517 LSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPV-----ERIAYLLSDARPVL 591
Cdd:PRK12582 81 VTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSLmshdhAKLKHLFDLVKPRV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 592 V-VTDAATADR----LGPDDITGLVVLEETD-TGGYP----ATEPP--AVPAGHS-------AYVIYTSGSTGRPKGVVI 652
Cdd:PRK12582 161 VfAQSGAPFARalaaLDLLDVTVVHVTGPGEgIASIAfadlAATPPtaAVAAAIAaitpdtvAKYLFTSGSTGMPKAVIN 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 653 TRAALDNFLAAMAERFPLTAEDRVlattTVSFD-------IAGLELYLPLRSGAGVVLAD---------ADTARNpaaLI 716
Cdd:PRK12582 241 TQRMMCANIAMQEQLRPREPDPPP----PVSLDwmpwnhtMGGNANFNGLLWGGGTLYIDdgkplpgmfEETIRN---LR 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 717 DLAGrhrvTLAQATPTLWQALVPEL-SGPALA-----GIRVL-VGGEALPAELARRLGD-AGAE------VTNMYGPTET 782
Cdd:PRK12582 314 EISP----TVYGNVPAGYAMLAEAMeKDDALRrsffkNLRLMaYGGATLSDDLYERMQAlAVRTtghripFYTGYGATET 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 783 TiwSTSGPTSEDSIRRGSIGVPIDNTQVYVldanlhpAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgppgtrm 862
Cdd:PRK12582 390 A--PTTTGTHWDTERVGLIGLPLPGVELKL-------APVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF------- 453
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 653678460 863 YRTGDLVRWSAAGDLE----YLGRTDHQVKL-RGFRIELGEIETTLINA-GPVRRAAAVVREDRP 921
Cdd:PRK12582 454 YRLGDAARFVDPDDPEkgliFDGRVAEDFKLsTGTWVSVGTLRPDAVAAcSPVIHDAVVAGQDRA 518
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
1533-2033 |
8.31e-15 |
|
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: 80.23 E-value: 8.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1533 VHQLVEAQADRTPGWTALR-----TGDRSLTFAGLDAQANRLAhalhtGALGAPPVGPETPVLLLLDRSPELVVAMLAVL 1607
Cdd:cd05968 63 VEQLLDKWLADTRTRPALRwegedGTSRTLTYGELLYEVKRLA-----NGLRALGVGKGDRVGIYLPMIPEIVPAFLAVA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1608 KAGGYFIPVDPGY-PMARLTRIADTVTPALV-------------LTRTGQGGCLPGAEV----------FGDVPVVALDR 1663
Cdd:cd05968 138 RIGGIVVPIFSGFgKEAAATRLQDAEAKALItadgftrrgrevnLKEEADKACAQCPTVekvvvvrhlgNDFTPAKGRDL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1664 VADRLTAMPDQRPEVT--VDPRGLaysIFTSGSTGQPKGVAVEHIGIVryLSWAA-ASYPTAGRRGTLAH--SSVGFDLT 1738
Cdd:cd05968 218 SYDEEKETAGDGAERTesEDPLMI---IYTSGTTGKPKGTVHVHAGFP--LKAAQdMYFQFDLKPGDLLTwfTDLGWMMG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1739 MSALFEPLVSGRGVTL------MPADATLADLAEELSgplaYDYIRLTPSHLRHLVGH---WTGQELPPAARGWVVGGET 1809
Cdd:cd05968 293 PWLIFGGLILGATMVLydgapdHPKADRLWRMVEDHE----ITHLGLSPTLIRALKPRgdaPVNAHDLSSLRVLGSTGEP 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1810 LDPALVKQLLELRPDAE--VINHYGPTET---VIGRVvhPVREAGELAVDSPLPlgrplgETRLQVLDAwlEAVPV-GAV 1883
Cdd:cd05968 369 WNPEPWNWLFETVGKGRnpIINYSGGTEIsggILGNV--LIKPIKPSSFNGPVP------GMKADVLDE--SGKPArPEV 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1884 GELFIGGD--GIARGYLGRPALTAEKFLPDPAGepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARM 1961
Cdd:cd05968 439 GELVLLAPwpGMTRGFWRDEDRYLETYWSRFDN-----VWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVL 513
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 653678460 1962 AEHPGVEQAVVL-----VRDQQLVGWFIPAEDHPPVTVSA--LRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:cd05968 514 NAHPAVLESAAIgvphpVKGEAIVCFVVLKPGVTPTEALAeeLMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVI 592
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
1084-1406 |
1.05e-14 |
|
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: 79.02 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1084 PLSPMQESIW---LADQvsAGDsVYNVPLALRLigpLDRGALRR---TLNRVVDRHEMLRTRIHpgPDGM--PVQV---- 1151
Cdd:cd19544 3 PLAPLQEGILfhhLLAE--EGD-PYLLRSLLAF---DSRARLDAflaALQQVIDRHDILRTAIL--WEGLsePVQVvwrq 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1152 ---------ADPAGGGAALTERDAAPGtdlaqlllaeaalGFTLATEHP--LRAVLWRlDER--EHVLLLTAHHVAVDAW 1218
Cdd:cd19544 75 aelpveeltLDPGDDALAQLRARFDPR-------------RYRLDLRQAplLRAHVAE-DPAngRWLLLLLFHHLISDHT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1219 SMDLIQRDLTELYAAdtghREPELDEPAL-----AQAdyavwqRQSAQRGRYAAeldFWRTELtgavatevaGDLPRPAT 1293
Cdd:cd19544 141 SLELLLEEIQAILAG----RAAALPPPVPyrnfvAQA------RLGASQAEHEA---FFREML---------GDVDEPTA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1294 P---------GGGGGAVEFALAPRQIQGIRELARRCGTTVSTV-------VLSALqtllyriTGGADVVIGSTVSGR--G 1355
Cdd:cd19544 199 PfglldvqgdGSDITEARLALDAELAQRLRAQARRLGVSPASLfhlawalVLARC-------SGRDDVVFGTVLSGRmqG 271
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 653678460 1356 NPRLDNLVGCLVNTVVLRGDLSGAPTfHELLRRTHARTADALAHqelpfEH 1406
Cdd:cd19544 272 GAGADRALGMFINTLPLRVRLGGRSV-REAVRQTHARLAELLRH-----EH 316
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
514-903 |
1.18e-14 |
|
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: 78.93 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 514 DTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARPVLVV 593
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 594 TDAatadrlgpdditglvvleetdtggypateppavpaghsAYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAE 673
Cdd:cd05940 81 VDA--------------------------------------ALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPS 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 674 DRvLATTTVSFDIAGLELYLP--LRSGAGVVLADADTARNpaaLIDLAGRHRVTLAQATPTLWQAL--VPELSGPALAGI 749
Cdd:cd05940 123 DV-LYTCLPLYHSTALIVGWSacLASGATLVIRKKFSASN---FWDDIRKYQATIFQYIGELCRYLlnQPPKPTERKHKV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 750 RVLVGGEALPA---ELARRLGDagAEVTNMYGPTETTI--WSTSGptsedsiRRGSIG--------------VPID-NTQ 809
Cdd:cd05940 199 RMIFGNGLRPDiweEFKERFGV--PRIAEFYAATEGNSgfINFFG-------KPGAIGrnpsllrkvaplalVKYDlESG 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 810 VYVLDAN--LHPAPIGVLGEL--HIAGEGLARGYWNrPGLTAEKFLPDPFgPPGTRMYRTGDLVRWSAAGDLEYLGRTDH 885
Cdd:cd05940 270 EPIRDAEgrCIKVPRGEPGLLisRINPLEPFDGYTD-PAATEKKILRDVF-KKGDAWFNTGDLMRLDGEGFWYFVDRLGD 347
|
410
....*....|....*...
gi 653678460 886 QVKLRGFRIELGEIETTL 903
Cdd:cd05940 348 TFRWKGENVSTTEVAAVL 365
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
1679-2033 |
1.19e-14 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 80.35 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1679 TVDPRGLAYSIFTSGSTGQPKGVAVEHIGIVRYLSwAAASYPTAGRRGTLAHS-----SVGFDLTmsaLFEPLVSGRGVT 1753
Cdd:PRK08633 778 TFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIE-QISDVFNLRNDDVILSSlpffhSFGLTVT---LWLPLLEGIKVV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1754 LM--PADA-TLADLAEELSGPL---------AY-DYIRLTP---SHLRhLVghwtgqelppaargwVVGGETLDPAlVKQ 1817
Cdd:PRK08633 854 YHpdPTDAlGIAKLVAKHRATIllgtptflrLYlRNKKLHPlmfASLR-LV---------------VAGAEKLKPE-VAD 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1818 LLELRPDAEVINHYGPTET--VIGRVVHPVREAG--ELAVDSPLPLGRPLGETRLQVLDA-WLEAVPVGAVGELFIGGDG 1892
Cdd:PRK08633 917 AFEEKFGIRILEGYGATETspVASVNLPDVLAADfkRQTGSKEGSVGMPLPGVAVRIVDPeTFEELPPGEDGLILIGGPQ 996
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1893 IARGYLGRPALTAEkFLPDPagePGARMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAE---HPGVEQ 1969
Cdd:PRK08633 997 VMKGYLGDPEKTAE-VIKDI---DGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKalgGEEVVF 1072
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 653678460 1970 AVVLVRD----QQLVGWFIPAEDhppvTVSALRRFCAE-QLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:PRK08633 1073 AVTAVPDekkgEKLVVLHTCGAE----DVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
1860-2033 |
1.36e-14 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 79.26 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1860 GRPL-GETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFlpDPAGepgarMYRTGDLVRWRGDGLLDFV 1938
Cdd:PRK10946 356 GRPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAF--DANG-----FYCSGDLVSIDPDGYITVV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1939 GRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRDQQLVG----WFIPAEDhpPVTVSALRRFCAEQ-LPEFMVPNQ 2013
Cdd:PRK10946 429 GREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGekscAFLVVKE--PLKAVQLRRFLREQgIAEFKLPDR 506
|
170 180
....*....|....*....|
gi 653678460 2014 WVALDAFPLTPHGKVNHRAL 2033
Cdd:PRK10946 507 VECVDSLPLTAVGKVDKKQL 526
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1082-1399 |
1.37e-14 |
|
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: 78.68 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1082 PLPLSPMQESIWL---ADQVSAGDS--VYnvplaLRLIGP-LDRGALRRTLNRVVDRHEMLRTRIHpgPDGMPVQVADPA 1155
Cdd:cd19535 1 PFPLTDVQYAYWIgrqDDQELGGVGchAY-----LEFDGEdLDPDRLERAWNKLIARHPMLRAVFL--DDGTQQILPEVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1156 ggGAALTERDaapgtdlaqlllaeaalgFTLATEHPLRAVLWRLDER-EHVLLLTAH------------------HV--- 1213
Cdd:cd19535 74 --WYGITVHD------------------LRGLSEEEAEAALEELRERlSHRVLDVERgplfdirlsllpegrtrlHLsid 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1214 --AVDAWSMDLIQRDLTELYaadtghREPELDEPALAQ--ADYaVWQRQSAQRGRYAAELDFWRTELTgavatevagDLP 1289
Cdd:cd19535 134 llVADALSLQILLRELAALY------EDPGEPLPPLELsfRDY-LLAEQALRETAYERARAYWQERLP---------TLP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1290 RP-----ATPGGGGGAVEFA-----LAPRQIQGIRELARRCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGR--GNP 1357
Cdd:cd19535 198 PApqlplAKDPEEIKEPRFTrrehrLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRFLLNLTLFNRlpLHP 277
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 653678460 1358 RLDNLVGCLVNTVVLRGDLSGAPTFHELLRRTHARTADALAH 1399
Cdd:cd19535 278 DVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQLWEDLDH 319
|
|
| GrsT |
COG3208 |
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ... |
2159-2309 |
1.78e-14 |
|
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442441 [Multi-domain] Cd Length: 237 Bit Score: 75.27 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 2159 VFCVHPSGGGVAWYLPLARALPAGHPVHAFQPLGMDGR--EAPAETIEDMAAGYLADLRLvQPEGPYVVVGWSLGGTIAF 2236
Cdd:COG3208 9 LFCFPYAGGSASAYRPWAAALPPDIEVLAVQLPGRGDRlgEPPLTSLEELADDLAEELAP-LLDRPFALFGHSMGALLAF 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 653678460 2237 EMARQLDRLG--EPVQLIL---LEPTLPEVARTIDLhrpardsyLRGADLAERILRLpAGDPEGDRLRAELTRLLEDA 2309
Cdd:COG3208 88 ELARRLERRGrpLPAHLFVsgrRAPHLPRRRRPLHD--------LSDAELLAELRRL-GGTPEEVLADPELLELFLPI 156
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
1681-1989 |
2.00e-14 |
|
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: 78.80 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1681 DPRGLAYSIFTSGSTGQPKGVAVEHIGIV------------------RYLSWaaasYPtagrrgtLAHSsvgFDLTmsal 1742
Cdd:cd17639 86 KPDDLACIMYTSGSTGNPKGVMLTHGNLVagiaglgdrvpellgpddRYLAY----LP-------LAHI---FELA---- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1743 FEPLVSGRGV--------TLMpaDATLA----DLAE----ELSG-PLAYDYIRLT--------PSHLRHLVghWTGQELP 1797
Cdd:cd17639 148 AENVCLYRGGtigygsprTLT--DKSKRgckgDLTEfkptLMVGvPAIWDTIRKGvlaklnpmGGLKRTLF--WTAYQSK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1798 PAARGWVVGGETLDP---ALVKQLL--ELR----------PDA---------EVINHYGPTETVIGrvvHPVREAGELAV 1853
Cdd:cd17639 224 LKALKEGPGTPLLDElvfKKVRAALggRLRymlsggaplsADTqeflnivlcPVIQGYGLTETCAG---GTVQDPGDLET 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1854 DSplpLGRPLGETRLQVLDaWLEAvpvGAV-------GELFIGGDGIARGYLGRPALTAEKFLPDpagepgaRMYRTGDL 1926
Cdd:cd17639 301 GR---VGPPLPCCEIKLVD-WEEG---GYStdkppprGEILIRGPNVFKGYYKNPEKTKEAFDGD-------GWFHTGDI 366
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 653678460 1927 VRWRGDGLLDFVGRVDDQVKLR-GYRIELGEIEARMAEHPGVEQAVVLVRDQQ--LVGWFIPAEDH 1989
Cdd:cd17639 367 GEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYADPDKsyPVAIVVPNEKH 432
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
517-942 |
3.00e-14 |
|
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: 78.41 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 517 LSYRELDERANRLARLLMERGA--GAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARPVLVVT 594
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 595 DAatadrlgpdDITgLVVLEETDTGG--YPATEPPAVPAgHSAYVIYTSGSTGRPKGVVITRAALDNFLAAM----AERF 668
Cdd:cd05927 86 DA---------GVK-VYSLEEFEKLGkkNKVPPPPPKPE-DLATICYTSGTTGNPKGVMLTHGNIVSNVAGVfkilEILN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 669 PLTAEDRVLAtttvsfdiaglelYLPL-------------RSGAGV--------VLAD---------------------- 705
Cdd:cd05927 155 KINPTDVYIS-------------YLPLahifervvealflYHGAKIgfysgdirLLLDdikalkptvfpgvprvlnriyd 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 706 ---ADTARNPA---ALIDLAGRHRVTLAQATP----TLWQALVPELSGPALAG-IRVLVGGEA-LPAELARRLGDA-GAE 772
Cdd:cd05927 222 kifNKVQAKGPlkrKLFNFALNYKLAELRSGVvrasPFWDKLVFNKIKQALGGnVRLMLTGSApLSPEVLEFLRVAlGCP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 773 VTNMYGPTETTIWSTSgpTSEDSIRRGSIGVPIDNTQVYVLDA---NLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEK 849
Cdd:cd05927 302 VLEGYGQTECTAGATL--TLPGDTSVGHVGGPLPCAEVKLVDVpemNYDAKDPNPRGEVCIRGPNVFSGYYKDPEKTAEA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 850 FLPDPFgppgtrmYRTGDLVRWSAAGDLEYLGRTDHQVKL-RGFRIELGEIETTLINAGPVrrAAAVVRedrpGD-LR-- 925
Cdd:cd05927 380 LDEDGW-------LHTGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSPFV--AQIFVY----GDsLKsf 446
|
490
....*....|....*..
gi 653678460 926 LVAYVIPDgpvaPDALR 942
Cdd:cd05927 447 LVAIVVPD----PDVLK 459
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
1826-2033 |
4.63e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 77.88 E-value: 4.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1826 EVINHYGPTETVIGRVVHPvREAGELAVdsplpLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTA 1905
Cdd:PRK05677 353 AICEGYGMTETSPVVSVNP-SQAIQVGT-----IGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATD 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1906 EKFlpDPAGepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQ-AVVLVRDQ---QLVG 1981
Cdd:PRK05677 427 EIL--DSDG-----WLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQcAAIGVPDEksgEAIK 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 653678460 1982 WFIPAEDHPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:PRK05677 500 VFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1683-2028 |
5.13e-14 |
|
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: 75.76 E-value: 5.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1683 RGLAYSIFTSGSTGQPKGVAVEH--------IGIVRYLSWAAASYptagrrgTLAHSSVGFDLTMSALFEPLVSGRGVTL 1754
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANktffavpdILQKEGLNWVVGDV-------TYLPLPATHIGGLWWILTCLIHGGLCVT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1755 MPADATLADLAEELSgplAYDY--IRLTPSHLRHLVGHWTGQ-ELPPAARGWVVGGETLDPAlVKQLLELRPDAEVINHY 1831
Cdd:cd17635 74 GGENTTYKSLFKILT---TNAVttTCLVPTLLSKLVSELKSAnATVPSLRLIGYGGSRAIAA-DVRFIEATGLTNTAQVY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1832 GPTETviGRVVHPVREAGELAVDSplpLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPD 1911
Cdd:cd17635 150 GLSET--GTALCLPTDDDSIEINA---VGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1912 pagepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGV-EQAVVLVRDQ---QLVGWFIPA- 1986
Cdd:cd17635 225 --------WVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVqECACYEISDEefgELVGLAVVAs 296
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 653678460 1987 EDHPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKV 2028
Cdd:cd17635 297 AELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKV 338
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
514-977 |
5.85e-14 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 77.08 E-value: 5.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 514 DTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARPVLVV 593
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 594 TDAATAdrlgpdditglvvLEETDTggypaTEPPAVPAG--HSAYV-IYTSGSTGRPKGVVITRAALDNFLAAMAERFPL 670
Cdd:cd05939 81 FNLLDP-------------LLTQSS-----TEPPSQDDVnfRDKLFyIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 671 TAEDRVLATTTVSFDIAG-LELYLPLRSGAGVVLADADTARNpaaLIDLAGRHRVTLAQATPTLWQALVPELSGPALAGI 749
Cdd:cd05939 143 RPEDVVYDCLPLYHSAGGiMGVGQALLHGSTVVIRKKFSASN---FWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 750 RV-LVGGEALPAEL----ARRLGDagAEVTNMYGPTEttiwSTSGPTSEDSiRRGSIG-VPIDNTQVY------------ 811
Cdd:cd05939 220 NVrLAVGNGLRPQIweqfVRRFGI--PQIGEFYGATE----GNSSLVNIDN-HVGACGfNSRILPSVYpirlikvdedtg 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 812 --VLDANLH-----PAPIGVLGELHIAGEGLAR--GYWNRpGLTAEKFLPDPFgPPGTRMYRTGDLVRWSAAGDLEYLGR 882
Cdd:cd05939 293 elIRDSDGLcipcqPGEPGLLVGKIIQNDPLRRfdGYVNE-GATNKKIARDVF-KKGDSAFLSGDVLVMDELGYLYFKDR 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 883 TDHQVKLRGFRIELGEIETTLINAgpVRRAAAVV-------REDRPGdlrLVAYVIPDGPVAPDALRTELSRTLPDYMIP 955
Cdd:cd05939 371 TGDTFRWKGENVSTTEVEGILSNV--LGLEDVVVygvevpgVEGRAG---MAAIVDPERKVDLDRFSAVLAKSLPPYARP 445
|
490 500
....*....|....*....|..
gi 653678460 956 AVIVPVPDFPTTPNGKLDRAAL 977
Cdd:cd05939 446 QFIRLLPEVDKTGTFKLQKTDL 467
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
512-977 |
6.29e-14 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 77.52 E-value: 6.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 512 EGDTTLSYRELDERANRLARLLMER-GAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARPV 590
Cdd:PRK05620 34 AEQEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 591 LVVTDAATADRLGPdditglvVLEETDT-------GGYPATEP--------------------------PAVPAGHSAYV 637
Cdd:PRK05620 114 VIVADPRLAEQLGE-------ILKECPCvravvfiGPSDADSAaahmpegikvysyealldgrstvydwPELDETTAAAI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 638 IYTSGSTGRPKGVVITRAALdnFLAAMAerfpLTAEDRVLATTTVSFdIAGLELY------LPL---RSGAGVVLADADT 708
Cdd:PRK05620 187 CYSTGTTGAPKGVVYSHRSL--YLQSLS----LRTTDSLAVTHGESF-LCCVPIYhvlswgVPLaafMSGTPLVFPGPDL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 709 ARNPAALIDLAGRHRVtlAQATPTLW-QALVPELSGPA--LAGIRVLVGGEALPAELARRLGDA-GAEVTNMYGPTET-T 783
Cdd:PRK05620 260 SAPTLAKIIATAMPRV--AHGVPTLWiQLMVHYLKNPPerMSLQEIYVGGSAVPPILIKAWEERyGVDVVHVWGMTETsP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 784 IWSTSGPTS------EDSIRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRP----GLTAEKF--- 850
Cdd:PRK05620 338 VGTVARPPSgvsgeaRWAYRVSQGRFPASLEYRIVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPteegGGAASTFrge 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 851 ----LPDPFGPPGtrMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVRED-----RP 921
Cdd:PRK05620 418 dvedANDRFTADG--WLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDdkwgeRP 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 653678460 922 GDLRLVAYVIPDGPVAPDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:PRK05620 496 LAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
544-976 |
7.62e-14 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 77.09 E-value: 7.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 544 VAVLLPRSADLLVTLLAVIKAGAAYLPI-DPDFP--VERIAYLLSDARPVLVVTDAATAD-------RLGPDDITGLVVL 613
Cdd:PRK12476 95 VAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVVLTTTAAAEavegflrNLPRLRRPRVIAI 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 614 EETDTGGYPATEPPAVPAGHSAYVIYTSGSTGRPKGVVITRAALDNFLAAMaerfpltaedrVLATTTVSFDIAGLElYL 693
Cdd:PRK12476 175 DAIPDSAGESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQM-----------ILSIDLLDRNTHGVS-WL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 694 PLRSGAGV-------VLADADTARNPAALI----------DLAGRHRVTLAqATPTL---WQA---LVPELSGPALAGIR 750
Cdd:PRK12476 243 PLYHDMGLsmigfpaVYGGHSTLMSPTAFVrrpqrwikalSEGSRTGRVVT-AAPNFayeWAAqrgLPAEGDDIDLSNVV 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 751 VLVGGEALPAELARRLGDAGAE-------VTNMYGPTETTIW-STSGPTSE------------------------DSIRR 798
Cdd:PRK12476 322 LIIGSEPVSIDAVTTFNKAFAPyglprtaFKPSYGIAEATLFvATIAPDAEpsvvyldreqlgagravrvaadapNAVAH 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 799 GSIGVPIDNTQVYVLDANL-HPAPIGVLGELHIAGEGLARGYWNRPGLTAEKF-------LPDPF----GPPGTRMYRTG 866
Cdd:PRK12476 402 VSCGQVARSQWAVIVDPDTgAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrLAEGShadgAADDGTWLRTG 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 867 DLVRWsAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGP-VRR---AAAVVREDRPGDLRLVAYVIP-----DGPVA 937
Cdd:PRK12476 482 DLGVY-LDGELYITGRIADLIVIDGRNHYPQDIEATVAEASPmVRRgyvTAFTVPAEDNERLVIVAERAAgtsraDPAPA 560
|
490 500 510
....*....|....*....|....*....|....*....
gi 653678460 938 PDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAA 976
Cdd:PRK12476 561 IDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRA 599
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
1859-2033 |
7.83e-14 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 76.98 E-value: 7.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1859 LGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPDPagepgarMYRTGDLVRWRGDGLLDFV 1938
Cdd:PRK07059 382 IGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADG-------FFRTGDVGVMDERGYTKIV 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1939 GRVDDQVKLRGYRIELGEIEARMAEHPGV-EQAVVLVRDQ---QLVGWFIPAEDhPPVTVSALRRFCAEQLPEFMVPNQW 2014
Cdd:PRK07059 455 DRKKDMILVSGFNVYPNEIEEVVASHPGVlEVAAVGVPDEhsgEAVKLFVVKKD-PALTEEDVKAFCKERLTNYKRPKFV 533
|
170
....*....|....*....
gi 653678460 2015 VALDAFPLTPHGKVNHRAL 2033
Cdd:PRK07059 534 EFRTELPKTNVGKILRREL 552
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
505-782 |
9.23e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 76.91 E-value: 9.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 505 PGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGA--------------AY-- 568
Cdd:PRK08162 32 PDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAvlntlntrldaasiAFml 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 569 -------LPIDPDF-PVERIAYLLSDARPVLVVTDA----ATADRLGPDDITGLvvLEETD---TGGYPATEPPAVPAGh 633
Cdd:PRK08162 112 rhgeakvLIVDTEFaEVAREALALLPGPKPLVIDVDdpeyPGGRFIGALDYEAF--LASGDpdfAWTLPADEWDAIALN- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 634 sayviYTSGSTGRPKGVVI-TRAAldnFLAAMAerfpltaedrvlatTTVSFDIAGLELYL-----------------PL 695
Cdd:PRK08162 189 -----YTSGTTGNPKGVVYhHRGA---YLNALS--------------NILAWGMPKHPVYLwtlpmfhcngwcfpwtvAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 696 RSGAGVVLADADtarnPAALIDLAGRHRVTLAQATPTLWQALV--PELSGPALAG-IRVLVGGEALPAELARRLGDAGAE 772
Cdd:PRK08162 247 RAGTNVCLRKVD----PKLIFDLIREHGVTHYCGAPIVLSALInaPAEWRAGIDHpVHAMVAGAAPPAAVIAKMEEIGFD 322
|
330
....*....|
gi 653678460 773 VTNMYGPTET 782
Cdd:PRK08162 323 LTHVYGLTET 332
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
1532-2033 |
1.33e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 76.22 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1532 TVHQLVEAQA-DRTPGwtaLRTGDRSLTFAGLDAQANRLAHALhtGALGAPPvGPeTPVLLLLDRSPELVVAMLAVLKAG 1610
Cdd:PRK13388 4 TIAQLLRDRAgDDTIA---VRYGDRTWTWREVLAEAAARAAAL--IALADPD-RP-LHVGVLLGNTPEMLFWLAAAALGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1611 GYFIPVDP---GYPMARLTRIADTvtpALVLTRTGQGGCLPGAEVFGD-VPVVALDRVADRLTAMPDQRPEVTVDPRGLA 1686
Cdd:PRK13388 77 YVLVGLNTtrrGAALAADIRRADC---QLLVTDAEHRPLLDGLDLPGVrVLDVDTPAYAELVAAAGALTPHREVDAMDPF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1687 YSIFTSGSTGQPKGVAVEHiGIVrylswAAASYPTAGRRG-----------TLAHSSvgfdlTMSALFEP-LVSGRGVTL 1754
Cdd:PRK13388 154 MLIFTSGTTGAPKAVRCSH-GRL-----AFAGRALTERFGltrddvcyvsmPLFHSN-----AVMAGWAPaVASGAAVAL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1755 MP---ADATLADLAE-------ELSGPLAydYIRLTPSH-------LRHLVGHWTGQElppaargwvvggetlDPALVKQ 1817
Cdd:PRK13388 223 PAkfsASGFLDDVRRygatyfnYVGKPLA--YILATPERpddadnpLRVAFGNEASPR---------------DIAEFSR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1818 llelRPDAEVINHYGPTETVIGRVVHPVREAGElavdsplpLGRPL-------GETRLQVLDAWLEAV-----PVGAVGE 1885
Cdd:PRK13388 286 ----RFGCQVEDGYGSSEGAVIVVREPGTPPGS--------IGRGApgvaiynPETLTECAVARFDAHgallnADEAIGE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1886 LF-IGGDGIARGYLGRPALTAEKFlpdpagepgaR--MYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMA 1962
Cdd:PRK13388 354 LVnTAGAGFFEGYYNNPEATAERM----------RhgMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILL 423
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 653678460 1963 EHPGVEQAVVL-VRDQ----QLVGWFIPAEDHpPVTVSALRRFCAEQ--LPEFMVPNQ-WVAlDAFPLTPHGKVNHRAL 2033
Cdd:PRK13388 424 RHPAINRVAVYaVPDErvgdQVMAALVLRDGA-TFDPDAFAAFLAAQpdLGTKAWPRYvRIA-ADLPSTATNKVLKREL 500
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
1548-2028 |
1.50e-13 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 75.80 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1548 TALRTGDRSLTFAGLDAQANRLAHALhtGALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDpgypmARLTr 1627
Cdd:cd12118 21 TSIVYGDRRYTWRQTYDRCRRLASAL--AALG---ISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALN-----TRLD- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1628 iADTVtpALVLTRTGqggclpgAEV-FGDVPVVALDRVAdrlTAMPD---QRPEVTVDPRGLAYsifTSGSTGQPKGVAV 1703
Cdd:cd12118 90 -AEEI--AFILRHSE-------AKVlFVDREFEYEDLLA---EGDPDfewIPPADEWDPIALNY---TSGTTGRPKGVVY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1704 EHIGIvrYLSWAAASYptagrRGTLAHSSV-------------GFDLTMSAlfeplVSGRGVTLMPADAtladlaeelsg 1770
Cdd:cd12118 154 HHRGA--YLNALANIL-----EWEMKQHPVylwtlpmfhcngwCFPWTVAA-----VGGTNVCLRKVDA----------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1771 PLAYDYIRLtpshlrHLVGHWTGQ--------ELPPAARG---WVV----GGETLDPALVKQLLELRPDaeVINHYGPTE 1835
Cdd:cd12118 211 KAIYDLIEK------HKVTHFCGAptvlnmlaNAPPSDARplpHRVhvmtAGAPPPAAVLAKMEELGFD--VTHVYGLTE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1836 T---VIGRVVHPvrEAGELAVDSPLPLG-----RPLGETRLQVLDA-WLEAVPVGA--VGELFIGGDGIARGYLGRPALT 1904
Cdd:cd12118 283 TygpATVCAWKP--EWDELPTEERARLKarqgvRYVGLEEVDVLDPeTMKPVPRDGktIGEIVFRGNIVMKGYLKNPEAT 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1905 AEKFlpdpagEPGarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGV-EQAVVLVRDQQlvgW- 1982
Cdd:cd12118 361 AEAF------RGG--WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVlEAAVVARPDEK---Wg 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 653678460 1983 -----FIPAEDHPPVTVSALRRFCAEQLPEFMVPNQWVALDaFPLTPHGKV 2028
Cdd:cd12118 430 evpcaFVELKEGAKVTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKI 479
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
1529-2033 |
1.60e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 76.23 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1529 DDRTVHQLVEAQADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHTgaLGappVGPETPVLLLLDRSPELVVAMLAVLK 1608
Cdd:PRK06710 22 DIQPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQK--LG---VEKGDRVAIMLPNCPQAVIGYYGTLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1609 AGGYFIPVDPGYPM-----------ARLTRIADTVTPA------------LVLTRTGQGGCLPGAEVFgdvPVVALDR-- 1663
Cdd:PRK06710 97 AGGIVVQTNPLYTEreleyqlhdsgAKVILCLDLVFPRvtnvqsatkiehVIVTRIADFLPFPKNLLY---PFVQKKQsn 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1664 ------------VADRLTAMPDQRPEVTVDPRG-LAYSIFTSGSTGQPKGVAVEHIGIVRY----LSW----------AA 1716
Cdd:PRK06710 174 lvvkvsesetihLWNSVEKEVNTGVEVPCDPENdLALLQYTGGTTGFPKGVMLTHKNLVSNtlmgVQWlynckegeevVL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1717 ASYPTAGRRGTLAHSSVG------------FDLTMsaLFEPLVSGRgVTLMPADATLadlaeelsgplaydYIRLTPSHL 1784
Cdd:PRK06710 254 GVLPFFHVYGMTAVMNLSimqgykmvlipkFDMKM--VFEAIKKHK-VTLFPGAPTI--------------YIALLNSPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1785 RhlvghwtgQELPPAARGWVVGGETLDPALVKQLLELRPDAEVINHYGPTETvigrvvHPVREAGEL-AVDSPLPLGRPL 1863
Cdd:PRK06710 317 L--------KEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTES------SPVTHSNFLwEKRVPGSIGVPW 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1864 GETRLQVLDAWL-EAVPVGAVGELFIGGDGIARGYLGRPALTAeKFLPDPagepgarMYRTGDLVRWRGDGLLDFVGRVD 1942
Cdd:PRK06710 383 PDTEAMIMSLETgEALPPGEIGEIVVKGPQIMKGYWNKPEETA-AVLQDG-------WLHTGDVGYMDEDGFFYVKDRKK 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1943 DQVKLRGYRIELGEIEARMAEHPGVEQAVVL-VRDQ---QLVGWFIPAEDHPPVTVSALRRFCAEQLPEFMVPNQWVALD 2018
Cdd:PRK06710 455 DMIVASGFNVYPREVEEVLYEHEKVQEVVTIgVPDPyrgETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRD 534
|
570
....*....|....*
gi 653678460 2019 AFPLTPHGKVNHRAL 2033
Cdd:PRK06710 535 ELPKTTVGKILRRVL 549
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
518-976 |
1.61e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 75.80 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 518 SYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARPVLVVTDAA 597
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWAEDTLRVIGMIGAK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 598 TA------DRLGPD-DITGLVVLEETDTGGYPATEPPAVPAGHSAYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPL 670
Cdd:PRK07768 111 AVvvgepfLAAAPVlEEKGIRVLTVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEF 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 671 TAEDRVLATTTVSFDIAGLELYL--PLRSGAGVVL-ADADTARNPAALIDLAGRHRVTLAqATPTLWQALV-------PE 740
Cdd:PRK07768 191 DVETDVMVSWLPLFHDMGMVGFLtvPMYFGAELVKvTPMDFLRDPLLWAELISKYRGTMT-AAPNFAYALLarrlrrqAK 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 741 LSGPALAGIRV-LVGGEALPAELARRLGDAGAE-------VTNMYGPTETTI---WSTSG-------------------- 789
Cdd:PRK07768 270 PGAFDLSSLRFaLNGAEPIDPADVEDLLDAGARfglrpeaILPAYGMAEATLavsFSPCGaglvvdevdadllaalrrav 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 790 PTSEDSIRR-GSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYwnrpgLTAEKFLP--DPFGppgtrMYRTG 866
Cdd:PRK07768 350 PATKGNTRRlATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY-----LTMDGFIPaqDADG-----WLDTG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 867 DLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAV-VREDRPGDLRLVAYVIPDGPVAPDALRTEL 945
Cdd:PRK07768 420 DLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVaVRLDAGHSREGFAVAVESNAFEDPAEVRRI 499
|
490 500 510
....*....|....*....|....*....|....*....
gi 653678460 946 SRTLPDYMIPAV--------IVPVPDFPTTPNGKLDRAA 976
Cdd:PRK07768 500 RHQVAHEVVAEVgvrprnvvVLGPGSIPKTPSGKLRRAN 538
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
1548-1974 |
2.24e-13 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 75.30 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1548 TALRTGD-RSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMARLT 1626
Cdd:PRK07514 19 PFIETPDgLRYTYGDLDAASARLANLLV--ALG---VKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1627 RIADTVTPALVLTRTGQGGCL-PGAEVFGDVPVVALDR-----VADRLTAMPDQRPEVTVDPRGLAYSIFTSGSTGQPKG 1700
Cdd:PRK07514 94 YFIGDAEPALVVCDPANFAWLsKIAAAAGAPHVETLDAdgtgsLLEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1701 VAVEH-------IGIVRYLSWAAAS--------YPTAG----RRGTL-AHSSVGFdltmSALFEPlvsGRGVTLMPaDAT 1760
Cdd:PRK07514 174 AMLSHgnllsnaLTLVDYWRFTPDDvlihalpiFHTHGlfvaTNVALlAGASMIF----LPKFDP---DAVLALMP-RAT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1761 LadlaeeLSG-PLAY----DYIRLTPSHLRHLvghwtgqelppaaRGWVVGGETLDPALVKQLLElRPDAEVINHYGPTE 1835
Cdd:PRK07514 246 V------MMGvPTFYtrllQEPRLTREAAAHM-------------RLFISGSAPLLAETHREFQE-RTGHAILERYGMTE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1836 TVIgRVVHPV---REAGelAVdsplplGRPLGETRLQVLD-AWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLPD 1911
Cdd:PRK07514 306 TNM-NTSNPYdgeRRAG--TV------GFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRAD 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 653678460 1912 PagepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGV-EQAVVLV 1974
Cdd:PRK07514 377 G-------FFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVvESAVIGV 433
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
508-974 |
3.54e-13 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 75.18 E-value: 3.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 508 VAVI-EGD-----TTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIA 581
Cdd:PRK00174 84 VAIIwEGDdpgdsRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSAEALA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 582 YLLSDARPVLVVT-----------------DAATADrlgPDDITGLVVLEETD----------------TGGYPAT-EPP 627
Cdd:PRK00174 164 DRIIDAGAKLVITadegvrggkpiplkanvDEALAN---CPSVEKVIVVRRTGgdvdwvegrdlwwhelVAGASDEcEPE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 628 AVPAGHSAYVIYTSGSTGRPKGVVITRAALdNFLAAMaerfpltaedrvlaTTTVSFDIAGLE----------------- 690
Cdd:PRK00174 241 PMDAEDPLFILYTSGSTGKPKGVLHTTGGY-LVYAAM--------------TMKYVFDYKDGDvywctadvgwvtghsyi 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 691 LYLPLRSGAGVVLAD-ADTARNPAALIDLAGRHRVTLAQATPTLwqalvpelsgpalagIRVLVG-GEALPAE--LA--R 764
Cdd:PRK00174 306 VYGPLANGATTLMFEgVPNYPDPGRFWEVIDKHKVTIFYTAPTA---------------IRALMKeGDEHPKKydLSslR 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 765 RLGDAG------------AEVTNMYGPTETTIWSTS----------GPTSedsIRRGSIGVPIDNTQVYVLDANLHPAPI 822
Cdd:PRK00174 371 LLGSVGepinpeawewyyKVVGGERCPIVDTWWQTEtggimitplpGATP---LKPGSATRPLPGIQPAVVDEEGNPLEG 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 823 GVLGELHIAGE--GLARGYWNRPgltaEKFLPDPFGP-PGtrMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEI 899
Cdd:PRK00174 448 GEGGNLVIKDPwpGMMRTIYGDH----ERFVKTYFSTfKG--MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEI 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 900 ETTLInAGPVRRAAAVVreDRPGDLR---LVAYVIPDGPVAP-DALRTEL----SRTLPDYMIPAVIVPVPDFPTTPNGK 971
Cdd:PRK00174 522 ESALV-AHPKVAEAAVV--GRPDDIKgqgIYAFVTLKGGEEPsDELRKELrnwvRKEIGPIAKPDVIQFAPGLPKTRSGK 598
|
...
gi 653678460 972 LDR 974
Cdd:PRK00174 599 IMR 601
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
518-977 |
6.25e-13 |
|
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: 74.04 E-value: 6.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 518 SYRELDERANRLARLL-----MERGagaeTFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARPVLV 592
Cdd:cd05928 43 SFRELGSLSRKAANVLsgacgLQRG----DRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 593 VTDAATADRLG------PDDITGLVVLEETDTG--------GYPATEPPAVPAGHS-AYVIY-TSGSTGRPKGVVITRAA 656
Cdd:cd05928 119 VTSDELAPEVDsvasecPSLKTKLLVSEKSRDGwlnfkellNEASTEHHCVETGSQePMAIYfTSGTTGSPKMAEHSHSS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 657 LDNFLAAMAERF-PLTAEDRVLATTTVSFDIAGL-ELYLPLRSGAgVVLADADTARNPAALIDLAGRHRVTLAQATPTLW 734
Cdd:cd05928 199 LGLGLKVNGRYWlDLTASDIMWNTSDTGWIKSAWsSLFEPWIQGA-CVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVY 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 735 QALVPE-LSGPALAGIR-VLVGGEAL-PAELARRLGDAGAEVTNMYGPTETTIwsTSGPTSEDSIRRGSIGVPIDNTQVY 811
Cdd:cd05928 278 RMLVQQdLSSYKFPSLQhCVTGGEPLnPEVLEKWKAQTGLDIYEGYGQTETGL--ICANFKGMKIKPGSMGKASPPYDVQ 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 812 VLDANLHPAPIGVLGELHIAGE-----GLARGYWNRPGLTAEKFLPDpfgppgtrMYRTGDLVRWSAAGDLEYLGRTDHQ 886
Cdd:cd05928 356 IIDDNGNVLPPGTEGDIGIRVKpirpfGLFSGYVDNPEKTAATIRGD--------FYLTGDRGIMDEDGYFWFMGRADDV 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 887 VKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIPDGPV---APDALRTEL-----SRTLPdYMIPAVI 958
Cdd:cd05928 428 INSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFlshDPEQLTKELqqhvkSVTAP-YKYPRKV 506
|
490
....*....|....*....
gi 653678460 959 VPVPDFPTTPNGKLDRAAL 977
Cdd:cd05928 507 EFVQELPKTVTGKIQRNEL 525
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
1917-2034 |
7.18e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 73.15 E-value: 7.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1917 GARMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRDQQLVGWFIPAE--DHPPVTV 1994
Cdd:PRK08308 289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKviSHEEIDP 368
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 653678460 1995 SALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRALP 2034
Cdd:PRK08308 369 VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
511-977 |
1.00e-12 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 73.25 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 511 IEGDTT-LSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARP 589
Cdd:PRK06018 33 VEGPIVrTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAED 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 590 VLVVTD-------AATADRLgpDDITGLVVLeeTDTGGYPATEPP-------------------AVPAGHSAYVIYTSGS 643
Cdd:PRK06018 113 RVVITDltfvpilEKIADKL--PSVERYVVL--TDAAHMPQTTLKnavayeewiaeadgdfawkTFDENTAAGMCYTSGT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 644 TGRPKGVVITRAA--LDNFLAAMAERFPLTAEDRVLATTTVSFDIA-GLELYLPlRSGAGVVLADADTarNPAALIDLAG 720
Cdd:PRK06018 189 TGDPKGVLYSHRSnvLHALMANNGDALGTSAADTMLPVVPLFHANSwGIAFSAP-SMGTKLVMPGAKL--DGASVYELLD 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 721 RHRVTLAQATPTLWQALVPELSG-----PALAgiRVLVGGEALPAELARRLGDAGAEVTNMYGPTETTIWSTSgptseds 795
Cdd:PRK06018 266 TEKVTFTAGVPTVWLMLLQYMEKeglklPHLK--MVVCGGSAMPRSMIKAFEDMGVEVRHAWGMTEMSPLGTL------- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 796 irrGSIGVPIDNTQVyvlDANLHP------APIGV------------------LGELHIAGEGLARGYWNRPG--LTAEK 849
Cdd:PRK06018 337 ---AALKPPFSKLPG---DARLDVlqkqgyPPFGVemkitddagkelpwdgktFGRLKVRGPAVAAAYYRVDGeiLDDDG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 850 FlpdpfgppgtrmYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLR--LV 927
Cdd:PRK06018 411 F------------FDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERplLI 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 653678460 928 AYVIPDGPVAPDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:PRK06018 479 VQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
1532-2039 |
1.59e-12 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 72.73 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1532 TVHQLVEAQADRTPGWTALRTGD--RSLTFAGLDAQANRLAhalhtGALGAPPVGPETPVLLLLDRSPELVVAMLAVLKA 1609
Cdd:PRK05857 15 TVLDRVFEQARQQPEAIALRRCDgtSALRYRELVAEVGGLA-----ADLRAQSVSRGSRVLVISDNGPETYLSVLACAKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1610 GGYFIPVDPGYPMARLTRIADTVTPALVLTRTGQG-GCLPGAEVFGDVPVVALDRVADRL-------TAMPDQRPEVTVD 1681
Cdd:PRK05857 90 GAIAVMADGNLPIAAIERFCQITDPAAALVAPGSKmASSAVPEALHSIPVIAVDIAAVTResehsldAASLAGNADQGSE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1682 pRGLAYsIFTSGSTGQPKGV--------AVEHIGIVRYLSWAaasyptagrrgtlahSSVGFDLTMSALFEPLVSG---- 1749
Cdd:PRK05857 170 -DPLAM-IFTSGTTGEPKAVllanrtffAVPDILQKEGLNWV---------------TWVVGETTYSPLPATHIGGlwwi 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1750 -----RGVTLMPADATLADLAEELSGPlAYDYIRLTPSHLRHLVGHW-TGQELPPAARGWVVGGETLDPALVK--QLLEL 1821
Cdd:PRK05857 233 ltclmHGGLCVTGGENTTSLLEILTTN-AVATTCLVPTLLSKLVSELkSANATVPSLRLVGYGGSRAIAADVRfiEATGV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1822 RpDAEVinhYGPTETVIGRVVHPVrEAGELAVDSPLPLGRPLG--ETRLQVLDAWLEAVPVGA----VGELFIGGDGIAR 1895
Cdd:PRK05857 312 R-TAQV---YGLSETGCTALCLPT-DDGSIVKIEAGAVGRPYPgvDVYLAATDGIGPTAPGAGpsasFGTLWIKSPANML 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1896 GYLGRPALTAEKFLPDpagepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEaRMAEH-PGV-EQAVVL 1973
Cdd:PRK05857 387 GYWNNPERTAEVLIDG--------WVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVD-RIAEGvSGVrEAACYE 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 653678460 1974 VRDQQ---LVGW-FIPAEDHPPVTVSALRRFCAEQL---PEFMV-PNQWVALDAFPLTPHGKVNHRALPGPTSG 2039
Cdd:PRK05857 458 IPDEEfgaLVGLaVVASAELDESAARALKHTIAARFrreSEPMArPSTIVIVTDIPRTQSGKVMRASLAAAATA 531
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
631-868 |
1.84e-12 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 72.52 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 631 AGHSAYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDRVLATTTVSFDIAGLELYL-PLRSGAG-VVLADADT 708
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLaPLIAGMNqYLMPTRLF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 709 ARNPAALIDLAGRHRVTLAQ----ATPTLWQALVPELSGPA-LAGIRVLV-GGEALPAELARRLGDAGAE-------VTN 775
Cdd:cd05908 185 IRRPILWLKKASEHKATIVSspnfGYKYFLKTLKPEKANDWdLSSIRMILnGAEPIDYELCHEFLDHMSKyglkrnaILP 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 776 MYGPTETTIWSTSGPTSEDSI-----RRG---------------------SIGVPIDNTQVYVLDANLHPAPIGVLGELH 829
Cdd:cd05908 265 VYGLAEASVGASLPKAQSPFKtitlgRRHvthgepepevdkkdsecltfvEVGKPIDETDIRICDEDNKILPDGYIGHIQ 344
|
250 260 270
....*....|....*....|....*....|....*....
gi 653678460 830 IAGEGLARGYWNRPGLTAEKFLPDPFgppgtrmYRTGDL 868
Cdd:cd05908 345 IRGKNVTPGYYNNPEATAKVFTDDGW-------LKTGDL 376
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
508-977 |
2.17e-12 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 72.32 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 508 VAVIEGDT--TLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLS 585
Cdd:PLN02330 45 VAFVEAVTgkAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 586 DARPVLVVTDAATADR----------LGPDDITGLV----VLEETDTGGYPA-------TEPPAVPaghsayviYTSGST 644
Cdd:PLN02330 125 AAGAKLIVTNDTNYGKvkglglpvivLGEEKIEGAVnwkeLLEAADRAGDTSdneeilqTDLCALP--------FSSGTT 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 645 GRPKGVVITRAaldNFLAAMAERFPLTAEDRVLATTTVS----FDIAGLE--LYLPLRS-GAGVVLADADTARNPAALId 717
Cdd:PLN02330 197 GISKGVMLTHR---NLVANLCSSLFSVGPEMIGQVVTLGlipfFHIYGITgiCCATLRNkGKVVVMSRFELRTFLNALI- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 718 lagRHRVTLAQATPTLWQALVP-----ELSGPALAGIRVLVGGEALPAEL--ARRLGDAGAEVTNMYGPTE-TTIWSTSG 789
Cdd:PLN02330 273 ---TQEVSFAPIVPPIILNLVKnpiveEFDLSKLKLQAIMTAAAPLAPELltAFEAKFPGVQVQEAYGLTEhSCITLTHG 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 790 -PTSEDSI-RRGSIGVPIDNTQVYVLDA-NLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgppgtrmYRTG 866
Cdd:PLN02330 350 dPEKGHGIaKKNSVGFILPNLEVKFIDPdTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGW-------LHTG 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 867 DLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAV-VREDRPGDLRLVAYVI-PDGPVAPDALRTE 944
Cdd:PLN02330 423 DIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVpLPDEEAGEIPAACVVInPKAKESEEDILNF 502
|
490 500 510
....*....|....*....|....*....|...
gi 653678460 945 LSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:PLN02330 503 VAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
487-977 |
2.78e-12 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 71.79 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 487 PLPAASLRERFQQWCRR---TPGAVAVIEGDT--TLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAV 561
Cdd:cd17642 10 PLEDGTAGEQLHKAMKRyasVPGTIAFTDAHTgvNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 562 IKAGAAYLPIDPDFPVERIAYLLSDARPVLVVTDAATADRLGP-----DDITGLVVLE-ETDTGGYPATE---PPAVPAG 632
Cdd:cd17642 90 LFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNvqkklKIIKTIIILDsKEDYKGYQCLYtfiTQNLPPG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 633 HSAY---------------VIYTSGSTGRPKGVVIT-RAALDNFLAAMAERF-----PLTAEDRVL-------ATTTVSF 684
Cdd:cd17642 170 FNEYdfkppsfdrdeqvalIMNSSGSTGLPKGVQLThKNIVARFSHARDPIFgnqiiPDTAILTVIpfhhgfgMFTTLGY 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 685 DIAGLELYLPLRSGAGVVLAdadtarnpaALIDlagrHRVTLAQATPTLWQALV--PELSGPALAGIRVLVGGEAlpaEL 762
Cdd:cd17642 250 LICGFRVVLMYKFEEELFLR---------SLQD----YKVQSALLVPTLFAFFAksTLVDKYDLSNLHEIASGGA---PL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 763 ARRLGDAGAEVTNM------YGPTETTiwSTSGPTSEDSIRRGSIGVPIDNTQVYVLDANLHPApIGV--LGELHIAGEG 834
Cdd:cd17642 314 SKEVGEAVAKRFKLpgirqgYGLTETT--SAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKT-LGPneRGELCVKGPM 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 835 LARGYWNRPGLTAEKFLPDPFgppgtrmYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAA- 913
Cdd:cd17642 391 IMKGYVNNPEATKALIDKDGW-------LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGv 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 653678460 914 AVVREDRPGDLRLVAYVIPDGpvapdalRTELSRTLPDYMIPAV---------IVPVPDFPTTPNGKLDRAAL 977
Cdd:cd17642 464 AGIPDEDAGELPAAVVVLEAG-------KTMTEKEVMDYVASQVstakrlrggVKFVDEVPKGLTGKIDRRKI 529
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
516-889 |
4.52e-12 |
|
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: 71.33 E-value: 4.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 516 TLSYRELDERANRLARLL-MERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARPVLVVT 594
Cdd:cd17632 67 TITYAELWERVGAVAAAHdPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 595 DAAT------------------------------------ADRLGPDDITGLVVLEETDTGGYPATEPPAVPAGHS---A 635
Cdd:cd17632 147 SAEHldlaveavleggtpprlvvfdhrpevdahraalesaRERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEPDDdplA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 636 YVIYTSGSTGRPKGVVITRaaldNFLAAMAERFPLTAEDRVLATTTVSF----DIAG-LELYLPL-RSGAGVVLADADTa 709
Cdd:cd17632 227 LLIYTSGSTGTPKGAMYTE----RLVATFWLKVSSIQDIRPPASITLNFmpmsHIAGrISLYGTLaRGGTAYFAAASDM- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 710 rnpAALIDLAGRHRVTLAQATPTLW----QALVPELSGPALAGIRVLVGGEALPAELARRL----------GDA------ 769
Cdd:cd17632 302 ---STLFDDLALVRPTELFLVPRVCdmlfQRYQAELDRRSVAGADAETLAERVKAELRERVlggrllaavcGSAplsaem 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 770 --------GAEVTNMYGPTETTIwstsgptsedSIRRGSIGVP--IDNTQV------YVLDANLHPApigvlGELHIAGE 833
Cdd:cd17632 379 kafmesllDLDLHDGYGSTEAGA----------VILDGVIVRPpvLDYKLVdvpelgYFRTDRPHPR-----GELLVKTD 443
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 653678460 834 GLARGYWNRPGLTAEKFLPDPFgppgtrmYRTGDLVRWSAAGDLEYLGRTDHQVKL 889
Cdd:cd17632 444 TLFPGYYKRPEVTAEVFDEDGF-------YRTGDVMAELGPDRLVYVDRRNNVLKL 492
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
1831-2029 |
5.06e-12 |
|
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: 69.61 E-value: 5.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1831 YGPTETVIGRVVHPVREAgelavdsPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLP 1910
Cdd:cd17637 143 YGQTETSGLVTLSPYRER-------PGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRN 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1911 DpagepgarMYRTGDLVRWRGDGLLDFVGRV--DDQVKLRGYRIELGEIEARMAEHPGVEQAVVL-VRDQQLvGWFIPA- 1986
Cdd:cd17637 216 G--------WHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIgVPDPKW-GEGIKAv 286
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 653678460 1987 -EDHPPVTVSA--LRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVN 2029
Cdd:cd17637 287 cVLKPGATLTAdeLIEFVGSRIARYKKPRYVVFVEALPKTADGSID 332
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
1690-1972 |
5.27e-12 |
|
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: 70.96 E-value: 5.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1690 FTSGSTGQPKgvAVEHigivRYLSWAAASYPTAGRRGTLAHSSVGFDLT--------MSALFEPLVSGRGV--TLMPADA 1759
Cdd:cd05928 181 FTSGTTGSPK--MAEH----SHSSLGLGLKVNGRYWLDLTASDIMWNTSdtgwiksaWSSLFEPWIQGACVfvHHLPRFD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1760 TLADLAEELSGPLAYdyIRLTPSHLRHLVGhwtgQELP----PAARGWVVGGETLDPALVKQLLElRPDAEVINHYGPTE 1835
Cdd:cd05928 255 PLVILKTLSSYPITT--FCGAPTVYRMLVQ----QDLSsykfPSLQHCVTGGEPLNPEVLEKWKA-QTGLDIYEGYGQTE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1836 TVIgrvVHPVREAGELavdSPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGD-----GIARGYLGRPALTAEKFLP 1910
Cdd:cd05928 328 TGL---ICANFKGMKI---KPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKpirpfGLFSGYVDNPEKTAATIRG 401
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 653678460 1911 DpagepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGV-EQAVV 1972
Cdd:cd05928 402 D--------FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVvESAVV 456
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
1541-2019 |
5.55e-12 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 70.67 E-value: 5.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1541 ADRTPGWTALRTGDRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGY 1620
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFA--QQG---VVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1621 PMARLTRIADTVTPALVLTRTGQGgclpgaevfgdvpvvALDRVADRLTAMPDQRPEVTVDPRGLAYSIFTSGSTGQPKg 1700
Cdd:PRK09029 88 PQPLLEELLPSLTLDFALVLEGEN---------------TFSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPK- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1701 vAVEHigivrylswaaasypTAGrrgtlAH--SSVG------FDLTMSALFE-PL--VSGRGVT---LMpADATL----- 1761
Cdd:PRK09029 152 -AAVH---------------TAQ-----AHlaSAEGvlslmpFTAQDSWLLSlPLfhVSGQGIVwrwLY-AGATLvvrdk 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1762 ADLAEELSGplaYDYIRLTPSHLRHLVGHWtgqELPPAARGWVVGGETLDPALVKQllelrpdAEVIN-----HYGPTE- 1835
Cdd:PRK09029 210 QPLEQALAG---CTHASLVPTQLWRLLDNR---SEPLSLKAVLLGGAAIPVELTEQ-------AEQQGircwcGYGLTEm 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1836 --TVIgrvvhpVREAGELA-VDSPLPlGRplgETRLqvldawleavpVGavGELFIGGDGIARGYLGRPALTAekfLPDP 1912
Cdd:PRK09029 277 asTVC------AKRADGLAgVGSPLP-GR---EVKL-----------VD--GEIWLRGASLALGYWRQGQLVP---LVND 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1913 AGepgarMYRTGDLVRWRGDGLLdFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLvrdqqlvgwfiPAED---- 1988
Cdd:PRK09029 331 EG-----WFATRDRGEWQNGELT-ILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVV-----------PVADaefg 393
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 653678460 1989 HPPV---------TVSALRRFCAEQLPEFMVPNQWVALDA 2019
Cdd:PRK09029 394 QRPVavvesdseaAVVNLAEWLQDKLARFQQPVAYYLLPP 433
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
1493-1705 |
6.10e-12 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 71.06 E-value: 6.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1493 AAAVRTPELAVTRLAITSESDTVRTSRwgrSEQHVGD-DRTVHQLVEAQADRTPG--WTALRTGD---RSLTFAGLDAQA 1566
Cdd:PRK08180 3 PARYRPVAFAPPAVEVERRADGTIYLR---SAEPLGDyPRRLTDRLVHWAQEAPDrvFLAERGADggwRRLTYAEALERV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1567 NRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGY-----PMARLTRIADTVTPALVLTRT 1641
Cdd:PRK08180 80 RAIAQALL--DRG---LSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAYslvsqDFGKLRHVLELLTPGLVFADD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 653678460 1642 GQ--GGCLpGAEVFGDVPVVAL-----DRVADRLTAMPDQRPEVTVD-------PRGLAYSIFTSGSTGQPKGVAVEH 1705
Cdd:PRK08180 155 GAafARAL-AAVVPADVEVVAVrgavpGRAATPFAALLATPPTAAVDaahaavgPDTIAKFLFTSGSTGLPKAVINTH 231
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
514-977 |
6.46e-12 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 71.08 E-value: 6.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 514 DTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARPVLVV 593
Cdd:PLN02654 118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 594 TdaATADRLGP-----DDITGLVVLEETDTG-----------------------------------GYPAT-EPPAVPAG 632
Cdd:PLN02654 198 T--CNAVKRGPktinlKDIVDAALDESAKNGvsvgicltyenqlamkredtkwqegrdvwwqdvvpNYPTKcEVEWVDAE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 633 HSAYVIYTSGSTGRPKGVVITRAALDNFLAAMAER-FPLTAEDRVLATTTVSFdIAGLEL--YLPLRSGAGVVLAD-ADT 708
Cdd:PLN02654 276 DPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYaFDYKPTDVYWCTADCGW-ITGHSYvtYGPMLNGATVLVFEgAPN 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 709 ARNPAALIDLAGRHRVTLAQATPTLWQALVPELSGP----ALAGIRVL--VGGEALPAelARR-----LGDAGAEVTNMY 777
Cdd:PLN02654 355 YPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYvtrhSRKSLRVLgsVGEPINPS--AWRwffnvVGDSRCPISDTW 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 778 GPTETTIWSTSGPTSEDSIRRGSIGVPIDNTQVYVLDANlhpapiGVLGELHIAGEGLARGYWnrPGL------TAEKFL 851
Cdd:PLN02654 433 WQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEK------GKEIEGECSGYLCVKKSW--PGAfrtlygDHERYE 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 852 PDPFGP-PGtrMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYV 930
Cdd:PLN02654 505 TTYFKPfAG--YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFV 582
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 653678460 931 -IPDGPVAPDALRTELSRTLPD----YMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:PLN02654 583 tLVEGVPYSEELRKSLILTVRNqigaFAAPDKIHWAPGLPKTRSGKIMRRIL 634
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
1530-1947 |
6.95e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 70.85 E-value: 6.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1530 DRTVHQLVEAQADRTPG--WTALRTGD----RSLTFAgldaQANRLAHALhTGALGAPPVGPETPVLLLLDRSPELVVAM 1603
Cdd:PRK12582 48 PRSIPHLLAKWAAEAPDrpWLAQREPGhgqwRKVTYG----EAKRAVDAL-AQALLDLGLDPGRPVMILSGNSIEHALMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1604 LAVLKAGGYFIPVDPGYPM-----ARLTRIADTVTPALVLTRTGQ--GGCLPGAEvFGDVPVVALDRVADRLTAMPDQ-- 1674
Cdd:PRK12582 123 LAAMQAGVPAAPVSPAYSLmshdhAKLKHLFDLVKPRVVFAQSGApfARALAALD-LLDVTVVHVTGPGEGIASIAFAdl 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1675 -----RPEV-----TVDPRGLAYSIFTSGSTGQPKGVAVEHigivRYLSWAAASYPTAGRRGTLAHSSVGFDL-----TM 1739
Cdd:PRK12582 202 aatppTAAVaaaiaAITPDTVAKYLFTSGSTGMPKAVINTQ----RMMCANIAMQEQLRPREPDPPPPVSLDWmpwnhTM 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1740 --SALFEPLVSGRGvTL-------MPA--DATLADLAEelSGPLAYDYirlTPSHLRHLVGHwtgQELPPAARGWVV--- 1805
Cdd:PRK12582 278 ggNANFNGLLWGGG-TLyiddgkpLPGmfEETIRNLRE--ISPTVYGN---VPAGYAMLAEA---MEKDDALRRSFFknl 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1806 -----GGETLDPALVKQLLELRPDAE-----VINHYGPTETV-IGRVVHPVREAGELavdsplpLGRPLGETRLQVldaw 1874
Cdd:PRK12582 349 rlmayGGATLSDDLYERMQALAVRTTghripFYTGYGATETApTTTGTHWDTERVGL-------IGLPLPGVELKL---- 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1875 leaVPVGAVGELFIGGDGIARGYLGRPALTAEKFlpDPAGepgarMYRTGDLVRW-------RGdglLDFVGRVDDQVKL 1947
Cdd:PRK12582 418 ---APVGDKYEVRVKGPNVTPGYHKDPELTAAAF--DEEG-----FYRLGDAARFvdpddpeKG---LIFDGRVAEDFKL 484
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
1682-2028 |
9.59e-12 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 70.21 E-value: 9.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1682 PRGLAYSIFTSGSTGQPKGVAVEHIG-IVRYLS-WAAASYP-------TA------GRRGTLAHSSVG--------FDlt 1738
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSAlIVQSLAkIAIVGYGeddvylhTAplchigGLSSALAMLMVGachvllpkFD-- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1739 MSALFEPLVSGRGVTLMPADATLADLAEelsgplaydYIRLTpshlrhlvGHWTGQelpPAARGWVVGGETLDPALVKQL 1818
Cdd:PLN02860 249 AKAALQAIKQHNVTSMITVPAMMADLIS---------LTRKS--------MTWKVF---PSVRKILNGGGSLSSRLLPDA 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1819 LELRPDAEVINHYGPTETVIGRVVHPVREAgelAVDSPLPLGRPLGETRLQVLDAwLEAVPVGAVG---ELFIGGDGIAR 1895
Cdd:PLN02860 309 KKLFPNAKLFSAYGMTEACSSLTFMTLHDP---TLESPKQTLQTVNQTKSSSVHQ-PQGVCVGKPAphvELKIGLDESSR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1896 -------------GYLGRPALTAEKfLPDPAgepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMA 1962
Cdd:PLN02860 385 vgriltrgphvmlGYWGQNSETASV-LSNDG------WLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLS 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1963 EHPGVEQAVVL-VRDQQLV-----------GWFIPAEDHP----PVTVSA--LRRFCAEQ-LPEFMVPN---QWvaLDAF 2020
Cdd:PLN02860 458 QHPGVASVVVVgVPDSRLTemvvacvrlrdGWIWSDNEKEnakkNLTLSSetLRHHCREKnLSRFKIPKlfvQW--RKPF 535
|
....*...
gi 653678460 2021 PLTPHGKV 2028
Cdd:PLN02860 536 PLTTTGKI 543
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
2056-2113 |
1.63e-11 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 61.43 E-value: 1.63e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 653678460 2056 QLLAELWSTVLG--TDRIGIEDNFFDLGGTSISVIQLSGACRRA-GVEISPKDVFEQPTVR 2113
Cdd:pfam00550 1 ERLRELLAEVLGvpAEEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLA 61
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
782-1036 |
2.31e-11 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 67.08 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 782 TTIWSTSGPTSEDSIRRGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFLPDPFGPPGTR 861
Cdd:COG3433 1 IAIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 862 MYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIPDGPVAPDAL 941
Cdd:COG3433 81 QADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 942 RTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAALPAPDY------GTRSTARPPRDDRERFLCTAFAEVLGLP--EVA 1013
Cdd:COG3433 161 ALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAaeallaAASPAPALETALTEEELRADVAELLGVDpeEID 240
|
250 260
....*....|....*....|...
gi 653678460 1014 VSDNFFELGGHSLLAFRLLARIR 1036
Cdd:COG3433 241 PDDNLFDLGLDSIRLMQLVERWR 263
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
511-977 |
2.32e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 68.96 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 511 IEGDT-TLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARP 589
Cdd:PRK07008 33 VEGDIhRYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAED 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 590 VLVVTDA----------------------ATADRLgPDDITGLVVLEETDTGGYPATEPPAVPAGHSAYVIYTSGSTGRP 647
Cdd:PRK07008 113 RYVLFDLtflplvdalapqcpnvkgwvamTDAAHL-PAGSTPLLCYETLVGAQDGDYDWPRFDENQASSLCYTSGTTGNP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 648 KGVVITR--AALDNFLAAMAERFPLTAEDRVLATTTVsFDIA--GLELYLPLrSGAGVVLADADTarNPAALIDLAGRHR 723
Cdd:PRK07008 192 KGALYSHrsTVLHAYGAALPDAMGLSARDAVLPVVPM-FHVNawGLPYSAPL-TGAKLVLPGPDL--DGKSLYELIEAER 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 724 VTLAQATPTLWQALVPELSGpalAGI------RVLVGGEALPAELARRLGDA-GAEVTNMYGPTE--------TTIWSTS 788
Cdd:PRK07008 268 VTFSAGVPTVWLGLLNHMRE---AGLrfstlrRTVIGGSACPPAMIRTFEDEyGVEVIHAWGMTEmsplgtlcKLKWKHS 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 789 G-PTSEDSIRRGSIGVPIDNTQVYVLDANLHPAPI-GV-LGELHIAGEGLARGYWNRPGltaekflpdpfGPPGTRMYRT 865
Cdd:PRK07008 345 QlPLDEQRKLLEKQGRVIYGVDMKIVGDDGRELPWdGKaFGDLQVRGPWVIDRYFRGDA-----------SPLVDGWFPT 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 866 GDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVR-----EDRPgdlrLVAYVI-PDGPVAPD 939
Cdd:PRK07008 414 GDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACahpkwDERP----LLVVVKrPGAEVTRE 489
|
490 500 510
....*....|....*....|....*....|....*...
gi 653678460 940 ALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:PRK07008 490 ELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKL 527
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
1528-2033 |
2.69e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 68.94 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1528 GDDRTVHQLVEAQADrtpgwtalrTGDRSLTFAG-LDAQANRLAHALHTGALGAPPVGPETP--VLLLLDRSPELVVAML 1604
Cdd:PRK07867 2 SSAPTVAELLLPLAE---------DDDRGLYFEDsFTSWREHIRGSAARAAALRARLDPTRPphVGVLLDNTPEFSLLLG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1605 AVLKAGGYFIPVDPGYPMARLTRIADTVTPALVLTRTGQGGCLPGAEvfGDVPVVALDRV--ADRLTAMPDQRPE-VTVD 1681
Cdd:PRK07867 73 AAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGLD--PGVRVINVDSPawADELAAHRDAEPPfRVAD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1682 PRGLAYSIFTSGSTGQPKGVAVEHIGIvrylswAAASYPTAGRRGT-----------LAHSSvgfdlTMSALFEPLVSGR 1750
Cdd:PRK07867 151 PDDLFMLIFTSGTSGDPKAVRCTHRKV------ASAGVMLAQRFGLgpddvcyvsmpLFHSN-----AVMAGWAVALAAG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1751 GVTLMP----ADATLADL-------AEELSGPLAydYIRLTPshlrhlvghwtgqELPPAARG---WVVGGETLDPALVK 1816
Cdd:PRK07867 220 ASIALRrkfsASGFLPDVrrygatyANYVGKPLS--YVLATP-------------ERPDDADNplrIVYGNEGAPGDIAR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1817 qlLELRPDAEVINHYGPTETVIGRVVHPVREAGELAvdsPLPLGrplgetrLQVLDA-WLEAVPVG------------AV 1883
Cdd:PRK07867 285 --FARRFGCVVVDGFGSTEGGVAITRTPDTPPGALG---PLPPG-------VAIVDPdTGTECPPAedadgrllnadeAI 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1884 GELF-IGGDGIARGYLGRPALTAEKFlpdpagepGARMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMA 1962
Cdd:PRK07867 353 GELVnTAGPGGFEGYYNDPEADAERM--------RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILL 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1963 EHPGVEQAVVL------VRDQQLVGwfIPAEDHPPVTVSALRRFCAEQlPEFMvPNQWVAL----DAFPLTPHGKVNHRA 2032
Cdd:PRK07867 425 RYPDATEVAVYavpdpvVGDQVMAA--LVLAPGAKFDPDAFAEFLAAQ-PDLG-PKQWPSYvrvcAELPRTATFKVLKRQ 500
|
.
gi 653678460 2033 L 2033
Cdd:PRK07867 501 L 501
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
1859-2033 |
4.05e-11 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 68.16 E-value: 4.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1859 LGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEkFLPDPagepgarMYRTGDLVRWRGDGLLDFV 1938
Cdd:PRK08974 380 IGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDE-VIKDG-------WLATGDIAVMDEEGFLRIV 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1939 GRVDDQVKLRGYRIELGEIEARMAEHPGV-EQAVVLVRDQ---QLVGWFIPAEDhPPVTVSALRRFCAEQLPEFMVPNQW 2014
Cdd:PRK08974 452 DRKKDMILVSGFNVYPNEIEDVVMLHPKVlEVAAVGVPSEvsgEAVKIFVVKKD-PSLTEEELITHCRRHLTGYKVPKLV 530
|
170
....*....|....*....
gi 653678460 2015 VALDAFPLTPHGKVNHRAL 2033
Cdd:PRK08974 531 EFRDELPKSNVGKILRREL 549
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
516-977 |
4.56e-11 |
|
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: 67.84 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 516 TLSYRELDERANRLAR-LLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAylpidPDFpverIAYLLSDA------- 587
Cdd:cd05937 5 TWTYSETYDLVLRYAHwLHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA-----PAF----INYNLSGDplihclk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 588 --RPVLVVTDaatadrlgPDDITGLvvleetdtggypateppavpaghsayvIYTSGSTGRPKGVVITRAALDNFLAAMA 665
Cdd:cd05937 76 lsGSRFVIVD--------PDDPAIL---------------------------IYTSGTTGLPKAAAISWRRTLVTSNLLS 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 666 ERFPLTAEDRVLATTTVSFDIAG-LELYLPLRSGAGVVLADADTAR--------NPAALIDLAG---------------- 720
Cdd:cd05937 121 HDLNLKNGDRTYTCMPLYHGTAAfLGACNCLMSGGTLALSRKFSASqfwkdvrdSGATIIQYVGelcryllstppspydr 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 721 RHRVTLAQAT---PTLWQAL-----VPElsgpalagIRVLVGG-EALPAELARRLGDAGAEVTNMYGPTETTIWSTS--- 788
Cdd:cd05937 201 DHKVRVAWGNglrPDIWERFrerfnVPE--------IGEFYAAtEGVFALTNHNVGDFGAGAIGHHGLIRRWKFENQvvl 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 789 ---GPTSEDSIRRGSIGVPIDntqvyvldanlhpAPIG----VLGELHIAGEGLARGYWNRPGLTAEKFLPDPFgPPGTR 861
Cdd:cd05937 273 vkmDPETDDPIRDPKTGFCVR-------------APVGepgeMLGRVPFKNREAFQGYLHNEDATESKLVRDVF-RKGDI 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 862 MYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLiNAGPVRRAAAVVREDRP---GDLRLVAYVIPDGPVAP 938
Cdd:cd05937 339 YFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVL-GAHPDIAEANVYGVKVPghdGRAGCAAITLEESSAVP 417
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 653678460 939 DALR----TELSRT-LPDYMIPAVIVPVPDFPTTPNGKLDRAAL 977
Cdd:cd05937 418 TEFTksllASLARKnLPSYAVPLFLRLTEEVATTDNHKQQKGVL 461
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
997-1049 |
9.39e-11 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 59.11 E-value: 9.39e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 653678460 997 RFLCTAFAEVLGLP--EVAVSDNFFELGGHSLLAFRLLARIRDEFGAGFSLRRLL 1049
Cdd:pfam00550 1 ERLRELLAEVLGVPaeEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLF 55
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
1681-2028 |
1.65e-10 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 66.20 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1681 DPRGLAYsifTSGSTGQPKGVAVEHIGIvrYLS-------WAAASYPTAGRRGTLAHSSvGFDLTMSalfeplVSGRGVT 1753
Cdd:PLN03102 187 DPISLNY---TSGTTADPKGVVISHRGA--YLStlsaiigWEMGTCPVYLWTLPMFHCN-GWTFTWG------TAARGGT 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1754 LMpadatladLAEELSGPLAYDYIRL--------TPSHLRHLV-GHWTGQELPPAARGWVVGGETLDPALVKQLLELrpD 1824
Cdd:PLN03102 255 SV--------CMRHVTAPEIYKNIEMhnvthmccVPTVFNILLkGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRL--G 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1825 AEVINHYGPTETViGRVVH----------PVREAGELAVDSPLplgRPLGETRLQVLDA-WLEAVPVGA--VGELFIGGD 1891
Cdd:PLN03102 325 FQVMHAYGLTEAT-GPVLFcewqdewnrlPENQQMELKARQGV---SILGLADVDVKNKeTQESVPRDGktMGEIVIKGS 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1892 GIARGYLGRPALTAEKFlpdpagEPGarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAV 1971
Cdd:PLN03102 401 SIMKGYLKNPKATSEAF------KHG--WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETA 472
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 653678460 1972 VLVRDQQLVG----WFI----------PAEDHPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKV 2028
Cdd:PLN03102 473 VVAMPHPTWGetpcAFVvlekgettkeDRVDKLVTRERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKI 543
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
1545-2033 |
2.26e-10 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 66.02 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1545 PGWTALRtgDRSLTFAGLDAQANRLAHALHTGALGAPPVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMAR 1624
Cdd:PLN02574 53 NGDTALI--DSSTGFSISYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1625 L-TRIADTvTPALVLTRTGQGGCLP--GAEVFGDVPVVALDRVADR-------LTAMPDQRPEVTVDPRGLAYSIFTSGS 1694
Cdd:PLN02574 131 IkKRVVDC-SVGLAFTSPENVEKLSplGVPVIGVPENYDFDSKRIEfpkfyelIKEDFDFVPKPVIKQDDVAAIMYSSGT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1695 TGQPKGVAVEH---IGIVR-YLSWAAASYPTAGRRgtlahssvgfDLTMSALfePLVSGRGVTLMPADatLADLAEELSG 1770
Cdd:PLN02574 210 TGASKGVVLTHrnlIAMVElFVRFEASQYEYPGSD----------NVYLAAL--PMFHIYGLSLFVVG--LLSLGSTIVV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1771 PLAYDYIRLTPSHLRHLVGHWTgqELPP-------AARGwvVGGETLDP-------------ALVKQLLELRPDAEVINH 1830
Cdd:PLN02574 276 MRRFDASDMVKVIDRFKVTHFP--VVPPilmaltkKAKG--VCGEVLKSlkqvscgaaplsgKFIQDFVQTLPHVDFIQG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1831 YGPTE-TVIGrvvhpVR--EAGELAVDSPLPLGRPlgETRLQVLDaWLEA--VPVGAVGELFIGGDGIARGYLGRPALTA 1905
Cdd:PLN02574 352 YGMTEsTAVG-----TRgfNTEKLSKYSSVGLLAP--NMQAKVVD-WSTGclLPPGNCGELWIQGPGVMKGYLNNPKATQ 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1906 EKFLPDPagepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRDQQLVG---- 1981
Cdd:PLN02574 424 STIDKDG-------WLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGeipv 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 653678460 1982 WFIPAEDHPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:PLN02574 497 AFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRREL 548
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
2155-2277 |
2.29e-10 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440361 [Multi-domain] Cd Length: 221 Bit Score: 62.71 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 2155 DGRPVFCVHPSGGGVAWYLPLARALPAGHPVHAFQPLGMDGREAPAE--TIEDMAAgYLADLRLVQPEGPYVVVGWSLGG 2232
Cdd:COG0596 22 DGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGgyTLDDLAD-DLAALLDALGLERVVLVGHSMGG 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 653678460 2233 TIAFEMARqldRLGEPVQ-LILLEPTLPEVARTIDLHRPARDSYLR 2277
Cdd:COG0596 101 MVALELAA---RHPERVAgLVLVDEVLAALAEPLRRPGLAPEALAA 143
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
1552-2011 |
2.37e-10 |
|
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: 65.53 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1552 TGDRSLTFAGLDAQANRLAHALHtGALGappVGPETPVLLLLDRSPELVVAMLAVLKAGgyfipvdpgypmarltriadt 1631
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHWLH-DDLG---VQAGDFVAIDLTNSPEFVFLWLGLWSIG--------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1632 VTPALVLTRTGqggclpgaevfGDVPVVALDRVADRLtampdqrpeVTVDPRGLAYSIFTSGSTGQPKGVAVehigivry 1711
Cdd:cd05937 56 AAPAFINYNLS-----------GDPLIHCLKLSGSRF---------VIVDPDDPAILIYTSGTTGLPKAAAI-------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1712 lSWAAaSYPTAGRRGTLAHSSVGfDLTMSALfePLVSGRG-----VTLMPADATLAdLAEELSGPLAYDYIRLTPSHLRH 1786
Cdd:cd05937 108 -SWRR-TLVTSNLLSHDLNLKNG-DRTYTCM--PLYHGTAaflgaCNCLMSGGTLA-LSRKFSASQFWKDVRDSGATIIQ 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1787 LVGHwTGQEL---PP-----AARGWVVGGETLDPALVKQLLElRPDAEVINH-YGPTETVIGRVVHPVREAGELAVDSPL 1857
Cdd:cd05937 182 YVGE-LCRYLlstPPspydrDHKVRVAWGNGLRPDIWERFRE-RFNVPEIGEfYAATEGVFALTNHNVGDFGAGAIGHHG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1858 PLGRPLGETRLQVL-------DAWL-------EAVPVGAVGE----LFIGGDGIARGYLGRPALTAEKFLPDpAGEPGAR 1919
Cdd:cd05937 260 LIRRWKFENQVVLVkmdpetdDPIRdpktgfcVRAPVGEPGEmlgrVPFKNREAFQGYLHNEDATESKLVRD-VFRKGDI 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1920 MYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVlvrdqqlVGWFIP-------------- 1985
Cdd:cd05937 339 YFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANV-------YGVKVPghdgragcaaitle 411
|
490 500
....*....|....*....|....*...
gi 653678460 1986 --AEDHPPVTVSALRRFCAEQLPEFMVP 2011
Cdd:cd05937 412 esSAVPTEFTKSLLASLARKNLPSYAVP 439
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
1552-1709 |
2.75e-10 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 65.39 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1552 TGdRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMARLTRIADT 1631
Cdd:PLN02246 47 TG-RVYTYADVELLSRRVAAGLH--KLG---IRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1632 VTPALVLTRTGQGGCLPGAEVFGDVPVVALDRVADR-------LTAMPDQRPEVTVDPRGLAYSIFTSGSTGQPKGVAVE 1704
Cdd:PLN02246 121 SGAKLIITQSCYVDKLKGLAEDDGVTVVTIDDPPEGclhfselTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLT 200
|
....*
gi 653678460 1705 HIGIV 1709
Cdd:PLN02246 201 HKGLV 205
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
1556-1972 |
3.20e-10 |
|
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: 65.55 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1556 SLTFAGLDAQANRLAHALHTGAlgapPVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMARLTRIADTVTPA 1635
Cdd:cd17632 67 TITYAELWERVGAVAAAHDPEQ----PVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPR 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1636 LV----------LTRTGQGGCLPGAEVFGDVPVV-----ALDRVADRL------------------TAMPDQRPEVTVDP 1682
Cdd:cd17632 143 LLavsaehldlaVEAVLEGGTPPRLVVFDHRPEVdahraALESARERLaavgipvttltliavrgrDLPPAPLFRPEPDD 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1683 RGLAYSIFTSGSTGQPKGVAVEHIGIVRY---LSWAAASYPT-------------AGRR---GTLAHSSVGFDLT---MS 1740
Cdd:cd17632 223 DPLALLIYTSGSTGTPKGAMYTERLVATFwlkVSSIQDIRPPasitlnfmpmshiAGRIslyGTLARGGTAYFAAasdMS 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1741 ALFEPLVSGR--GVTLMP--ADATLADLAEELSGPLAYDYIRLTpshLRHLVGHWTGQELPPAARGWVVGGETLDPALVK 1816
Cdd:cd17632 303 TLFDDLALVRptELFLVPrvCDMLFQRYQAELDRRSVAGADAET---LAERVKAELRERVLGGRLLAAVCGSAPLSAEMK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1817 QLLELRPDAEVINHYGPTET----VIGRVVHP---------VREAGELAVDSPLPLGrplgetrlqvldawleavpvgav 1883
Cdd:cd17632 380 AFMESLLDLDLHDGYGSTEAgaviLDGVIVRPpvldyklvdVPELGYFRTDRPHPRG----------------------- 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1884 gELFIGGDGIARGYLGRPALTAEKFlpDPAGepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKL-RGYRIELGEIEARMA 1962
Cdd:cd17632 437 -ELLVKTDTLFPGYYKRPEVTAEVF--DEDG-----FYRTGDVMAELGPDRLVYVDRRNNVLKLsQGEFVTVARLEAVFA 508
|
490
....*....|
gi 653678460 1963 EHPGVEQAVV 1972
Cdd:cd17632 509 ASPLVRQIFV 518
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
2049-2116 |
3.65e-10 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 58.33 E-value: 3.65e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 653678460 2049 APRTPGEQLLAELWSTVLG--TDRIGIEDNFF-DLGGTSISVIQLSGACRRA-GVEISPKDVFEQPTVRGQA 2116
Cdd:COG0236 1 MPREELEERLAEIIAEVLGvdPEEITPDDSFFeDLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADLA 72
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
505-979 |
3.95e-10 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 65.25 E-value: 3.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 505 PGAVAVIEGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLL 584
Cdd:PLN02479 34 PTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 585 SDAR-------------------------------PVLVVTDAATADRLGPDDI--TGLVVLEETDTGGYP--ATEPPAv 629
Cdd:PLN02479 114 EHSKsevvmvdqefftlaeealkilaekkkssfkpPLLIVIGDPTCDPKSLQYAlgKGAIEYEKFLETGDPefAWKPPA- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 630 PAGHSAYVIYTSGSTGRPKGVVIT-RAAldnFLAAMAErfPLT---AEDRVLATTTVSFDIAG--LELYLPLRSGAGVVL 703
Cdd:PLN02479 193 DEWQSIALGYTSGTTASPKGVVLHhRGA---YLMALSN--ALIwgmNEGAVYLWTLPMFHCNGwcFTWTLAALCGTNICL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 704 ADADTArnpaALIDLAGRHRVTLAQATPTLWQALV----PELSGPALAGIRVLVGGEALPAELARRLGDAGAEVTNMYGP 779
Cdd:PLN02479 268 RQVTAK----AIYSAIANYGVTHFCAAPVVLNTIVnapkSETILPLPRVVHVMTAGAAPPPSVLFAMSEKGFRVTHTYGL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 780 TETTIWST---------SGPTSEDS---IRRGSIGVPIDNTQVyVLDANLHPAPI--GVLGELHIAGEGLARGYWNRPGL 845
Cdd:PLN02479 344 SETYGPSTvcawkpewdSLPPEEQArlnARQGVRYIGLEGLDV-VDTKTMKPVPAdgKTMGEIVMRGNMVMKGYLKNPKA 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 846 TAEKFlpdpfgppGTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLR 925
Cdd:PLN02479 423 NEEAF--------ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGES 494
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 653678460 926 LVAYVIPDGPV--------APDALRTELSRtLPDYMIPAVIVPVPdFPTTPNGKLDRAALPA 979
Cdd:PLN02479 495 PCAFVTLKPGVdksdeaalAEDIMKFCRER-LPAYWVPKSVVFGP-LPKTATGKIQKHVLRA 554
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
1549-2036 |
4.08e-10 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 65.10 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1549 ALRTGDRSLTFAGLDAQANRLAhalhtGALGAPPVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMARLTRI 1628
Cdd:PRK12406 4 TIISGDRRRSFDELAQRAARAA-----GGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1629 -ADTVTPALV----LTRTGQGGCLPGAEVFgDVP----VVALDRVADRLTAMP-----------DQRPEVTVDPRGLAYS 1688
Cdd:PRK12406 79 lEDSGARVLIahadLLHGLASALPAGVTVL-SVPtppeIAAAYRISPALLTPPagaidwegwlaQQEPYDGPPVPQPQSM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1689 IFTSGSTGQPKGV--------AVEHIGIVRYLSWAAASYPTAGRRGTLAHSSV-GFDLTMSALFEPLVsgrgvtLMP--- 1756
Cdd:PRK12406 158 IYTSGTTGHPKGVrraaptpeQAAAAEQMRALIYGLKPGIRALLTGPLYHSAPnAYGLRAGRLGGVLV------LQPrfd 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1757 ADATLADLAEElsgplAYDYIRLTPSHLRHLVghwtgqELPPAARG--------WVVGGETLDPALVKQLLELRPDAEVI 1828
Cdd:PRK12406 232 PEELLQLIERH-----RITHMHMVPTMFIRLL------KLPEEVRAkydvsslrHVIHAAAPCPADVKRAMIEWWGPVIY 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1829 NHYGPTETviGRVVHPVREAgelAVDSPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIAR-GYLGRPALTAEK 1907
Cdd:PRK12406 301 EYYGSTES--GAVTFATSED---ALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1908 flpDPAGepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVL-VRDQQLvGWFIPA 1986
Cdd:PRK12406 376 ---DRGG-----FITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFgIPDAEF-GEALMA 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 653678460 1987 --EDHPPVTVSA--LRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRALPGP 2036
Cdd:PRK12406 447 vvEPQPGATLDEadIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
1682-1982 |
7.98e-10 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 64.37 E-value: 7.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1682 PRGLAYSIFTSGSTGQPKGVAVEHIGIVRYLSWAAASYPTAGRRGT------LAH--------------SSVGFD--LTM 1739
Cdd:PLN02387 249 PNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDVylaylpLAHilelaaesvmaavgAAIGYGspLTL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1740 SALFEPL-------VSGRGVTLMPADATLADLAE-------ELSGPLA---YD--YIRltpsHLRHLVGHWTGqelppaA 1800
Cdd:PLN02387 329 TDTSNKIkkgtkgdASALKPTLMTAVPAILDRVRdgvrkkvDAKGGLAkklFDiaYKR----RLAAIEGSWFG------A 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1801 RG-----W----------VVGGEtldpalVKQLLE----LRPDAE-VIN---------HYGPTETV------------IG 1839
Cdd:PLN02387 399 WGlekllWdalvfkkiraVLGGR------IRFMLSggapLSGDTQrFINiclgapigqGYGLTETCagatfsewddtsVG 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1840 RVVHPV----------REAGELAVDSPLPLGrplgetrlqvldawleavpvgavgELFIGGDGIARGYLGRPALTAEKFL 1909
Cdd:PLN02387 473 RVGPPLpccyvklvswEEGGYLISDKPMPRG------------------------EIVIGGPSVTLGYFKNQEKTDEVYK 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1910 PDpagEPGARMYRTGDLVRWRGDGLLDFVGRVDDQVKLR-GYRIELGEIEARMAEHPGVEQ-------------AVVLVR 1975
Cdd:PLN02387 529 VD---ERGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAALSVSPYVDNimvhadpfhsycvALVVPS 605
|
....*..
gi 653678460 1976 DQQLVGW 1982
Cdd:PLN02387 606 QQALEKW 612
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
826-978 |
8.05e-10 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 63.86 E-value: 8.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 826 GELHIAGEGLARGYWnrpgltaekflPDPFGPPgtRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLIN 905
Cdd:PRK07445 302 GNITIQAQSLALGYY-----------PQILDSQ--GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILA 368
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 653678460 906 AGPVRRAAAVVREDRPGDLRLVAYVIP-DGPVAPDALRTELSRTLPDYMIPAVIVPVPDFPTTPNGKLDRAALP 978
Cdd:PRK07445 369 TGLVQDVCVLGLPDPHWGEVVTAIYVPkDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
503-972 |
8.57e-10 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 64.05 E-value: 8.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 503 RTPGAVAVI-----EGDTTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDF-- 575
Cdd:PRK03584 96 RRDDRPAIIfrgedGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFgv 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 576 -----------P---------------------VERIAYLLSDARPVLVVTDAATADRLGPDDitgLVVLEETDTGGYPA 623
Cdd:PRK03584 176 qgvldrfgqiePkvliavdgyryggkafdrrakVAELRAALPSLEHVVVVPYLGPAAAAAALP---GALLWEDFLAPAEA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 624 TEPP--AVPAGHSAYVIYTSGSTGRPKGVVITRA-ALDNFLAAMAERFPLTAEDRVLATTTVS-----FDIAGLElylpl 695
Cdd:PRK03584 253 AELEfePVPFDHPLWILYSSGTTGLPKCIVHGHGgILLEHLKELGLHCDLGPGDRFFWYTTCGwmmwnWLVSGLL----- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 696 rSGAGVVLAD-ADTARNPAALIDLAGRHRVTLAQATPTLWQA-----LVPELSGpALAGIR-VLVGGEALPAELARRLGD 768
Cdd:PRK03584 328 -VGATLVLYDgSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDAcekagLVPGETH-DLSALRtIGSTGSPLPPEGFDWVYE 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 769 AGAEvtnmygptetTIW--STSG------------PTSedSIRRGSIGVPIDNTQVYVLDANLHPApIGVLGELHIageg 834
Cdd:PRK03584 406 HVKA----------DVWlaSISGgtdicscfvggnPLL--PVYRGEIQCRGLGMAVEAWDEDGRPV-VGEVGELVC---- 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 835 lAR-------GYWNRPG---LTAEKFlpDPFgpPGTrmYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIeTTLI 904
Cdd:PRK03584 469 -TKpfpsmplGFWNDPDgsrYRDAYF--DTF--PGV--WRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEI-YRQV 540
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 653678460 905 NAGP-VRRAAAVVREDRPGDLRLVAYVIP-DGPVAPDALRTELSRTLPDYM----IPAVIVPVPDFPTTPNGKL 972
Cdd:PRK03584 541 EALPeVLDSLVIGQEWPDGDVRMPLFVVLaEGVTLDDALRARIRTTIRTNLsprhVPDKIIAVPDIPRTLSGKK 614
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
584-904 |
1.03e-09 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 63.98 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 584 LSDARPVLVVTDAATADRLGPDDITGLVV--LEETDTGGYPATEPPAVPAGHSAYVI-YTSGSTGRPKGVVITRAAL--- 657
Cdd:PLN02387 199 LETVKRVIYMDDEGVDSDSSLSGSSNWTVssFSEVEKLGKENPVDPDLPSPNDIAVImYTSGSTGLPKGVMMTHGNIvat 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 658 --------------DNFLA--AMAERFPLTAEDRVLAT------------TTVSFDIA------------GLELYLP--- 694
Cdd:PLN02387 279 vagvmtvvpklgknDVYLAylPLAHILELAAESVMAAVgaaigygspltlTDTSNKIKkgtkgdasalkpTLMTAVPail 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 695 --LRSGagvVLADADTARNPA-ALIDLAGRHRVTLAQAT--------PTLWQALVPELSGPALAG-IR-VLVGGEALPAE 761
Cdd:PLN02387 359 drVRDG---VRKKVDAKGGLAkKLFDIAYKRRLAAIEGSwfgawgleKLLWDALVFKKIRAVLGGrIRfMLSGGAPLSGD 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 762 LARRLGDA-GAEVTNMYGPTETTiwstSGPT-SE-DSIRRGSIGVPIDNTQVYVLD-------ANLHPAPigvLGELHIA 831
Cdd:PLN02387 436 TQRFINIClGAPIGQGYGLTETC----AGATfSEwDDTSVGRVGPPLPCCYVKLVSweeggylISDKPMP---RGEIVIG 508
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 653678460 832 GEGLARGYWNRPGLTAEKFLPDPfgpPGTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLR-GFRIELGEIETTLI 904
Cdd:PLN02387 509 GPSVTLGYFKNQEKTDEVYKVDE---RGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAALS 579
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
1860-2029 |
1.04e-09 |
|
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: 62.70 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1860 GRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEKFlpdpagepGARMYRTGDLVRWRGDGLLDFVG 1939
Cdd:cd17636 166 GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT--------RGGWHHTNDLGRREPDGSLSFVG 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1940 RVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVL-VRDQ---QLVGWFIPAEDHPPVTVSALRRFCAEQLPEFMVPNQWV 2015
Cdd:cd17636 238 PKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIgVPDPrwaQSVKAIVVLKPGASVTEAELIEHCRARIASYKKPKSVE 317
|
170
....*....|....
gi 653678460 2016 ALDAFPLTPHGKVN 2029
Cdd:cd17636 318 FADALPRTAGGADD 331
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
1554-2033 |
1.04e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 63.77 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1554 DRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPV--------------DPG 1619
Cdd:PRK08276 9 GEVVTYGELEARSNRLAHGLR--ALG---LREGDVVAILLENNPEFFEVYWAARRSGLYYTPInwhltaaeiayivdDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1620 ypmARL----TRIADTVTPALVLTRTG------QGGCLPGAEVFGDvpvvALDRVADrlTAMPDQRPEVTvdprgLAYSi 1689
Cdd:PRK08276 84 ---AKVlivsAALADTAAELAAELPAGvplllvVAGPVPGFRSYEE----ALAAQPD--TPIADETAGAD-----MLYS- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1690 ftSGSTGQPKGV--AVEHIGI-----VRYLSWAAASYPTAGRR----GTLAHSSVG-FDLTMSALFEPLVsgrgvtLMP- 1756
Cdd:PRK08276 149 --SGTTGRPKGIkrPLPGLDPdeapgMMLALLGFGMYGGPDSVylspAPLYHTAPLrFGMSALALGGTVV------VMEk 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1757 --ADATLAdlaeelsgplAYDYIRLTPSHL------RHLvghwtgqELPPAARG--------WVVGGETLDPALVK-QLL 1819
Cdd:PRK08276 221 fdAEEALA----------LIERYRVTHSQLvptmfvRML-------KLPEEVRArydvsslrVAIHAAAPCPVEVKrAMI 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1820 ELRPDAeVINHYGPTE----TVIGrvvhpvreaGELAVDSPLPLGRPLgETRLQVLDAWLEAVPVGAVGELFIGGDGIAR 1895
Cdd:PRK08276 284 DWWGPI-IHEYYASSEgggvTVIT---------SEDWLAHPGSVGKAV-LGEVRILDEDGNELPPGEIGTVYFEMDGYPF 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1896 GYLGRPALTAEKFLPDpagepgaRMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVL-V 1974
Cdd:PRK08276 353 EYHNDPEKTAAARNPH-------GWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFgV 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 653678460 1975 RD----QQLVGWFIPAEDH--PPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:PRK08276 426 PDeemgERVKAVVQPADGAdaGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
1531-2033 |
1.07e-09 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 63.82 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1531 RTVHQLVEAQADRTPGWTALR---TGDR-----SLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVA 1602
Cdd:PRK07529 25 ASTYELLSRAAARHPDAPALSfllDADPldrpeTWTYAELLADVTRTANLLH--SLG---VGPGDVVAFLLPNLPETHFA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1603 MLAVLKAGGYFiPVDP---GYPMARL-----------------TRIADTVTPAL-------VLTRTGQGGCLPGAEVFGD 1655
Cdd:PRK07529 100 LWGGEAAGIAN-PINPllePEQIAELlraagakvlvtlgpfpgTDIWQKVAEVLaalpelrTVVEVDLARYLPGPKRLAV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1656 VPVV--ALDRVADRLTAMPDQRPEVTVDPRG-----LAYSIFTSGSTGQPKGVAVEHIGIVrYLSWAAAsyptagrrgTL 1728
Cdd:PRK07529 179 PLIRrkAHARILDFDAELARQPGDRLFSGRPigpddVAAYFHTGGTTGMPKLAQHTHGNEV-ANAWLGA---------LL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1729 AHSSVGfDLTMSALfePL--VSGRGVTLMPADATLADLAeeLSGPLAYDYIRLTpSHLRHLVGHW-------------TG 1793
Cdd:PRK07529 249 LGLGPG-DTVFCGL--PLfhVNALLVTGLAPLARGAHVV--LATPQGYRGPGVI-ANFWKIVERYrinflsgvptvyaAL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1794 QELPPAA------RGWVVGGETLdPALVKQLLELRPDAEVINHYGPTETVIGRVVHPVReaGELAVDSplpLGRPLGETR 1867
Cdd:PRK07529 323 LQVPVDGhdisslRYALCGAAPL-PVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPD--GERRIGS---VGLRLPYQR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1868 LQVL-----DAWLEAVPVGAVGELFIGGDGIARGYLgrpalTAEKflpDPAGEPGARMYRTGDLVRWRGDGLLDFVGRVD 1942
Cdd:PRK07529 397 VRVVilddaGRYLRDCAVDEVGVLCIAGPNVFSGYL-----EAAH---NKGLWLEDGWLNTGDLGRIDADGYFWLTGRAK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1943 DQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRDQQLVG----WFIPAEDHPPVTVSALRRFCAEQLPE-FMVPNQWVAL 2017
Cdd:PRK07529 469 DLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGelpvAYVQLKPGASATEAELLAFARDHIAErAAVPKHVRIL 548
|
570
....*....|....*.
gi 653678460 2018 DAFPLTPHGKVNHRAL 2033
Cdd:PRK07529 549 DALPKTAVGKIFKPAL 564
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
637-973 |
1.42e-09 |
|
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: 62.32 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 637 VIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDRVLATTTVsFDIAGLELYLP--LRSGAGVVLADADtarnPAA 714
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPL-FHIGTLMFTLAtfHAGGTNVFVRRVD----AEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 715 LIDLAGRHRVTLAQATPTLWQALVpELSGPALAGIRVLVGGEALPAELARRLGDAGAEVTNM--YGPTETT-IWSTSGPT 791
Cdd:cd17636 80 VLELIEAERCTHAFLLPPTIDQIV-ELNADGLYDLSSLRSSPAAPEWNDMATVDTSPWGRKPggYGQTEVMgLATFAALG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 792 SEDSirrGSIGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKFlpdpfgppGTRMYRTGDLVRW 871
Cdd:cd17636 159 GGAI---GGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT--------RGGWHHTNDLGRR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 872 SAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVI--PDGPVAPDALRTELSRTL 949
Cdd:cd17636 228 EPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVlkPGASVTEAELIEHCRARI 307
|
330 340
....*....|....*....|....
gi 653678460 950 PDYMIPAVIVPVPDFPTTPNGKLD 973
Cdd:cd17636 308 ASYKKPKSVEFADALPRTAGGADD 331
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
1554-2045 |
1.71e-09 |
|
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: 62.96 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1554 DRSLTFAGLDAQANRLAHALHtgALGappVGPETPVLLLLDRSPELVVAMLAVLKAG-------GYF------------- 1613
Cdd:cd05966 82 SRTITYRELLREVCRFANVLK--SLG---VKKGDRVAIYMPMIPELVIAMLACARIGavhsvvfAGFsaesladrindaq 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1614 ----IPVDPGYPMAR---LTRIAD-------TVTPALVLTRTGqggclpgaevfGDVPVVA-LDRVADRLtaMPDQRPEV 1678
Cdd:cd05966 157 cklvITADGGYRGGKvipLKEIVDealekcpSVEKVLVVKRTG-----------GEVPMTEgRDLWWHDL--MAKQSPEC 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1679 T---VDPRGLAYSIFTSGSTGQPKGVAVEHIGivrYLSWAAASYPTAgrrgtlahssvgFDLTMSALF------------ 1743
Cdd:cd05966 224 EpewMDSEDPLFILYTSGSTGKPKGVVHTTGG---YLLYAATTFKYV------------FDYHPDDIYwctadigwitgh 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1744 -----EPLVSG------RGVTLMPADATLADLAEEL------SGPLAydyIRL------------TPSHLRHLvgHWTGQ 1794
Cdd:cd05966 289 syivyGPLANGattvmfEGTPTYPDPGRYWDIVEKHkvtifyTAPTA---IRAlmkfgdewvkkhDLSSLRVL--GSVGE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1795 ELPPAARGW---VVGGEtldpalvkqllelrpDAEVINHYGPTET---VIgrvvhpvreagelavdSPLP---------L 1859
Cdd:cd05966 364 PINPEAWMWyyeVIGKE---------------RCPIVDTWWQTETggiMI----------------TPLPgatplkpgsA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1860 GRPLGETRLQVLDAWLEAVPVGAVGELFIGGD--GIARGYLGRPALTAEKFLPDpagEPGarMYRTGDLVRWRGDGLLDF 1937
Cdd:cd05966 413 TRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDHERYEDTYFSK---FPG--YYFTGDGARRDEDGYYWI 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1938 VGRVDDQVKLRGYRIELGEIEARMAEHPGV-EQAVVLVRD----QQLVGWFIPAEDHPP--VTVSALRRFCAEQLPEFMV 2010
Cdd:cd05966 488 TGRVDDVINVSGHRLGTAEVESALVAHPAVaEAAVVGRPHdikgEAIYAFVTLKDGEEPsdELRKELRKHVRKEIGPIAT 567
|
570 580 590
....*....|....*....|....*....|....*
gi 653678460 2011 PNQWVALDAFPLTPHGKVNHRALPGPTSGRPELED 2045
Cdd:cd05966 568 PDKIQFVPGLPKTRSGKIMRRILRKIAAGEEELGD 602
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
1541-2040 |
2.43e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 62.40 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1541 ADRTPGWTAL---RTGDrSLTFAGLDAQANRLAHALHTGALgappvGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVD 1617
Cdd:PRK13391 7 AQTTPDKPAVimaSTGE-VVTYRELDERSNRLAHLFRSLGL-----KRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1618 PGYPMARLTRIADTVTPALVLTRTGQGGCLPGAEvfGDVPVVALDRVADRLTAMP---------DQRPEVTVD--PRG-- 1684
Cdd:PRK13391 81 SHLTPAEAAYIVDDSGARALITSAAKLDVARALL--KQCPGVRHRLVLDGDGELEgfvgyaeavAGLPATPIAdeSLGtd 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1685 LAYSiftSGSTGQPKGVavehigivrylswaaasyptagrRGTLAHSSVGFDLTMSALFEPLVSGRGVTLMPADATLADl 1764
Cdd:PRK13391 159 MLYS---SGTTGRPKGI-----------------------KRPLPEQPPDTPLPLTAFLQRLWGFRSDMVYLSPAPLYH- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1765 aeelSGPLAYDYI------------RLTPSHLRHLVGHWT---GQ----------ELPPAARG--------WVVGGETLD 1811
Cdd:PRK13391 212 ----SAPQRAVMLvirlggtvivmeHFDAEQYLALIEEYGvthTQlvptmfsrmlKLPEEVRDkydlssleVAIHAAAPC 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1812 PALVKQllelrpdaEVINHYGPtetVIGRVVHPVREAGELAVDSPLPLGRP-------LGEtrLQVLDAWLEAVPVGAVG 1884
Cdd:PRK13391 288 PPQVKE--------QMIDWWGP---IIHEYYAATEGLGFTACDSEEWLAHPgtvgramFGD--LHILDDDGAELPPGEPG 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1885 ELFIGGdGIARGYLGRPALTAEKFLPDPAgepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEH 1964
Cdd:PRK13391 355 TIWFEG-GRPFEYLNDPAKTAEARHPDGT------WSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITH 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1965 PGVEQAVVL-VRDQQL------VGWFIPAEDHPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRALPGPT 2037
Cdd:PRK13391 428 PKVADAAVFgVPNEDLgeevkaVVQPVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDRY 507
|
...
gi 653678460 2038 SGR 2040
Cdd:PRK13391 508 WGN 510
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
544-882 |
3.19e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 62.44 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 544 VAVLLPRSADLLVTLLAVIKAGAAYLPI-DPDFP--VERIAYLLSDARP--VLVVTDAATADR-----LGPDDITGLVVL 613
Cdd:PRK07769 82 VAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPsaILTTTDSAEGVRkffraRPAKERPRVIAV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 614 EETDTGGYPATEPPAVPAGHSAYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDRVLATTTVSFDIAGLELYL 693
Cdd:PRK07769 162 DAVPDEVGATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 694 PLRSGAGVvladadTARNPAALIDLAGRHRVTLAQA---TPTLWQAL------------VPELSGPAL-----AGIrvLV 753
Cdd:PRK07769 242 PALLGHYI------TFMSPAAFVRRPGRWIRELARKpggTGGTFSAApnfafehaaargLPKDGEPPLdlsnvKGL--LN 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 754 GGEALPAELARRLGDAGA-------EVTNMYGPTETTIWSTSGP-------------------------TSEDSIRRGSI 801
Cdd:PRK07769 314 GSEPVSPASMRKFNEAFApyglpptAIKPSYGMAEATLFVSTTPmdeeptviyvdrdelnagrfvevpaDAPNAVAQVSA 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 802 G-VPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARGYWNRPGLTAEKF-------LPDPFG---PPGTRMYRTGDLVR 870
Cdd:PRK07769 394 GkVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrLSESHAegaPDDALWVRTGDYGV 473
|
410
....*....|..
gi 653678460 871 WsAAGDLEYLGR 882
Cdd:PRK07769 474 Y-FDGELYITGR 484
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
1827-2033 |
3.28e-09 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 62.20 E-value: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1827 VINHYGPTETVIGRVVHPVReagelAVDSPLPLGRPLGETRLQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAE 1906
Cdd:PRK08751 357 LVEAYGLTETSPAACINPLT-----LKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAK 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1907 KFlpDPAGepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGV-EQAVVLVRDQQ---LVGW 1982
Cdd:PRK08751 432 VM--DADG-----WLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVlEVAAVGVPDEKsgeIVKV 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 653678460 1983 FIPAEDhPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:PRK08751 505 VIVKKD-PALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
517-976 |
5.43e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 61.56 E-value: 5.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 517 LSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAG--AAYLPIDPDFP-----VERIAYLLSDARP 589
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGlvPVPLPLPMGFGgresyIAQLRGMLASAQP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 590 VLVV--------TDAATADRLGPDDITGlvvlEETDTGGYPATEPPAVPAGHSAYVIYTSGSTGRPKGVVITRAALDNFL 661
Cdd:PRK09192 130 AAIItpdellpwVNEATHGNPLLHVLSH----AWFKALPEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 662 AAMAER-FPLTAEDR----------------VLA--TTTVSFDiaglelYLPLRsgagvvladaDTARNPAALIDLAGRH 722
Cdd:PRK09192 206 RAISHDgLKVRPGDRcvswlpfyhdmglvgfLLTpvATQLSVD------YLPTR----------DFARRPLQWLDLISRN 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 723 RVTLAQAtPTLW----------QALVP-ELSGPALAGIrvlvGGEALPAELARRLGDAGAEV-------TNMYGPTETTI 784
Cdd:PRK09192 270 RGTISYS-PPFGyelcarrvnsKDLAElDLSCWRVAGI----GADMIRPDVLHQFAEAFAPAgfddkafMPSYGLAEATL 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 785 WSTSGP----------------------TSEDSIRRGS----IGVPIDNTQVYVLDANLHPAPIGVLGELHIAGEGLARG 838
Cdd:PRK09192 345 AVSFSPlgsgivveevdrdrleyqgkavAPGAETRRVRtfvnCGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSG 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 839 YWNRPgLTAEKFLPDPFgppgtrmYRTGDLvRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVR-RAAAVVR 917
Cdd:PRK09192 425 YFRDE-ESQDVLAADGW-------LDTGDL-GYLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsGDAAAFS 495
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 653678460 918 EDRPGDLRLVAYV---IPDgPVAPDALRTELSRTLpdYMIPAV-----IVPVPDFPTTPNGKLDRAA 976
Cdd:PRK09192 496 IAQENGEKIVLLVqcrISD-EERRGQLIHALAALV--RSEFGVeaaveLVPPHSLPRTSSGKLSRAK 559
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1691-2033 |
7.35e-09 |
|
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: 60.19 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1691 TSGSTGQPKGVAVEHIGIVrYLSWAAASYPTAGRRGTLahssvgfdltMSALfePL--VSGRGVTLMPADATLADLAeeL 1768
Cdd:cd05944 10 TGGTTGTPKLAQHTHSNEV-YNAWMLALNSLFDPDDVL----------LCGL--PLfhVNGSVVTLLTPLASGAHVV--L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1769 SGPLAYDYIRLTPSHLRhLVGHWTGQELP--PAA----------------RGWVVGGETLDPALVKQLlELRPDAEVINH 1830
Cdd:cd05944 75 AGPAGYRNPGLFDNFWK-LVERYRITSLStvPTVyaallqvpvnadisslRFAMSGAAPLPVELRARF-EDATGLPVVEG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1831 YGPTETVIGRVVHPVREAGEL-AVDSPLPLGRplgeTRLQVLDA---WLEAVPVGAVGELFIGGDGIARGYL----GRPA 1902
Cdd:cd05944 153 YGLTEATCLVAVNPPDGPKRPgSVGLRLPYAR----VRIKVLDGvgrLLRDCAPDEVGEICVAGPGVFGGYLytegNKNA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1903 LTAEKFLpdpagepgarmyRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRDQQLVG- 1981
Cdd:cd05944 229 FVADGWL------------NTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGe 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 653678460 1982 ---WFIPAEDHPPVTVSALRRFCAEQLPE-FMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:cd05944 297 lpvAYVQLKPGAVVEEEELLAWARDHVPErAAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
635-904 |
8.35e-09 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 60.60 E-value: 8.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 635 AYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLTAEDRVLATT----TVSFDIAGLelyLPLRSGAGVVLadADTAR 710
Cdd:PRK06334 186 AVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLppfhAYGFNSCTL---FPLLSGVPVVF--AYNPL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 711 NPAALIDLAGRHRVTLAQATPTLWQALV--PELSGPALAGIR-VLVGGEALPAELARRLGDAGAEVT--NMYGPTETTIW 785
Cdd:PRK06334 261 YPKKIVEMIDEAKVTFLGSTPVFFDYILktAKKQESCLPSLRfVVIGGDAFKDSLYQEALKTFPHIQlrQGYGTTECSPV 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 786 STSgpTSEDSIRRGS-IGVPIDNTQVYVLDANLH-PAPIGVLGELHIAGEGLARGYW-NRPGltaEKFLpdPFGppGTRM 862
Cdd:PRK06334 341 ITI--NTVNSPKHEScVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLgEDFG---QGFV--ELG--GETW 411
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 653678460 863 YRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLI 904
Cdd:PRK06334 412 YVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILM 453
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
1956-2027 |
1.06e-08 |
|
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: 54.09 E-value: 1.06e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 653678460 1956 EIEARMAEHPGVEQ-AVVLVRD----QQLVGwFIPAEDHPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGK 2027
Cdd:pfam13193 1 EVESALVSHPAVAEaAVVGVPDelkgEAPVA-FVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
1859-2034 |
1.72e-08 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 59.62 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1859 LGRPLGETRLQVLDawleavpvGAVGELFIGGDGIARGYLgrpaltaekflpdPAGEPGARMYRTGDLVRWRGDGLLDFV 1938
Cdd:PRK07445 285 SGQVLPHAQITIPA--------NQTGNITIQAQSLALGYY-------------PQILDSQGIFETDDLGYLDAQGYLHIL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1939 GRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVL-VRD----QQLVGWFIPAedHPPVTVSALRRFCAEQLPEFMVPNQ 2013
Cdd:PRK07445 344 GRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLgLPDphwgEVVTAIYVPK--DPSISLEELKTAIKDQLSPFKQPKH 421
|
170 180
....*....|....*....|.
gi 653678460 2014 WVALDAFPLTPHGKVNHRALP 2034
Cdd:PRK07445 422 WIPVPQLPRNPQGKINRQQLQ 442
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
991-1048 |
1.82e-08 |
|
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: 53.32 E-value: 1.82e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 653678460 991 PRDDRERFLCTAFAEVLGLP--EVAVSDNFF-ELGGHSLLAFRLLARIRDEFGAGFSLRRL 1048
Cdd:COG0236 2 PREELEERLAEIIAEVLGVDpeEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTEL 62
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
1538-2033 |
2.09e-08 |
|
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: 59.31 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1538 EAQADRTPGWTALRtgdRSLTFAGLDAQANRLAHALHTGalgapPVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVD 1617
Cdd:cd05929 2 EARDLDRAQVFHQR---RLLLLDVYSIALNRNARAAAAE-----GVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1618 PGYPMARLTRIADTVTPALVLTRTGQGGCLPGAEVFgdvpvvaldrvadrlTAMPDQRPEVTVDPRGLAYSIFTS-GSTG 1696
Cdd:cd05929 74 SRAPRAEACAIIEIKAAALVCGLFTGGGALDGLEDY---------------EAAEGGSPETPIEDEAAGWKMLYSgGTTG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1697 QPKGVAVEH----IGIVRYLSWAAASYPTAGRR----GTLAHSSvGFDLTMSALFeplvSGRGVTLMP---ADATLADLA 1765
Cdd:cd05929 139 RPKGIKRGLpggpPDNDTLMAAALGFGPGADSVylspAPLYHAA-PFRWSMTALF----MGGTLVLMEkfdPEEFLRLIE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1766 EElsgplAYDYIRLTPSHLRHLVghwtgqELPPAARG----------WVVGGETldPALVKQ-LLELRPDAeVINHYGPT 1834
Cdd:cd05929 214 RY-----RVTFAQFVPTMFVRLL------KLPEAVRNaydlsslkrvIHAAAPC--PPWVKEqWIDWGGPI-IWEYYGGT 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1835 E----TVIgrvvhpvreAGELAVDSPLPLGRPLGeTRLQVLDAWLEAVPVGAVGEL-FIGGDGIArgYLGRPALTAEKFl 1909
Cdd:cd05929 280 EgqglTII---------NGEEWLTHPGSVGRAVL-GKVHILDEDGNEVPPGEIGEVyFANGPGFE--YTNDPEKTAAAR- 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1910 pdpagepGARMYRT-GDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVL-VRDQQL------VG 1981
Cdd:cd05929 347 -------NEGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVgVPDEELgqrvhaVV 419
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 653678460 1982 WFIPAEDHPPVTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:cd05929 420 QPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
1553-1980 |
2.56e-08 |
|
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: 58.99 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1553 GDRSLTFAGLDAQANRLAHALHTGalgapPVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMARLTRIADTV 1632
Cdd:cd05914 4 GGEPLTYKDLADNIAKFALLLKIN-----GVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1633 TPALVLTRtgqggclpgaevfgdvpvvaldrvadrltampdqrpevtvDPRGLAYSIFTSGSTGQPKGVAVEHIGIVRYL 1712
Cdd:cd05914 79 EAKAIFVS----------------------------------------DEDDVALINYTSGTTGNSKGVMLTYRNIVSNV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1713 SWAAASYPTAGRRGTLA----HSSVGFDLTMsalFEPLVSGRGVTLM--PADATLADLAEE-------LSGPLAYDYIRL 1779
Cdd:cd05914 119 DGVKEVVLLGKGDKILSilplHHIYPLTFTL---LLPLLNGAHVVFLdkIPSAKIIALAFAqvtptlgVPVPLVIEKIFK 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1780 T---PS-----------------HLRHLVGHWTGQELPPAARGWVVGGETLDPALVKQLLELrpDAEVINHYGPTETvig 1839
Cdd:cd05914 196 MdiiPKltlkkfkfklakkinnrKIRKLAFKKVHEAFGGNIKEFVIGGAKINPDVEEFLRTI--GFPYTIGYGMTET--- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1840 rvvhpvreagelavdSPLPLGRPLGETRL----QVLDAwLEA-----VPVGAVGELFIGGDGIARGYLGRPALTAEKFLP 1910
Cdd:cd05914 271 ---------------APIISYSPPNRIRLgsagKVIDG-VEVridspDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDK 334
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 653678460 1911 DPagepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKL-RGYRIELGEIEARMAEHPGVEQAVVLVRDQQLV 1980
Cdd:cd05914 335 DG-------WFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLV 398
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
1541-2028 |
4.22e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1541 ADRTPGWTALRTGDrSLTFAGLDAQANRLAHALHTGALGAPPVgpetpVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGY 1620
Cdd:PRK13390 10 APDRPAVIVAETGE-QVSYRQLDDDSAALARVLYDAGLRTGDV-----VALLSDNSPEALVVLWAALRSGLYITAINHHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1621 PMARLTRI-ADTVTPALVLTRTGQGgclPGAEVFGDVPVV-----ALDRVADRLTAMPDQRPEVTVDPRGlAYSIFTSGS 1694
Cdd:PRK13390 84 TAPEADYIvGDSGARVLVASAALDG---LAAKVGADLPLRlsfggEIDGFGSFEAALAGAGPRLTEQPCG-AVMLYSSGT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1695 TGQPKGVAVEHIGivryLSWAAASYPTAGRRGTLahssvgFDLTMSALF---EPLVSG---RGVTLMPADATLADLAEEL 1768
Cdd:PRK13390 160 TGFPKGIQPDLPG----RDVDAPGDPIVAIARAF------YDISESDIYyssAPIYHAaplRWCSMVHALGGTVVLAKRF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1769 SGPLAYDYI---RLTPSH--------LRHLVGHWTGQELPPAARGwVVGGETLDPALVKQLLELRPDAEVINHYGPTEtv 1837
Cdd:PRK13390 230 DAQATLGHVeryRITVTQmvptmfvrLLKLDADVRTRYDVSSLRA-VIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1838 igrvVHpvreaGELAVDSPLPLGRPLGETR-----LQVLDAWLEAVPVGAVGELFIGGDGIARGYLGRPALTAEkflpdp 1912
Cdd:PRK13390 307 ----AH-----GMTFIDSPDWLAHPGSVGRsvlgdLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAA------ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1913 AGEPGARMYRT-GDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQ-AVVLVRDQ----------QLV 1980
Cdd:PRK13390 372 AQHPAHPFWTTvGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDvAVIGVPDPemgeqvkaviQLV 451
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 653678460 1981 GWFIPAEDhppvTVSALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKV 2028
Cdd:PRK13390 452 EGIRGSDE----LARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKL 495
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
1654-2033 |
4.44e-08 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 58.82 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1654 GDVPVVALDRVADRLTAM-------PDQRPEVTV---DPRGLAYSIFTSGSTGQPKGVAVEHIGIVRYLSWAAASYPtAG 1723
Cdd:PRK06814 754 FGIRIIYLEDVRAQIGLAdkikgllAGRFPLVYFcnrDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARID-FS 832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1724 RRGT------LAHSsvgFDLTMSALFePLVSGRGVTLMP--------------ADATL-----------ADLAEelsgpl 1772
Cdd:PRK06814 833 PEDKvfnalpVFHS---FGLTGGLVL-PLLSGVKVFLYPsplhyriipeliydTNATIlfgtdtflngyARYAH------ 902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1773 AYDYIRLtpshlrhlvghwtgqelppaaRGWVVGGETLDPALVKQLLE---LRpdaeVINHYGPTETVigrvvhPVreag 1849
Cdd:PRK06814 903 PYDFRSL---------------------RYVFAGAEKVKEETRQTWMEkfgIR----ILEGYGVTETA------PV---- 947
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1850 eLAVDSPL-----PLGR--PLGETRLqvldawlEAVP-VGAVGELFIGGDGIARGYLgrpalTAEKflPDPAGEPGARMY 1921
Cdd:PRK06814 948 -IALNTPMhnkagTVGRllPGIEYRL-------EPVPgIDEGGRLFVRGPNVMLGYL-----RAEN--PGVLEPPADGWY 1012
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1922 RTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAE-HPGVEQAVVLVRDQ----QLVgWFIPAEDhppVTVSA 1996
Cdd:PRK06814 1013 DTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAElWPDALHAAVSIPDArkgeRII-LLTTASD---ATRAA 1088
|
410 420 430
....*....|....*....|....*....|....*...
gi 653678460 1997 LRRFC-AEQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:PRK06814 1089 FLAHAkAAGASELMVPAEIITIDEIPLLGTGKIDYVAV 1126
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
628-949 |
8.26e-08 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 57.08 E-value: 8.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 628 AVPAGHSAYVIYTSGSTGRPKGVVITRAALDNFLAAMAERF---PLTAEDRVLATTTVSFDIAGLELYLPL-RSGAGVVL 703
Cdd:COG1541 79 AVPLEEIVRIHASSGTTGKPTVVGYTRKDLDRWAELFARSLraaGVRPGDRVQNAFGYGLFTGGLGLHYGAeRLGATVIP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 704 AdadTARNPAALIDLAGRHRVTLAQATPTlwQAL----VPELSG--PALAGIRV-LVGGEALPAELARRLGDA-GAEVTN 775
Cdd:COG1541 159 A---GGGNTERQLRLMQDFGPTVLVGTPS--YLLylaeVAEEEGidPRDLSLKKgIFGGEPWSEEMRKEIEERwGIKAYD 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 776 MYGPTETtiwstsGPT--SEDSIRRGSIgvpIDNTQVYV--LD-ANLHPAPIGVLGEL---HIAGEG--LARgywnrpgl 845
Cdd:COG1541 234 IYGLTEV------GPGvaYECEAQDGLH---IWEDHFLVeiIDpETGEPVPEGEEGELvvtTLTKEAmpLIR-------- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 846 taekflpdpfgppgtrmYRTGDLVRWSAAGD--------LEY-LGRTDHQVKLRGFRIELGEIETTLINAGPVrRAAAVV 916
Cdd:COG1541 297 -----------------YRTGDLTRLLPEPCpcgrthprIGRiLGRADDMLIIRGVNVFPSQIEEVLLRIPEV-GPEYQI 358
|
330 340 350
....*....|....*....|....*....|....
gi 653678460 917 REDRPGDL-RLVAYVIPDGPVAPDALRTELSRTL 949
Cdd:COG1541 359 VVDREGGLdELTVRVELAPGASLEALAEAIAAAL 392
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
515-979 |
1.17e-07 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 57.27 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 515 TTLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARPVLVVT 594
Cdd:PRK10524 83 RTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPVLIVS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 595 -----------------DAATA------------DR-LGPD-DITGLVVLEETDTGGYPATEPPA--VPAGHSAYVIYTS 641
Cdd:PRK10524 163 adagsrggkvvpykpllDEAIAlaqhkprhvllvDRgLAPMaRVAGRDVDYATLRAQHLGARVPVewLESNEPSYILYTS 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 642 GSTGRPKGVVITRAALDNFLAA-MAERFPLTAEDRVLATTTV------SFDIaglelYLPLRSGAGVVLADADTAR-NPA 713
Cdd:PRK10524 243 GTTGKPKGVQRDTGGYAVALATsMDTIFGGKAGETFFCASDIgwvvghSYIV-----YAPLLAGMATIMYEGLPTRpDAG 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 714 ALIDLAGRHRVTLAQATPTLWQALvpELSGPA------LAGIRVL-VGGEALPAELARRLGDA-GAEVTNMYGPTETTiW 785
Cdd:PRK10524 318 IWWRIVEKYKVNRMFSAPTAIRVL--KKQDPAllrkhdLSSLRALfLAGEPLDEPTASWISEAlGVPVIDNYWQTETG-W 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 786 S--TSGPTSEDS-IRRGSIGVPIDNTQVYVLD-ANLHPAPIGVLGELHIAG---EGLARGYWNrpglTAEKFLPDPFGPP 858
Cdd:PRK10524 395 PilAIARGVEDRpTRLGSPGVPMYGYNVKLLNeVTGEPCGPNEKGVLVIEGplpPGCMQTVWG----DDDRFVKTYWSLF 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 859 GTRMYRTGDLVRWSAAGDLEYLGRTDHQVKLRGFRIELGEIETTLINAGPVRRAAAVVREDRPGDLRLVAYVIP------ 932
Cdd:PRK10524 471 GRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPkdsdsl 550
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 653678460 933 DGPVAPDALRTELSRTLPDYM----IPAVIVPVPDFPTTPNGKLDRAALPA 979
Cdd:PRK10524 551 ADREARLALEKEIMALVDSQLgavaRPARVWFVSALPKTRSGKLLRRAIQA 601
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
898-971 |
1.17e-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: 51.01 E-value: 1.17e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 653678460 898 EIETTLINAGPVRRAAAV-VREDRPGDlRLVAYVIPDGPVAP--DALRTELSRTLPDYMIPAVIVPVPDFPTTPNGK 971
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVgVPDELKGE-APVAFVVLKPGVELleEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1585-1949 |
2.34e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 56.28 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1585 PETPVLLLLDRSPELVVAMLAVLKAGGYFIPV-DPGYP--MARLTRIADTVTPALVLTRTGqggclpGAE----VFGDVP 1657
Cdd:PRK07769 78 PGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAILTTTD------SAEgvrkFFRARP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1658 ------VVALDRVADRLTAMPdQRPEVTVDPrgLAYSIFTSGSTGQPKGVAVEHIGI-VRYLSWAAASYPTAGRRGT--- 1727
Cdd:PRK07769 152 akerprVIAVDAVPDEVGATW-VPPEANEDT--IAYLQYTSGSTRIPAGVQITHLNLpTNVLQVIDALEGQEGDRGVswl 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1728 -LAHssvgfDLTMSALFEPLVSGRGVTLMpadatladlaeelsGPLAydYIRLTPSHLRHL--VGHWTGQELP------- 1797
Cdd:PRK07769 229 pFFH-----DMGLITVLLPALLGHYITFM--------------SPAA--FVRRPGRWIRELarKPGGTGGTFSaapnfaf 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1798 --PAARGWVVGGE-TLDPALVKQLLE---------LRPDAEVINHYGPTETVI---------------------GRVVHP 1844
Cdd:PRK07769 288 ehAAARGLPKDGEpPLDLSNVKGLLNgsepvspasMRKFNEAFAPYGLPPTAIkpsygmaeatlfvsttpmdeePTVIYV 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1845 VREagELA------VDSPLPLGRPLGETRLQVLDAWLEAV--------PVGAVGELFIGGDGIARGYLGRPALTAEKF-- 1908
Cdd:PRK07769 368 DRD--ELNagrfveVPADAPNAVAQVSAGKVGVSEWAVIVdpetaselPDGQIGEIWLHGNNIGTGYWGKPEETAATFqn 445
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 653678460 1909 -----LPDPAGE---PGARMYRTGDLVRWRgDGLLDFVGRVDDQVKLRG 1949
Cdd:PRK07769 446 ilksrLSESHAEgapDDALWVRTGDYGVYF-DGELYITGRVKDLVIIDG 493
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
1861-2033 |
2.63e-07 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 56.01 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1861 RPLGETRLQVLDAwLEAVPVGA----VGELFIGGDGIARGYLGRPALTAEKFlpdpagepGARMYRTGDLVRWRGDGLLD 1936
Cdd:PLN02479 377 RYIGLEGLDVVDT-KTMKPVPAdgktMGEIVMRGNMVMKGYLKNPKANEEAF--------ANGWFHSGDLGVKHPDGYIE 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1937 FVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVR-DQQlvgW------FIPAED-----HPPVTVSALRRFCAEQ 2004
Cdd:PLN02479 448 IKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARpDER---WgespcaFVTLKPgvdksDEAALAEDIMKFCRER 524
|
170 180
....*....|....*....|....*....
gi 653678460 2005 LPEFMVPNQwVALDAFPLTPHGKVNHRAL 2033
Cdd:PLN02479 525 LPAYWVPKS-VVFGPLPKTATGKIQKHVL 552
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
1689-2033 |
2.69e-07 |
|
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: 56.00 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1689 IFTSGSTGQPKGVAVEHIGIVRYLSwaAASYPTAGRR--------------------GTLAHSSVGFDLTMSALFEPLVS 1748
Cdd:cd17642 190 MNSSGSTGLPKGVQLTHKNIVARFS--HARDPIFGNQiipdtailtvipfhhgfgmfTTLGYLICGFRVVLMYKFEEELF 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1749 GRGV------------TLMP--ADATLADlaeelsgplAYDYirltpSHLRHLVGhwtgqelppaargwvvGGETLDPAL 1814
Cdd:cd17642 268 LRSLqdykvqsallvpTLFAffAKSTLVD---------KYDL-----SNLHEIAS----------------GGAPLSKEV 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1815 VKQLLELRPDAEVINHYGPTETVIGRVVHPVREagelavDSPLPLGR--PLGETRLQVLDAWlEAVPVGAVGELFIGGDG 1892
Cdd:cd17642 318 GEAVAKRFKLPGIRQGYGLTETTSAILITPEGD------DKPGAVGKvvPFFYAKVVDLDTG-KTLGPNERGELCVKGPM 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1893 IARGYLGRPALTAEkfLPDPAGepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVV 1972
Cdd:cd17642 391 IMKGYVNNPEATKA--LIDKDG-----WLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGV 463
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1973 L-VRDQ---QLVGWFIPAEDHPPVTVSALRRFCAEQLPefmvPNQW-----VALDAFPLTPHGKVNHRAL 2033
Cdd:cd17642 464 AgIPDEdagELPAAVVVLEAGKTMTEKEVMDYVASQVS----TAKRlrggvKFVDEVPKGLTGKIDRRKI 529
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
513-653 |
4.27e-07 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 55.38 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 513 GDTTLSYRELDERANRLAR-LLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLLSDARPVL 591
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARaLLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 592 VVTDAATADRLGP-------DDITGLVVLEETDTGGY-------PATEPPAVPAGHSAYV--------IYTSGSTGRPKG 649
Cdd:cd05938 82 LVVAPELQEAVEEvlpalraDGVSVWYLSHTSNTEGVislldkvDAASDEPVPASLRAHVtikspalyIYTSGTTGLPKA 161
|
....
gi 653678460 650 VVIT 653
Cdd:cd05938 162 ARIS 165
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
1533-2033 |
4.55e-07 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 54.99 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1533 VHQLVEAQADRTPGWTALrTGdRSLTFAGLDAQANRLAHALHTGALGAPPVgpetpVLLLLDRSPELVVAMLAVLKAGGY 1612
Cdd:PLN02330 34 VLQDAELYADKVAFVEAV-TG-KAVTYGEVVRDTRRFAKALRSLGLRKGQV-----VVVVLPNVAEYGIVALGIMAAGGV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1613 FIPVDPGYPMARLTRIADTVTPALVLTRTGQGGCLPGAEVfgdvPVVALDRV--------------ADRLTAMPDQRPEV 1678
Cdd:PLN02330 107 FSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGLGL----PVIVLGEEkiegavnwkelleaADRAGDTSDNEEIL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1679 TVDPRGLAysiFTSGSTGQPKGVAVEHIGIVRYL--SWAAASYPTAGRRGTLAHSSVGFDLTMSALFEPLVSGRGVTLMP 1756
Cdd:PLN02330 183 QTDLCALP---FSSGTTGISKGVMLTHRNLVANLcsSLFSVGPEMIGQVVTLGLIPFFHIYGITGICCATLRNKGKVVVM 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1757 ADATL-----ADLAEELSgplaydYIRLTPSHLRHLVGHWTGQELPPAA---RGWVVGGETLDPALVKQLLELRPDAEVI 1828
Cdd:PLN02330 260 SRFELrtflnALITQEVS------FAPIVPPIILNLVKNPIVEEFDLSKlklQAIMTAAAPLAPELLTAFEAKFPGVQVQ 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1829 NHYGPTETVIGRVVHPVREAGE-LAVDSPLPLGRPLGETRLQVLDAWLeAVPVGAVGELFIGGDGIARGYLGRPALTAEK 1907
Cdd:PLN02330 334 EAYGLTEHSCITLTHGDPEKGHgIAKKNSVGFILPNLEVKFIDPDTGR-SLPKNTPGELCVRSQCVMQGYYNNKEETDRT 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1908 FlpDPAGepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRDQQLVGWfIPAe 1987
Cdd:PLN02330 413 I--DEDG-----WLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGE-IPA- 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 653678460 1988 dhPPVTVSALRRFCAEQLPEFMVPN----------QWValDAFPLTPHGKVNHRAL 2033
Cdd:PLN02330 484 --ACVVINPKAKESEEDILNFVAANvahykkvrvvQFV--DSIPKSLSGKIMRRLL 535
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1548-2032 |
5.57e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 55.00 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1548 TALRTGDRSLTFAGLDA-----------QANRLAhalhtGALGAPPVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPV 1616
Cdd:PRK07768 10 ANARTSPRGMVTGEPDApvrhtwgevheRARRIA-----GGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTML 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1617 DPGYPMARLTR-IADTVTpalVLTRTGQGGCLPGAEVFGDVPV-----VALDRVADRLTAMPDQRPEVTVDprGLAYSIF 1690
Cdd:PRK07768 85 HQPTPRTDLAVwAEDTLR---VIGMIGAKAVVVGEPFLAAAPVleekgIRVLTVADLLAADPIDPVETGED--DLALMQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1691 TSGSTGQPKGVAVEHIGIvrylsWAAASYPTAGrrgtlAHSSVGFDLTMSALfePLVSGRGVT---LMP----ADATLAD 1763
Cdd:PRK07768 160 TSGSTGSPKAVQITHGNL-----YANAEAMFVA-----AEFDVETDVMVSWL--PLFHDMGMVgflTVPmyfgAELVKVT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1764 LAEELSGPLAY----DYIRLT----PSHLRHLVGHWTGQELPPAA------RGWVVGGETLDPALVKQLLE------LRP 1823
Cdd:PRK07768 228 PMDFLRDPLLWaeliSKYRGTmtaaPNFAYALLARRLRRQAKPGAfdlsslRFALNGAEPIDPADVEDLLDagarfgLRP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1824 DAeVINHYGPTETVI---------GRVVHPVR----EAGELAVDSPLP-------LGRPLGETRLQVLDAWLEAVPVGAV 1883
Cdd:PRK07768 308 EA-ILPAYGMAEATLavsfspcgaGLVVDEVDadllAALRRAVPATKGntrrlatLGPPLPGLEVRVVDEDGQVLPPRGV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1884 GELFIGGDGIARGYlgrpaLTAEKFLP--DPAGepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARM 1961
Cdd:PRK07768 387 GVIELRGESVTPGY-----LTMDGFIPaqDADG-----WLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAA 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1962 AEHPGVEQ----AVVLVRDQQLVGWFIPAE---DHPPVTVSALRR-FCAEQLPEFMV-PNQWVALDA--FPLTPHGKVNH 2030
Cdd:PRK07768 457 ARVEGVRPgnavAVRLDAGHSREGFAVAVEsnaFEDPAEVRRIRHqVAHEVVAEVGVrPRNVVVLGPgsIPKTPSGKLRR 536
|
..
gi 653678460 2031 RA 2032
Cdd:PRK07768 537 AN 538
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1879-1998 |
7.45e-07 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 54.75 E-value: 7.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1879 PVGAVGELFIGGDGIARGYLGRPALTAEKF-----LPDPAG------EPGARMYRTGDLVRWRgDGLLDFVGRVDDQVKL 1947
Cdd:PRK12476 425 PDGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqSRLAEGshadgaADDGTWLRTGDLGVYL-DGELYITGRIADLIVI 503
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 653678460 1948 RGYRIELGEIEARMAEhpgveqAVVLVRDQQLVGWFIPAEDHPPVTVSALR 1998
Cdd:PRK12476 504 DGRNHYPQDIEATVAE------ASPMVRRGYVTAFTVPAEDNERLVIVAER 548
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
1070-1607 |
1.07e-06 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 54.49 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1070 DAVHLAPVPRDEPLPLSPMQ-ESIWLADQVSAGDSVYNVPLALRLIGPLDRGALRRTLNRVVDRHEMLRTRIHPGPDGMP 1148
Cdd:COG3321 850 SALYPGRGRRRVPLPTYPFQrEDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAAL 929
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1149 VQVADPAGGGAALTERDAAPGTDLAQLLLAEAALGFTLATEHPLR--AVLWRLDEREHVLLLTAHHVAVDAWSMDLIQRD 1226
Cdd:COG3321 930 LALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAaaAAAAAAAAAAAAAAAAAAALAAAAALALLAAAA 1009
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1227 LTELYAADTGHREPELDEPALAQADYAVWQRQSAQRGRYAAELDFWRTELTGAVATEVAGDLPRPATPGGGGGAVEFALA 1306
Cdd:COG3321 1010 LLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAA 1089
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1307 PRQIQGIRELARRCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGRGNPRLDnLVGCLVNTVVLRGDLSGAPTFHELL 1386
Cdd:COG3321 1090 LAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAA-AAAAAALALAAAAAALAAALAAALL 1168
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1387 RRTHARTADALAHQELPFEHLVADRGAGNGPLFRimysfsSQEPAGRSAGDVDLEPVPVPVTTCKFDLVLTVVDGGSTLE 1466
Cdd:COG3321 1169 AAAALLLALALALAAALAAALAGLAALLLAALLA------ALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAA 1242
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1467 GVLEYADDLYLPGTAERLVTSLTNLLAAAVRTPELAVTRLAITSESDTVRTSRWGRSEQHVGDDRTVHQLVEAQADRTPG 1546
Cdd:COG3321 1243 AAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALA 1322
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 653678460 1547 WTALRTGDRSLTFAGLDAQANRLAHALHTGALGAPPVGPETPVLLLLDRSPELVVAMLAVL 1607
Cdd:COG3321 1323 AALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAA 1383
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
516-921 |
1.84e-06 |
|
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: 53.20 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 516 TLSYRELDERANRLARLLMERGAGAETFVAVLLPRSADLLVTLLAVIKAGAAYLPIDPDFPVERIAYLL--SDARpVLVV 593
Cdd:cd17641 11 EFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLnyTGAR-VVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 594 TDAATADRLGP--DDITGL---VVLEETDTGGY------------------PATEP----PAVPAGH---SAYVIYTSGS 643
Cdd:cd17641 90 EDEEQVDKLLEiaDRIPSVryvIYCDPRGMRKYddprlisfedvvalgralDRRDPglyeREVAAGKgedVAVLCTTSGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 644 TGRPKGVVITRAALDNFLAAMAERFPLTAEDRVLAT--------------------TTVSF------------DIAGLEL 691
Cdd:cd17641 170 TGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVlplpwigeqmysvgqalvcgFIVNFpeepetmmedlrEIGPTFV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 692 YLPLRSGAGVvLAD-----ADTARNPAALIDLA-GRHRVTLAQ----ATPTLWQALVPELSGPALAGI-----------R 750
Cdd:cd17641 250 LLPPRVWEGI-AADvrarmMDATPFKRFMFELGmKLGLRALDRgkrgRPVSLWLRLASWLADALLFRPlrdrlgfsrlrS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 751 VLVGGEALPAELARRLGDAGAEVTNMYGPTETTIWSTSGPTseDSIRRGSIGVPIDNTQVYVLDAnlhpapigvlGELHI 830
Cdd:cd17641 329 AATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRD--GDVDPDTVGVPFPGTEVRIDEV----------GEILV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 831 AGEGLARGYWNRPGLTAEKFLPDPFgppgtrmYRTGDLVRWSAAGDLEYLGRTDHQVKL-RGFRIELGEIETTLiNAGPV 909
Cdd:cd17641 397 RSPGVFVGYYKNPEATAEDFDEDGW-------LHTGDAGYFKENGHLVVIDRAKDVGTTsDGTRFSPQFIENKL-KFSPY 468
|
490
....*....|..
gi 653678460 910 RRAAAVVREDRP 921
Cdd:cd17641 469 IAEAVVLGAGRP 480
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
605-903 |
2.34e-06 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 52.63 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 605 DDITGLVVLEETDTGGYPATEPPAVPAGHSAYVIYTSGSTGRPKGVVITRAALDNFLAAMA---ERFPLTAEDRVLATTT 681
Cdd:cd05913 51 DDLRKLPFTTKEDLRDNYPFGLFAVPREKVVRIHASSGTTGKPTVVGYTKNDLDVWAELVArclDAAGVTPGDRVQNAYG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 682 VSFDIAGLELYLPL-RSGAGVVLADA-DTARNPAALIDLagrhRVTLAQATPTLWQALVPELS----GPALAGIRV-LVG 754
Cdd:cd05913 131 YGLFTGGLGFHYGAeRLGALVIPAGGgNTERQLQLIKDF----GPTVLCCTPSYALYLAEEAEeegiDPRELSLKVgIFG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 755 GEALPAELARRLGDA-GAEVTNMYGPTETTiwstsGP-TSEDSIRRGSIGVPIDNTQVYVLD-ANLHPAPIGVLGELHIA 831
Cdd:cd05913 207 AEPWTEEMRKRIERRlGIKAYDIYGLTEII-----GPgVAFECEEKDGLHIWEDHFIPEIIDpETGEPVPPGEVGELVFT 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 832 geglargywnrpGLTAEkflpdpfGPPGTRmYRTGDLVR--WSAAG-------DLEYLGRTDHQVKLRGFRIELGEIETT 902
Cdd:cd05913 282 ------------TLTKE-------AMPLIR-YRTRDITRllPGPCPcgrthrrIDRITGRSDDMLIIRGVNVFPSQIEDV 341
|
.
gi 653678460 903 L 903
Cdd:cd05913 342 L 342
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
1691-1974 |
2.71e-06 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 52.46 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1691 TSGSTGQPKGVAVEHIGIVRylsWA---AASYPTAG-RRGTLAHSSVGFDLTMSALFepLVSG---RGVTLMPA-----D 1758
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDLDR---WAelfARSLRAAGvRPGDRVQNAFGYGLFTGGLG--LHYGaerLGATVIPAgggntE 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1759 ATLaDLAEELsGPlayDYIRLTPSHLRHLVGHWTGQELPPAA---RGWVVGGETLDPALVKQLLElRPDAEVINHYGPTE 1835
Cdd:COG1541 166 RQL-RLMQDF-GP---TVLVGTPSYLLYLAEVAEEEGIDPRDlslKKGIFGGEPWSEEMRKEIEE-RWGIKAYDIYGLTE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1836 TVIGrvvhpvreageLAVDSPLPLGRPLGETRL--QVLD-AWLEAVPVGAVGELFIggdgiargylgrPALTAEKFlpdp 1912
Cdd:COG1541 240 VGPG-----------VAYECEAQDGLHIWEDHFlvEIIDpETGEPVPEGEEGELVV------------TTLTKEAM---- 292
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 653678460 1913 agePGARmYRTGDLVRWRGDGL--------LDFV-GRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLV 1974
Cdd:COG1541 293 ---PLIR-YRTGDLTRLLPEPCpcgrthprIGRIlGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIV 359
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
1557-1972 |
4.09e-06 |
|
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: 52.09 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1557 LTFAGLDAQANRLAHALHtgALGAPPvgpETPVLLLLDRSPELVVAMLAVLKAGGYFIPVdpgYPmarlTRIADTVtpAL 1636
Cdd:cd05932 7 FTWGEVADKARRLAAALR--ALGLEP---GSKIALISKNCAEWFITDLAIWMAGHISVPL---YP----TLNPDTI--RY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1637 VLTRTGQGGCLPG---------AEVFGDVPVVAL--------DRVADRLTAM-PDQRPEVTVDPRGLAYSIFTSGSTGQP 1698
Cdd:cd05932 73 VLEHSESKALFVGklddwkamaPGVPEGLISISLpppsaancQYQWDDLIAQhPPLEERPTRFPEQLATLIYTSGTTGQP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1699 KGV-------------AVEHIGIV---RYLSWAAasyptagrrgtLAHSSVGFDLTMSALFEplvsgrGVTLMpadatla 1762
Cdd:cd05932 153 KGVmltfgsfawaaqaGIEHIGTEendRMLSYLP-----------LAHVTERVFVEGGSLYG------GVLVA------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1763 dLAEELSGPLAyDYIRLTPSHLRHLvghwtgqelppaARGWVVGGETLDPALVKQLLELRPDAEVINhygpteTVIGRVV 1842
Cdd:cd05932 209 -FAESLDTFVE-DVQRARPTLFFSV------------PRLWTKFQQGVQDKIPQQKLNLLLKIPVVN------SLVKRKV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1843 HP------VREAGELAvdSPLPLG-----RPLGetrLQVLDAWL----------------------EAVP-----VGAVG 1884
Cdd:cd05932 269 LKglgldqCRLAGCGS--APVPPAllewyRSLG---LNILEAYGmtenfayshlnypgrdkigtvgNAGPgvevrISEDG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1885 ELFIGGDGIARGYLGRPALTAEKFLPDPagepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKL-RGYRIELGEIEARMAE 1963
Cdd:cd05932 344 EILVRSPALMMGYYKDPEATAEAFTADG-------FLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAE 416
|
....*....
gi 653678460 1964 HPGVEQAVV 1972
Cdd:cd05932 417 HDRVEMVCV 425
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
2139-2288 |
9.17e-06 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 49.23 E-value: 9.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 2139 GHTGTTRTVVTLRGEGDGRP-VFCVHPSGGGVAWYLPLARAL-PAGHPVHAFQPLGMDGREAPAETIEDMAAgYLADLRL 2216
Cdd:COG2267 10 TRDGLRLRGRRWRPAGSPRGtVVLVHGLGEHSGRYAELAEALaAAGYAVLAFDLRGHGRSDGPRGHVDSFDD-YVDDLRA 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 653678460 2217 V------QPEGPYVVVGWSLGGTIAfemARQLDRLGEPVQ-LILLEPTLPEvartiDLHRPARDSYLRGADLAERILRL 2288
Cdd:COG2267 89 AldalraRPGLPVVLLGHSMGGLIA---LLYAARYPDRVAgLVLLAPAYRA-----DPLLGPSARWLRALRLAEALARI 159
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
600-976 |
4.58e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 48.61 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 600 DRLGPDDiTGLVVLEETDTGGYPATEP-PAVPAGHSAYVIYTSGSTGRPKGVVITRAALDNFLAAMAERFPLT-AEDRVL 677
Cdd:PRK05851 120 ERLRAVD-SSVTVHDLATAAHTNRSASlTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDaATDVGC 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 678 A----------TTTVSFDIAGLELYL---------PLR-------SGAGVVLAdadtarnPAALIDLAGRHrvtlaqatp 731
Cdd:PRK05851 199 SwlplyhdmglAFLLTAALAGAPLWLapttafsasPFRwlswlsdSRATLTAA-------PNFAYNLIGKY--------- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 732 tlwqalVPELSGPALAGIRV-LVGGEALPAELARRLG--------DAGAeVTNMYGPTETTIWST-SGP---------TS 792
Cdd:PRK05851 263 ------ARRVSDVDLGALRVaLNGGEPVDCDGFERFAtamapfgfDAGA-AAPSYGLAESTCAVTvPVPgiglrvdevTT 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 793 ED--SIRRGSI-GVPIDNTQVYVlDANLHPAPIGV--LGELHIAGEGLARGYWNRPGLTAEKFLPdpfgppgtrmyrTGD 867
Cdd:PRK05851 336 DDgsGARRHAVlGNPIPGMEVRI-SPGDGAAGVAGreIGEIEIRGASMMSGYLGQAPIDPDDWFP------------TGD 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 868 LVRWSAAGdLEYLGRTDHQVKLRGFRIELGEIETTlinAGPVR--RAAAVV------REDRPGDLRLVAYVIPDGPVApd 939
Cdd:PRK05851 403 LGYLVDGG-LVVCGRAKELITVAGRNIFPTEIERV---AAQVRgvREGAVVavgtgeGSARPGLVIAAEFRGPDEAGA-- 476
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 653678460 940 alRTELSRTLPDY--MIPAVIVPVP--DFPTTPNGKLDRAA 976
Cdd:PRK05851 477 --RSEVVQRVASEcgVVPSDVVFVApgSLPRTSSGKLRRLA 515
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
1598-1949 |
5.52e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 48.40 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1598 ELVVAMLAVLKAGgyFIPVDPGYPMARLT--RI----ADTvTPALVLT------RTGQGGCLPGAEVfgDVPVVALDRVA 1665
Cdd:PRK05850 71 EYIVAFLGALQAG--LIAVPLSVPQGGAHdeRVsavlRDT-SPSVVLTtsavvdDVTEYVAPQPGQS--APPVIEVDLLD 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1666 drltamPDQRPEVTVDPRGL---AYSIFTSGSTGQPKGVAVEHIG-IVRYLSWAAASYPTAGRRGTLAHSSVGF-----D 1736
Cdd:PRK05850 146 ------LDSPRGSDARPRDLpstAYLQYTSGSTRTPAGVMVSHRNvIANFEQLMSDYFGDTGGVPPPDTTVVSWlpfyhD 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1737 L-TMSALFEPLVSGRGVTLMPADATLADLAEelsgplaydYIRLTPSHLRHlvghWT-----GQELppAAR--------- 1801
Cdd:PRK05850 220 MgLVLGVCAPILGGCPAVLTSPVAFLQRPAR---------WMQLLASNPHA----FSaapnfAFEL--AVRktsdddmag 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1802 -------GWVVGGETLDPALVKQLLE------LRPDAeVINHYGPTE-TV---IGRVVHP---VR-EAGEL----AVDSP 1856
Cdd:PRK05850 285 ldlggvlGIISGSERVHPATLKRFADrfapfnLRETA-IRPSYGLAEaTVyvaTREPGQPpesVRfDYEKLsaghAKRCE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1857 LPLGRPL---GETRLQVL-----DAWLEAvPVGAVGELFIGGDGIARGYLGRPALTAEKF---LPDP-AGEPGARMYRTG 1924
Cdd:PRK05850 364 TGGGTPLvsyGSPRSPTVrivdpDTCIEC-PAGTVGEIWVHGDNVAAGYWQKPEETERTFgatLVDPsPGTPEGPWLRTG 442
|
410 420
....*....|....*....|....*.
gi 653678460 1925 DL-VRWrgDGLLDFVGRVDDQVKLRG 1949
Cdd:PRK05850 443 DLgFIS--EGELFIVGRIKDLLIVDG 466
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
2159-2306 |
6.32e-05 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 46.70 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 2159 VFCVHpsgGGVAWYLPLARALPAGHPVHAFQPLGMDGREAPAETIEDMAAgYLADLRLVQPEGPYVVVGWSLGGTIAFEM 2238
Cdd:pfam12697 1 VVLVH---GAGLSAAPLAALLAAGVAVLAPDLPGHGSSSPPPLDLADLAD-LAALLDELGAARPVVLVGHSLGGAVALAA 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 653678460 2239 ARQLDRLGepvqlILLEPT---LPEVARTIDLHRP-----ARDSYLRGADLAERILRLPAGDPEGDRLRAELTRLL 2306
Cdd:pfam12697 77 AAAALVVG-----VLVAPLaapPGLLAALLALLARlgaalAAPAWLAAESLARGFLDDLPADAEWAAALARLAALL 147
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
1226-1773 |
1.09e-04 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 47.94 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1226 DLTELYAADTGHRepeLDEPAlaqadYAvWQRQSAQRGRYAAELdfwRTELTGAVATEVAGDLPRPATPGGGGGAVEFAL 1305
Cdd:COG3321 848 DWSALYPGRGRRR---VPLPT-----YP-FQREDAAAALLAAAL---AAALAAAAALGALLLAALAAALAAALLALAAAA 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1306 APRQIQGIRELARRCGTTVSTVVLSALQTLLYRITGGADVVIGSTVSGRGNPRLDNLVGCLVNTVVLRGDLSGAPTFHEL 1385
Cdd:COG3321 916 AAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAA 995
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1386 LRRTHARTADALAHQELPFEHLVADRGAGNGPLFRimysfsSQEPAGRSAGDVDLEPVPVPVTTCKFDLVLTVVDGGSTL 1465
Cdd:COG3321 996 LAAAAALALLAAAALLLAAAAAAAALLALAALLAA------AAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALL 1069
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1466 EGVLEYADDLYLPGTAERLVTSLTNLLAAAVRTPELAVTRLAITSESDTVRTSRWGRSEQHVGDDRTVHQLVEAQADRTP 1545
Cdd:COG3321 1070 LLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAA 1149
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1546 GWTALRTGDRSLTFAGLDAQANRLAHALHTGALGAPPVGPETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDPGYPMARL 1625
Cdd:COG3321 1150 LALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAA 1229
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1626 TRIADTVTPALVLTRTGQGGCLPGAEVFGDVPVVALDRVADRLTAMPDQRPEVTVDPRGLAYSIFTSGSTGQPKGVAVEH 1705
Cdd:COG3321 1230 AAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAA 1309
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 653678460 1706 IGIVRYLSWAAASYPTAGRRGTLAHSSVGFDLTMSALFEPLVSGRGVTLMPADATLADLAEELSGPLA 1773
Cdd:COG3321 1310 AAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALA 1377
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
2158-2305 |
1.23e-04 |
|
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
Pssm-ID: 395444 [Multi-domain] Cd Length: 245 Bit Score: 45.96 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 2158 PVFCVHPSGGGVA--WYlPLARAL-PAGHPVHAFQPLGMdGREAPAETIEDMAAGYLAD--LRLVQPEG--PYVVVGWSL 2230
Cdd:pfam00561 1 PPVLLLHGLPGSSdlWR-KLAPALaRDGFRVIALDLRGF-GKSSRPKAQDDYRTDDLAEdlEYILEALGleKVNLVGHSM 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 653678460 2231 GGTIAFEMARQLDrlgEPVQ-LILLEPTLPEVArTIDLHRPARDSYLRGAD-LAERILRLPAGDPEGDRLRAELTRL 2305
Cdd:pfam00561 79 GGLIALAYAAKYP---DRVKaLVLLGALDPPHE-LDEADRFILALFPGFFDgFVADFAPNPLGRLVAKLLALLLLRL 151
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
1542-1701 |
1.37e-04 |
|
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: 47.04 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1542 DRTpgWTALRTGD---RSLTFAGLDAQANRLAHALHTGALGAppvgpETPVLLLLDRSPELVVAMLAVLKAGGYFIPVDP 1618
Cdd:cd05921 10 DRT--WLAEREGNggwRRVTYAEALRQVRAIAQGLLDLGLSA-----ERPLLILSGNSIEHALMALAAMYAGVPAAPVSP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1619 GYPM-----ARLTRIADTVTPALVLTRTGQ--GGCLpGAEVFGDVPVVALDR-VADR-------------LTAMPDQRPE 1677
Cdd:cd05921 83 AYSLmsqdlAKLKHLFELLKPGLVFAQDAApfARAL-AAIFPLGTPLVVSRNaVAGRgaisfaelaatppTAAVDAAFAA 161
|
170 180
....*....|....*....|....
gi 653678460 1678 VTvdPRGLAYSIFTSGSTGQPKGV 1701
Cdd:cd05921 162 VG--PDTVAKFLFTSGSTGLPKAV 183
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
1831-1984 |
1.70e-04 |
|
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: 47.03 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1831 YGPTETVIGRVVHPvreAGELAVDSplpLGRPLGETrlqvldawleAVPVGAVGELFIGGDGIARGYLGRPALTAEKFLP 1910
Cdd:cd17641 355 YGQTELAGAYTVHR---DGDVDPDT---VGVPFPGT----------EVRIDEVGEILVRSPGVFVGYYKNPEATAEDFDE 418
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 653678460 1911 DpagepgaRMYRTGDLVRWRGDGLLDFVGRVDDQVKL-RGYRIELGEIEARMAEHPGVEQAVVLVRDQQLVGWFI 1984
Cdd:cd17641 419 D-------GWLHTGDAGYFKENGHLVVIDRAKDVGTTsDGTRFSPQFIENKLKFSPYIAEAVVLGAGRPYLTAFI 486
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
1691-1968 |
2.19e-04 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 46.08 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1691 TSGSTGQPKGVAVEHIGIvRYLSWAAASYPTA--GRRGTLAHSSVGFDLTMSALfePLVSG---RGVTLMPADATLADLA 1765
Cdd:cd05913 86 SSGTTGKPTVVGYTKNDL-DVWAELVARCLDAagVTPGDRVQNAYGYGLFTGGL--GFHYGaerLGALVIPAGGGNTERQ 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1766 EELSGPLAYDYIRLTPSHLRHLV-----GHWTGQELPPaaRGWVVGGETLDPALvKQLLELRPDAEVINHYGPTETVIGR 1840
Cdd:cd05913 163 LQLIKDFGPTVLCCTPSYALYLAeeaeeEGIDPRELSL--KVGIFGAEPWTEEM-RKRIERRLGIKAYDIYGLTEIIGPG 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1841 VVHPVREAGELAVDSPLPLgrplgetrLQVLD-AWLEAVPVGAVGELFIggdgiargylgrPALTAEkflpdpaGEPGAR 1919
Cdd:cd05913 240 VAFECEEKDGLHIWEDHFI--------PEIIDpETGEPVPPGEVGELVF------------TTLTKE-------AMPLIR 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 653678460 1920 mYRTGDLVRWRGDG---------LLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVE 1968
Cdd:cd05913 293 -YRTRDITRLLPGPcpcgrthrrIDRITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLG 349
|
|
| PRK09294 |
PRK09294 |
phthiocerol/phthiodiolone dimycocerosyl transferase; |
73-207 |
2.58e-04 |
|
phthiocerol/phthiodiolone dimycocerosyl transferase;
Pssm-ID: 181765 [Multi-domain] Cd Length: 416 Bit Score: 45.86 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 73 LAVRLTGPLDVDALRAALDAVTARHEALRTVFRLGPDGEPVQQTAPAAPVALPVIDvTEADLPQAlrtaaeqPFDLERGP 152
Cdd:PRK09294 26 YTAHLRGVLDIDALSDAFDALLRAHPVLAAHLEQDSDGGWELVADDLLHPGIVVVD-GDAARPLP-------ELQLDQGV 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 653678460 153 LLRACLHRIGAKQHVLLVTVHHIVLDGWSCGLLLADLARAYAGELPAGVAAPAFR 207
Cdd:PRK09294 98 SLLALDVVPDDGGARVTLYIHHSIADAHHSASLLDELWSRYTDVVTTGDPGPIRP 152
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
777-905 |
2.59e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 46.25 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 777 YGPTETTiwstsGP---TSEDSIRRGSIGVPID-NTQVYVLDANLHPAPiGVL--GELHIAGEGLARGYWNRPGLTAEKF 850
Cdd:PTZ00342 493 YGLTETT-----GPifvQHADDNNTESIGGPISpNTKYKVRTWETYKAT-DTLpkGELLIKSDSIFSGYFLEKEQTKNAF 566
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 653678460 851 LPDPFgppgtrmYRTGDLVRWSAAGDLEYLGRTDHQVKLrgfriELGE-IETTLIN 905
Cdd:PTZ00342 567 TEDGY-------FKTGDIVQINKNGSLTFLDRSKGLVKL-----SQGEyIETDMLN 610
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
2132-2240 |
2.60e-04 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 45.71 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 2132 LDTVFGAGHTGTT--RTVVTLR-GEGDGRPVFCVHPSGGGVAWYLPLARALPAGHPVHAFQpL---GMDGREAPAETIED 2205
Cdd:PRK14875 104 EEDAGPAPRKARIggRTVRYLRlGEGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALD-LpghGASSKAVGAGSLDE 182
|
90 100 110
....*....|....*....|....*....|....*
gi 653678460 2206 MAAGYLADLRLVQPEgPYVVVGWSLGGTIAFEMAR 2240
Cdd:PRK14875 183 LAAAVLAFLDALGIE-RAHLVGHSMGGAVALRLAA 216
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
1915-2033 |
6.52e-04 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 44.89 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1915 EPGARMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVLVRDQQLVGW----FIPAEDHP 1990
Cdd:PLN02654 509 KPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQgiyaFVTLVEGV 588
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 653678460 1991 PVTV---SALRRFCAEQLPEFMVPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:PLN02654 589 PYSEelrKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
1553-1710 |
6.86e-04 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 44.97 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1553 GDRSLTFAGLDAQANRLAHALHTgalgAPPVGPETPVLLLLDRSPELVVAMLAVLKAggyfipvdpGYPMARL------- 1625
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLA----HAGLRPGDTVALLLGNEPAFLWIWLGLAKL---------GCPVAFLntnirsk 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1626 -----------------TRIADTVTPALVLTRTGqggclpGAEVF---GDVPVVALDRVADRLTAMPDQRP----EVTVD 1681
Cdd:cd05938 69 sllhcfrccgakvlvvaPELQEAVEEVLPALRAD------GVSVWylsHTSNTEGVISLLDKVDAASDEPVpaslRAHVT 142
|
170 180
....*....|....*....|....*....
gi 653678460 1682 PRGLAYSIFTSGSTGQPKGVAVEHIGIVR 1710
Cdd:cd05938 143 IKSPALYIYTSGTTGLPKAARISHLRVLQ 171
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
1870-2028 |
8.70e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 44.55 E-value: 8.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1870 VLD-AWLEAVPVGA--VGELFIGGDGIARGYLGRPALTAEKFlpdpAGEpgarMYRTGDLVRWRGDGLLDFVGRVDDQVK 1946
Cdd:PRK08162 372 VLDpDTMQPVPADGetIGEIMFRGNIVMKGYLKNPKATEEAF----AGG----WFHTGDLAVLHPDGYIKIKDRSKDIII 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1947 LRGYRIELGEIEARMAEHPGVEQAVVLVR-DQQlvgW------FIPAEDHPPVTVSALRRFCAEQLPEFMVPNQwVALDA 2019
Cdd:PRK08162 444 SGGENISSIEVEDVLYRHPAVLVAAVVAKpDPK---WgevpcaFVELKDGASATEEEIIAHCREHLAGFKVPKA-VVFGE 519
|
....*....
gi 653678460 2020 FPLTPHGKV 2028
Cdd:PRK08162 520 LPKTSTGKI 528
|
|
| bioH |
TIGR01738 |
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ... |
2154-2239 |
9.88e-04 |
|
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for the production of pimeloyl-coenzyme A, the substrate of the BioF protein early in the biosynthesis of biotin. Its exact function is unknown, but is proposed in ref 2. This enzyme belongs to the alpha/beta hydrolase fold family (pfam00561). Members of this family are restricted to the Proteobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
Pssm-ID: 273783 [Multi-domain] Cd Length: 245 Bit Score: 43.27 E-value: 9.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 2154 GDGRP-VFCVHPSGGGVAWYLPLARALPAGHPVHAFQPLGM-DGREAPAETIEDMAAGYLAdlrlvQPEGPYVVVGWSLG 2231
Cdd:TIGR01738 1 GQGNVhLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHgRSRGFGPLSLADMAEAIAA-----QAPDPAIWLGWSLG 75
|
....*...
gi 653678460 2232 GTIAFEMA 2239
Cdd:TIGR01738 76 GLVALHIA 83
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
1679-2033 |
1.08e-03 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 44.36 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1679 TVDPRGLAYSIFTSGSTGQPKGVAVEHIGIVryLSWAAASYPTAgrRGTLAHSSV----------GFDLTMSAlfePLVS 1748
Cdd:PRK06018 173 TFDENTAAGMCYTSGTTGDPKGVLYSHRSNV--LHALMANNGDA--LGTSAADTMlpvvplfhanSWGIAFSA---PSMG 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1749 GRGVtlMP-ADATLADLAEELSGPlAYDYIRLTPSHLRHLVGHWTGQELP-PAARGWVVGGETLDPALVKQLLELrpDAE 1826
Cdd:PRK06018 246 TKLV--MPgAKLDGASVYELLDTE-KVTFTAGVPTVWLMLLQYMEKEGLKlPHLKMVVCGGSAMPRSMIKAFEDM--GVE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1827 VINHYGPTET----VIGRVVHPVREA-GELAVDSPLPLGRPLGETRLQVLDAWLEAVPVG--AVGELFIGGDGIARGYLG 1899
Cdd:PRK06018 321 VRHAWGMTEMsplgTLAALKPPFSKLpGDARLDVLQKQGYPPFGVEMKITDDAGKELPWDgkTFGRLKVRGPAVAAAYYR 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1900 rpaltAEKFLPDPAGepgarMYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGVEQAVVlvrdqql 1979
Cdd:PRK06018 401 -----VDGEILDDDG-----FFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAV------- 463
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 653678460 1980 VGWFIPAEDHPPVTVSALRR---FCAEQLPEFM--------VPNQWVALDAFPLTPHGKVNHRAL 2033
Cdd:PRK06018 464 IGVYHPKWDERPLLIVQLKPgetATREEILKYMdgkiakwwMPDDVAFVDAIPHTATGKILKTAL 528
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
2055-2116 |
1.19e-03 |
|
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: 39.93 E-value: 1.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 653678460 2055 EQLLAELWSTVLG---TDRIGIEDNFFDLGGTSISVIQLSGACRRA-GVEISPKDVFEQPTVRGQA 2116
Cdd:smart00823 14 LDLVREQVAAVLGhaaAEAIDPDRPFRDLGLDSLMAVELRNRLEAAtGLRLPATLVFDHPTPAALA 79
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
1920-1972 |
2.18e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 43.21 E-value: 2.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 653678460 1920 MYRTGDLVRWRGDGLLDFVGRVDDQVKLRGYRIELGEIEARMAEHPGV-EQAVV 1972
Cdd:PRK00174 484 MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVaEAAVV 537
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
1673-1972 |
2.82e-03 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 42.97 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1673 DQRPEVTVDPRGLAYSIFTSGSTGQPKGVAVEHIGIVrylSWAAASYPTAGRRGTLAHSSVGFD-LTMSALFEPLV---- 1747
Cdd:cd05927 104 NKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIV---SNVAGVFKILEILNKINPTDVYISyLPLAHIFERVVealf 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1748 --SGRGV-------------------TLMPA---------DATLADLAEelSGPL-------AYDY--IRLTPSHLRH-- 1786
Cdd:cd05927 181 lyHGAKIgfysgdirlllddikalkpTVFPGvprvlnriyDKIFNKVQA--KGPLkrklfnfALNYklAELRSGVVRAsp 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1787 ----LVGHWTGQELPPAARGWVVGGETLDPAlVKQLLELRPDAEVINHYGPTETV-IGRVVHP-VREAGElaVDSPLPlg 1860
Cdd:cd05927 259 fwdkLVFNKIKQALGGNVRLMLTGSAPLSPE-VLEFLRVALGCPVLEGYGQTECTaGATLTLPgDTSVGH--VGGPLP-- 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 1861 rplgetrlqVLDAWLEAVP---------VGAvGELFIGGDGIARGYLGRPALTAEKFlpDPAGepgarMYRTGDLVRWRG 1931
Cdd:cd05927 334 ---------CAEVKLVDVPemnydakdpNPR-GEVCIRGPNVFSGYYKDPEKTAEAL--DEDG-----WLHTGDIGEWLP 396
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 653678460 1932 DGLLDFVGRVDDQVKL-RGYRIELGEIEARMAEHPGVEQAVV 1972
Cdd:cd05927 397 NGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSPFVAQIFV 438
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
1884-1953 |
5.47e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 42.01 E-value: 5.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 653678460 1884 GELFIGGDGIARGYLGRPALTAEKFLPDpagepgaRMYRTGDLVRWRGDGLLDFVGRVDDQVKL-RGYRIE 1953
Cdd:PTZ00342 542 GELLIKSDSIFSGYFLEKEQTKNAFTED-------GYFKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYIE 605
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
2155-2244 |
8.32e-03 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 38.27 E-value: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653678460 2155 DGRPVFCVHPSGGGVAWYLPLARALPA-GHPVHAFQplgMDGREAPAETIEDMAAGYLADLRLVQPEGPYVVVGWSLGGT 2233
Cdd:COG1075 4 TRYPVVLVHGLGGSAASWAPLAPRLRAaGYPVYALN---YPSTNGSIEDSAEQLAAFVDAVLAATGAEKVDLVGHSMGGL 80
|
90
....*....|.
gi 653678460 2234 IAFEMARQLDR 2244
Cdd:COG1075 81 VARYYLKRLGG 91
|
|
|