|
Name |
Accession |
Description |
Interval |
E-value |
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
38-665 |
0e+00 |
|
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: 1039.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 38 QSYHDLYRSSINDADEFWRTVSSELHFEQGTSKGLEWNFdskaGNVFVKFMDGAKTNISYNCLERNIKRgYGNKIAYIFE 117
Cdd:cd05966 1 EQYKELYKQSIEDPEEFWGEIAKELDWFKPWDKVLDWSK----GPPFIKWFEGGKLNISYNCLDRHLKE-RGDKVAIIWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 118 GNEPTDTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDA 197
Cdd:cd05966 76 GDEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 198 RCRVLVTADGVFRGAKPIGLKSIADAAAvlasQEDVKVEAIIMVEHLKRvtkpdgvelPKVDYTDITVIYDSEMLKCAGv 277
Cdd:cd05966 156 QCKLVITADGGYRGGKVIPLKEIVDEAL----EKCPSVEKVLVVKRTGG---------EVPMTEGRDLWWHDLMAKQSP- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 278 DSPVEWMDSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYTFDAQEDDVYWCTADCGWITGHSYLLYGPLMNGLK 357
Cdd:cd05966 222 ECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGAT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 358 GIWYEGVPTYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSRKTLKVIGTVGEPINPAAWMWLYKQVGLSN 437
Cdd:cd05966 302 TVMFEGTPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGKER 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 438 VSIVDTYWQTETGGHMITCLPGATPMKPGAAAMPFFGASPVLLDAEGRVIEGPGEGSLCFDRAWPGMMRGIYGDEQRFVK 517
Cdd:cd05966 382 CPIVDTWWQTETGGIMITPLPGATPLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPWPGMARTIYGDHERYED 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 518 TYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLN 597
Cdd:cd05966 462 TYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLK 541
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71982997 598 VGERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRKIAEGsESGIGDTTTLVD 665
Cdd:cd05966 542 DGEEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAG-EEELGDTSTLAD 608
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
21-680 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 977.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 21 IFLPPAPLLAGAHcAGLQSYHDLYRSSINDADEFWRTVSSELHFEQGTSKGLEWNfdskagNVFVKFMDGAKTNISYNCL 100
Cdd:PRK00174 1 VFPPPAEFAANAL-IDMEQYKALYQESVEDPEGFWAEQAKRLDWFKPFDTVLDWN------APFIKWFEDGELNVSYNCL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 101 ERNIKRGyGNKIAYIFEGNEPTDTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSV 180
Cdd:PRK00174 74 DRHLKTR-GDKVAIIWEGDDPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 181 VFAGFSAESLAARVVDARCRVLVTADGVFRGAKPIGLKSIADAAAVLASqedvKVEAIIMVEHLkrvtkpdGVELPKVDY 260
Cdd:PRK00174 153 VFGGFSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALANCP----SVEKVIVVRRT-------GGDVDWVEG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 261 TDItvIYDsEMLKCAGVDSPVEWMDSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYTFDAQEDDVYWCTADCGW 340
Cdd:PRK00174 222 RDL--WWH-ELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGW 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 341 ITGHSYLLYGPLMNGLKGIWYEGVPTYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSRKTLKVIGTVGEP 420
Cdd:PRK00174 299 VTGHSYIVYGPLANGATTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSSLRLLGSVGEP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 421 INPAAWMWLYKQVGLSNVSIVDTYWQTETGGHMITCLPGATPMKPGAAAMPFFGASPVLLDAEGRVIEGPGEGSLCFDRA 500
Cdd:PRK00174 379 INPEAWEWYYKVVGGERCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDP 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 501 WPGMMRGIYGDEQRFVKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVA 580
Cdd:PRK00174 459 WPGMMRTIYGDHERFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVG 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 581 APHDIKGSFPYAFVTLNVGERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRKIAEGsESGIGDT 660
Cdd:PRK00174 539 RPDDIKGQGIYAFVTLKGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEG-EEILGDT 617
|
650 660
....*....|....*....|
gi 71982997 661 TTLVDESVIKQLISGRSARA 680
Cdd:PRK00174 618 STLADPSVVEKLIEARQNRK 637
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
35-674 |
0e+00 |
|
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: 916.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 35 AGLQSYHDLYRSSINDADEFWRTVSSE-LHFEQGTSKGLEWNFDSkagnvFVKFMDGAKTNISYNCLERNIKRgYGNKIA 113
Cdd:TIGR02188 2 ANLEQYKELYEESIEDPDKFWAKLARElLDWFKPFTKVLDWSFPP-----FYKWFVGGELNVSYNCVDRHLEA-RPDKVA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 114 YIFEGNEPTDTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAAR 193
Cdd:TIGR02188 76 IIWEGDEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 194 VVDARCRVLVTADGVFRGAKPIGLKSIADAAAvlaSQEDVKVEAIIMVehlKRVTKPDGVELPKVDytditVIYDSEMLK 273
Cdd:TIGR02188 156 INDAGAKLVITADEGLRGGKVIPLKAIVDEAL---EKCPVSVEHVLVV---RRTGNPVVPWVEGRD-----VWWHDLMAK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 274 cAGVDSPVEWMDSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYTFDAQEDDVYWCTADCGWITGHSYLLYGPLM 353
Cdd:TIGR02188 225 -ASAYCEPEPMDSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 354 NGLKGIWYEGVPTYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSRKTLKVIGTVGEPINPAAWMWLYKQV 433
Cdd:TIGR02188 304 NGATTVMFEGVPTYPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 434 GLSNVSIVDTYWQTETGGHMITCLPGATPMKPGAAAMPFFGASPVLLDAEGRVIEGPGE-GSLCFDRAWPGMMRGIYGDE 512
Cdd:TIGR02188 384 GKERCPIVDTWWQTETGGIMITPLPGATPTKPGSATLPFFGIEPAVVDEEGNPVEGPGEgGYLVIKQPWPGMLRTIYGDH 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 513 QRFVKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYA 592
Cdd:TIGR02188 464 ERFVDTYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYA 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 593 FVTLNVGERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRKIAEGSESGIGDTTTLVDESVIKQL 672
Cdd:TIGR02188 544 FVTLKDGYEPDDELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEAEILGDTSTLEDPSVVEEL 623
|
..
gi 71982997 673 IS 674
Cdd:TIGR02188 624 IE 625
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
90-673 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 760.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 90 GAKTNISYNCLERNIKrGYGNKIAYIFEGnEPTDTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAML 169
Cdd:COG0365 5 GGRLNIAYNCLDRHAE-GRGDKVALIWEG-EDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 170 ACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTADGVFRGAKPIGLKSIADAAAVLASqedvKVEAIIMVEHLKRVTK 249
Cdd:COG0365 83 ACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELP----SLEHVIVVGRTGADVP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 250 PDGVelpkVDYTDItviydsemLKCAGVDSPVEWMDSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYTFDAQED 329
Cdd:COG0365 159 MEGD----LDWDEL--------LAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 330 DVYWCTADCGWITGHSYLLYGPLMNGLKGIWYEGVPTYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSRK 409
Cdd:COG0365 227 DVFWCTADIGWATGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 410 TLKVIGTVGEPINPAAWMWLYKQVGlsnVSIVDTYWQTETGGHMITCLPGaTPMKPGAAAMPFFGASPVLLDAEGRVIEG 489
Cdd:COG0365 307 SLRLLGSAGEPLNPEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLPG-LPVKPGSMGKPVPGYDVAVVDEDGNPVPP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 490 PGEGSLCFDRAWPGMMRGIYGDEQRFVKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVA 569
Cdd:COG0365 383 GEEGELVIKGPWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVS 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 570 HEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRKI 649
Cdd:COG0365 463 HPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKI 542
|
570 580
....*....|....*....|....
gi 71982997 650 AEGSEsgIGDTTTLVDESVIKQLI 673
Cdd:COG0365 543 AEGRP--LGDTSTLEDPEALDEIK 564
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
14-674 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 755.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 14 GEGL---DEDIFLPPAPLLAGAHCAGLQSYHDLYRSSINDADEFWRTVSSELHFEQ--GTSKGLEWNFDSKAGNVFVKFM 88
Cdd:PLN02654 3 GESLaseENDLVFPSKDFSAQALVSSPQQYMEMYKRSVDDPAGFWSDIASQFYWKQkwEGDEVCSENLDVRKGPISIEWF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 89 DGAKTNISYNCLERNIKRGYGNKIAYIFEGNEPTDTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAM 168
Cdd:PLN02654 83 KGGKTNICYNCLDRNVEAGNGDKIAIYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 169 LACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTADGVFRGAKPIGLKSIADAAAVLASQEDVKVEAIIMVEHLKRVT 248
Cdd:PLN02654 163 LACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITCNAVKRGPKTINLKDIVDAALDESAKNGVSVGICLTYENQLAMK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 249 KPDGVELPKVD--YTDITVIYDSemlKCagvdsPVEWMDSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYTFDA 326
Cdd:PLN02654 243 REDTKWQEGRDvwWQDVVPNYPT---KC-----EVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 327 QEDDVYWCTADCGWITGHSYLLYGPLMNGLKGIWYEGVPTYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESS 406
Cdd:PLN02654 315 KPTDVYWCTADCGWITGHSYVTYGPMLNGATVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRH 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 407 SRKTLKVIGTVGEPINPAAWMWLYKQVGLSNVSIVDTYWQTETGGHMITCLPGATPMKPGAAAMPFFGASPVLLDAEGRV 486
Cdd:PLN02654 395 SRKSLRVLGSVGEPINPSAWRWFFNVVGDSRCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGKE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 487 IEGPGEGSLCFDRAWPGMMRGIYGDEQRFVKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESA 566
Cdd:PLN02654 475 IEGECSGYLCVKKSWPGAFRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESA 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 567 LVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRIL 646
Cdd:PLN02654 555 LVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
|
650 660
....*....|....*....|....*...
gi 71982997 647 RKIAEGSESGIGDTTTLVDESVIKQLIS 674
Cdd:PLN02654 635 RKIASRQLDELGDTSTLADPGVVDQLIA 662
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
40-641 |
0e+00 |
|
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: 613.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 40 YHDLYRSSINDADEFWrtvsselhFEQGTSKGLEW------NFDSKAGNVFVKFMDGAKTNISYNCLERNIKRGyGNKIA 113
Cdd:cd17634 1 YETKYRQSINDPDTFW--------GEAGKILDWITpyqkvkNTSFAPGAPSIKWFEDATLNLAANALDRHLREN-GDRTA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 114 YIFEGNEPTDTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAAR 193
Cdd:cd17634 72 IIYEGDDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 194 VVDARCRVLVTADGVFRGAKPIGLKSIADAAAVLASqedVKVEAIIMVehlKRVTKP-DGVELPKVDYtditviyDSEML 272
Cdd:cd17634 152 IIDSSSRLLITADGGVRAGRSVPLKKNVDDALNPNV---TSVEHVIVL---KRTGSDiDWQEGRDLWW-------RDLIA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 273 KCAGVDSPVEwMDSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYTFDAQEDDVYWCTADCGWITGHSYLLYGPL 352
Cdd:cd17634 219 KASPEHQPEA-MNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 353 MNGLKGIWYEGVPTYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSRKTLKVIGTVGEPINPAAWMWLYKQ 432
Cdd:cd17634 298 ACGATTLLYEGVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 433 VGLSNVSIVDTYWQTETGGHMITCLPGATPMKPGAAAMPFFGASPVLLDAEGRVIEGPGEGSLCFDRAWPGMMRGIYGDE 512
Cdd:cd17634 378 IGKEKCPVVDTWWQTETGGFMITPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWPGQTRTLFGDH 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 513 QRFVKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYA 592
Cdd:cd17634 458 ERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYA 537
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 71982997 593 FVTLNVGERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKV 641
Cdd:cd17634 538 YVVLNHGVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
40-672 |
2.74e-177 |
|
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: 518.79 E-value: 2.74e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 40 YHDLYRSSINDADEFWRTVSSELHFEQGTSKGLEwnfDSKAGnvFVKFMDGAKTNISYNCLERNIKRGYGNKIAYIFEGN 119
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARLIDWFKPPEKILD---NSNPP--FTRWFVGGRLNTCYNALDRHVEAGRGDQIALIYDSP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 120 EPTDTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARC 199
Cdd:cd05967 76 VTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 200 RVLVTADGVFRGAKPIGLKSIADAAAVLASQEDVKVeaIImvehLKRVTKPDGVELPKVDYTditviYDSEMLKCAGVDs 279
Cdd:cd05967 156 KLIVTASCGIEPGKVVPYKPLLDKALELSGHKPHHV--LV----LNRPQVPADLTKPGRDLD-----WSELLAKAEPVD- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 280 PVeWMDSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYTFDAQEDDVYWCTADCGWITGHSYLLYGPLMNGLKGI 359
Cdd:cd05967 224 CV-PVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 360 WYEGVPT-YPTPSRMWDVTDKYGVTKLYTSPTAARALMA--LGNQWLESSSRKTLKVIGTVGEPINPAAWMWLYKQVGls 436
Cdd:cd05967 303 LYEGKPVgTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKedPDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLG-- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 437 nVSIVDTYWQTETGGHMITCLPG--ATPMKPGAAAMPFFGASPVLLDAEGRVIEGPGEGSLCFDRAW-PGMMRGIYGDEQ 513
Cdd:cd05967 381 -VPVIDHWWQTETGWPITANPVGlePLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPLpPGCLLTLWKNDE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 514 RFVKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAF 593
Cdd:cd05967 460 RFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGL 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 594 VTLNVGERIN-EKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRKIAEGSEsgIGDTTTLVDESVIKQL 672
Cdd:cd05967 540 VVLKEGVKITaEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGED--YTIPSTIEDPSVLDEI 617
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
38-672 |
3.26e-172 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 506.02 E-value: 3.26e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 38 QSYHDLYRSSINDADEFWRTVSSELHFEQGTSKGLEwnfDSKAGnvFVKFMDGAKTNISYNCLERNIKRgYGNKIAYIFE 117
Cdd:PRK10524 2 MSYSEFYQRSIDDPEAFWAEQARRIDWQTPFTQVLD---YSNPP--FARWFVGGRTNLCHNAVDRHLAK-RPEQLALIAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 118 GNEPTDTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDA 197
Cdd:PRK10524 76 STETDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 198 RCRVLVTADGVFRGAKPIGLKSIADAAAVLASqedVKVEAIIMVEhlkRVTKPdgveLPKVDYTDITviYDSEMLKCAGV 277
Cdd:PRK10524 156 KPVLIVSADAGSRGGKVVPYKPLLDEAIALAQ---HKPRHVLLVD---RGLAP----MARVAGRDVD--YATLRAQHLGA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 278 DSPVEWMDSEDPLFILYTSGSTGKPKGIQHTTAGYmTYAYATT-KYTFDAQEDDVYWCTADCGWITGHSYLLYGPLMNGL 356
Cdd:PRK10524 224 RVPVEWLESNEPSYILYTSGTTGKPKGVQRDTGGY-AVALATSmDTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGM 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 357 KGIWYEGVPTYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSRKTLKVIGTVGEPINPAAWMWLYKQVGls 436
Cdd:PRK10524 303 ATIMYEGLPTRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLDEPTASWISEALG-- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 437 nVSIVDTYWQTETGGHMITCLPG--ATPMKPGAAAMPFFGASPVLLDAEGRVIEGPGE-GSLCFDRAW-PGMMRGIYGDE 512
Cdd:PRK10524 381 -VPVIDNYWQTETGWPILAIARGveDRPTRLGSPGVPMYGYNVKLLNEVTGEPCGPNEkGVLVIEGPLpPGCMQTVWGDD 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 513 QRFVKTYLAPFNG-YYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPY 591
Cdd:PRK10524 460 DRFVKTYWSLFGRqVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAV 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 592 AFVTLNVGERINE-----KLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRKIAEGSESgiGDTTTLVDE 666
Cdd:PRK10524 540 AFVVPKDSDSLADrearlALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAEGRDP--GDLTTIEDP 617
|
....*.
gi 71982997 667 SVIKQL 672
Cdd:PRK10524 618 AALQQI 623
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
36-665 |
3.93e-150 |
|
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: 448.86 E-value: 3.93e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 36 GLQSYHDLYRSSINDADEFWRTVSSELhfeqgtskGLEW------NFDSKAGNVFVKFMDGAKTNISYNCLERNIkRGYG 109
Cdd:cd05968 5 GIPDLEAFLERSAEDNAWFWGEFVKDV--------GIEWyeppyqTLDLSGGKPWAAWFVGGRMNIVEQLLDKWL-ADTR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 110 NKIAYIFEGNEPTdTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAES 189
Cdd:cd05968 76 TRPALRWEGEDGT-SRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 190 LAARVVDARCRVLVTADGVFRGAKPIGLKSIADAAAvlasQEDVKVEAIIMVEHLKRvtkpdgvELPKVDYTDITviYDS 269
Cdd:cd05968 155 AATRLQDAEAKALITADGFTRRGREVNLKEEADKAC----AQCPTVEKVVVVRHLGN-------DFTPAKGRDLS--YDE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 270 EMlkcAGVDSPVEWMDSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYTFD-AQEDDVYWCTaDCGWITGhSYLL 348
Cdd:cd05968 222 EK---ETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDlKPGDLLTWFT-DLGWMMG-PWLI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 349 YGPLMNGLKGIWYEGVPTYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSRKTLKVIGTVGEPINPAAWMW 428
Cdd:cd05968 297 FGGLILGATMVLYDGAPDHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNW 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 429 LYKQVGLSNVSIVDTYWQTETGGHMITCLPgATPMKPGAAAMPFFGASPVLLDAEGRVIEgPGEGSLCFDRAWPGMMRGI 508
Cdd:cd05968 377 LFETVGKGRNPIINYSGGTEISGGILGNVL-IKPIKPSSFNGPVPGMKADVLDESGKPAR-PEVGELVLLAPWPGMTRGF 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 509 YGDEQRFVKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGS 588
Cdd:cd05968 455 WRDEDRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGE 534
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71982997 589 FPYAFVTLNVGERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRKIAEGSEsgIGDTTTLVD 665
Cdd:cd05968 535 AIVCFVVLKPGVTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGKE--LGDLSSLEN 609
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
26-665 |
5.47e-133 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 403.12 E-value: 5.47e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 26 APLLAGAHcaGLQSYHDLYRSsindadeF-WRTVSSELhfeqgtskglEWnfdskagnvfvkfMDGAKTNISYNCLERNI 104
Cdd:PRK04319 6 LPVIKGEP--NLKDYEETYAT-------FsWEEVEKEF----------SW-------------LETGKVNIAYEAIDRHA 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 105 KRGYGNKIAYIFEGNEPTDTstWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAG 184
Cdd:PRK04319 54 DGGRKDKVALRYLDASRKEK--YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 185 FSAESLAARVVDARCRVLVTADGVFRgakpiglKSIADAaavlasqedvkveaiimVEHLKRVTKPDGVelpkVDYTDIT 264
Cdd:PRK04319 132 FMEEAVRDRLEDSEAKVLITTPALLE-------RKPADD-----------------LPSLKHVLLVGED----VEEGPGT 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 265 VIYDSEMLKcAGVDSPVEWMDSEDPLFILYTSGSTGKPKGIQHTTaGYMTYAYATTKYTFDAQEDDVYWCTADCGWITGH 344
Cdd:PRK04319 184 LDFNALMEQ-ASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVH-NAMLQHYQTGKYVLDLHEDDVYWCTADPGWVTGT 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 345 SYLLYGPLMNGLKGIWYEGvptYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSRKTLKVIGTVGEPINPA 424
Cdd:PRK04319 262 SYGIFAPWLNGATNVIDGG---RFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDLSSLRHILSVGEPLNPE 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 425 AWMWLYKQVGLSnvsIVDTYWQTETGGHMITCLPgATPMKPGAAAMPFFGASPVLLDAEGRVIEGPGEGSLCFDRAWPGM 504
Cdd:PRK04319 339 VVRWGMKVFGLP---IHDNWWMTETGGIMIANYP-AMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGWPSM 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 505 MRGIYGDEQRFVKTYLapfNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHD 584
Cdd:PRK04319 415 MRGIWNNPEKYESYFA---GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDP 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 585 IKGSFPYAFVTLNVGERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRkiaeGSESGI--GDTTT 662
Cdd:PRK04319 492 VRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK----AWELGLpeGDLST 567
|
...
gi 71982997 663 LVD 665
Cdd:PRK04319 568 MED 570
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
127-650 |
3.14e-120 |
|
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: 366.06 E-value: 3.14e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 127 WTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTAd 206
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 207 gvfrgakpiglksiadaaavlasqedvkveaiimvEHLKrvtkpdgvelpkvdytditviydsemlkcagvdspvEWMDS 286
Cdd:cd05969 80 -----------------------------------EELY------------------------------------ERTDP 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 287 EDPLFILYTSGSTGKPKGIQHTTAGyMTYAYATTKYTFDAQEDDVYWCTADCGWITGHSYLLYGPLMNGLKGIWYEGvpt 366
Cdd:cd05969 89 EDPTLLHYTSGTTGTPKGVLHVHDA-MIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEG--- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 367 YPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSRKTLKVIGTVGEPINPAAWMWLYKQVglsNVSIVDTYWQ 446
Cdd:cd05969 165 RFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVF---GVPIHDTWWQ 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 447 TETGGHMITCLPGaTPMKPGAAAMPFFGASPVLLDAEGRVIEGPGEGSLCFDRAWPGMMRGIYGDEQRFVKTYLapfNGY 526
Cdd:cd05969 242 TETGSIMIANYPC-MPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPGWPSMFRGIWNDEERYKNSFI---DGW 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 527 YFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEKL 606
Cdd:cd05969 318 YLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDEL 397
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 71982997 607 VAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRKIA 650
Cdd:cd05969 398 KEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
127-648 |
4.39e-105 |
|
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: 326.22 E-value: 4.39e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 127 WTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTad 206
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 207 gvfrgakpiglksiadaaavlasqedvkveaiimvehlkrvtkpdgvelpkvdytditviydsemlkcagvdspvewmDS 286
Cdd:cd05972 79 ------------------------------------------------------------------------------DA 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 287 EDPLFILYTSGSTGKPKGIQHTtAGYMTYAYATTKYTFDAQEDDVYWCTADCGWITGHSYLLYGPLMNGLKGIWYEGVPT 366
Cdd:cd05972 81 EDPALIYFTSGTTGLPKGVLHT-HSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRF 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 367 ypTPSRMWDVTDKYGVTKLYTSPTAARALMALGnqwLESSSRKTLKVIGTVGEPINPAAWMWLYKQVGLSnvsIVDTYWQ 446
Cdd:cd05972 160 --DAERILELLERYGVTSFCGPPTAYRMLIKQD---LSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLP---IRDGYGQ 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 447 TETGGHMITCLpgATPMKPGAAAMPFFGASPVLLDAEGRVIeGPGE-GSLCFDRAWPGMMRGIYGDEQRFVKTYLapfNG 525
Cdd:cd05972 232 TETGLTVGNFP--DMPVKPGSMGRPTPGYDVAIIDDDGREL-PPGEeGDIAIKLPPPGLFLGYVGDPEKTEASIR---GD 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 526 YYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEK 605
Cdd:cd05972 306 YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEE 385
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 71982997 606 LVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRK 648
Cdd:cd05972 386 LAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
100-554 |
5.26e-104 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 323.11 E-value: 5.26e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 100 LERNIKRgYGNKIAYIFEGNEptdtsTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHS 179
Cdd:pfam00501 1 LERQAAR-TPDKTALEVGEGR-----RLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 180 VVFAGFSAESLAARVVDARCRVLVTADgvfrGAKPIGLKSIADAAAVLASQEDVKVEAIIMVEHLKRVTKPDGVELPkvd 259
Cdd:pfam00501 75 PLNPRLPAEELAYILEDSGAKVLITDD----ALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPP--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 260 ytditviydsemlkcagvdsPVEWMDSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYAT---TKYTFDAQEDDVYWCTA 336
Cdd:pfam00501 148 --------------------PPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIkrvRPRGFGLGPDDRVLSTL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 337 DCGWITGHSYLLYGPLMNGLKGIWYEGVPTyPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSRktLKVIGT 416
Cdd:pfam00501 208 PLFHDFGLSLGLLGPLLAGATVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSS--LRLVLS 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 417 VGEPINPAAWMWLYKQVGlsnVSIVDTYWQTETGGHMITCLPGATPM-KPGAAAMPFFGASPVLLDAEGRVIEGPGE-GS 494
Cdd:pfam00501 285 GGAPLPPELARRFRELFG---GALVNGYGLTETTGVVTTPLPLDEDLrSLGSVGRPLPGTEVKIVDDETGEPVPPGEpGE 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 495 LCFDRawPGMMRGIYGDEQRFVKTYLAPfnGYYFTGDGARRDEDGYLWITGRVDDLMNVS 554
Cdd:pfam00501 362 LCVRG--PGVMKGYLNDPELTAEAFDED--GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
100-654 |
5.23e-74 |
|
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: 245.49 E-value: 5.23e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 100 LERNIKRgYGNKIAYIFEGneptdtSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHS 179
Cdd:COG0318 5 LRRAAAR-HPDRPALVFGG------RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 180 VVFAGFSAESLAARVVDARCRVLVTAdgvfrgakpiglksiadaaavlasqedvkveaiimvehlkrvtkpdgvelpkvd 259
Cdd:COG0318 78 PLNPRLTAEELAYILEDSGARALVTA------------------------------------------------------ 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 260 ytditviydsemlkcagvdspvewmdsedplFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYtFDAQEDDVYWCTADCG 339
Cdd:COG0318 104 -------------------------------LILYTSGTTGRPKGVMLTHRNLLANAAAIAAA-LGLTPGDVVLVALPLF 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 340 WITGHSYLLYGPLMNGLKGIwyegVPTYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNqwLESSSRKTLKVIGTVGE 419
Cdd:COG0318 152 HVFGLTVGLLAPLLAGATLV----LLPRFDPERVLELIERERVTVLFGVPTMLARLLRHPE--FARYDLSSLRLVVSGGA 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 420 PINPAAWMWLYKQVGlsnVSIVDTYWQTETGGHMITCLPGATPMKPGAAAMPFFGASPVLLDAEGRVIeGPGE-GSLCFd 498
Cdd:COG0318 226 PLPPELLERFEERFG---VRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPGVEVRIVDEDGREL-PPGEvGEIVV- 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 499 RAwPGMMRGIYGDEQRFVKTYlapFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAV 578
Cdd:COG0318 301 RG-PNVMKGYWNDPEATAEAF---RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAV 376
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71982997 579 VAAPHDIKGSFPYAFVTLNVGERINEklvAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRKIAEGSE 654
Cdd:COG0318 377 VGVPDEKWGERVVAFVVLRPGAELDA---EELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGA 449
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
128-648 |
1.66e-73 |
|
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: 243.96 E-value: 1.66e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 128 TYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTadg 207
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 208 vfrgakpiglksiaDAAavlasqedvkveaiimvehlkrvtkpdgvELPKVDytditviydsemlkcagvdspvewmdsE 287
Cdd:cd05973 79 --------------DAA-----------------------------NRHKLD---------------------------S 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 288 DPLFILYTSGSTGKPKGIQHTTAGYMTYAyATTKYTFDAQEDDVYWCTADCGWITGHSYLLYGPLMNGLKGIWYEGVPTY 367
Cdd:cd05973 89 DPFVMMFTSGTTGLPKGVPVPLRALAAFG-AYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGFSV 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 368 PTpsrMWDVTDKYGVTKLYTSPTAARALMALGNQwLESSSRKTLKVIGTVGEPINPAAWMWLYKQVGlsnVSIVDTYWQT 447
Cdd:cd05973 168 ES---TWRVIERLGVTNLAGSPTAYRLLMAAGAE-VPARPKGRLRRVSSAGEPLTPEVIRWFDAALG---VPIHDHYGQT 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 448 ETGGHMITCLPGATPMKPGAAAMPFFGASPVLLDAEGRVIeGPGE-GSLCFDRAWPGMM--RGIYGDEQRfvktylAPFN 524
Cdd:cd05973 241 ELGMVLANHHALEHPVHAGSAGRAMPGWRVAVLDDDGDEL-GPGEpGRLAIDIANSPLMwfRGYQLPDTP------AIDG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 525 GYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINE 604
Cdd:cd05973 314 GYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTP 393
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 71982997 605 KLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRK 648
Cdd:cd05973 394 ALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
288-641 |
7.66e-70 |
|
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: 231.02 E-value: 7.66e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 288 DPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYTFDAqEDDVYWCTADCGWItGHSYLLYGPLMNGLKGIWYEGvpty 367
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLT-EGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 368 PTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSRktLKVIGTVGEPINPAAWMWLYKQVGlsnVSIVDTYWQT 447
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSS--LRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 448 ETGGHMITCLPGATPMKPGAAAMPFFGASPVLLDAEGRVIEGPGEGSLCFdRAwPGMMRGIYGDEQRfvkTYLAPFNGYY 527
Cdd:cd04433 150 ETGGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVV-RG-PSVMKGYWNNPEA---TAAVDEDGWY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 528 FTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEklv 607
Cdd:cd04433 225 RTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDA--- 301
|
330 340 350
....*....|....*....|....*....|....
gi 71982997 608 AELKKLVREKIGALAVPDVIQEAPGLPKTRSGKV 641
Cdd:cd04433 302 EELRAHVRERLAPYKVPRRVVFVDALPRTASGKI 335
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
37-654 |
8.97e-69 |
|
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: 236.40 E-value: 8.97e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 37 LQSYHDLYRSSINDADEFWRTVSSelHFEQGTSKGLEWNFDSKAGNVFVKFMDGAKTNISYNCLERnikRGYGNKIAYIF 116
Cdd:cd05943 16 LADYAALHRWSVDDPGAFWAAVWD--FSGVRGSKPYDVVVVSGRIMPGARWFPGARLNYAENLLRH---ADADDPAAIYA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 117 EGNEPTDTSTWtyNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVD 196
Cdd:cd05943 91 AEDGERTEVTW--AELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 197 ARCRVLVTADGVFRGAKPIGLksIADAAAVLASQEDVKveAIIMVEHLKRVTKPDGVELPKVdytditVIYDSEMLKCAG 276
Cdd:cd05943 169 IEPKVLFAVDAYTYNGKRHDV--REKVAELVKGLPSLL--AVVVVPYTVAAGQPDLSKIAKA------LTLEDFLATGAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 277 VDSPVEWMDSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYTFDAQEDDVYWCTADCGWITGHSylLYGPLMNGL 356
Cdd:cd05943 239 GELEFEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRLFYYTTCGWMMWNW--LVSGLAVGA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 357 KGIWYEGVPTYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSRKTLKVIGTVGEPINPAAWMWLYKQVGls 436
Cdd:cd05943 317 TIVLYDGSPFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIK-- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 437 nvsiVDTYWQTETGG-HMITCLPGATPMKP---GAAAMPFFGASPVLLDAEGR-VIEGPGEgsLCFDRAWPGMMRGIYGD 511
Cdd:cd05943 395 ----PDVLLASISGGtDIISCFVGGNPLLPvyrGEIQCRGLGMAVEAFDEEGKpVWGEKGE--LVCTKPFPSMPVGFWND 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 512 E--QRFVKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSF 589
Cdd:cd05943 469 PdgSRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDER 548
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71982997 590 PYAFVTLNVGERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRKIAEGSE 654
Cdd:cd05943 549 VILFVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKIIAGRP 613
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
29-646 |
3.61e-67 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 232.76 E-value: 3.61e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 29 LAGAHCAGLQSYHDLYRSSINDADEFWRTVSS--ELHFEQGTSKGLewnfdskAGNVF--VKFMDGAKTNISYNCLerni 104
Cdd:PRK03584 25 LAARRGLSFDDYAALWRWSVEDLEAFWQSVWDffGVIGSTPYTVVL-------AGRRMpgARWFPGARLNYAENLL---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 105 KRGYGNKIAYIFEGnEPTDTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAG 184
Cdd:PRK03584 94 RHRRDDRPAIIFRG-EDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 185 FSAESLAARVVDARCRVLVTADGVFRGAKPI-GLKSIADAAAVLASqedvkVEAIIMVEHLKrvTKPDGVELPKV-DYTD 262
Cdd:PRK03584 173 FGVQGVLDRFGQIEPKVLIAVDGYRYGGKAFdRRAKVAELRAALPS-----LEHVVVVPYLG--PAAAAAALPGAlLWED 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 263 ITVIYDSEMLKCagvdspvEWMDSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYTFDAQEDDVY-WCTAdCGWI 341
Cdd:PRK03584 246 FLAPAEAAELEF-------EPVPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDRFfWYTT-CGWM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 342 TgHSYLLYGpLMNGLKGIWYEGVPTYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSRKTLKVIGTVGEPI 421
Cdd:PRK03584 318 M-WNWLVSG-LLVGATLVLYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 422 NPAAWMWLYKQVG----LSNVSivdtywqtetGGHMI-TCLPGATPMKP---GAAAMPFFGASPVLLDAEGR-VIEGPGE 492
Cdd:PRK03584 396 PPEGFDWVYEHVKadvwLASIS----------GGTDIcSCFVGGNPLLPvyrGEIQCRGLGMAVEAWDEDGRpVVGEVGE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 493 gsLCFDRAWPGMMRGIYGDE--QRFVKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEI------- 563
Cdd:PRK03584 466 --LVCTKPFPSMPLGFWNDPdgSRYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIyrqveal 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 564 ---ESALVAHEKvaeaavvaAPHDikGSFPYAFVTLNVGERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGK 640
Cdd:PRK03584 544 pevLDSLVIGQE--------WPDG--DVRMPLFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGK 613
|
650
....*....|
gi 71982997 641 VT----RRIL 646
Cdd:PRK03584 614 KVelpvKKLL 623
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
123-647 |
9.56e-66 |
|
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: 223.46 E-value: 9.56e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 123 DTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVL 202
Cdd:cd05971 3 TPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 203 VTadgvfrgakpiglksiadaaavlasqedvkveaiimvehlkrvtkpDGvelpkvdytditviydsemlkcagvdspve 282
Cdd:cd05971 83 VT----------------------------------------------DG------------------------------ 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 283 wmdSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAyATTKYTFD--AQEDDVYWCTADCGWItghsyllyGPLMNGLKGIW 360
Cdd:cd05971 87 ---SDDPALIIYTSGTTGPPKGALHAHRVLLGHL-PGVQFPFNlfPRDGDLYWTPADWAWI--------GGLLDVLLPSL 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 361 YEGVP------TYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQwlESSSRKTLKVIGTVGEPINPAAWMWLYKQVG 434
Cdd:cd05971 155 YFGVPvlahrmTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQ--LKHAQVKLRAIATGGESLGEELLGWAREQFG 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 435 lsnVSIVDTYWQTEtGGHMITCLPGATPMKPGAAAMPFFGASPVLLDAEGRVIEGPGEGSLCFDRAWPGMMRGIYGDEQR 514
Cdd:cd05971 233 ---VEVNEFYGQTE-CNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDPVAFLGYWNNPSA 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 515 FVKTYLapfNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFV 594
Cdd:cd05971 309 TEKKMA---GDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFV 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 71982997 595 TLNVGERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILR 647
Cdd:cd05971 386 VLNPGETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
94-647 |
1.06e-57 |
|
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: 204.27 E-value: 1.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 94 NISYNCLERnIKRGYGNKIAYIFeGNEPTDTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACAR 173
Cdd:cd05970 17 NFAYDVVDA-MAKEYPDKLALVW-CDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 174 IGAMhsvvfagfsaeslaarVVDArCRVLVTADGVFRGAKpiglksiADAAAVLASQEDvkveaiIMVEHLKRVTKPDGV 253
Cdd:cd05970 95 LGAI----------------AIPA-THQLTAKDIVYRIES-------ADIKMIVAIAED------NIPEEIEKAAPECPS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 254 ELPKV----DYTDITVIYDSEMLKCAGVDSPVEWMDS---EDPLFILYTSGSTGKPKGIQHTtagyMTYAY---ATTKYT 323
Cdd:cd05970 145 KPKLVwvgdPVPEGWIDFRKLIKNASPDFERPTANSYpcgEDILLVYFSSGTTGMPKMVEHD----FTYPLghiVTAKYW 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 324 FDAQEDDVYWCTADCGWITGHSYLLYGPLMNGLKGIWYEgvptYP--TPSRMWDVTDKYGVTKLYTSPTAARALMalgNQ 401
Cdd:cd05970 221 QNVREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVYD----YDkfDPKALLEKLSKYGVTTFCAPPTIYRFLI---RE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 402 WLESSSRKTLKVIGTVGEPINPAAWMWLYKQVGLSnvsIVDTYWQTETGGHMITcLPGATPmKPGAAAMPFFGASPVLLD 481
Cdd:cd05970 294 DLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIK---LMEGFGQTETTLTIAT-FPWMEP-KPGSMGKPAPGYEIDLID 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 482 AEGRVIEGPGEGSLCF--DRAWP-GMMRGIYGDEQrfvKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLL 558
Cdd:cd05970 369 REGRSCEAGEEGEIVIrtSKGKPvGLFGGYYKDAE---KTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRI 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 559 STAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRS 638
Cdd:cd05970 446 GPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTIS 525
|
....*....
gi 71982997 639 GKVTRRILR 647
Cdd:cd05970 526 GKIRRVEIR 534
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
122-647 |
1.02e-52 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 188.05 E-value: 1.02e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 122 TDTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRV 201
Cdd:cd05919 6 AADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 202 LVTAdgvfrgakpiglksiADAAAvlasqedvkveaiimvehlkrvtkpdgvelpkvdytditviydsemlkcagvdspv 281
Cdd:cd05919 86 VVTS---------------ADDIA-------------------------------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 282 ewmdsedplFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYTFDAQEDDVYWCTADC--GWITGHSylLYGPLMNGLKGI 359
Cdd:cd05919 95 ---------YLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNS--LWFPLAVGASAV 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 360 WYegvPTYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNqwLESSSRKTLKVIGTVGEPINPAAWMWLYKQVGlsnVS 439
Cdd:cd05919 164 LN---PGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCA--GSPDALRSLRLCVSAGEALPRGLGERWMEHFG---GP 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 440 IVDTYWQTETGGHMITCLPGAtpMKPGAAAMPFFGASPVLLDAEGRVIeGPGEGSLCFDRAwPGMMRGIYGDEQRFVKTY 519
Cdd:cd05919 236 ILDGIGATEVGHIFLSNRPGA--WRLGSTGRPVPGYEIRLVDEEGHTI-PPGEEGDLLVRG-PSAAVGYWNNPEKSRATF 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 520 LapfNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVG 599
Cdd:cd05919 312 N---GGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSP 388
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 71982997 600 ERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILR 647
Cdd:cd05919 389 AAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
100-647 |
1.14e-52 |
|
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: 189.50 E-value: 1.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 100 LERNIKRGYGNKIAYIfegnepTDTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHS 179
Cdd:cd05959 9 VDLNLNEGRGDKTAFI------DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 180 VVFAGFSAESLAARVVDARCRVLVtADGVFrgakpiglksiADAAAVLASQEDVKVEAIImvehlkrVTKPDGVELPKVD 259
Cdd:cd05959 83 PVNTLLTPDDYAYYLEDSRARVVV-VSGEL-----------APVLAAALTKSEHTLVVLI-------VSGGAGPEAGALL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 260 YTDItVIYDSEMLKCAGVdspveWMDseDPLFILYTSGSTGKPKGIQHTTAG--YMTYAYAttKYTFDAQEDDVYWCTAD 337
Cdd:cd05959 144 LAEL-VAAEAEQLKPAAT-----HAD--DPAFWLYSSGSTGRPKGVVHLHADiyWTAELYA--RNVLGIREDDVCFSAAK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 338 CGWITGHSYLLYGPLMNGLKGIWYegvPTYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNqwLESSSRKTLKVIGTV 417
Cdd:cd05959 214 LFFAYGLGNSLTFPLSVGATTVLM---PERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPN--LPSRDLSSLRLCVSA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 418 GEPInPAawmwlykQVGLS-----NVSIVDTYWQTETGGHMITCLPGAtpMKPGAAAMPFFGASPVLLDAEGRVIEGPGE 492
Cdd:cd05959 289 GEAL-PA-------EVGERwkarfGLDILDGIGSTEMLHIFLSNRPGR--VRYGTTGKPVPGYEVELRDEDGGDVADGEP 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 493 GSLcFDRAwPGMMRGIYGDEQRFVKTylapFNGYYF-TGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHE 571
Cdd:cd05959 359 GEL-YVRG-PSSATMYWNNRDKTRDT----FQGEWTrTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHP 432
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71982997 572 KVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILR 647
Cdd:cd05959 433 AVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
127-648 |
3.68e-51 |
|
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: 186.13 E-value: 3.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 127 WTYNELHAQVVQFSAVLRSH-GVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTA 205
Cdd:cd05928 42 WSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 206 DgvfrgakpiglkSIADAAAVLASQ-EDVKVEaiIMVEHLKRvtkpDGvelpkvdYTDITviydsEMLKCAGVDSPVEWM 284
Cdd:cd05928 122 D------------ELAPEVDSVASEcPSLKTK--LLVSEKSR----DG-------WLNFK-----ELLNEASTEHHCVET 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 285 DSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYTFDAQEDDVYWCTADCGWITGHSYLLYGPLMNGlKGIWYEGV 364
Cdd:cd05928 172 GSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQG-ACVFVHHL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 365 PTYPTPSrMWDVTDKYGVTKLYTSPTAARALMalgNQWLESSSRKTLKVIGTVGEPINPAAWMWLYKQVGLSnvsIVDTY 444
Cdd:cd05928 251 PRFDPLV-ILKTLSSYPITTFCGAPTVYRMLV---QQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLD---IYEGY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 445 WQTETGghMITCLPGATPMKPGAAAMPFFGASPVLLDAEGRVIEGPGEGSLCFdRAWP----GMMRGIYGDEQRFVKTYL 520
Cdd:cd05928 324 GQTETG--LICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGI-RVKPirpfGLFSGYVDNPEKTAATIR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 521 APFngyYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVG- 599
Cdd:cd05928 401 GDF---YLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQf 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 71982997 600 -ERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRK 648
Cdd:cd05928 478 lSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
100-641 |
4.61e-50 |
|
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: 180.50 E-value: 4.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 100 LERNIKRgYGNKIAYIFEGneptdtSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHS 179
Cdd:cd17631 1 LRRRARR-HPDRTALVFGG------RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 180 VVFAGFSAESLAARVVDARCRVLVtadgvfrgakpiglksiadaaavlasqedvkveaiimvehlkrvtkpdgvelpkvd 259
Cdd:cd17631 74 PLNFRLTPPEVAYILADSGAKVLF-------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 260 ytditviydsemlkcagvdspvewmdsEDPLFILYTSGSTGKPKGIQHTTaGYMTYAYATTKYTFDAQEDDVYWCTADCG 339
Cdd:cd17631 98 ---------------------------DDLALLMYTSGTTGRPKGAMLTH-RNLLWNAVNALAALDLGPDDVLLVVAPLF 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 340 WITGHSYLLYGPLMNGLKGIwyegVPTYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNqwLESSSRKTLKVIGTVGE 419
Cdd:cd17631 150 HIGGLGVFTLPTLLRGGTVV----ILRKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPR--FATTDLSSLRAVIYGGA 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 420 PInPAAwmwLYKQVGLSNVSIVDTYWQTETGGhMITCL-PGATPMKPGAAAMPFFGASPVLLDAEGRVIEgPGE-GSLCF 497
Cdd:cd17631 224 PM-PER---LLRALQARGVKFVQGYGMTETSP-GVTFLsPEDHRRKLGSAGRPVFFVEVRIVDPDGREVP-PGEvGEIVV 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 498 dRAwPGMMRGIYGDEQRFVKTYlapFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAA 577
Cdd:cd17631 298 -RG-PHVMAGYWNRPEATAAAF---RDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVA 372
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71982997 578 VVAAPHDIKGSFPYAFVTLNVGERINEklvAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKV 641
Cdd:cd17631 373 VIGVPDEKWGEAVVAVVVPRPGAELDE---DELIAHCRERLARYKIPKSVEFVDALPRNATGKI 433
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
128-650 |
1.39e-48 |
|
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: 176.60 E-value: 1.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 128 TYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMhsvvfagfsaeslaarVVDARcrVLVTADG 207
Cdd:cd05974 2 SFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAV----------------VIPAT--TLLTPDD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 208 VfRGAKPIGlksiadaAAVLASQEDVkveaiimvehlkrvTKPDgvelpkvdytditviydsemlkcagvdspvewmdse 287
Cdd:cd05974 64 L-RDRVDRG-------GAVYAAVDEN--------------THAD------------------------------------ 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 288 DPLFILYTSGSTGKPKGIQHTTAGYmTYAYATTKYTFDAQEDDVYWCTADCGWITGHSYLLYGPLMNGLKGIWYegvpTY 367
Cdd:cd05974 86 DPMLLYFTSGTTSKPKLVEHTHRSY-PVGHLSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLF----NY 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 368 P--TPSRMWDVTDKYGVTKLYTSPTAARALMalgNQWLESSSRKTLKVIGTvGEPINP-------AAWmwlykqvglsNV 438
Cdd:cd05974 161 ArfDAKRVLAALVRYGVTTLCAPPTVWRMLI---QQDLASFDVKLREVVGA-GEPLNPevieqvrRAW----------GL 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 439 SIVDTYWQTETgghmiTCLPGATP---MKPGAAAMPFFGASPVLLDAEGRVIEgpgEGSLCFDRAWP---GMMRGIYGDE 512
Cdd:cd05974 227 TIRDGYGQTET-----TALVGNSPgqpVKAGSMGRPLPGYRVALLDPDGAPAT---EGEVALDLGDTrpvGLMKGYAGDP 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 513 QrfvKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYA 592
Cdd:cd05974 299 D---KTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKA 375
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 71982997 593 FVTLNVGERINEKLVAELKKLVREKIGALAVPDVIQEAPgLPKTRSGKVTRRILRKIA 650
Cdd:cd05974 376 FIVLRAGYEPSPETALEIFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRRRE 432
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
121-648 |
7.68e-48 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 175.96 E-value: 7.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 121 PTDTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCR 200
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 201 VLVTADGvfrGAKPIGLKSIADAAAVLASQEDVKVeaiimvehlkRVTKPDGVELPKVDYTDItviydsemlkcagVDSP 280
Cdd:cd05926 89 LVLTPKG---ELGPASRAASKLGLAILELALDVGV----------LIRAPSAESLSNLLADKK-------------NAKS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 281 VEWMDSEDPLFILYTSGSTGKPKGIQ--HTT-AGYMTYAYATTKYTFDaqeddvywctaDCGWITGHSYLLYGpLMNGLK 357
Cdd:cd05926 143 EGVPLPDDLALILHTSGTTGRPKGVPltHRNlAASATNITNTYKLTPD-----------DRTLVVMPLFHVHG-LVASLL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 358 GIWYEG----VPTYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQwLESSSRKTLKVIGTVGEPINPAAWMWLYKQV 433
Cdd:cd05926 211 STLAAGgsvvLPPRFSASTFWPDVRDYNATWYTAVPTIHQILLNRPEP-NPESPPPKLRFIRSCSASLPPAVLEALEATF 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 434 GlsnVSIVDTYWQTETGgHMITC--LPgATPMKPGAAAMPFfGASPVLLDAEGRVIEGPGEGSLCFdRAwPGMMRGIYGD 511
Cdd:cd05926 290 G---APVLEAYGMTEAA-HQMTSnpLP-PGPRKPGSVGKPV-GVEVRILDEDGEILPPGVVGEICL-RG-PNVTRGYLNN 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 512 EQrfvKTYLAPF-NGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFP 590
Cdd:cd05926 362 PE---ANAEAAFkDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEV 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 71982997 591 YAFVTLNVGERINEklvAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRK 648
Cdd:cd05926 439 AAAVVLREGASVTE---EELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
97-652 |
5.56e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 171.14 E-value: 5.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 97 YNCLERNIKRgYGNKIAYIFEGneptdtSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGA 176
Cdd:PRK06187 9 GRILRHGARK-HPDKEAVYFDG------RRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 177 -MHSV-VFagFSAESLAARVVDARCRVLVtADGVFrgakpigLKSIADAAAVLASqedvkVEAIIMVEhlkrvtkpdgvE 254
Cdd:PRK06187 82 vLHPInIR--LKPEEIAYILNDAEDRVVL-VDSEF-------VPLLAAILPQLPT-----VRTVIVEG-----------D 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 255 LPKVDyTDITVIYDSEMLKCAGVDSPVEWMDSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYtFDAQEDDVY-- 332
Cdd:PRK06187 136 GPAAP-LAPEVGEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAW-LKLSRDDVYlv 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 333 ---------WctadcGWItghsyllYGPLMNGLKGIwyegvptYP---TPSRMWDVTDKYGVTKLYTSPTAARALMAL-- 398
Cdd:PRK06187 214 ivpmfhvhaW-----GLP-------YLALMAGAKQV-------IPrrfDPENLLDLIETERVTFFFAVPTIWQMLLKApr 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 399 -GNQWLesSSRKtLKVIGtvGEPINPAawmwLYKQ-VGLSNVSIVDTYWQTETGGhMITCLP-----GATPMKPGAAAMP 471
Cdd:PRK06187 275 aYFVDF--SSLR-LVIYG--GAALPPA----LLREfKEKFGIDLVQGYGMTETSP-VVSVLPpedqlPGQWTKRRSAGRP 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 472 FFGASPVLLDAEGRVIEGPGE--GSLCFdRAwPGMMRGIYGDEQRFVKTYLapfNGYYFTGDGARRDEDGYLWITGRVDD 549
Cdd:PRK06187 345 LPGVEARIVDDDGDELPPDGGevGEIIV-RG-PWLMQGYWNRPEATAETID---GGWLHTGDVGYIDEDGYLYITDRIKD 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 550 LMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEKlvaELKKLVREKIGALAVPDVIQE 629
Cdd:PRK06187 420 VIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAK---ELRAFLRGRLAKFKLPKRIAF 496
|
570 580
....*....|....*....|....
gi 71982997 630 APGLPKTRSGKVTRRILR-KIAEG 652
Cdd:PRK06187 497 VDELPRTSVGKILKRVLReQYAEG 520
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
90-648 |
7.76e-45 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 170.31 E-value: 7.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 90 GAKTNISYNCLERNI----KRgygNKIAYIFEGNEPTDTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELA 165
Cdd:PTZ00237 55 GGELNTCYNVLDIHVknplKR---DQDALIYECPYLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 166 VAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTAD-GVFRGakpiglksiadaaavlasqedvkvEAIIMVEHL 244
Cdd:PTZ00237 132 IAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTNyGILND------------------------EIITFTPNL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 245 KRVT-----KPDGV-ELPKVDYT---------DITVI-----YDSEMLKCAGVDS-------PVEwmdSEDPLFILYTSG 297
Cdd:PTZ00237 188 KEAIelstfKPSNViTLFRNDITsesdlkkieTIPTIpntlsWYDEIKKIKENNQspfyeyvPVE---SSHPLYILYTSG 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 298 STGKPKGIQHTTAGYMTYAYATTKYTFDAQEDDVYWCTADCGWITGHSYLlYGPLMNGLKGIWYEGVPTYPT--PSRMWD 375
Cdd:PTZ00237 265 TTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFL-YGSLSLGNTFVMFEGGIIKNKhiEDDLWN 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 376 VTDKYGVTKLYTSPTAARALMALGNQWLESSSR---KTLKVIGTVGEPINPAAWMWLYKQVglsNVSIVDTYWQTETGGH 452
Cdd:PTZ00237 344 TIEKHKVTHTLTLPKTIRYLIKTDPEATIIRSKydlSNLKEIWCGGEVIEESIPEYIENKL---KIKSSRGYGQTEIGIT 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 453 MITCLpGATPMKPGAAAMPFFGASPVLLDAEGRVIEGPGEGSLCFDRAWP-GMMRGIYGDEQRFvKTYLAPFNGYYFTGD 531
Cdd:PTZ00237 421 YLYCY-GHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKLPMPpSFATTFYKNDEKF-KQLFSKFPGYYNSGD 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 532 GARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINE----KLV 607
Cdd:PTZ00237 499 LGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQSidlnKLK 578
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 71982997 608 AELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRK 648
Cdd:PTZ00237 579 NEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISK 619
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
92-648 |
8.31e-44 |
|
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: 164.63 E-value: 8.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 92 KTNISYNCLERNIKRGYGNKIAYIfegnepTDTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLAC 171
Cdd:TIGR02262 2 KYNAAEDLLDRNVVEGRGGKTAFI------DDISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 172 ARIGAMHSVVFAGFSAESLAARVVDARCRVlvtadgvfrgakpiglksiadaaaVLASQEDVKV--EAIIMVEHLKRVTK 249
Cdd:TIGR02262 76 IRAGIVPVALNTLLTADDYAYMLEDSRARV------------------------VFVSGALLPVikAALGKSPHLEHRVV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 250 PDGVELPKVDYTDItVIYDSEMLKCAGVDSpvewmdsEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYTFDAQED 329
Cdd:TIGR02262 132 VGRPEAGEVQLAEL-LATESEQFKPAATQA-------DDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIRED 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 330 DVYWCTADCGWITGHSYLLYGPLMNGLKGIWYegvPTYPTPSRMWDVTDKYGVTKLYTSPTAARALMAlgNQWLESSSRK 409
Cdd:TIGR02262 204 DVCFSAAKLFFAYGLGNALTFPMSVGATTVLM---GERPTPDAVFDRLRRHQPTIFYGVPTLYAAMLA--DPNLPSEDQV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 410 TLKVIGTVGEPInPAawmwlykQVGLS-----NVSIVDTYWQTETGGHMITCLPGAtpMKPGAAAMPFFGASPVLLDAEG 484
Cdd:TIGR02262 279 RLRLCTSAGEAL-PA-------EVGQRwqarfGVDIVDGIGSTEMLHIFLSNLPGD--VRYGTSGKPVPGYRLRLVGDGG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 485 RVIEGPGEGSLCFDRawPGMMRGIYGDEQRFVKTYLAPFNGyyfTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIE 564
Cdd:TIGR02262 349 QDVADGEPGELLISG--PSSATMYWNNRAKSRDTFQGEWTR---SGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIE 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 565 SALVAHEK---VAEAAVVAAPHDIKgsfPYAFVTLNVGErinEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKV 641
Cdd:TIGR02262 424 SALIQHPAvleAAVVGVADEDGLIK---PKAFVVLRPGQ---TALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKI 497
|
....*..
gi 71982997 642 TRRILRK 648
Cdd:TIGR02262 498 QRFKLRE 504
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
110-644 |
5.63e-43 |
|
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: 161.16 E-value: 5.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 110 NKIAYIFEGneptdtSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAES 189
Cdd:cd05930 2 DAVAVVDGD------QSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 190 LAARVVDARCRVLVTadgvfrgakpiglksiadaaavlasqedvkveaiimvehlkrvtkpdgvelpkvdytditviyds 269
Cdd:cd05930 76 LAYILEDSGAKLVLT----------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 270 emlkcagvdspvewmDSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKyTFDAQEDDVYWCTADCGWItGHSYLLY 349
Cdd:cd05930 91 ---------------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQE-AYPLTPGDRVLQFTSFSFD-VSVWEIF 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 350 GPLMNGLKGIWyegVP--TYPTPSRMWDVTDKYGVTKLYTSPTAARALMalgnQWLESSSRKTLKVIGTVGEPINPAAWM 427
Cdd:cd05930 154 GALLAGATLVV---LPeeVRKDPEALADLLAEEGITVLHLTPSLLRLLL----QELELAALPSLRLVLVGGEALPPDLVR 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 428 WLYKQvgLSNVSIVDTYWQTET--GGHMITCLPGATPMKPGAAAMPFFGASPVLLDAEGRV--IEGPGEgsLCFdrAWPG 503
Cdd:cd05930 227 RWREL--LPGARLVNLYGPTEAtvDATYYRVPPDDEEDGRVPIGRPIPNTRVYVLDENLRPvpPGVPGE--LYI--GGAG 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 504 MMRGIYGD----EQRFVKTylaPFNG---YYFTGDGARRDEDG---YLwitGRVDDLMNVSGHLLSTAEIESALVAHEKV 573
Cdd:cd05930 301 LARGYLNRpeltAERFVPN---PFGPgerMYRTGDLVRWLPDGnleFL---GRIDDQVKIRGYRIELGEIEAALLAHPGV 374
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71982997 574 AEAAVVAAPHDIKGSFPYAFVTLNVGERINEklvAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRR 644
Cdd:cd05930 375 REAAVVAREDGDGEKRLVAYVVPDEGGELDE---EELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRK 442
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
127-647 |
2.50e-42 |
|
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: 158.61 E-value: 2.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 127 WTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTad 206
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 207 gvfrgakpiglksiadaaavlasqedvkveaiimvehlkrvtkpdgvelpkvdytditviydsemlkcagvdspvewmds 286
Cdd:cd05934 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 287 eDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYtFDAQEDDVYWCTADCGWITGHSYLLYGPLMNGLKgiwYEGVPT 366
Cdd:cd05934 82 -DPASILYTSGTTGPPKGVVITHANLTFAGYYSARR-FGLGEDDVYLTVLPLFHINAQAVSVLAALSVGAT---LVLLPR 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 367 YpTPSRMWDVTDKYGVTKLYTSPTAARALMALGnqwlESSSRKTLKVIGTVGEPINPAAWMWLYKQVGlsnVSIVDTYWQ 446
Cdd:cd05934 157 F-SASRFWSDVRRYGATVTNYLGAMLSYLLAQP----PSPDDRAHRLRAAYGAPNPPELHEEFEERFG---VRLLEGYGM 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 447 TETGGHMITCLPGATPmkPGAAAMPFFGASPVLLDAEGR--VIEGPGEGSLCFDRAWpGMMRGIYGDEQrfvKTYLAPFN 524
Cdd:cd05934 229 TETIVGVIGPRDEPRR--PGSIGRPAPGYEVRIVDDDGQelPAGEPGELVIRGLRGW-GFFKGYYNMPE---ATAEAMRN 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 525 GYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERIne 604
Cdd:cd05934 303 GWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETL-- 380
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 71982997 605 kLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILR 647
Cdd:cd05934 381 -DPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
122-641 |
6.16e-42 |
|
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: 158.92 E-value: 6.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 122 TDTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRV 201
Cdd:cd05911 6 DTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 202 LVTAdgvfrgakPIGLKSIADAAAVLASQEDVkveaIIMVEHLKRVTKPDGVELPKVDYTDITVIYDSEMLKcagvdspv 281
Cdd:cd05911 86 IFTD--------PDGLEKVKEAAKELGPKDKI----IVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGK-------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 282 ewmdsEDPLFILYTSGSTGKPKGIQ--HTTAGYMTYAYATTKYTFDaQEDDVYWCTADCGWITGHSYLLYGPLmnglkgi 359
Cdd:cd05911 146 -----DDTAAILYSSGTTGLPKGVClsHRNLIANLSQVQTFLYGND-GSNDVILGFLPLYHIYGLFTTLASLL------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 360 wyEGVPTY----PTPSRMWDVTDKYGVTKLYTSPTAARALmalgnqwLESSSRK-----TLKVIGTVGEPINPAawmwLY 430
Cdd:cd05911 213 --NGATVIimpkFDSELFLDLIEKYKITFLYLVPPIAAAL-------AKSPLLDkydlsSLRVILSGGAPLSKE----LQ 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 431 KQVG--LSNVSIVDTYWQTETGGhMITCLPGaTPMKPGAAA--MPFFGASpvLLDAEGRVIEGPGE-GSLCFDRawPGMM 505
Cdd:cd05911 280 ELLAkrFPNATIKQGYGMTETGG-ILTVNPD-GDDKPGSVGrlLPNVEAK--IVDDDGKDSLGPNEpGEICVRG--PQVM 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 506 RGIYGDEQRFVKTYlaPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDI 585
Cdd:cd05911 354 KGYYNNPEATKETF--DEDGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEV 431
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71982997 586 KGSFPYAFVTLNVGERINEKlvaELKKLVREKI--------GALAVPDviqeapgLPKTRSGKV 641
Cdd:cd05911 432 SGELPRAYVVRKPGEKLTEK---EVKDYVAKKVasykqlrgGVVFVDE-------IPKSASGKI 485
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
112-647 |
1.45e-41 |
|
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: 157.89 E-value: 1.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 112 IAYIFEGneptdtSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLA 191
Cdd:cd17651 12 PALVAEG------RRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 192 ARVVDARCRVLVTADGvfrgakpiglksiadaaavLASQEDVKVEAIIMVEHLKRVTKPDgvelpkvdytditviydsem 271
Cdd:cd17651 86 FMLADAGPVLVLTHPA-------------------LAGELAVELVAVTLLDQPGAAAGAD-------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 272 lkcagvDSPVEWMDSEDPLFILYTSGSTGKPKGIQ------------HTTAGYMTYAYATTKY---TFDAQEDDVYwcta 336
Cdd:cd17651 127 ------AEPDPALDADDLAYVIYTSGSTGRPKGVVmphrslanlvawQARASSLGPGARTLQFaglGFDVSVQEIF---- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 337 dcgwitghSYLLYGplmnglKGIWYEGVPTYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGnqWLESSSRKTLKVIGT 416
Cdd:cd17651 197 --------STLCAG------ATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRALAEHG--RPLGVRLAALRYLLT 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 417 VGEP--INPAAWMWLYKQVGLSnvsIVDTYWQTETggHMITC--LPGATPMKPGAAAM--PFFGASPVLLDAEGRVIEGP 490
Cdd:cd17651 261 GGEQlvLTEDLREFCAGLPGLR---LHNHYGPTET--HVVTAlsLPGDPAAWPAPPPIgrPIDNTRVYVLDAALRPVPPG 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 491 GEGSLCFdrAWPGMMRGIYGD----EQRFVKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESA 566
Cdd:cd17651 336 VPGELYI--GGAGLARGYLNRpeltAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAA 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 567 LVAHEKVAEAAVVAAPHDIKGSFPYAFVtlnVGERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRIL 646
Cdd:cd17651 414 LARHPGVREAVVLAREDRPGEKRLVAYV---VGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRAL 490
|
.
gi 71982997 647 R 647
Cdd:cd17651 491 P 491
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
120-650 |
3.00e-41 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 159.35 E-value: 3.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 120 EPTDTS-TWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLAcariGAMHSVVFA---GFSAESLAARVV 195
Cdd:PRK07529 51 DPLDRPeTWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG----GEAAGIANPinpLLEPEQIAELLR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 196 DARCRVLVTAdGVFRGAkpiglkSIAD-AAAVLASQEDVKveAIIMVEHLKRVTKPDG--VELPKVDYTDITVIYDSEML 272
Cdd:PRK07529 127 AAGAKVLVTL-GPFPGT------DIWQkVAEVLAALPELR--TVVEVDLARYLPGPKRlaVPLIRRKAHARILDFDAELA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 273 KCagvdsPVEWMDSEDP--------LFilYTSGSTGKPKGIQHTTAG--YMTYAYATTkytFDAQEDDVYWC-------- 334
Cdd:PRK07529 198 RQ-----PGDRLFSGRPigpddvaaYF--HTGGTTGMPKLAQHTHGNevANAWLGALL---LGLGPGDTVFCglplfhvn 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 335 ----TADCGWITGHSYLLYGPLmnGLKGiwyEGVPtyptpSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSrkt 410
Cdd:PRK07529 268 allvTGLAPLARGAHVVLATPQ--GYRG---PGVI-----ANFWKIVERYRINFLSGVPTVYAALLQVPVDGHDISS--- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 411 LKVIGTVGEPINPAAWMWLYKQVGlsnVSIVDTYWQTETgghmiTCL----PGATPMKPGAAA--MPFFGASPVLLDAEG 484
Cdd:PRK07529 335 LRYALCGAAPLPVEVFRRFEAATG---VRIVEGYGLTEA-----TCVssvnPPDGERRIGSVGlrLPYQRVRVVILDDAG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 485 RVIE--GPGE-GSLCFdrAWPGMMRGiYGDEQRFVKTYLAPfnGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTA 561
Cdd:PRK07529 407 RYLRdcAVDEvGVLCI--AGPNVFSG-YLEAAHNKGLWLED--GWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPA 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 562 EIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEklvAELKKLVREKIGA-LAVPDVIQEAPGLPKTRSGK 640
Cdd:PRK07529 482 AIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATE---AELLAFARDHIAErAAVPKHVRILDALPKTAVGK 558
|
570
....*....|
gi 71982997 641 VTRRILRKIA 650
Cdd:PRK07529 559 IFKPALRRDA 568
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
100-647 |
2.19e-40 |
|
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: 154.26 E-value: 2.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 100 LERNIKRgYGNKIAYIFEGneptdtSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAmhs 179
Cdd:cd05936 5 LEEAARR-FPDKTALIFMG------RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 180 vvfagfsaeslaaRVVDarCRVLVTADGvfrgakpiglksiadaaavLASQ-EDVKVEAIIMVEHLKRVTKPDgvelpkv 258
Cdd:cd05936 75 -------------VVVP--LNPLYTPRE-------------------LEHIlNDSGAKALIVAVSFTDLLAAG------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 259 dytditviydsemlkcAGVDSPVEwMDSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYTFDAQEDD-------- 330
Cdd:cd05936 114 ----------------APLGERVA-LTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEGDdvvlaalp 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 331 ---VYWCTADC--GWITGHSYLLygplmnglkgiwyegVPTyPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNqwLES 405
Cdd:cd05936 177 lfhVFGLTVALllPLALGATIVL---------------IPR-FRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPE--FKK 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 406 SSRKTLKVIGTVGEPINPAawmwLYKQVG-LSNVSIVDTYWQTETGGhMITCLPGATPMKPGAAAMPFFGASPVLLDAEG 484
Cdd:cd05936 239 RDFSSLRLCISGGAPLPVE----VAERFEeLTGVPIVEGYGLTETSP-VVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 485 rVIEGPGE-GSLCFdrAWPGMMRGIYGD----EQRFVktylapfNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLS 559
Cdd:cd05936 314 -EELPPGEvGELWV--RGPQVMKGYWNRpeetAEAFV-------DGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVY 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 560 TAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEklvAELKKLVREKIGALAVPDVIQEAPGLPKTRSG 639
Cdd:cd05936 384 PREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTE---EEIIAFCREQLAGYKVPRQVEFRDELPKSAVG 460
|
....*...
gi 71982997 640 KVTRRILR 647
Cdd:cd05936 461 KILRRELR 468
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
286-647 |
2.44e-38 |
|
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: 147.62 E-value: 2.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 286 SEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYTFDAQEDDVYWCTADCGWITGHSYLLYGPLMNGLKGIWYEGVp 365
Cdd:cd05958 96 SDDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEA- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 366 typTPSRMWDVTDKYGVTKLYTSPTAARALMALG--NQWLESSSRKTLkvigTVGEPINPAAWMWLYKQVGlsnVSIVDT 443
Cdd:cd05958 175 ---TPDLLLSAIARYKPTVLFTAPTAYRAMLAHPdaAGPDLSSLRKCV----SAGEALPAALHRAWKEATG---IPIIDG 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 444 YWQTETGGHMITCLPGAtpMKPGAAAMPFFGASPVLLDAEGRVIEgPGEGSLCFDRAwPGMMRGIYGDEQRfvkTYLApf 523
Cdd:cd05958 245 IGSTEMFHIFISARPGD--ARPGATGKPVPGYEAKVVDDEGNPVP-DGTIGRLAVRG-PTGCRYLADKRQR---TYVQ-- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 524 NGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERIN 603
Cdd:cd05958 316 GGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPG 395
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 71982997 604 EKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILR 647
Cdd:cd05958 396 PVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
128-571 |
4.26e-37 |
|
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: 143.56 E-value: 4.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 128 TYNELHAQVVQFSAVLRS-HGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTAD 206
Cdd:TIGR01733 1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 207 GvfrgakpiglksiadaaavLASQEDVKVEAIIMVEHLKRVTKPDGVELPKVDytditviydsemlkcagvdspvEWMDS 286
Cdd:TIGR01733 81 A-------------------LASRLAGLVLPVILLDPLELAALDDAPAPPPPD----------------------APSGP 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 287 EDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYtFDAQEDDVywctadcgWITGHSYL-------LYGPLMNGLKGI 359
Cdd:TIGR01733 120 DDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARR-YGLDPDDR--------VLQFASLSfdasveeIFGALLAGATLV 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 360 WYEGVPTYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNqwlesSSRKTLKVIGTVGEPINPAA---WMWLYkqvglS 436
Cdd:TIGR01733 191 VPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALLAAALP-----PALASLRLVILGGEALTPALvdrWRARG-----P 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 437 NVSIVDTYWQTETGGHmITCLPGATPMKPGAAAM----PFFGASPVLLDAEGRV--IEGPGEgsLCFdrAWPGMMRGIYG 510
Cdd:TIGR01733 261 GARLINLYGPTETTVW-STATLVDPDDAPRESPVpigrPLANTRLYVLDDDLRPvpVGVVGE--LYI--GGPGVARGYLN 335
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71982997 511 DE----QRFVKTYLAPFNGY--YFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHE 571
Cdd:TIGR01733 336 RPeltaERFVPDPFAGGDGArlYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHP 402
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
123-646 |
5.34e-37 |
|
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: 143.99 E-value: 5.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 123 DTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVL 202
Cdd:cd17643 9 EDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 203 VTadgvfrgakpiglksiadaaavlasqedvkveaiimvehlkrvtkpdgvelpkvdytditviydsemlkcagvdspve 282
Cdd:cd17643 89 LT------------------------------------------------------------------------------ 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 283 wmDSEDPLFILYTSGSTGKPKGIQhTTAGYMTYAYATTKYTFDAQEDDVywctadcgWITGHSYL-------LYGPLMNG 355
Cdd:cd17643 91 --DPDDLAYVIYTSGSTGRPKGVV-VSHANVLALFAATQRWFGFNEDDV--------WTLFHSYAfdfsvweIWGALLHG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 356 LKGIwyegVPTYPT---PSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSRKTLKVIGtvGEPINPAAWMWLYKQ 432
Cdd:cd17643 160 GRLV----VVPYEVarsPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFG--GEALEAAMLRPWAGR 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 433 VGLSNVSIVDTYWQTETGGHmITCLPGATPMKPGAAAMPFFGASPVL----LDAEGRVIE--GPGEGSLCfdraWPGMMR 506
Cdd:cd17643 234 FGLDRPQLVNMYGITETTVH-VTFRPLDAADLPAAAASPIGRPLPGLrvyvLDADGRPVPpgVVGELYVS----GAGVAR 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 507 GIYGDE----QRFVktyLAPFNG----YYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAV 578
Cdd:cd17643 309 GYLGRPeltaERFV---ANPFGGpgsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAV 385
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71982997 579 VAAPHDIKGSFPYAFVtlnVGERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRIL 646
Cdd:cd17643 386 IVREDEPGDTRLVAYV---VADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
106-652 |
2.47e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 143.53 E-value: 2.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 106 RGYGNKIAYIFEGneptdtSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGF 185
Cdd:PRK08316 22 RRYPDKTALVFGD------RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFML 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 186 SAESLAARVVDARCRVLVTADGvfrgakpigLKSIADAAAVLASQEDVKVEaiimvehlkRVTKPDGVELPKVDYTDitv 265
Cdd:PRK08316 96 TGEELAYILDHSGARAFLVDPA---------LAPTAEAALALLPVDTLILS---------LVLGGREAPGGWLDFAD--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 266 iydseMLKCAGVDSPVEWMDSEDPLFILYTSGSTGKPKGIQHTT----AGYMTyayattkytfdaqeddvywCTADCGW- 340
Cdd:PRK08316 155 -----WAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTHraliAEYVS-------------------CIVAGDMs 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 341 ---ITGHSYLLY---------GP-LMNGLKGIWYEGvptyPTPSRMWDVTDKYGVTKLYTSPTAARALM---ALGNQWLe 404
Cdd:PRK08316 211 addIPLHALPLYhcaqldvflGPyLYVGATNVILDA----PDPELILRTIEAERITSFFAPPTVWISLLrhpDFDTRDL- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 405 SSSRKtlkviGTVGEPINPAA----WMWLYKQVGLSNVsivdtYWQTETGghmitclPGATPM-------KPGAAAMPFF 473
Cdd:PRK08316 286 SSLRK-----GYYGASIMPVEvlkeLRERLPGLRFYNC-----YGQTEIA-------PLATVLgpeehlrRPGSAGRPVL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 474 GASPVLLDAEGRVIeGPGE-GSLCFdRAwPGMMRGIYGDEQrfvKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMN 552
Cdd:PRK08316 349 NVETRVVDDDGNDV-APGEvGEIVH-RS-PQLMLGYWDDPE---KTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIK 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 553 VSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEklvAELKKLVREKIGALAVPDVIQEAPG 632
Cdd:PRK08316 423 TGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTE---DELIAHCRARLAGFKVPKRVIFVDE 499
|
570 580
....*....|....*....|
gi 71982997 633 LPKTRSGKVTRRILRKIAEG 652
Cdd:PRK08316 500 LPRNPSGKILKRELRERYAG 519
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
126-646 |
3.87e-33 |
|
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: 133.48 E-value: 3.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 126 TWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTA 205
Cdd:cd12117 22 SLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLTD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 206 DGVFRGAKpiglksiADAAAVLASQEDVKVEAiimvehlkrvtkpdgvelpkvdytditviydsemlkcagvDSPVEWMD 285
Cdd:cd12117 102 RSLAGRAG-------GLEVAVVIDEALDAGPA----------------------------------------GNPAVPVS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 286 SEDPLFILYTSGSTGKPKGIQHTTAGyMTYAYATTKYTfDAQEDDVYWCTADCGWiTGHSYLLYGPLMNGLKGIWYEGvP 365
Cdd:cd12117 135 PDDLAYVMYTSGSTGRPKGVAVTHRG-VVRLVKNTNYV-TLGPDDRVLQTSPLAF-DASTFEIWGALLNGARLVLAPK-G 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 366 TYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLEsssrkTLKVIGTVGEPINPAAWMWLYKQVGlsNVSIVDTYW 445
Cdd:cd12117 211 TLLDPDALGALIAEEGVTVLWLTAALFNQLADEDPECFA-----GLRELLTGGEVVSPPHVRRVLAACP--GLRLVNGYG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 446 QTETGGHMITCLPGATPMKPGAAAM--PFFGASPVLLDAEGRVIEgPGE-GSLCFdrAWPGMMRGIYGDE----QRFVKt 518
Cdd:cd12117 284 PTENTTFTTSHVVTELDEVAGSIPIgrPIANTRVYVLDEDGRPVP-PGVpGELYV--GGDGLALGYLNRPaltaERFVA- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 519 ylAPFNG---YYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVt 595
Cdd:cd12117 360 --DPFGPgerLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYV- 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 71982997 596 lnVGERinEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRIL 646
Cdd:cd12117 437 --VAEG--ALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
28-648 |
1.68e-32 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 134.05 E-value: 1.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 28 LLAGAHCAGLQSYHDLYRSSINDADEFWRTVSSEL--HFEQGTSKGLEWNFDSKAGNVFVKfmdGAKTNISYNCLERNIK 105
Cdd:PLN03052 110 LLGSKYKDPISSFSEFQRFSVENPEVYWSIVLDELslVFSVPPRCILDTSDESNPGGQWLP---GAVLNVAECCLTPKPS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 106 RgYGNKIAYIF--EGNEPTDTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLAcarigamhsVVFA 183
Cdd:PLN03052 187 K-TDDSIAIIWrdEGSDDLPVNRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLA---------IILA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 184 GFS----AESLAARVVDARCRV-----LVTADGVFRGAKPIGLKS-IADAAAVLAsqedvkveaiimvehlkrVTKPDGV 253
Cdd:PLN03052 257 GCVvvsiADSFAPSEIATRLKIskakaIFTQDVIVRGGKSIPLYSrVVEAKAPKA------------------IVLPADG 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 254 ELPKVDYTDITVIYDSEMLKCAGVDSPVEWMDSEDPL----FILYTSGSTGKPKGIQHTTAGYMTYAyATTKYTFDAQED 329
Cdd:PLN03052 319 KSVRVKLREGDMSWDDFLARANGLRRPDEYKAVEQPVeaftNILFSSGTTGEPKAIPWTQLTPLRAA-ADAWAHLDIRKG 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 330 DVY-WCTaDCGWITGHsYLLYGPLMNGLKGIWYEGVPTYPTPSRMwdVTDKyGVTKLYTSPTAARAlmalgnqWLESSSR 408
Cdd:PLN03052 398 DIVcWPT-NLGWMMGP-WLVYASLLNGATLALYNGSPLGRGFAKF--VQDA-KVTMLGTVPSIVKT-------WKNTNCM 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 409 KTL-----KVIGTVGEPINPAAWMWLYKQVGLSnvSIVDTYWQTETGGHMITclpgATPMKP---GAAAMPFFGASPVLL 480
Cdd:PLN03052 466 AGLdwssiRCFGSTGEASSVDDYLWLMSRAGYK--PIIEYCGGTELGGGFVT----GSLLQPqafAAFSTPAMGCKLFIL 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 481 DAEGRVI--EGPGEGSLCFDrawPGMM----RGIYGDEQRFVKTYLAPFNGYYFT--GDGARRDEDGYLWITGRVDDLMN 552
Cdd:PLN03052 540 DDSGNPYpdDAPCTGELALF---PLMFgassTLLNADHYKVYFKGMPVFNGKILRrhGDIFERTSGGYYRAHGRADDTMN 616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 553 VSGHLLSTAEIESAL-VAHEKVAEAAVVAAPHdiKGSFPYAFVTLNVGERINEKLVA--ELKKL----VREKIGALAVPD 625
Cdd:PLN03052 617 LGGIKVSSVEIERVCnAADESVLETAAIGVPP--PGGGPEQLVIAAVLKDPPGSNPDlnELKKIfnsaIQKKLNPLFKVS 694
|
650 660
....*....|....*....|...
gi 71982997 626 VIQEAPGLPKTRSGKVTRRILRK 648
Cdd:PLN03052 695 AVVIVPSFPRTASNKVMRRVLRQ 717
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
126-646 |
2.02e-32 |
|
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: 131.26 E-value: 2.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 126 TWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVT- 204
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTd 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 205 ---ADGVFRGAKPIGLKSIADAAAVLASQEDVkveaiimvehlkrvtkpdgvelpkvdytditviydsemlkcagvdspv 281
Cdd:cd12116 92 dalPDRLPAGLPVLLLALAAAAAAPAAPRTPV------------------------------------------------ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 282 ewmDSEDPLFILYTSGSTGKPKGI---------------QHTTAGYMTYAYATTKYTFDAqeddvywctadcgwitghSY 346
Cdd:cd12116 124 ---SPDDLAYVIYTSGSTGRPKGVvvshrnlvnflhsmrERLGLGPGDRLLAVTTYAFDI------------------SL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 347 L-LYGPLMNGLKGIWYEGVPTYpTPSRMWDVTDKYGVTKLYTSPTAARalMALGNQWLEsssRKTLKVI-GtvGEPINPA 424
Cdd:cd12116 183 LeLLLPLLAGARVVIAPRETQR-DPEALARLIEAHSITVMQATPATWR--MLLDAGWQG---RAGLTALcG--GEALPPD 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 425 AWMWLYKQVG-LSNVsivdtYWQTETgghmiTCLPGATPMKPGAAAM----PFFGASPVLLDAEGR-VIEG-PGEgsLCF 497
Cdd:cd12116 255 LAARLLSRVGsLWNL-----YGPTET-----TIWSTAARVTAAAGPIpigrPLANTQVYVLDAALRpVPPGvPGE--LYI 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 498 drAWPGMMRGIYGD----EQRFVK-TYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEK 572
Cdd:cd12116 323 --GGDGVAQGYLGRpaltAERFVPdPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPG 400
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71982997 573 VAEAAVVAAPHDIKGSFpYAFVTLNVGERINEklvAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRIL 646
Cdd:cd12116 401 VAQAAVVVREDGGDRRL-VAYVVLKAGAAPDA---AALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
92-646 |
2.52e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 132.01 E-value: 2.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 92 KTNISYNcLERNIKRgYGNKIAYIFEGNEptdtstWTYNELHAQVVQFSAVLRSH-GVKRGDVVALYLPMIPELAVAMLA 170
Cdd:PRK08314 9 ETSLFHN-LEVSARR-YPDKTAIVFYGRA------ISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 171 CARIGAMHSVVFAGFSAESLAARVVDARCRVLVT----ADGVFRGAKPIGLKSI--ADAAAVLASQEDVKVEAIIMVEHl 244
Cdd:PRK08314 81 ILRANAVVVPVNPMNREEELAHYVTDSGARVAIVgselAPKVAPAVGNLRLRHVivAQYSDYLPAEPEIAVPAWLRAEP- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 245 krvtkpdgvelPKVDYTDITVIYDSEMLKCAGVDSPVEwMDSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYtF 324
Cdd:PRK08314 160 -----------PLQALAPGGVVAWKEALAAGLAPPPHT-AGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLW-S 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 325 DAQEDDVYWCTADCGWITGHSYLLYGPLmnglkgiwYEGVPTYPTPSrmWD------VTDKYGVTKLYTSPTAARALMAL 398
Cdd:PRK08314 227 NSTPESVVLAVLPLFHVTGMVHSMNAPI--------YAGATVVLMPR--WDreaaarLIERYRVTHWTNIPTMVVDFLAS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 399 GNqwLESSSRKTLKVIGTVGEPINPAAWMWLYKQVGLSnvsIVDTYWQTETGGHMITCLPGATpmKPGAAAMPFFGaspv 478
Cdd:PRK08314 297 PG--LAERDLSSLRYIGGGGAAMPEAVAERLKELTGLD---YVEGYGLTETMAQTHSNPPDRP--KLQCLGIPTFG---- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 479 lLDAegRVIE-------GPGE-------GslcfdrawPGMMRGIYGDEQRFVKTYLApFNGYYF--TGDGARRDEDGYLW 542
Cdd:PRK08314 366 -VDA--RVIDpetleelPPGEvgeivvhG--------PQVFKGYWNRPEATAEAFIE-IDGKRFfrTGDLGRMDEEGYFF 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 543 ITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERIneKLVAE-LKKLVREKIGAL 621
Cdd:PRK08314 434 ITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARG--KTTEEeIIAWAREHMAAY 511
|
570 580
....*....|....*....|....*
gi 71982997 622 AVPDVIQEAPGLPKTRSGKVTRRIL 646
Cdd:PRK08314 512 KYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
111-652 |
3.32e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 131.70 E-value: 3.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 111 KIAYIFEGneptdtSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESL 190
Cdd:PRK06178 49 RPAIIFYG------HVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 191 AARVVDARCRVLVTADGVFRGAKPI----GLKSIA--DAAAVLASQEDVKVeaiimvehlkrvtkPDGVELPKVDYTDIT 264
Cdd:PRK06178 123 SYELNDAGAEVLLALDQLAPVVEQVraetSLRHVIvtSLADVLPAEPTLPL--------------PDSLRAPRLAAAGAI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 265 VIYDSemLKCAGVDSPVEWMDSEDPLFILYTSGSTGKPKGIQHTTaGYMTY-AYATTKYTFDAQEDDVYWCTADCGWITG 343
Cdd:PRK06178 189 DLLPA--LRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQ-RDMVYtAAAAYAVAVVGGEDSVFLSFLPEFWIAG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 344 HSYLLYGPLMNGLkgiwyegvpTYPTPSRmWD------VTDKYGVTKLYTSPTAARALMAL-GNQWLESSSRKTLKVIGT 416
Cdd:PRK06178 266 ENFGLLFPLFSGA---------TLVLLAR-WDavafmaAVERYRVTRTVMLVDNAVELMDHpRFAEYDLSSLRQVRVVSF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 417 VgEPINPAawmwlYKQ--VGLSNVSIVDTYW-QTETggHmiTCLPGATPMKPG---AAAMPFFGASPV------LLDAE- 483
Cdd:PRK06178 336 V-KKLNPD-----YRQrwRALTGSVLAEAAWgMTET--H--TCDTFTAGFQDDdfdLLSQPVFVGLPVpgtefkICDFEt 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 484 GRVIEGPGEGSLCFdRAwPGMMRGIYGDEQrfvKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEI 563
Cdd:PRK06178 406 GELLPLGAEGEIVV-RT-PSLLKGYWNKPE---ATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 564 ESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEklvAELKKLVREKIGALAVPDV-IQEApgLPKTRSGKVT 642
Cdd:PRK06178 481 EALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTA---AALQAWCRENMAVYKVPEIrIVDA--LPMTATGKVR 555
|
570
....*....|
gi 71982997 643 RRILRKIAEG 652
Cdd:PRK06178 556 KQDLQALAEE 565
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
126-648 |
1.51e-31 |
|
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: 127.88 E-value: 1.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 126 TWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTA 205
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 206 DgVFRGAKPiglksiadaaavlasqedvkveaiimvehlkrvtkpdgVELPkvdytditviydsemlkcagvdspvewmd 285
Cdd:cd05903 81 E-RFRQFDP--------------------------------------AAMP----------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 286 sEDPLFILYTSGSTGKPKGIQHT--TAGYMTYAYATtKYTFDaqEDDVYWCTADCGWITGHSYLLYGPLMNG----LKGI 359
Cdd:cd05903 93 -DAVALLLFTSGTTGEPKGVMHShnTLSASIRQYAE-RLGLG--PGDVFLVASPMAHQTGFVYGFTLPLLLGapvvLQDI 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 360 WyegvptypTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSRktLKVIGTVGEPInPAAWMWLYKQVGLSNVS 439
Cdd:cd05903 169 W--------DPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSR--LRTFVCGGATV-PRSLARRAAELLGAKVC 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 440 IVdtYWQTETGGHMITCLPGATPMKPGAAAMPFFGASPVLLDAEGRVIEGPGEGSLcFDRAwPGMMRGIYGDEQrfvKTY 519
Cdd:cd05903 238 SA--YGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGEL-LSRG-PSVFLGYLDRPD---LTA 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 520 LAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVG 599
Cdd:cd05903 311 DAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSG 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 71982997 600 ERIN-EKLVAELKklvREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRK 648
Cdd:cd05903 391 ALLTfDELVAYLD---RQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
112-653 |
1.85e-31 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 129.40 E-value: 1.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 112 IAYIFEGNEPTdtsTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLA 191
Cdd:PRK13295 44 TAVRLGTGAPR---RFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 192 ARVVDARCRVLVtADGVFRGAkpiglksiaDAAAVLAS-QEDVKveaiimveHLKRVTKPDGVELPKVDYTDITVIYDSE 270
Cdd:PRK13295 121 FMLKHAESKVLV-VPKTFRGF---------DHAAMARRlRPELP--------ALRHVVVVGGDGADSFEALLITPAWEQE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 271 MLKCAGVDSPVewMDSEDPLFILYTSGSTGKPKGIQHTT----AGYMTYAYAttkytFDAQEDDVYWCTADCGWITGHSY 346
Cdd:PRK13295 183 PDAPAILARLR--PGPDDVTQLIYTSGTTGEPKGVMHTAntlmANIVPYAER-----LGLGADDVILMASPMAHQTGFMY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 347 LLYGPLMNG----LKGIWyegvptypTPSRMWDVTDKYGVTklYTSPTAARALMALGNQWLESSSRKTLKVIGTVGEPIN 422
Cdd:PRK13295 256 GLMMPVMLGatavLQDIW--------DPARAAELIRTEGVT--FTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 423 PA----AWMWLykqvGLSnvsIVDTYWQTETGGHMITClPGATPMKPGAA-AMPFFGASPVLLDAEGRVIEGPGEGSLCF 497
Cdd:PRK13295 326 GAlverARAAL----GAK---IVSAWGMTENGAVTLTK-LDDPDERASTTdGCPLPGVEVRVVDADGAPLPAGQIGRLQV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 498 dRAwPGMMRGIYGDEQRfvktYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAA 577
Cdd:PRK13295 398 -RG-CSNFGGYLKRPQL----NGTDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVA 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71982997 578 VVAAPHDIKGSFPYAFVTLNVGERIN-EKLVAELKklvREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRKIAEGS 653
Cdd:PRK13295 472 IVAYPDERLGERACAFVVPRPGQSLDfEEMVEFLK---AQKVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRGE 545
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
100-651 |
6.82e-31 |
|
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: 127.57 E-value: 6.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 100 LERNIKRgYGNKIAYIFEGNEptdtstWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMhs 179
Cdd:COG1021 31 LRRRAER-HPDRIAVVDGERR------LSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 180 VVFAGFS---AESLA-ARVVDARCrvLVTADgVFRGAKPIGLksiadAAAVLASQEDVKVeaiIMVehlkrVTKPDgvel 255
Cdd:COG1021 102 PVFALPAhrrAEISHfAEQSEAVA--YIIPD-RHRGFDYRAL-----ARELQAEVPSLRH---VLV-----VGDAG---- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 256 pkvDYTDITVIYDsemlkcAGVDSPVEWMDSEDPLFILYTSGSTGKPKGIQHTTAGYMtyayattkYTFDA-------QE 328
Cdd:COG1021 162 ---EFTSLDALLA------APADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYL--------YSVRAsaeicglDA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 329 DDVYWCTADcgwiTGHSYLLYGPlmnGLKGIWYEG----VPTYPTPSRMWDVTDKYGVTklYTS--PTAARAlmalgnqW 402
Cdd:COG1021 225 DTVYLAALP----AAHNFPLSSP---GVLGVLYAGgtvvLAPDPSPDTAFPLIERERVT--VTAlvPPLALL-------W 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 403 LESSSR-----KTLKVIGtVG---------EPINPAAWMWLyKQV-----GLSNVSIVD--TYWQTETGGHMItclpgat 461
Cdd:COG1021 289 LDAAERsrydlSSLRVLQ-VGgaklspelaRRVRPALGCTL-QQVfgmaeGLVNYTRLDdpEEVILTTQGRPI------- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 462 pmkpgaaampffgaSP---VL-LDAEGRVIEgPGE-GSLCFdRAwPGMMRGIYGDEQR----FVKtylapfNGYYFTGDG 532
Cdd:COG1021 360 --------------SPddeVRiVDEDGNPVP-PGEvGELLT-RG-PYTIRGYYRAPEHnaraFTP------DGFYRTGDL 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 533 ARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNvGERINeklVAELKK 612
Cdd:COG1021 417 VRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPR-GEPLT---LAELRR 492
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 71982997 613 LVREK-IGALAVPDVIQEAPGLPKTRSGKVTRRILRKIAE 651
Cdd:COG1021 493 FLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
110-652 |
7.29e-31 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 126.62 E-value: 7.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 110 NKIAYIFEGneptdtSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMhsVVFAG--FSA 187
Cdd:PRK03640 17 DRTAIEFEE------KKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAV--AVLLNtrLSR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 188 ESLAARVVDARCRVLVTADgvfrgakpiglksiaDAAAVLASQEDVKVEaiimvehlkrvtkpdgvELPKVDYTDITviy 267
Cdd:PRK03640 89 EELLWQLDDAEVKCLITDD---------------DFEAKLIPGISVKFA-----------------ELMNGPKEEAE--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 268 dsemlkcagvdsPVEWMDSEDPLFILYTSGSTGKPKGIQHTTAGYmtYAYAT-TKYTFDAQEDDVYWCTADCGWITGHSY 346
Cdd:PRK03640 134 ------------IQEEFDLDEVATIMYTSGTTGKPKGVIQTYGNH--WWSAVgSALNLGLTEDDCWLAAVPIFHISGLSI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 347 LLygplmnglKGIWYeGVPTYptpsrmwdVTDKYGVTKLytsptaaralmalgNQWLESSSRKTLKVIGTV--------- 417
Cdd:PRK03640 200 LM--------RSVIY-GMRVV--------LVEKFDAEKI--------------NKLLQTGGVTIISVVSTMlqrllerlg 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 418 --------------GEPINPAawmwLYKQVGLSNVSIVDTYWQTETGGHMITCLPGATPMKPGAAAMPFFGASpVLLDAE 483
Cdd:PRK03640 249 egtypssfrcmllgGGPAPKP----LLEQCKEKGIPVYQSYGMTETASQIVTLSPEDALTKLGSAGKPLFPCE-LKIEKD 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 484 GRVIEGPGEGSLcfdraW---PGMMRGIYGDEQrfvKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLST 560
Cdd:PRK03640 324 GVVVPPFEEGEI-----VvkgPNVTKGYLNRED---ATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYP 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 561 AEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLnvGERINEklvAELKKLVREKIGALAVPDVIQEAPGLPKTRSGK 640
Cdd:PRK03640 396 AEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVTE---EELRHFCEEKLAKYKVPKRFYFVEELPRNASGK 470
|
570
....*....|..
gi 71982997 641 VTRRILRKIAEG 652
Cdd:PRK03640 471 LLRHELKQLVEE 482
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
294-650 |
1.42e-30 |
|
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: 123.36 E-value: 1.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 294 YTSGSTGKPKGIQHTTAGyMTYAYATTKYTFDAQEDDVYWCTADCGWITGHSYLLYGPLMNGLKGIWyegvptyPTPS-- 371
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVL-------AGPAgy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 372 -------RMWDVTDKYGVTKLYTSPTAARALMAL-GNQWLESssrktLKVIGTVGEPInPAAwmwLYKQV-GLSNVSIVD 442
Cdd:cd05944 81 rnpglfdNFWKLVERYRITSLSTVPTVYAALLQVpVNADISS-----LRFAMSGAAPL-PVE---LRARFeDATGLPVVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 443 TYWQTETGGhMITCLPGATPMKPGAA--AMPFFGASPVLLDAEGRVIE--GPGE-GSLCFdrAWPGMMRGiYGDEQRFVK 517
Cdd:cd05944 152 GYGLTEATC-LVAVNPPDGPKRPGSVglRLPYARVRIKVLDGVGRLLRdcAPDEvGEICV--AGPGVFGG-YLYTEGNKN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 518 TYLAPfnGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLN 597
Cdd:cd05944 228 AFVAD--GWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLK 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 71982997 598 VGERINEklvAELKKLVREKIGA-LAVPDVIQEAPGLPKTRSGKVTRRILRKIA 650
Cdd:cd05944 306 PGAVVEE---EELLAWARDHVPErAAVPKHIEVLEELPVTAVGKVFKPALRADA 356
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
108-648 |
8.50e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 123.86 E-value: 8.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 108 YGNKIAYIFEGNeptdtsTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSA 187
Cdd:PRK07656 18 FGDKEAYVFGDQ------RLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 188 ESLAARVVDARCRVLVTADGvFRGAkpiglksiaDAAAVlasqedvkvEAIIMVEHLKRVTKPDGVELPKVDYTDitviy 267
Cdd:PRK07656 92 DEAAYILARGDAKALFVLGL-FLGV---------DYSAT---------TRLPALEHVVICETEEDDPHTEKMKTF----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 268 dSEMLKCAGVDSPVEWMDSEDPLFILYTSGSTGKPKGIQhTTAGYMTYAYATTKYTFDAQEDDVYWC----------TAd 337
Cdd:PRK07656 148 -TDFLAAGDPAERAPEVDPDDVADILFTSGTTGRPKGAM-LTHRQLLSNAADWAEYLGLTEGDRYLAanpffhvfgyKA- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 338 cGWITghsyllygPLMNGLKGIwyeGVPTYpTPSRMWDVTDKYGVTKLYTSPTAARALMALGNqwLESSSRKTLKVIGTV 417
Cdd:PRK07656 225 -GVNA--------PLMRGATIL---PLPVF-DPDEVFRLIETERITVLPGPPTMYNSLLQHPD--RSAEDLSSLRLAVTG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 418 GEPINPAawmwLYKQV-GLSNVSIVDT-YWQTETGGhmITCL--PGATP-MKPGAAAMPFFGASPVLLDAEGRVIeGPGE 492
Cdd:PRK07656 290 AASMPVA----LLERFeSELGVDIVLTgYGLSEASG--VTTFnrLDDDRkTVAGTIGTAIAGVENKIVNELGEEV-PVGE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 493 -GSLCFdRAwPGMMRGIYGDEQRFVKTYLApfNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHE 571
Cdd:PRK07656 363 vGELLV-RG-PNVMKGYYDDPEATAAAIDA--DGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHP 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71982997 572 KVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEklvAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRK 648
Cdd:PRK07656 439 AVAEAAVIGVPDERLGEVGKAYVVLKPGAELTE---EELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
126-648 |
7.63e-29 |
|
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: 121.04 E-value: 7.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 126 TWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTA 205
Cdd:TIGR03098 25 TLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 206 DGVFRGAKPiglksiadaaaVLASQEDVKVEAIIMVEHLKRVTKPDGvelpkvdytdiTVIYDSEMLKCAGVDSPVEWMD 285
Cdd:TIGR03098 105 SERLDLLHP-----------ALPGCHDLRTLIIVGDPAHASEGHPGE-----------EPASWPKLLALGDADPPHPVID 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 286 SeDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYtFDAQEDDVYWCTADCGWITGHSYLLYGplmnglkgiWYEG-- 363
Cdd:TIGR03098 163 S-DMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATY-LENRPDDRLLAVLPLSFDYGFNQLTTA---------FYVGat 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 364 -VP-TYPTPSRMWDVTDKYGVTKLYTSPTAARALMALgnQWLESSSRkTLKVIGTVGEPINPAAWMWLykQVGLSNVSIV 441
Cdd:TIGR03098 232 vVLhDYLLPRDVLKALEKHGITGLAAVPPLWAQLAQL--DWPESAAP-SLRYLTNSGGAMPRATLSRL--RSFLPNARLF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 442 DTYWQTEtgGHMITCL-PGATPMKPGA--AAMPFfgASPVLLDAEGRVIEgPGE-GSLCfdRAWPGMMRGIYGDEQRFVK 517
Cdd:TIGR03098 307 LMYGLTE--AFRSTYLpPEEVDRRPDSigKAIPN--AEVLVLREDGSECA-PGEeGELV--HRGALVAMGYWNDPEKTAE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 518 TY--LAPFNGY-------YFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGS 588
Cdd:TIGR03098 380 RFrpLPPFPGElhlpelaVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQ 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 589 FPYAFVTLNVGERINEklvAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRK 648
Cdd:TIGR03098 460 AIVLVVTPPGGEELDR---AALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
128-646 |
9.07e-29 |
|
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: 119.73 E-value: 9.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 128 TYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTadg 207
Cdd:cd12115 26 TYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 208 vfrgakpiglksiadaaavlasqedvkveaiimvehlkrvtkpdgvelpkvdytditviydsemlkcagvdspvewmDSE 287
Cdd:cd12115 103 -----------------------------------------------------------------------------DPD 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 288 DPLFILYTSGSTGKPKG--IQHTTAG-------------YMTYAYATTKYTFDAQeddvywctadcgwitghSYLLYGPL 352
Cdd:cd12115 106 DLAYVIYTSGSTGRPKGvaIEHRNAAaflqwaaaafsaeELAGVLASTSICFDLS-----------------VFELFGPL 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 353 MNGLKGIWYEGV---PTYPTPSrmwdvtdkyGVTKLYTSPTAARALMALGNqwLESSsrktLKVIGTVGEPINPAAWMWL 429
Cdd:cd12115 169 ATGGKVVLADNVlalPDLPAAA---------EVTLINTVPSAAAELLRHDA--LPAS----VRVVNLAGEPLPRDLVQRL 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 430 YKQVGLSNVsiVDTYWQTETgghmiTCLPGATPMKPGAAAMPFFGAsPV------LLDAEGRVIeGPGE-GSLCFDRAwp 502
Cdd:cd12115 234 YARLQVERV--VNLYGPSED-----TTYSTVAPVPPGASGEVSIGR-PLantqayVLDRALQPV-PLGVpGELYIGGA-- 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 503 GMMRGIYGD----EQRFVKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAV 578
Cdd:cd12115 303 GVARGYLGRpgltAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVV 382
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71982997 579 VAaphdIKGSFP----YAFVTLNVGERINeklVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRIL 646
Cdd:cd12115 383 VA----IGDAAGerrlVAYIVAEPGAAGL---VEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
128-646 |
1.13e-28 |
|
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: 120.42 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 128 TYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTAdg 207
Cdd:cd05904 34 TYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTT-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 208 vfrgakPIGLKSIADAAA-VLASQEDVKVEAiimvEHLKRVTKPDGVELPKVDytditviydsemlkcagvdspvewMDS 286
Cdd:cd05904 112 ------AELAEKLASLALpVVLLDSAEFDSL----SFSDLLFEADEAEPPVVV------------------------IKQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 287 EDPLFILYTSGSTGKPKGIQHTTAGYMTyayATTKYTFDAQE----DDVYWCTADCGWITGHSYLLYGPLMNGLKGIwye 362
Cdd:cd05904 158 DDVAALLYSSGTTGRSKGVMLTHRNLIA---MVAQFVAGEGSnsdsEDVFLCVLPMFHIYGLSSFALGLLRLGATVV--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 363 GVPTYPTPSrMWDVTDKYGVTKLYTSPTAaraLMALGNQWLESS-SRKTLKVIGTVGEPInPAAWMWLYKQVgLSNVSIV 441
Cdd:cd05904 232 VMPRFDLEE-LLAAIERYKVTHLPVVPPI---VLALVKSPIVDKyDLSSLRQIMSGAAPL-GKELIEAFRAK-FPNVDLG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 442 DTYWQTETGG--HMiTCLPGATPMKPGAAAMpffgaspVLLDAEGRVI-------EGPGE-GSLCFdRAwPGMMRGIYGD 511
Cdd:cd05904 306 QGYGMTESTGvvAM-CFAPEKDRAKYGSVGR-------LVPNVEAKIVdpetgesLPPNQtGELWI-RG-PSIMKGYLNN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 512 EQRFVKTYLapFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPY 591
Cdd:cd05904 376 PEATAATID--KEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPM 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71982997 592 AFVTLNVGERINE--------KLVAELKKlVRekigALAVPDVIqeapglPKTRSGKVTRRIL 646
Cdd:cd05904 454 AFVVRKPGSSLTEdeimdfvaKQVAPYKK-VR----KVAFVDAI------PKSPSGKILRKEL 505
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
102-658 |
3.34e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 119.32 E-value: 3.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 102 RNIKRgYGNKIAYIFegneptDTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPE----LAVAMLACARIGAM 177
Cdd:PRK06188 20 SALKR-YPDRPALVL------GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEvlmaIGAAQLAGLRRTAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 178 HSVVfagfSAESLAARVVDARCRVLVTADGVFrgakpiglksiADAAAVLASQedvkveaiimVEHLKRVTKPDGVELpK 257
Cdd:PRK06188 93 HPLG----SLDDHAYVLEDAGISTLIVDPAPF-----------VERALALLAR----------VPSLKHVLTLGPVPD-G 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 258 VDYTDITVIYDSEMLKCAGVDSPVEWMdsedplfiLYTSGSTGKPKGIQHTTAGYMTYAYattkytfdaqeddvyWCTAD 337
Cdd:PRK06188 147 VDLLAAAAKFGPAPLVAAALPPDIAGL--------AYTGGTTGKPKGVMGTHRSIATMAQ---------------IQLAE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 338 CGWITGHSYLLYGPLMNGlkgiwyEGVPTYPT--------------PSRMWDVTDKYGVTKLYTSPTAARALMALGNqwL 403
Cdd:PRK06188 204 WEWPADPRFLMCTPLSHA------GGAFFLPTllrggtvivlakfdPAEVLRAIEEQRITATFLVPTMIYALLDHPD--L 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 404 ESSSRKTLKVIGTVGEPINPAAWMWLYKQVGlsNVsIVDTYWQTETGgHMITCLP-----GATPMKPGAAAMPFFGASPV 478
Cdd:PRK06188 276 RTRDLSSLETVYYGASPMSPVRLAEAIERFG--PI-FAQYYGQTEAP-MVITYLRkrdhdPDDPKRLTSCGRPTPGLRVA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 479 LLDAEGRVIEgPGE-GSLCFdRAwPGMMRGIYG--DEqrfvkTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDlMNVSG 555
Cdd:PRK06188 352 LLDEDGREVA-QGEvGEICV-RG-PLVMDGYWNrpEE-----TAEAFRDGWLHTGDVAREDEDGFYYIVDRKKD-MIVTG 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 556 HL-LSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEklvAELKKLVREKIGALAVPDVIQEAPGLP 634
Cdd:PRK06188 423 GFnVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDA---AELQAHVKERKGSVHAPKQVDFVDSLP 499
|
570 580
....*....|....*....|....*
gi 71982997 635 KTRSGKVTRRILR-KIAEGSESGIG 658
Cdd:PRK06188 500 LTALGKPDKKALRaRYWEGRGRAVG 524
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
108-648 |
4.11e-28 |
|
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: 118.56 E-value: 4.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 108 YGNKIAYIFEGneptdtSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSA 187
Cdd:cd12118 17 YPDRTSIVYGD------RRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 188 ESLAARVVDARCRVLVtADGVFrgakpiglksiaDAAAVLASQedvkveaiimvehlkrvtKPDGVELPKVDytditviy 267
Cdd:cd12118 91 EEIAFILRHSEAKVLF-VDREF------------EYEDLLAEG------------------DPDFEWIPPAD-------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 268 dsemlkcagvdspvEWmdseDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTkYTFDAQEDDVYWCTAD----CGWItg 343
Cdd:cd12118 132 --------------EW----DPIALNYTSGTTGRPKGVVYHHRGAYLNALANI-LEWEMKQHPVYLWTLPmfhcNGWC-- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 344 hsyLLYGPLMNGLKGIWYEGVptypTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSRKtlkVIGTVGEPINP 423
Cdd:cd12118 191 ---FPWTVAAVGGTNVCLRKV----DAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHR---VHVMTAGAPPP 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 424 AAWMWLYKQVGLSnvsIVDTYWQTETGGHMITCL--PG--ATPMKPGAAAM-----PFFGASPV-LLDAEGrVIEGPGEG 493
Cdd:cd12118 261 AAVLAKMEELGFD---VTHVYGLTETYGPATVCAwkPEwdELPTEERARLKarqgvRYVGLEEVdVLDPET-MKPVPRDG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 494 SLCFDRAWPG--MMRGIYGDEQrfvKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHE 571
Cdd:cd12118 337 KTIGEIVFRGniVMKGYLKNPE---ATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHP 413
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71982997 572 KVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEklvAELKKLVREKIGALAVPDVIQEAPgLPKTRSGKVTRRILRK 648
Cdd:cd12118 414 AVLEAAVVARPDEKWGEVPCAFVELKEGAKVTE---EEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVLRD 486
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
126-648 |
4.90e-28 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 117.06 E-value: 4.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 126 TWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAmhSVVFAG--FSAESLAARVVDArcrvlv 203
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGA--EAVLLNtrLTPNELAFQLKDS------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 204 tadgvfrgakpiglksiadaaavlasqedvkveaiimvehlkrvtkpdgvelpKVDYTDITVIydsemlkcagvdspvew 283
Cdd:cd05912 73 -----------------------------------------------------DVKLDDIATI----------------- 82
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 284 mdsedplfiLYTSGSTGKPKGIQHTTAgyMTYAYAT-TKYTFDAQEDDVYWCTADCGWITGHSYLLygplmnglKGIWYe 362
Cdd:cd05912 83 ---------MYTSGTTGKPKGVQQTFG--NHWWSAIgSALNLGLTEDDNWLCALPLFHISGLSILM--------RSVIY- 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 363 GVPTYptpsrmwdVTDKYGVTKLYTS------------PTAARALMALGNQWLESSSRKTLkvIGtvGEPINPAawmwLY 430
Cdd:cd05912 143 GMTVY--------LVDKFDAEQVLHLinsgkvtiisvvPTMLQRLLEILGEGYPNNLRCIL--LG--GGPAPKP----LL 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 431 KQVGLSNVSIVDTYWQTETGGHMITCLPGATPMKPGAAAMPFFGASPVLLDAEGRViEGPGEGSLcfdrAWPGMMRGIYG 510
Cdd:cd05912 207 EQCKEKGIPVYQSYGMTETCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPP-YEVGEILL----KGPNVTKGYLN 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 511 DEQRfvkTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFP 590
Cdd:cd05912 282 RPDA---TEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVP 358
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 71982997 591 YAFVtlnVGERinEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRK 648
Cdd:cd05912 359 VAFV---VSER--PISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
126-646 |
6.06e-28 |
|
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: 117.35 E-value: 6.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 126 TWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAmhsvVFAGFSAESLAARVvdarcrvlvta 205
Cdd:cd05945 16 TLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGH----AYVPLDASSPAERI----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 206 dgvfrgakpiglKSIADAAavlasqedvKVEAIIMVEHlkrvtkpdgvelpkvdytditviydsemlkcagvdspvewmd 285
Cdd:cd05945 81 ------------REILDAA---------KPALLIADGD------------------------------------------ 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 286 seDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYtFDAQEDDVYWCTAD-----------CGWITGHSYLLYGPLMN 354
Cdd:cd05945 98 --DNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSD-FPLGPGDVFLNQAPfsfdlsvmdlyPALASGATLVPVPRDAT 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 355 GLKGIWYEGVPtyptpsrmwdvtdKYGVTKLYTSPTAARALMALGNqwLESSSRKTLKVIGTVGEPI-NPAAWMWLYKqv 433
Cdd:cd05945 175 ADPKQLFRFLA-------------EHGITVWVSTPSFAAMCLLSPT--FTPESLPSLRHFLFCGEVLpHKTARALQQR-- 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 434 gLSNVSIVDTYWQTETgghMITC---------LPGATPM-----KPGAAAmpffgaspVLLDAEGRVIEGPGEGSLCFdr 499
Cdd:cd05945 238 -FPDARIYNTYGPTEA---TVAVtyievtpevLDGYDRLpigyaKPGAKL--------VILDEDGRPVPPGEKGELVI-- 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 500 AWPGMMRGIYGD----EQRFVktylaPFNGY--YFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKV 573
Cdd:cd05945 304 SGPSVSKGYLNNpektAAAFF-----PDEGQraYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGV 378
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71982997 574 AEAAVVAAPHDIKGSFPYAFVTLNVGEriNEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRIL 646
Cdd:cd05945 379 KEAVVVPKYKGEKVTELIAFVVPKPGA--EAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
100-570 |
1.34e-27 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 117.89 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 100 LERNIKRgYGNKIAYifegNEPTDTS--TWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAM 177
Cdd:COG1022 17 LRRRAAR-FPDRVAL----REKEDGIwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 178 HSVVFAGFSAESLAARVVDARCRVLVTADGvfrgakpiglksiADAAAVLASQEDV-KVEAIIMVEhlkrvtkpdgvelP 256
Cdd:COG1022 92 TVPIYPTSSAEEVAYILNDSGAKVLFVEDQ-------------EQLDKLLEVRDELpSLRHIVVLD-------------P 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 257 KVDYTDITVIYDSEMLK-CAGVDSPVEW------MDSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYtFDAQED 329
Cdd:COG1022 146 RGLRDDPRLLSLDELLAlGREVADPAELearraaVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLER-LPLGPG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 330 DVY-----WCtadcgWITGHSyLLYGPLMNGLKgIWY-EGV-----------PTY-PTPSRMWDvtdkygvtKLYT---- 387
Cdd:COG1022 225 DRTlsflpLA-----HVFERT-VSYYALAAGAT-VAFaESPdtlaedlrevkPTFmLAVPRVWE--------KVYAgiqa 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 388 ----SPTAARAL----MALGNQWLESSSRKT----------------------------LKVIGTVGEPINP--AAWMWl 429
Cdd:COG1022 290 kaeeAGGLKRKLfrwaLAVGRRYARARLAGKspslllrlkhaladklvfsklrealggrLRFAVSGGAALGPelARFFR- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 430 ykqvGLsNVSIVDTYWQTETGGhMITC-LPGAtpMKPGAAAMPFFGASpVLLDAEGRV-IEGpgegslcfdrawPGMMRG 507
Cdd:COG1022 369 ----AL-GIPVLEGYGLTETSP-VITVnRPGD--NRIGTVGPPLPGVE-VKIAEDGEIlVRG------------PNVMKG 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71982997 508 IYGDEQRFVKTYLApfNGYYFTGDGARRDEDGYLWITGRVDDLMNVS-GHLLSTAEIESALVAH 570
Cdd:COG1022 428 YYKNPEATAEAFDA--DGWLHTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKAS 489
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
128-646 |
2.01e-27 |
|
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: 116.61 E-value: 2.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 128 TYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTAdg 207
Cdd:cd17646 25 TYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLTT-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 208 vfrgakpiglksiADAAAVLASQEDVKVeaiimVEHLKRVTKPDGVELPKVDytditviydsemlkcagvdspvewmdSE 287
Cdd:cd17646 103 -------------ADLAARLPAGGDVAL-----LGDEALAAPPATPPLVPPR--------------------------PD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 288 DPLFILYTSGSTGKPKGIQHTTAGYMTY-AYATTKYTFDAqeDDVYWCTADCGWITGhSYLLYGPLMNGLKGIWYE---- 362
Cdd:cd17646 139 NLAYVIYTSGSTGRPKGVMVTHAGIVNRlLWMQDEYPLGP--GDRVLQKTPLSFDVS-VWELFWPLVAGARLVVARpggh 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 363 GVPTYptpsrMWDVTDKYGVTKLYTSPTAARALMalgnQWLESSSRKTLKVIGTVGEPINPAAWMWLYKQVG--LSN--- 437
Cdd:cd17646 216 RDPAY-----LAALIREHGVTTCHFVPSMLRVFL----AEPAAGSCASLRRVFCSGEALPPELAARFLALPGaeLHNlyg 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 438 ---VSIVDTYWQTeTGGHMITCLPGATPMkPGAAAmpffgaspVLLDAEGRVIEGPGEGSLCFdrAWPGMMRGIYG---- 510
Cdd:cd17646 287 pteAAIDVTHWPV-RGPAETPSVPIGRPV-PNTRL--------YVLDDALRPVPVGVPGELYL--GGVQLARGYLGrpal 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 511 DEQRFVKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFP 590
Cdd:cd17646 355 TAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARL 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 71982997 591 YAFVTLNVGERinEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRIL 646
Cdd:cd17646 435 VGYVVPAAGAA--GPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
128-646 |
2.39e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 117.06 E-value: 2.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 128 TYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTADG 207
Cdd:PRK06710 51 TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 208 VFrgakpiglksiadaAAVLASQEDVKVEAIIMVEHLKRVTKPDGVELP-----------KVDYTDITVIYDS-EMLKCA 275
Cdd:PRK06710 131 VF--------------PRVTNVQSATKIEHVIVTRIADFLPFPKNLLYPfvqkkqsnlvvKVSESETIHLWNSvEKEVNT 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 276 GVDSPVewmDSEDPLFIL-YTSGSTGKPKGIQHTTAGYMTYAYATTKYTFDAQE-DDVYWCTADCGWITGHSYLLYGPLM 353
Cdd:PRK06710 197 GVEVPC---DPENDLALLqYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEgEEVVLGVLPFFHVYGMTAVMNLSIM 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 354 NGLKGIWyegVPTYPTpSRMWDVTDKYGVTKLYTSPTAARALM--ALGNQWLESSSRKTLKviGTVGEPINpaawmwlyk 431
Cdd:PRK06710 274 QGYKMVL---IPKFDM-KMVFEAIKKHKVTLFPGAPTIYIALLnsPLLKEYDISSIRACIS--GSAPLPVE--------- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 432 qvglsnvsiVDTYWQTETGGHMITC--LPGATPMK----------PGAAAMPFFGASPVLLDAEGRVIEGPGE-GSLCFD 498
Cdd:PRK06710 339 ---------VQEKFETVTGGKLVEGygLTESSPVThsnflwekrvPGSIGVPWPDTEAMIMSLETGEALPPGEiGEIVVK 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 499 RawPGMMRGIYGDEQrfvKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAV 578
Cdd:PRK06710 410 G--PQIMKGYWNKPE---ETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVT 484
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71982997 579 VAAPHDIKGSFPYAFVTLNVGERINEKlvaELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRIL 646
Cdd:PRK06710 485 IGVPDPYRGETVKAFVVLKEGTECSEE---ELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
110-662 |
2.65e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 116.80 E-value: 2.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 110 NKIAYIFEGNeptdTSTWtyNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAES 189
Cdd:PRK07786 32 DAPALRFLGN----TTTW--RELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 190 LAARVVDARCRVLVTADgvfrgakpiglkSIADAAAvlASQEDVKVEAIIMVEHlkrvtkpdgvelpkvDYTDITVIYDS 269
Cdd:PRK07786 106 IAFLVSDCGAHVVVTEA------------ALAPVAT--AVRDIVPLLSTVVVAG---------------GSSDDSVLGYE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 270 EMLKCAGVDSPVEWMDSEDPLFILYTSGSTGKPKG--IQHT--TAGYMTYAYATTKYTfdaqEDDVYWCTADCGWITGHS 345
Cdd:PRK07786 157 DLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGavLTHAnlTGQAMTCLRTNGADI----NSDVGFVGVPLFHIAGIG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 346 YLLYGPLMnglkgiwyeGVPT--YPT----PSRMWDVTDKYGVTKLYTSPTAARALMALGnqwlESSSRK-TLKVIGTVG 418
Cdd:PRK07786 233 SMLPGLLL---------GAPTviYPLgafdPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQ----QARPRDlALRVLSWGA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 419 EPINPAAWMWLYKQvgLSNVSIVDTYWQTETGGhmITClpgatpMKPGAAAMPFFGA-SPVLLDAEGRVIE------GPG 491
Cdd:PRK07786 300 APASDTLLRQMAAT--FPEAQILAAFGQTEMSP--VTC------MLLGEDAIRKLGSvGKVIPTVAARVVDenmndvPVG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 492 E-GSLCFdRAwPGMMRGIYGDEQrfvKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAH 570
Cdd:PRK07786 370 EvGEIVY-RA-PTLMSGYWNNPE---ATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASH 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 571 EKVAEAAVVAAPHDIKGSFPYAFVTLNVGEriNEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRK-- 648
Cdd:PRK07786 445 PDIVEVAVIGRADEKWGEVPVAVAAVRNDD--AALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELREry 522
|
570
....*....|....*...
gi 71982997 649 ----IAEGSESGIGDTTT 662
Cdd:PRK07786 523 gacvNVERRSASAGFTER 540
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
111-647 |
2.84e-27 |
|
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: 115.54 E-value: 2.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 111 KIAYIFEGNEptdtstWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESL 190
Cdd:cd17649 3 AVALVFGDQS------LSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 191 AARVVDARCRVLVTADGvfrgakpiglksiadaaavlasqedvkveaiimvehlkrvtkpdgvelpkvdytditviydse 270
Cdd:cd17649 77 RYMLEDSGAGLLLTHHP--------------------------------------------------------------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 271 mlkcagvdspvewmdsEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYtFDAQEDDVYWCTADCGWITGHSYLlYG 350
Cdd:cd17649 94 ----------------RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGDRELQFASFNFDGAHEQL-LP 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 351 PLMNGlKGIWYEGVPTYPTPSRMWDVTDKYGVTKLYTSPtaaralmALGNQWLE------SSSRKTLKVIGTVGEPINPA 424
Cdd:cd17649 156 PLICG-ACVVLRPDELWASADELAEMVRELGVTVLDLPP-------AYLQQLAEeadrtgDGRPPSLRLYIFGGEALSPE 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 425 awmwLYKQVGLSNVSIVDTYWQTETgghMITCL--PGATPMKPGAAAMP----FFGASPVLLDAEGRV--IEGPGE---G 493
Cdd:cd17649 228 ----LLRRWLKAPVRLFNAYGPTEA---TVTPLvwKCEAGAARAGASMPigrpLGGRSAYILDADLNPvpVGVTGElyiG 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 494 SLCFDRAW---PGMMrgiygdEQRFV-KTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVA 569
Cdd:cd17649 301 GEGLARGYlgrPELT------AERFVpDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLE 374
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71982997 570 HEKVAEAAVVAAPHDIKGSFpYAFVTLNVGERINEkLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILR 647
Cdd:cd17649 375 HPGVREAAVVALDGAGGKQL-VAYVVLRAAAAQPE-LRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
136-647 |
3.72e-27 |
|
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: 115.23 E-value: 3.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 136 VVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAgfsaeSLAARVVDARCRVLVTadgvfrgakpi 215
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFV-----PLNPTLKESVLRYLVA----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 216 glksIADAAAVLASQEdvkveaiiMVEHLKRVTkpdgvelpkVDYTDITVIYDSEMLKCAGVDSPVEWMDSEDPLFILYT 295
Cdd:cd05922 67 ----DAGGRIVLADAG--------AADRLRDAL---------PASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYT 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 296 SGSTGKPKGIQHTTAGYMTYAYATTKYtFDAQEDDVYWCTADCGWITGHSYLLYGPLMNGLKGIWYEGVPtyptPSRMWD 375
Cdd:cd05922 126 SGSTGSPKLVRLSHQNLLANARSIAEY-LGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVL----DDAFWE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 376 VTDKYGVTKLYTSPTAARALMALGnqwLESSSRKTLKVIGTVGEPInPAAWMWLYKQVGlSNVSIVDTYWQTETGGHMIT 455
Cdd:cd05922 201 DLREHGATGLAGVPSTYAMLTRLG---FDPAKLPSLRYLTQAGGRL-PQETIARLRELL-PGAQVYVMYGQTEATRRMTY 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 456 CLPGATPMKPGAAAMPFFGASPVLLDAEGRvIEGPGE-GSLCFDRawPGMMRGIYGDEQRFVKtyLAPFNGYYFTGDGAR 534
Cdd:cd05922 276 LPPERILEKPGSIGLAIPGGEFEILDDDGT-PTPPGEpGEIVHRG--PNVMKGYWNDPPYRRK--EGRGGGVLHTGDLAR 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 535 RDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPhDIKGSFPYAFVTlnvgeRINEKLVAELKKLV 614
Cdd:cd05922 351 RDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLP-DPLGEKLALFVT-----APDKIDPKDVLRSL 424
|
490 500 510
....*....|....*....|....*....|...
gi 71982997 615 REKIGALAVPDVIQEAPGLPKTRSGKVTRRILR 647
Cdd:cd05922 425 AERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
128-646 |
4.54e-27 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 114.50 E-value: 4.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 128 TYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVtadg 207
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 208 vfrgakpiglksiadaaaVLASQEDVKVeaiimvehlkrvtkpdgvelpkvdytditviydsemlkcagvdspvewmdse 287
Cdd:cd05935 79 ------------------VGSELDDLAL---------------------------------------------------- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 288 dplfILYTSGSTGKPKGIQHTTAGYMTYAYATTKYtFDAQEDDVYWCTADCGWITGHSYLLYGPLMNG----LKGIW-YE 362
Cdd:cd05935 89 ----IPYTSGTTGLPKGCMHTHFSAAANALQSAVW-TGLTPSDVILACLPLFHVTGFVGSLNTAVYVGgtyvLMARWdRE 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 363 GVPtyptpsrmwDVTDKYGVTKLYTSPTAARALMALGNqwLESSSRKTLKVIGTVGEPINPAAWMWLYKQVGLSNVSIvd 442
Cdd:cd05935 164 TAL---------ELIEKYKVTFWTNIPTMLVDLLATPE--FKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEG-- 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 443 tYWQTETGGHMITCLPGAtpMKPGAAAMPFFGASPVLLDAEGRVIEGPGEGSLCFDRAwPGMMRGIYGDEQRFVKTYLAp 522
Cdd:cd05935 231 -YGLTETMSQTHTNPPLR--PKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRG-PQIFKGYWNRPEETEESFIE- 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 523 FNG--YYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGE 600
Cdd:cd05935 306 IKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEY 385
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 71982997 601 R--INEKlvaELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRIL 646
Cdd:cd05935 386 RgkVTEE---DIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
209-650 |
4.69e-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: 115.51 E-value: 4.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 209 FRGAKPIGLKSIADAAAVLASQEDVKVEAII----MVEHLKRVTKPDGVELPKVDYTDITVIYDSEMLKC---AGVDSPV 281
Cdd:cd05909 53 LSGKVPVMLNYTAGLRELRACIKLAGIKTVLtskqFIEKLKLHHLFDVEYDARIVYLEDLRAKISKADKCkafLAGKFPP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 282 EWM---------DSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYtFDAQEDDVYwctadCGWITG-HSYLLYG- 350
Cdd:cd05909 133 KWLlrifgvapvQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAI-FDPNPEDVV-----FGALPFfHSFGLTGc 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 351 ---PLMNGLKGIWYEGvPTYptPSRMWDVTDKYGVTKLYTSPTaarALMALGNQWlESSSRKTLKVIGTVGEPINPAAW- 426
Cdd:cd05909 207 lwlPLLSGIKVVFHPN-PLD--YKKIPELIYDKKATILLGTPT---FLRGYARAA-HPEDFSSLRLVVAGAEKLKDTLRq 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 427 MWLYKQvglsNVSIVDTYWQTETGGhMITCLPGATPMKPGAAAMPFFGASPVLLDAEGRVIEGPGEGSLCFDRAwPGMMR 506
Cdd:cd05909 280 EFQEKF----GIRILEGYGTTECSP-VISVNTPQSPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRG-PNVML 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 507 GIYGDEQrfvKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAH-EKVAEAAVVAAPHDI 585
Cdd:cd05909 354 GYLNEPE---LTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGR 430
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71982997 586 KGSFPYAFVTLNVGERinEKLVAELKKlvrEKIGALAVPDVIQEAPGLPKTRSGKVTRRILRKIA 650
Cdd:cd05909 431 KGEKIVLLTTTTDTDP--SSLNDILKN---AGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
158-647 |
5.77e-27 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 115.30 E-value: 5.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 158 LPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTADGVFRGAKPIGLKSiadaAAVLASQEDVKVea 237
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYS----KVVEAAPAKAIV-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 238 iimvehLKRVTKPDGVELPKVDYTDITVIYDSEMLKCAGVD--SPVeWMDSEDPLFILYTSGSTGKPKGIQHTTAGYMTY 315
Cdd:PLN03051 75 ------LPAAGEPVAVPLREQDLSWCDFLGVAAAQGSVGGNeySPV-YAPVESVTNILFSSGTTGEPKAIPWTHLSPLRC 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 316 AYATTKYtFDAQEDDVYWCTADCGWITGhSYLLYGPLMNGLKGIWYEGVPTypTPSRMWDVTDKyGVTKLYTSPTAARAL 395
Cdd:PLN03051 148 ASDGWAH-MDIQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGAPL--GRGFGKFVQDA-GVTVLGLVPSIVKAW 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 396 MALGNQWLESSSRKTLKVIGTVGEPINPAAWMWLYKQVGLSNvSIVDTYWQTETGGHMITCLPgATPMKPGAAAMPFFGA 475
Cdd:PLN03051 223 RHTGAFAMEGLDWSKLRVFASTGEASAVDDVLWLSSVRGYYK-PVIEYCGGTELASGYISSTL-LQPQAPGAFSTASLGT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 476 SPVLLDAEGrviEGPGEGSLCFDRAwpGMMRGIYGDEQRFV-----KTYLAPFNGYYFTGDGARRDED-------GYLWI 543
Cdd:PLN03051 301 RFVLLNDNG---VPYPDDQPCVGEV--ALAPPMLGASDRLLnadhdKVYYKGMPMYGSKGMPLRRHGDimkrtpgGYFCV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 544 TGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERIN-------EKLVAELKKLVRE 616
Cdd:PLN03051 376 QGRADDTMNLGGIKTSSVEIERACDRAVAGIAETAAVGVAPPDGGPELLVIFLVLGEEKKgfdqarpEALQKKFQEAIQT 455
|
490 500 510
....*....|....*....|....*....|.
gi 71982997 617 KIGALAVPDVIQEAPGLPKTRSGKVTRRILR 647
Cdd:PLN03051 456 NLNPLFKVSRVKIVPELPRNASNKLLRRVLR 486
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
127-647 |
1.90e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 113.36 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 127 WTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTAD 206
Cdd:PRK09088 23 WTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 207 GVfRGAKPIGLksiaDAAAVLASqedvkveaiimvehlkrvtkpdgvelpkvdytditviydsemLKCAGVDsPVEWMDS 286
Cdd:PRK09088 103 AV-AAGRTDVE----DLAAFIAS------------------------------------------ADALEPA-DTPSIPP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 287 EDPLFILYTSGSTGKPKGI-------QHTTAGYMTyayaTTKYTfdaqEDDVYWCTADCGWITGHSYLLYGPLMNGLKGI 359
Cdd:PRK09088 135 ERVSLILFTSGTSGQPKGVmlsernlQQTAHNFGV----LGRVD----AHSSFLCDAPMFHIIGLITSVRPVLAVGGSIL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 360 WYEGVPTYPTPSRMWDVTdkYGVTKLYTSPTAARALMAlgNQWLESSSRKTLKVIGTVGEPiNPAAWM--WLYKqvglsN 437
Cdd:PRK09088 207 VSNGFEPKRTLGRLGDPA--LGITHYFCVPQMAQAFRA--QPGFDAAALRHLTALFTGGAP-HAAEDIlgWLDD-----G 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 438 VSIVDTYWQTETG---GHMITClpGATPMKPGAAAMPFFGASPVLLDAEGRVIEG--PGEGSLCFDRAWPGMMRgiygDE 512
Cdd:PRK09088 277 IPMVDGFGMSEAGtvfGMSVDC--DVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAgvPGELLLRGPNLSPGYWR----RP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 513 QRFVKTYLApfNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYA 592
Cdd:PRK09088 351 QATARAFTG--DGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYL 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 71982997 593 FVTLNVGERInekLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILR 647
Cdd:PRK09088 429 AIVPADGAPL---DLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
106-647 |
1.08e-25 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 111.31 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 106 RGYGNKIAYIFEgNEPTDTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGF 185
Cdd:PRK08008 18 DVYGHKTALIFE-SSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 186 SAESLAARVVDARCRVLVTAdgvfrgakpiglksiadaAAVLASQEDVKVEAIIMVEHLKRVTKPDGVELPKVDYTDITV 265
Cdd:PRK08008 97 LREESAWILQNSQASLLVTS------------------AQFYPMYRQIQQEDATPLRHICLTRVALPADDGVSSFTQLKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 266 IYDSEMLKcagvdspVEWMDSEDPLFILYTSGSTGKPKGIQHTT-----AGYMTyAYATTkytfdAQEDDVYW------- 333
Cdd:PRK08008 159 QQPATLCY-------APPLSTDDTAEILFTSGTTSRPKGVVITHynlrfAGYYS-AWQCA-----LRDDDVYLtvmpafh 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 334 ----CTAdcgwitghsylLYGPLMNGLKGIWYEgvpTYpTPSRMWDVTDKYGVTKLYTSPTAARALMAlgnqwlesssrk 409
Cdd:PRK08008 226 idcqCTA-----------AMAAFSAGATFVLLE---KY-SARAFWGQVCKYRATITECIPMMIRTLMV------------ 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 410 tlkvigtvgEPinPAAW--------MWLYkqVGLS-----------NVSIVDTYWQTETGGHMITCLPGATPMKPgAAAM 470
Cdd:PRK08008 279 ---------QP--PSANdrqhclreVMFY--LNLSdqekdafeerfGVRLLTSYGMTETIVGIIGDRPGDKRRWP-SIGR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 471 PFFGASPVLLDAEGRVIEgPGE-GSLCFdRAWPG--MMRGIYGDEQRFVKTyLAPfNGYYFTGDGARRDEDGYLWITGRV 547
Cdd:PRK08008 345 PGFCYEAEIRDDHNRPLP-AGEiGEICI-KGVPGktIFKEYYLDPKATAKV-LEA-DGWLHTGDTGYVDEEGFFYFVDRR 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 548 DDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEKlvaELKKLVREKIGALAVPDVI 627
Cdd:PRK08008 421 CNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEE---EFFAFCEQNMAKFKVPSYL 497
|
570 580
....*....|....*....|
gi 71982997 628 QEAPGLPKTRSGKVTRRILR 647
Cdd:PRK08008 498 EIRKDLPRNCSGKIIKKNLK 517
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
110-571 |
2.69e-25 |
|
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: 112.26 E-value: 2.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 110 NKIAYIFEGNeptdtsTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAmhsvvfA------ 183
Cdd:COG1020 491 DAVAVVFGDQ------SLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGA------Ayvpldp 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 184 GFSAESLAARVVDARCRVLVTAdgvfrgakpiglksiADAAAVLASQedvkveaiimvehlkrvtkpdgvelpkvdytDI 263
Cdd:COG1020 559 AYPAERLAYMLEDAGARLVLTQ---------------SALAARLPEL-------------------------------GV 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 264 TVIY-DSEMLKCAGVDSPVEWMDSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYtFDAQEDDVywctadCGWIT 342
Cdd:COG1020 593 PVLAlDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRR-YGLGPGDR------VLQFA 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 343 GHS-----YLLYGPLMNGlkgiwyeG----VP--TYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESssrktL 411
Cdd:COG1020 666 SLSfdasvWEIFGALLSG-------AtlvlAPpeARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEALPS-----L 733
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 412 KVIGTVGEPINPAAWMWLYKQvgLSNVSIVDTYWQTETggHMITCLPGATPMKPGAAAMPfFGaSPV------LLDAEGR 485
Cdd:COG1020 734 RLVLVGGEALPPELVRRWRAR--LPGARLVNLYGPTET--TVDSTYYEVTPPDADGGSVP-IG-RPIantrvyVLDAHLQ 807
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 486 -VIEG-PGE----GslcfdrawPGMMRGIYGDE----QRFVKTylaPFNG----YYFTGDGARRDEDG---YLwitGRVD 548
Cdd:COG1020 808 pVPVGvPGElyigG--------AGLARGYLNRPeltaERFVAD---PFGFpgarLYRTGDLARWLPDGnleFL---GRAD 873
|
490 500
....*....|....*....|...
gi 71982997 549 DLMNVSGHLLSTAEIESALVAHE 571
Cdd:COG1020 874 DQVKIRGFRIELGEIEAALLQHP 896
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
128-643 |
4.57e-25 |
|
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: 108.69 E-value: 4.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 128 TYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTADg 207
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 208 vfrgakpiglksiadaaavLASQEDVkvEAIImvehLKRVTKPDGVELpkvdytditviydsemlkcagvdSPVEWMDSE 287
Cdd:TIGR01923 80 -------------------LLEEKDF--QADS----LDRIEAAGRYET-----------------------SLSASFNMD 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 288 DPLFILYTSGSTGKPKGIQHTTAGYMTYAYATtKYTFDAQEDDvywctadcgwitghSYLLYGPL--MNGLKGIW---YE 362
Cdd:TIGR01923 112 QIATLMFTSGTTGKPKAVPHTFRNHYASAVGS-KENLGFTEDD--------------NWLLSLPLyhISGLSILFrwlIE 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 363 GVpTYPTPSRMWDVTD---KYGVTKLYTSPTAARALMAlgnqwlESSSRKTLKVIGTVGEPInPAAwmwLYKQVGLSNVS 439
Cdd:TIGR01923 177 GA-TLRIVDKFNQLLEmiaNERVTHISLVPTQLNRLLD------EGGHNENLRKILLGGSAI-PAP---LIEEAQQYGLP 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 440 IVDTYWQTETGGHMITCLPGATPMKPGAAaMPFFGASpVLLDAEGRVIEGpgegslcfdRAW---PGMMRGIYGDEQrfv 516
Cdd:TIGR01923 246 IYLSYGMTETCSQVTTATPEMLHARPDVG-RPLAGRE-IKIKVDNKEGHG---------EIMvkgANLMKGYLYQGE--- 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 517 KTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTL 596
Cdd:TIGR01923 312 LTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVS 391
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 71982997 597 NvgeriNEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTR 643
Cdd:TIGR01923 392 E-----SDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILR 433
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
127-646 |
7.68e-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: 108.57 E-value: 7.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 127 WTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMhsVVFAGFSaeslaarvvdarcrvlvtad 206
Cdd:cd05920 41 LTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--PVLALPS-------------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 207 gvFRGAKPIGLKSIADAAAVLASqedvkveaiimvehlKRVTKPDGVELPKvdytditviydsEMLKCAGvdspvewmds 286
Cdd:cd05920 99 --HRRSELSAFCAHAEAVAYIVP---------------DRHAGFDHRALAR------------ELAESIP---------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 287 eDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYT-FDaqEDDVYWCTADcgwiTGHSYLLYGPlmnGLKGIWYEG-- 363
Cdd:cd05920 140 -EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCgLD--QDTVYLAVLP----AAHNFPLACP---GVLGTLLAGgr 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 364 --VPTYPTPSRMWDVTDKYGVTKLYTSPTAARalmalgnQWLESSSR-----KTLKVIGTVGEPINPAAWMWLYK----- 431
Cdd:cd05920 210 vvLAPDPSPDAAFPLIEREGVTVTALVPALVS-------LWLDAAASrradlSSLRLLQVGGARLSPALARRVPPvlgct 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 432 --QV-----GLSNVSIVDTywqtetgGHMITCLPGATPMKPGAAAMpffgaspvLLDAEGRVIeGPGEGSLCFDRAwPGM 504
Cdd:cd05920 283 lqQVfgmaeGLLNYTRLDD-------PDEVIIHTQGRPMSPDDEIR--------VVDEEGNPV-PPGEEGELLTRG-PYT 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 505 MRGIYGDEQRFVKTYLApfNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHD 584
Cdd:cd05920 346 IRGYYRAPEHNARAFTP--DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDE 423
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71982997 585 IKGSFPYAFVTLNvGERINeklVAELKKLVREK-IGALAVPDVIQEAPGLPKTRSGKVTRRIL 646
Cdd:cd05920 424 LLGERSCAFVVLR-DPPPS---AAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
128-651 |
1.87e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 107.91 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 128 TYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTADG 207
Cdd:PRK06164 37 SRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 208 vFRGakpIGLKSIADAAAvlaSQEDVKVEAIIMVEhlkrvtkPDGVELPKVDYTDITVIYDSEMLkcAGVDSPVEWMDSE 287
Cdd:PRK06164 117 -FKG---IDFAAILAAVP---PDALPPLRAIAVVD-------DAADATPAPAPGARVQLFALPDP--APPAAAGERAADP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 288 DPLFILYT-SGSTGKPKGIQHTTAGYMTYAYAttkytfdaqeddvywCTADCGWITGHSYLLYGPL-----MNGLKGIWY 361
Cdd:PRK06164 181 DAGALLFTtSGTTSGPKLVLHRQATLLRHARA---------------IARAYGYDPGAVLLAALPFcgvfgFSTLLGALA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 362 EGVP--------TYPTPSRMWDvtdkYGVTKLYTSPTAARALMALGNQWLESSSRKTLKVIGTVGEPINPAAW-----MW 428
Cdd:PRK06164 246 GGAPlvcepvfdAARTARALRR----HRVTHTFGNDEMLRRILDTAGERADFPSARLFGFASFAPALGELAALarargVP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 429 LYKQVGLSNVSIVDTYWQTETG-GHMItcLPGATPMKPgaaampffgaspvlldaEGRV-IEGPGEGSLCFD-------- 498
Cdd:PRK06164 322 LTGLYGSSEVQALVALQPATDPvSVRI--EGGGRPASP-----------------EARVrARDPQDGALLPDgesgeiei 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 499 RAwPGMMRGIYGDEQRFVKTYLApfNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAV 578
Cdd:PRK06164 383 RA-PSLMRGYLDNPDATARALTD--DGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQV 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71982997 579 VAAPHDIKgSFPYAFVTLNVGERINEklvAELKKLVREKIGALAVPDVIQEAPGLPKTRSG---KVTRRILRKIAE 651
Cdd:PRK06164 460 VGATRDGK-TVPVAFVIPTDGASPDE---AGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMAQ 531
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
288-650 |
2.10e-24 |
|
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: 104.72 E-value: 2.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 288 DPLFILYTSGSTGKPKGIQHTTAGyMTYAYATTKYTFDAQEDDVYWCTADCGWITGhsyllYGPLMNGLkgiwYEGVPTY 367
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAAN-LLASAAGLHSRLGFGGGDSWLLSLPLYHVGG-----LAILVRSL----LAGAELV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 368 PtPSRMWDV---TDKYGVTKLYTSPTAARALMALGnqwLESSSRKTLKVIGTVGEPINPAawmwLYKQVGLSNVSIVDTY 444
Cdd:cd17630 71 L-LERNQALaedLAPPGVTHVSLVPTQLQRLLDSG---QGPAALKSLRAVLLGGAPIPPE----LLERAADRGIPLYTTY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 445 WQTETGGHMITCLPGATPMKpgaaampffGASPVLLDAEGRVIEGpgegslcfDRAWPG--MMRGIYGDEQRfvkTYLAP 522
Cdd:cd17630 143 GMTETASQVATKRPDGFGRG---------GVGVLLPGRELRIVED--------GEIWVGgaSLAMGYLRGQL---VPEFN 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 523 FNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNvgeri 602
Cdd:cd17630 203 EDGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGR----- 277
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 71982997 603 NEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRKIA 650
Cdd:cd17630 278 GPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
109-648 |
5.15e-24 |
|
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: 106.55 E-value: 5.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 109 GNKIAYIFEGNEPTDTSTWTYNELHAQVVQFSAVLRSHGvKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFA---GF 185
Cdd:cd05931 7 PDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPptpGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 186 SAESLAARVVDARCRVLVTADGVfrgakpiglksIADAAAVLASQEDVKVEAIIMVEhLKRVTKPDGVELPKVdytditv 265
Cdd:cd05931 86 HAERLAAILADAGPRVVLTTAAA-----------LAAVRAFAASRPAAGTPRLLVVD-LLPDTSAADWPPPSP------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 266 iydsemlkcagvdspvewmDSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKyTFDAQEDD--VYW--CTADCGwi 341
Cdd:cd05931 147 -------------------DPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRR-AYGLDPGDvvVSWlpLYHDMG-- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 342 tghsyllygpLMNGLKGIWYEGVPTY---PT-----PSRMWDVTDKYGVTklYT-SPT-----AARALMALGNQWLESSS 407
Cdd:cd05931 205 ----------LIGGLLTPLYSGGPSVlmsPAaflrrPLRWLRLISRYRAT--ISaAPNfaydlCVRRVRDEDLEGLDLSS 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 408 rktLKVIGTVGEPINPAAwmwL------YKQVGLSNVSIVDTYWQTETGGHMITCLPGATPM-----------------K 464
Cdd:cd05931 273 ---WRVALNGAEPVRPAT---LrrfaeaFAPFGFRPEAFRPSYGLAEATLFVSGGPPGTGPVvlrvdrdalagravavaA 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 465 PGAAAMPFFGASPVLLDAEGRVIEgPGEGSLCFDRA----W---PGMMRGIYGD----EQRFVKTYLAPFNGYYFTGD-G 532
Cdd:cd05931 347 DDPAARELVSCGRPLPDQEVRIVD-PETGRELPDGEvgeiWvrgPSVASGYWGRpeatAETFGALAATDEGGWLRTGDlG 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 533 ARRdeDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEkvaeaavvaaPHDIKGSfPYAFVTLNVGERInEKLVAE--- 609
Cdd:cd05931 426 FLH--DGELYITGRLKDLIIVRGRNHYPQDIEATAEEAH----------PALRPGC-VAAFSVPDDGEER-LVVVAEver 491
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 71982997 610 ---------LKKLVREKIGA---LAVPDVIQEAPG-LPKTRSGKVTRRILRK 648
Cdd:cd05931 492 gadpadlaaIAAAIRAAVARehgVAPADVVLVRPGsIPRTSSGKIQRRACRA 543
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
110-649 |
7.09e-24 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 105.71 E-value: 7.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 110 NKIAYIfegnepTDTSTWTYNELHAQVVQFSAVLRSH-GVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAE 188
Cdd:PRK06839 17 DRIAII------TEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 189 SLAARVVDARCRVLVTAdgvfrgakpiglKSIADAAAVLasqedvkvEAIIMVEHLKRVTKPDGVELPKVDytditviyd 268
Cdd:PRK06839 91 ELIFQLKDSGTTVLFVE------------KTFQNMALSM--------QKVSYVQRVISITSLKEIEDRKID--------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 269 semlkcaGVDSPVEwmdsEDPLFILYTSGSTGKPKGIQHTTAGyMTYAYATTKYTFDAQEDDVYWCTADCGWITGHSYLL 348
Cdd:PRK06839 142 -------NFVEKNE----SASFIICYTSGTTGKPKGAVLTQEN-MFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 349 YGPLMNGLKGIwyegVPTYPTPSRMWDVTDKYGVTKLYTSPTAARALmaLGNQWLESSSRKTLKVIGTVGEPInPAAWMW 428
Cdd:PRK06839 210 FPTLFAGGVII----VPRKFEPTKALSMIEKHKVTVVMGVPTIHQAL--INCSKFETTNLQSVRWFYNGGAPC-PEELMR 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 429 LYKQVGLSnvsIVDTYWQTETGGHMITCLPGATPMKPGAAAMP-FFGASPVLLDAEGRVieGPGEGSLCFDRAwPGMMRG 507
Cdd:PRK06839 283 EFIDRGFL---FGQGFGMTETSPTVFMLSEEDARRKVGSIGKPvLFCDYELIDENKNKV--EVGEVGELLIRG-PNVMKE 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 508 IYgdeQRFVKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKG 587
Cdd:PRK06839 357 YW---NRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWG 433
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71982997 588 SFPYAFVTLNVGERINEKlvaELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRKI 649
Cdd:PRK06839 434 EIPIAFIVKKSSSVLIEK---DVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
123-571 |
2.53e-23 |
|
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: 103.44 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 123 DTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVL 202
Cdd:cd05907 2 VWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 203 VTADGvfrgakpiglksiadaaavlasqedvkveaiimvehlkrvtkpdgvelpkvdytditviydsemlkcagvdspve 282
Cdd:cd05907 82 FVEDP--------------------------------------------------------------------------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 283 wmdsEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYtFDAQEDDVYWCTADCGWITGHSYLLYGPLMNGLKGIWYE 362
Cdd:cd05907 87 ----DDLATIIYTSGTTGRPKGVMLSHRNILSNALALAER-LPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFAS 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 363 GV-----------PTY-PTPSRMWDvtdkygvtKLY------TSPTAARALMAL---GNqwlesssrktLKVIGTVGEPI 421
Cdd:cd05907 162 SAetllddlsevrPTVfLAVPRVWE--------KVYaaikvkAVPGLKRKLFDLavgGR----------LRFAASGGAPL 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 422 NPAAWMWlYKQVGlsnVSIVDTYWQTETGGhMITCLPGATPmKPGAAAMPFFGASpVLLDAEGRV-IEGPGegslcfdra 500
Cdd:cd05907 224 PAELLHF-FRALG---IPVYEGYGLTETSA-VVTLNPPGDN-RIGTVGKPLPGVE-VRIADDGEIlVRGPN--------- 287
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71982997 501 wpgMMRGIYGDEQRFVKTYLApfNGYYFTGDGARRDEDGYLWITGRVDDLM-NVSGHLLSTAEIESALVAHE 571
Cdd:cd05907 288 ---VMLGYYKNPEATAEALDA--DGWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASP 354
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
127-650 |
2.81e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 104.47 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 127 WTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTAD 206
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICAD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 207 GvFRGAKPIG-----LKSIADAAAVLASQEDVKveaiimveHLKRVTKPDGVELPK-VDYTDitVIYDSEMLKCAGVDSP 280
Cdd:PRK12583 126 A-FKTSDYHAmlqelLPGLAEGQPGALACERLP--------ELRGVVSLAPAPPPGfLAWHE--LQARGETVSREALAER 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 281 VEWMDSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYTFDAQEDDV------YWC----TADCGWITGHSYLLY- 349
Cdd:PRK12583 195 QASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLcvpvplYHCfgmvLANLGCMTVGACLVYp 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 350 ----GPLMNgLKGIWYE------GVPTY-----PTPSRmwdvtDKYGVTKLYTsptaarALMAlgnqwlesssrktlkvi 414
Cdd:PRK12583 275 neafDPLAT-LQAVEEErctalyGVPTMfiaelDHPQR-----GNFDLSSLRT------GIMA----------------- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 415 gtvGEPINPAAWMWLYKQVGLSNVSIvdTYWQTETGGhmITCLPGAT-PMKPGAAAM----PFFGASpvLLDAEGRVIeG 489
Cdd:PRK12583 326 ---GAPCPIEVMRRVMDEMHMAEVQI--AYGMTETSP--VSLQTTAAdDLERRVETVgrtqPHLEVK--VVDPDGATV-P 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 490 PGE-GSLCFdRAWpGMMRGIYGDEQRFVKTYLApfNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALV 568
Cdd:PRK12583 396 RGEiGELCT-RGY-SVMKGYWNNPEATAESIDE--DGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLF 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 569 AHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEKlvaELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRK 648
Cdd:PRK12583 472 THPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEE---ELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMRE 548
|
..
gi 71982997 649 IA 650
Cdd:PRK12583 549 IS 550
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
112-657 |
1.24e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 101.90 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 112 IAYIFEGneptDTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLA 191
Cdd:PRK08276 1 PAVIMAP----SGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 192 ARVVDARCRVLVTADGVfrgakpiglksiADAAAVLASQEdvkveaiimvehlkrvtkPDGVELPKVDYTDITviydsem 271
Cdd:PRK08276 77 YIVDDSGAKVLIVSAAL------------ADTAAELAAEL------------------PAGVPLLLVVAGPVP------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 272 lkcaGVDSPVEWMD--SEDPL-------FILYTSGSTGKPKGI--------QHTTAGYMTyayATTKYTFDAQEDDVYWC 334
Cdd:PRK08276 120 ----GFRSYEEALAaqPDTPIadetagaDMLYSSGTTGRPKGIkrplpgldPDEAPGMML---ALLGFGMYGGPDSVYLS 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 335 TADcgwitghsylLY--GPL---MNGLKGiwyeGVPTYPT----PSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLES 405
Cdd:PRK08276 193 PAP----------LYhtAPLrfgMSALAL----GGTVVVMekfdAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRAR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 406 SSRKTLKVIGTVGEPINPA------AWmWlykqvglsNVSIVDTYWQTEtgGHMITCLPGATPM-KPGAAAMPFFGASPV 478
Cdd:PRK08276 259 YDVSSLRVAIHAAAPCPVEvkramiDW-W--------GPIIHEYYASSE--GGGVTVITSEDWLaHPGSVGKAVLGEVRI 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 479 LlDAEGRVIeGPGE-GSLCFDRawPGMMRGIYGDEQRFVKTYLApfNGYYFTGDGARRDEDGYLWITGRVDDlMNVSGHL 557
Cdd:PRK08276 328 L-DEDGNEL-PPGEiGTVYFEM--DGYPFEYHNDPEKTAAARNP--HGWVTVGDVGYLDEDGYLYLTDRKSD-MIISGGV 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 558 -LSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKT 636
Cdd:PRK08276 401 nIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRT 480
|
570 580
....*....|....*....|..
gi 71982997 637 RSGKVTRRILR-KIAEGSESGI 657
Cdd:PRK08276 481 PTGKLYKRRLRdRYWEGRQRAI 502
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
288-643 |
1.29e-22 |
|
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: 99.40 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 288 DPLFILYTSGSTGKPKGIQHTTAGYMTyayattkyTFDAQEDDVYWCTADCGWITG---HSYLLYGpLMNGLkgiwYEG- 363
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIE--------SFVCNEDLFNISGEDAILAPGplsHSLFLYG-AISAL----YLGg 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 364 ---VPTYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLesssrkTLKVIGTVGEPINPAAWMWLYKQVGLSNvsI 440
Cdd:cd17633 68 tfiGQRKFNPKSWIRKINQYNATVIYLVPTMLQALARTLEPES------KIKSIFSSGQKLFESTKKKLKNIFPKAN--L 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 441 VDTYWQTETGghMITCLPGATPMKPGAAAMPFFGASPVLLDAEGRVIegpgeGSLCFDRAwpgMMRGIYGDEQRFVKTyl 520
Cdd:cd17633 140 IEFYGTSELS--FITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEI-----GKIFVKSE---MVFSGYVRGGFSNPD-- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 521 apfnGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTlnvGE 600
Cdd:cd17633 208 ----GWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS---GD 280
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 71982997 601 RINEK--LVAELKKLVREKIgalavPDVIQEAPGLPKTRSGKVTR 643
Cdd:cd17633 281 KLTYKqlKRFLKQKLSRYEI-----PKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
100-649 |
1.54e-22 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 102.14 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 100 LERNIKRgYGNKIAYIFEGNEptdtstWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHS 179
Cdd:PRK06155 27 LARQAER-YPDRPLLVFGGTR------WTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 180 VVFAGFSAESLAARVVDARCRVLVTAdgvfrgakpiglksiADAAAVLASQE--DVKVEAIIMVEHLKRVTKPDG---VE 254
Cdd:PRK06155 100 PINTALRGPQLEHILRNSGARLLVVE---------------AALLAALEAADpgDLPLPAVWLLDAPASVSVPAGwstAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 255 LPKVDytditviydsEMLKCAGVdSPvewmdsEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKyTFDAQEDDVYWC 334
Cdd:PRK06155 165 LPPLD----------APAPAAAV-QP------GDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAE-DLEIGADDVLYT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 335 TADCGWITGHSyLLYGPLMNGLKgiwYEGVPTYpTPSRMWDVTDKYGVTKLYTspTAARALMALGNQWLESSSRKTLKVI 414
Cdd:PRK06155 227 TLPLFHTNALN-AFFQALLAGAT---YVLEPRF-SASGFWPAVRRHGATVTYL--LGAMVSILLSQPARESDRAHRVRVA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 415 GTVGEPinPAAWMWLYKQVGlsnVSIVDTYWQTETGGHMITCLPGATPMKPGAAAmPFFGASPVllDAEGRVIEgPGE-G 493
Cdd:PRK06155 300 LGPGVP--AALHAAFRERFG---VDLLDGYGSTETNFVIAVTHGSQRPGSMGRLA-PGFEARVV--DEHDQELP-DGEpG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 494 SLCFDRAWPG-MMRGIYGDEQrfvKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEK 572
Cdd:PRK06155 371 ELLLRADEPFaFATGYFGMPE---KTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPA 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71982997 573 VAEAAVVAAPHDIKGSFPYAFVTLNVGERINEklvAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRKI 649
Cdd:PRK06155 448 VAAAAVFPVPSELGEDEVMAAVVLRDGTALEP---VALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
128-648 |
1.91e-22 |
|
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: 101.55 E-value: 1.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 128 TYNELHAQVVQFSAVLRSHGVKRGDVVAL-------YLpmipelaVAMLACARIGAMHSVVFAGFSAESLAARVVDARCR 200
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATlawnthrHL-------ELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 201 VLVTaDGVFrgaKPIgLKSIADAAAVlasqedvkVEAIIMVEHLKRVTKPDGVELPkvDYTDITviydsemlkcAGVDSP 280
Cdd:cd12119 100 VVFV-DRDF---LPL-LEAIAPRLPT--------VEHVVVMTDDAAMPEPAGVGVL--AYEELL----------AAESPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 281 VEW--MDSEDPLFILYTSGSTGKPKGIQ--------HTTAGYMTYAYATTkytfdaqEDDVY-----------WCTADCG 339
Cdd:cd12119 155 YDWpdFDENTAAAICYTSGTTGNPKGVVyshrslvlHAMAALLTDGLGLS-------ESDVVlpvvpmfhvnaWGLPYAA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 340 WITGHSYLLYGPlmnglkgiwyegvptYPTPSRMWDVTDKYGVTKLYTSPTAARALMalgnQWLESSSRK--TLKVIgTV 417
Cdd:cd12119 228 AMVGAKLVLPGP---------------YLDPASLAELIEREGVTFAAGVPTVWQGLL----DHLEANGRDlsSLRRV-VI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 418 GEPINPAAWMWLYKQVGlsnVSIVDTYWQTETG--GHMITCLPGATPMKPGAAA-------MPFFGASPVLLDAEGRVIE 488
Cdd:cd12119 288 GGSAVPRSLIEAFEERG---VRVIHAWGMTETSplGTVARPPSEHSNLSEDEQLalrakqgRPVPGVELRIVDDDGRELP 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 489 GPGE--GSLCFDRAW--PGMMRGIYGDEQRFVktylapfNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIE 564
Cdd:cd12119 365 WDGKavGELQVRGPWvtKSYYKNDEESEALTE-------DGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELE 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 565 SALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEKlvaELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRR 644
Cdd:cd12119 438 NAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAE---ELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKK 514
|
....
gi 71982997 645 ILRK 648
Cdd:cd12119 515 ALRE 518
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
128-648 |
3.51e-22 |
|
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: 99.69 E-value: 3.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 128 TYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTADG 207
Cdd:cd17653 24 TYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLLTTDS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 208 VfrgakpiglksiadaaavlasqedvkveaiimvehlkrvtkpdgvelpkvdytditviydsemlkcagvdspvewmdsE 287
Cdd:cd17653 104 P------------------------------------------------------------------------------D 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 288 DPLFILYTSGSTGKPKG--IQH-TTAGYMTYAYATTKYT------------FDAqeddvywCTADcgwitghsylLYGPL 352
Cdd:cd17653 106 DLAYIIFTSGSTGIPKGvmVPHrGVLNYVSQPPARLDVGpgsrvaqvlsiaFDA-------CIGE----------IFSTL 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 353 MNGlkgiwyeGVPTYPTPSRMWdVTDKYGVTKLYTSPTAAralmalgnQWLESSSRKTLKVIGTVGEPINPA---AWmwl 429
Cdd:cd17653 169 CNG-------GTLVLADPSDPF-AHVARTVDALMSTPSIL--------STLSPQDFPNLKTIFLGGEAVPPSlldRW--- 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 430 ykqvgLSNVSIVDTYWQTETgghmiTCLPGATPMKPG-----AAAMPffGASPVLLDAEGRVIEGPGEGSLCFdrAWPGM 504
Cdd:cd17653 230 -----SPGRRLYNAYGPTEC-----TISSTMTELLPGqpvtiGKPIP--NSTCYILDADLQPVPEGVVGEICI--SGVQV 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 505 MRGIYGDEQRFVKTYL-APFNG---YYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVA 580
Cdd:cd17653 296 ARGYLGNPALTASKFVpDPFWPgsrMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAI 375
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71982997 581 APHDikgsFPYAFVTlnvGERINeklVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRK 648
Cdd:cd17653 376 VVNG----RLVAFVT---PETVD---VDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
126-640 |
4.85e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 100.34 E-value: 4.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 126 TWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVtA 205
Cdd:PRK07798 28 RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALV-Y 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 206 DGVFRGAkpiglksiadAAAVLASQEDVKveaiimveHLKRVTKPDGVELPK--VDYTDITVIYDSEMLKCAGvdspvew 283
Cdd:PRK07798 107 EREFAPR----------VAEVLPRLPKLR--------TLVVVEDGSGNDLLPgaVDYEDALAAGSPERDFGER------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 284 mdSEDPLFILYTSGSTGKPKGI---QHTTagYMTYAYATTKYTFDAQEDDvYWCTADCGWITGHSYLLYGPLMNGlKGIW 360
Cdd:PRK07798 162 --SPDDLYLLYTGGTTGMPKGVmwrQEDI--FRVLLGGRDFATGEPIEDE-EELAKRAAAGPGMRRFPAPPLMHG-AGQW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 361 ------YEG--VPTYPTPS----RMWDVTDKYGVTKLYTSPTA-ARALMA---LGNQWLESSsrktLKVIGTVGEPINPA 424
Cdd:PRK07798 236 aafaalFSGqtVVLLPDVRfdadEVWRTIEREKVNVITIVGDAmARPLLDaleARGPYDLSS----LFAIASGGALFSPS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 425 ---AWMWLykqvgLSNVSIVDTYWQTETGghmiTCLPGATPMKPGAAAMPFFGASP--VLLDAEGRVIEgPGEGSlcfdr 499
Cdd:PRK07798 312 vkeALLEL-----LPNVVLTDSIGSSETG----FGGSGTVAKGAVHTGGPRFTIGPrtVVLDEDGNPVE-PGSGE----- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 500 awPGMMR-------GIYGDEQRFVKTYLApFNG--YYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAH 570
Cdd:PRK07798 377 --IGWIArrghiplGYYKDPEKTAETFPT-IDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAH 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 571 EKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEklvAELKKLVREKIGALAVPDVIQEAPGLPKTRSGK 640
Cdd:PRK07798 454 PDVADALVVGVPDERWGQEVVAVVQLREGARPDL---AELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
110-646 |
2.56e-21 |
|
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: 97.54 E-value: 2.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 110 NKIAYIFegneptDTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAES 189
Cdd:cd17650 2 DAIAVSD------ATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 190 LAARVVDARCRVLVTadgvfrgakpiglksiadaaavlasqedvkveaiimvehlkrvtkpdgvelpkvdytditviyds 269
Cdd:cd17650 76 LQYMLEDSGAKLLLT----------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 270 emlkcagvdspvewmDSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTK-YTFDAQED----------DVY---WCT 335
Cdd:cd17650 91 ---------------QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRReYELDSFPVrllqmasfsfDVFagdFAR 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 336 AdcgwitghsyLLYGPLM----NGLKGiwyegvptypTPSRMWDVTDKYGVTKLYTSPTAARALMA-LGNQWLESSSRKT 410
Cdd:cd17650 156 S----------LLNGGTLvicpDEVKL----------DPAALYDLILKSRITLMESTPALIRPVMAyVYRNGLDLSAMRL 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 411 LkVIGTVGEPINPAAW--------MWLYKQVGLSNVSIVDTYWQTETGGhmiTCLPGATPMkpgaaAMPFFGASPVLLDA 482
Cdd:cd17650 216 L-IVGSDGCKAQDFKTlaarfgqgMRIINSYGVTEATIDSTYYEEGRDP---LGDSANVPI-----GRPLPNTAMYVLDE 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 483 EGRVIEGPGEGSLCFDRAwpGMMRGIYGD----EQRFVKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLL 558
Cdd:cd17650 287 RLQPQPVGVAGELYIGGA--GVARGYLNRpeltAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRI 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 559 STAEIESALVAHEKVAEAAVVAApHDIKG-----SFPYAFVTLNvgerineklVAELKKLVREKIGALAVPDVIQEAPGL 633
Cdd:cd17650 365 ELGEIESQLARHPAIDEAVVAVR-EDKGGearlcAYVVAAATLN---------TAELRAFLAKELPSYMIPSYYVQLDAL 434
|
570
....*....|...
gi 71982997 634 PKTRSGKVTRRIL 646
Cdd:cd17650 435 PLTPNGKVDRRAL 447
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
98-648 |
4.83e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 97.03 E-value: 4.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 98 NCLERNIKRgYGNKIAYIFegneptDTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAm 177
Cdd:PRK07470 11 HFLRQAARR-FPDRIALVW------GDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 178 hsvvfagfsaeslaarvvdarcrVLVtadgvfrgakPIGLKSIADAAAVLASQEDVKVeaiiMV------EHLK--RVTK 249
Cdd:PRK07470 83 -----------------------VWV----------PTNFRQTPDEVAYLAEASGARA----MIchadfpEHAAavRAAS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 250 PDGVELPKVDYTDITVIYDSEMLKCAGVDSPVEWMDSEDPLFILYTSGSTGKPKgiqhttAGYMTY---AYATTKYTFD- 325
Cdd:PRK07470 126 PDLTHVVAIGGARAGLDYEALVARHLGARVANAAVDHDDPCWFFFTSGTTGRPK------AAVLTHgqmAFVITNHLADl 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 326 ---AQEDDVYWCTAdcgwitghsyllygPLMNGlKGIWY-----EGVPTYPTPSR------MWDVTDKYGVTKLYTSPTA 391
Cdd:PRK07470 200 mpgTTEQDASLVVA--------------PLSHG-AGIHQlcqvaRGAATVLLPSErfdpaeVWALVERHRVTNLFTVPTI 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 392 ARALM--ALGNQWLESSSR---------------KTLKVIGTVgepinpaawmwLYKQVGLSNVsivdtywqteTGGhmI 454
Cdd:PRK07470 265 LKMLVehPAVDRYDHSSLRyviyagapmyradqkRALAKLGKV-----------LVQYFGLGEV----------TGN--I 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 455 TCLPGA------TPM-KPGAAAMPFFGASPVLLDAEGRVIeGPGE-GSLCFdrAWPGMMRGIYGDEQRFVKTYLapfNGY 526
Cdd:PRK07470 322 TVLPPAlhdaedGPDaRIGTCGFERTGMEVQIQDDEGREL-PPGEtGEICV--IGPAVFAGYYNNPEANAKAFR---DGW 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 527 YFTGDGARRDEDGYLWITGRVDDlMNVS-GHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEk 605
Cdd:PRK07470 396 FRTGDLGHLDARGFLYITGRASD-MYISgGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDE- 473
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 71982997 606 lvAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRK 648
Cdd:PRK07470 474 --AELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
123-648 |
7.03e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 98.31 E-value: 7.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 123 DTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVL 202
Cdd:PRK12467 534 GEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLL 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 203 VTADgvfrgakpiglksiadaaavlasqedvkveaiimvEHLKRVTKPDGVELPKVDYTDitviydSEMLKCAGVDSPVE 282
Cdd:PRK12467 614 LTQS-----------------------------------HLLAQLPVPAGLRSLCLDEPA------DLLCGYSGHNPEVA 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 283 wMDSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYtFDAQEDDVYWCTADCGWITGHsYLLYGPLMNGlKGIWYE 362
Cdd:PRK12467 653 -LDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAER-LQLAADDSMLMVSTFAFDLGV-TELFGALASG-ATLHLL 728
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 363 GVPTYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQwLESSSRKTLKVIGTVGEPINPAAWMWLYKQVGLSNvsivd 442
Cdd:PRK12467 729 PPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRV-ALPRPQRALVCGGEALQVDLLARVRALGPGARLIN----- 802
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 443 TYWQTETGGHMIT--CLPGATPMKPGAAAMPFFGASPVLLDAEGRVIEGPGEGSLCFDRAwpGMMRGIYG----DEQRFV 516
Cdd:PRK12467 803 HYGPTETTVGVSTyeLSDEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGA--GLARGYHRrpalTAERFV 880
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 517 KTYLAPFNG-YYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDiKGSFPYAFVT 595
Cdd:PRK12467 881 PDPFGADGGrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGD-AGLQLVAYLV 959
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 71982997 596 LNVGERINEKLVA--ELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRK 648
Cdd:PRK12467 960 PAAVADGAEHQATrdELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPK 1014
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
126-652 |
7.30e-21 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 96.59 E-value: 7.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 126 TWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTa 205
Cdd:PLN02246 50 VYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIIT- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 206 dgvfrgakpigLKSIADAAAVLASQEDVKVEAIIMVE----HLKRVTKPDGVELPKVDytditviydsemlkcagvdspv 281
Cdd:PLN02246 129 -----------QSCYVDKLKGLAEDDGVTVVTIDDPPegclHFSELTQADENELPEVE---------------------- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 282 ewMDSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAyattkytfdAQEDD-----VYWCTAD---CGWITGHSYLLYGPLM 353
Cdd:PLN02246 176 --ISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSV---------AQQVDgenpnLYFHSDDvilCVLPMFHIYSLNSVLL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 354 NGLK-GIWYEGVPTYPTPsRMWDVTDKYGVTKLYTSPTAARALM---ALGNQWLeSSSRKTLKVIGTVGEPINPAAwmwl 429
Cdd:PLN02246 245 CGLRvGAAILIMPKFEIG-ALLELIQRHKVTIAPFVPPIVLAIAkspVVEKYDL-SSIRMVLSGAAPLGKELEDAF---- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 430 ykQVGLSNVSIVDTYWQTETGGHMITCLPGA---TPMKPGAAAMpffgaspVLLDAEGRVIEgPGEG-SLcfDRAWPGMM 505
Cdd:PLN02246 319 --RAKLPNAVLGQGYGMTEAGPVLAMCLAFAkepFPVKSGSCGT-------VVRNAELKIVD-PETGaSL--PRNQPGEI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 506 --RGiygdeQRFVKTYL----APFN-----GYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVA 574
Cdd:PLN02246 387 ciRG-----PQIMKGYLndpeATANtidkdGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIA 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 575 EAAVVAAPHDIKGSFPYAFVTLNVGERINEKLVAEL--KKLV-REKIGALAVPDVIqeapglPKTRSGKVTRRILR-KIA 650
Cdd:PLN02246 462 DAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFvaKQVVfYKRIHKVFFVDSI------PKAPSGKILRKDLRaKLA 535
|
..
gi 71982997 651 EG 652
Cdd:PLN02246 536 AG 537
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
108-652 |
1.14e-20 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 96.24 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 108 YGNKIAYIFegneptDTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSA 187
Cdd:PLN03102 27 YPNRTSIIY------GKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 188 ESLAARVVDARCRVLVtadgVFRGAKPIglksIADAAAVLASQEDVKVEAIIMVEHLKRVTKPDGVELpkvdytditviy 267
Cdd:PLN03102 101 TSIAAILRHAKPKILF----VDRSFEPL----AREVLHLLSSEDSNLNLPVIFIHEIDFPKRPSSEEL------------ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 268 DSEMLKCAGVDSPVEWM------DSEDPLFILYTSGSTGKPKGIQHTTAGymtyAYATTkytfdaqeddvywCTADCGWI 341
Cdd:PLN03102 161 DYECLIQRGEPTPSLVArmfriqDEHDPISLNYTSGTTADPKGVVISHRG----AYLST-------------LSAIIGWE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 342 TG--HSYLLYGPLM--NGLKGIWyeGVPT---------YPTPSRMWDVTDKYGVTKLYTSPTAARALMAlGNQWLESSSR 408
Cdd:PLN03102 224 MGtcPVYLWTLPMFhcNGWTFTW--GTAArggtsvcmrHVTAPEIYKNIEMHNVTHMCCVPTVFNILLK-GNSLDLSPRS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 409 KTLKVIgTVGEPiNPAAwmwLYKQVGLSNVSIVDTYWQTETGGHMITC--------LPGATPMKPGA-AAMPFFGASPVL 479
Cdd:PLN03102 301 GPVHVL-TGGSP-PPAA---LVKKVQRLGFQVMHAYGLTEATGPVLFCewqdewnrLPENQQMELKArQGVSILGLADVD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 480 LDAEGRVIEGPGEGSLCFDRAWPG--MMRGIYGDEQrfvKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHL 557
Cdd:PLN03102 376 VKNKETQESVPRDGKTMGEIVIKGssIMKGYLKNPK---ATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGEN 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 558 LSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINE----KLVA---ELKKLVREKIGALAVPDVIQEA 630
Cdd:PLN03102 453 ISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEdrvdKLVTrerDLIEYCRENLPHFMCPRKVVFL 532
|
570 580
....*....|....*....|..
gi 71982997 631 PGLPKTRSGKVTRRILRKIAEG 652
Cdd:PLN03102 533 QELPKNGNGKILKPKLRDIAKG 554
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
100-648 |
2.64e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 95.07 E-value: 2.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 100 LERNIKRgYGNKIAYIFEGneptdtSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMhs 179
Cdd:PRK05605 38 YDNAVAR-FGDRPALDFFG------ATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAV-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 180 VVFAG--FSAESLAARVVDARCRVLVTADGVfrgakpiglksiadAAAVLASQEDVKVEAIIMVE------HLKRV---- 247
Cdd:PRK05605 109 VVEHNplYTAHELEHPFEDHGARVAIVWDKV--------------APTVERLRRTTPLETIVSVNmiaampLLQRLalrl 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 248 ------TKPDGVELPKVDYTDITVIYDSEMLKCAGVDSPVEwMDSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAyattk 321
Cdd:PRK05605 175 pipalrKARAALTGPAPGTVPWETLVDAAIGGDGSDVSHPR-PTPDDVALILYTSGTTGKPKGAQLTHRNLFANA----- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 322 ytfdAQEDdvywctadcGWITG---------------HSYllyGPLMNGLKGIWYEG----VPTYPTPSRMwDVTDKYGV 382
Cdd:PRK05605 249 ----AQGK---------AWVPGlgdgpervlaalpmfHAY---GLTLCLTLAVSIGGelvlLPAPDIDLIL-DAMKKHPP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 383 TKLYTSPTAARALMAlgnqwlesSSRKTLKVIGTVGEPINPAAWMwlykqvglsNVSIVDTyWQTETGGHMIT------C 456
Cdd:PRK05605 312 TWLPGVPPLYEKIAE--------AAEERGVDLSGVRNAFSGAMAL---------PVSTVEL-WEKLTGGLLVEgyglteT 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 457 LPGAT--PM----KPGAAAMPFfgasPvllDAEGRVI--EGPGEgslcfDRAwPG-----MMRGiygdEQRFvKTYL--- 520
Cdd:PRK05605 374 SPIIVgnPMsddrRPGYVGVPF----P---DTEVRIVdpEDPDE-----TMP-DGeegelLVRG----PQVF-KGYWnrp 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 521 ---APF--NGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVT 595
Cdd:PRK05605 436 eetAKSflDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVV 515
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 71982997 596 LNVGERINEklvAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRK 648
Cdd:PRK05605 516 LEPGAALDP---EGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
128-649 |
3.32e-20 |
|
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: 94.52 E-value: 3.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 128 TYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTADG 207
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 208 VFRgaKPIGLKS---IADAAAVLASQEDVKVeaiiMVEHLKRVTKPDGVELPKVDYTditviydsemlkcagvdsPVEWM 284
Cdd:cd17642 126 GLQ--KVLNVQKklkIIKTIIILDSKEDYKG----YQCLYTFITQNLPPGFNEYDFK------------------PPSFD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 285 DSEDPLFILYTSGSTGKPKGIQHTTAGYMTyayattkyTFDAQEDDVYWC-----TADCGWITGHS----YLLYGPLMNG 355
Cdd:cd17642 182 RDEQVALIMNSSGSTGLPKGVQLTHKNIVA--------RFSHARDPIFGNqiipdTAILTVIPFHHgfgmFTTLGYLICG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 356 LKGIWyegVPTYPTPSRMWDVTDkYGVTKLYTSPTaaraLMALGNQ--WLESSSRKTLKVIGTVGEPINPAAWMWLYKQV 433
Cdd:cd17642 254 FRVVL---MYKFEEELFLRSLQD-YKVQSALLVPT----LFAFFAKstLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 434 GLSNVSivDTYWQTETGGHMITclpgaTP---MKPGAAA--MPFFGASPVLLDAeGRVIeGPGE-GSLCFDRawPGMMRG 507
Cdd:cd17642 326 KLPGIR--QGYGLTETTSAILI-----TPegdDKPGAVGkvVPFFYAKVVDLDT-GKTL-GPNErGELCVKG--PMIMKG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 508 IYGDEQrfVKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKG 587
Cdd:cd17642 395 YVNNPE--ATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAG 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 588 SFPYAFVTLNVGERINEKLVAEL--------KKLvreKIGALAVPDViqeapglPKTRSGKVTRRILRKI 649
Cdd:cd17642 473 ELPAAVVVLEAGKTMTEKEVMDYvasqvstaKRL---RGGVKFVDEV-------PKGLTGKIDRRKIREI 532
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
128-652 |
3.48e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 94.18 E-value: 3.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 128 TYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAmhsvVFAgfsaeslaarvvdarcrvlvtadg 207
Cdd:PRK06145 29 SYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGA----VFL------------------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 208 vfrgakPIGLKSIADAAAVLASQEDVKveaIIMVEhlKRVTKPDGVELPKVdYTDITVIYDSEMLKCAGVDSPVEWMDSE 287
Cdd:PRK06145 81 ------PINYRLAADEVAYILGDAGAK---LLLVD--EEFDAIVALETPKI-VIDAAAQADSRRLAQGGLEIPPQAAVAP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 288 DPLF-ILYTSGSTGKPKGIQHTTagymtyayattkytfdaqeDDVYWCTAD----CGWITGHSYLLYGPL-------MNG 355
Cdd:PRK06145 149 TDLVrLMYTSGTTDRPKGVMHSY-------------------GNLHWKSIDhviaLGLTASERLLVVGPLyhvgafdLPG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 356 LKGIWYEG---VPTYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSRKTLKVIGtvGEPiNPAAWMWLYKQ 432
Cdd:PRK06145 210 IAVLWVGGtlrIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGG--GEK-TPESRIRDFTR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 433 VgLSNVSIVDTYWQTETGGHMITCLPGATPMKPGAAAMPFFGASPVLLDAEGRVIEGPGEGSLCFdrAWPGMMRGIYGDE 512
Cdd:PRK06145 287 V-FTRARYIDAYGLTETCSGDTLMEAGREIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICM--RGPKVTKGYWKDP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 513 QrfvKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYA 592
Cdd:PRK06145 364 E---KTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITA 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 593 FVTLNVGERINeklVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRKIAEG 652
Cdd:PRK06145 441 VVVLNPGATLT---LEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDELNG 497
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
110-646 |
3.54e-20 |
|
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: 94.08 E-value: 3.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 110 NKIAYIFEgneptdTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAES 189
Cdd:cd17656 3 DAVAVVFE------NQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 190 LAARVVDARCRVLVTadgvfrgakpiglksiadaaavlasqedvKVEAIIMVEHLKRVTKPDGVELPKVDYTDITVIYDS 269
Cdd:cd17656 77 RIYIMLDSGVRVVLT-----------------------------QRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 270 EMLkcagvdspvewmdsedpLFILYTSGSTGKPKGIQ---HTTAGYMTYAYATTKYTFdaqEDDVYW---CTADCGWITG 343
Cdd:cd17656 128 DDL-----------------LYIIYTSGTTGKPKGVQlehKNMVNLLHFEREKTNINF---SDKVLQfatCSFDVCYQEI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 344 HSYLLYGPLMNGLKGIWYEGVPtyptpsRMWDVTDKYGVTKLYTsPTAARALMALGNQWLESSSrKTLKVIGTVGEPI-- 421
Cdd:cd17656 188 FSTLLSGGTLYIIREETKRDVE------QLFDLVKRHNIEVVFL-PVAFLKFIFSEREFINRFP-TCVKHIITAGEQLvi 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 422 -NPAAWMWLYKQVGLSNvsivdTYWQTETggHMITclpgATPMKPGA--AAMPFFGASPV-----LLDAEGRVIEGPGEG 493
Cdd:cd17656 260 tNEFKEMLHEHNVHLHN-----HYGPSET--HVVT----TYTINPEAeiPELPPIGKPISntwiyILDQEQQLQPQGIVG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 494 SLCFDRAwpGMMRGIYGDEQRFVKTYLA-PFNGY---YFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVA 569
Cdd:cd17656 329 ELYISGA--SVARGYLNRQELTAEKFFPdPFDPNermYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLN 406
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71982997 570 HEKVAEAAVVAAPHDIKGSFPYAFVTLNVgeRINeklVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRIL 646
Cdd:cd17656 407 HPGVSEAVVLDKADDKGEKYLCAYFVMEQ--ELN---ISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
128-648 |
1.02e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 94.64 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 128 TYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARcrvlvtadg 207
Cdd:PRK12316 2030 SYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSG--------- 2100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 208 vfrgakpiglksiadaAAVLASQEDVkveaiimvehLKRVTKPDGVElpkvdytditviydsemlkCAGVDSPVEWMD-- 285
Cdd:PRK12316 2101 ----------------AALLLTQRHL----------LERLPLPAGVA-------------------RLPLDRDAEWADyp 2135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 286 SEDPL---------FILYTSGSTGKPKG--------IQHTTAGYMTYAYATT-------KYTFDAQEDDVYWctadcgwi 341
Cdd:PRK12316 2136 DTAPAvqlagenlaYVIYTSGSTGLPKGvavshgalVAHCQAAGERYELSPAdcelqfmSFSFDGAHEQWFH-------- 2207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 342 tghsyllygPLMNGLK------GIWyegvptypTPSRMWDVTDKYGVTKLYTSPTAaraLMALGNQWLESSSRKTLKVIG 415
Cdd:PRK12316 2208 ---------PLLNGARvlirddELW--------DPEQLYDEMERHGVTILDFPPVY---LQQLAEHAERDGRPPAVRVYC 2267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 416 TVGEPInPAAwmwLYKQV--GLSNVSIVDTYWQTETgghMITCLP-GATPMKPGAAAMPFFGA-----SPVLLDAEGRVI 487
Cdd:PRK12316 2268 FGGEAV-PAA---SLRLAweALRPVYLFNGYGPTEA---VVTPLLwKCRPQDPCGAAYVPIGRalgnrRAYILDADLNLL 2340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 488 EGPGEGSLCFdrAWPGMMRGIYG----DEQRFVKTylaPFNG----YYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLS 559
Cdd:PRK12316 2341 APGMAGELYL--GGEGLARGYLNrpglTAERFVPD---PFSAsgerLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIE 2415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 560 TAEIESALVAHEKVAEAAVVaaphDIKGSFPYAFVTLNVGERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSG 639
Cdd:PRK12316 2416 LGEIEARLQAHPAVREAVVV----AQDGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNG 2491
|
....*....
gi 71982997 640 KVTRRILRK 648
Cdd:PRK12316 2492 KLDRKALPK 2500
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
126-651 |
1.59e-19 |
|
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: 92.22 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 126 TWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAmhsvVFAGFSAESLAARvvdarcrvlvta 205
Cdd:cd05918 24 SLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGG----AFVPLDPSHPLQR------------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 206 dgvfrgakpigLKSI---ADAAAVLASQEDvkveaiimvehlkrvtkpdgvelpkvdytditviydsemlkcagvdspve 282
Cdd:cd05918 88 -----------LQEIlqdTGAKVVLTSSPS-------------------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 283 wmdseDPLFILYTSGSTGKPKG--IQH----TTAGYMTYAYATTK---------YTFDAqeddvywCTADcgwitghsyl 347
Cdd:cd05918 107 -----DAAYVIFTSGSTGKPKGvvIEHralsTSALAHGRALGLTSesrvlqfasYTFDV-------SILE---------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 348 LYGPLMNGLkgiwyegvpTYPTPS---RMWDVTD---KYGVTKLYTSPTAARALmalgnqwlESSSRKTLKVIGTVGEPI 421
Cdd:cd05918 165 IFTTLAAGG---------CLCIPSeedRLNDLAGfinRLRVTWAFLTPSVARLL--------DPEDVPSLRTLVLGGEAL 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 422 NPA---AWMwlykqvglSNVSIVDTYWQTETGGHMIT--CLPGATPMKPGAAampfFGAS-----------PVLLDAEGR 485
Cdd:cd05918 228 TQSdvdTWA--------DRVRLINAYGPAECTIAATVspVVPSTDPRNIGRP----LGATcwvvdpdnhdrLVPIGAVGE 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 486 -VIEGP--GEG--------SLCF--DRAWpgMMRGIYGDEQRFvktylapfngyYFTGDGARRDEDGYLWITGRVDDLMN 552
Cdd:cd05918 296 lLIEGPilARGylndpektAAAFieDPAW--LKQEGSGRGRRL-----------YRTGDLVRYNPDGSLEYVGRKDTQVK 362
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 553 VSGHLLSTAEIESALVAH-EKVAEAAVVAAPHDIKGSFPY--AFVTLNVGERIN--------------EKLVAELKKLVR 615
Cdd:cd05918 363 IRGQRVELGEIEHHLRQSlPGAKEVVVEVVKPKDGSSSPQlvAFVVLDGSSSGSgdgdslflepsdefRALVAELRSKLR 442
|
570 580 590
....*....|....*....|....*....|....*.
gi 71982997 616 EKIGALAVPDVIQEAPGLPKTRSGKVTRRILRKIAE 651
Cdd:cd05918 443 QRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAE 478
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
122-661 |
1.61e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 92.40 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 122 TDTSTWTYNE-LHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAmhsvVFAGFS----AESLAARVVD 196
Cdd:PRK13388 22 YGDRTWTWREvLAEAAARAAALIALADPDRPLHVGVLLGNTPEMLFWLAAAALGGY----VLVGLNttrrGAALAADIRR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 197 ARCRVLVTADgvfrgakpiglksiadaaavlasqedvkveaiimvEHLKRVtkpDGVELPKVDYTDITVIYDSEMLKCAG 276
Cdd:PRK13388 98 ADCQLLVTDA-----------------------------------EHRPLL---DGLDLPGVRVLDVDTPAYAELVAAAG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 277 VDSPVEWMDSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKyTFDAQEDDVYWCTAdcgwitghsyllygPLM--N 354
Cdd:PRK13388 140 ALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTE-RFGLTRDDVCYVSM--------------PLFhsN 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 355 GLKGIWYEGV---------PTYpTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQwlESSSRKTLKV-IGTVGEPINPA 424
Cdd:PRK13388 205 AVMAGWAPAVasgaavalpAKF-SASGFLDDVRRYGATYFNYVGKPLAYILATPER--PDDADNPLRVaFGNEASPRDIA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 425 AWMwlyKQVGlsnVSIVDTYWQTETGGhMITCLPGaTPmkPGAAAMPFFGAS-----------PVLLDAEGRVI---EGP 490
Cdd:PRK13388 282 EFS---RRFG---CQVEDGYGSSEGAV-IVVREPG-TP--PGSIGRGAPGVAiynpetltecaVARFDAHGALLnadEAI 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 491 GEgslCFDRAWPGMMRGIYGDE----QRFVktylapfNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESA 566
Cdd:PRK13388 352 GE---LVNTAGAGFFEGYYNNPeataERMR-------HGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERI 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 567 LVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEKLVAELkkLV-REKIGALAVPDVIQEAPGLPKTRSGKVTRRI 645
Cdd:PRK13388 422 LLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAF--LAaQPDLGTKAWPRYVRIAADLPSTATNKVLKRE 499
|
570
....*....|....*.
gi 71982997 646 LRkiAEGSESGIGDTT 661
Cdd:PRK13388 500 LI--AQGWATGDPVTL 513
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
123-647 |
1.96e-19 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 92.13 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 123 DTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAArVVDARCRVL 202
Cdd:PRK13382 65 ELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAE-VVTREGVDT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 203 VTADGVFRGAKPIGLKSIADAAAVLA---SQEDVKVEAIImvehlkrvTKPDGVELPKVDYTDITviydsemlkcagvds 279
Cdd:PRK13382 144 VIYDEEFSATVDRALADCPQATRIVAwtdEDHDLTVEVLI--------AAHAGQRPEPTGRKGRV--------------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 280 pvewmdsedplfILYTSGSTGKPKGIQHT-TAGYMTYAYATTKYTFDAQEDDVYWCTADCGWitGHSYLLYGPLMNGlkg 358
Cdd:PRK13382 201 ------------ILLTSGTTGTPKGARRSgPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAW--GFSQLVLAASLAC--- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 359 iwyegvpTYPT-----PSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSRKTLKVIGTVGEPINPAAWMWLYKQV 433
Cdd:PRK13382 264 -------TIVTrrrfdPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQF 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 434 GlsNVsIVDTYWQTETGghMITClpgATP----MKPGAAAMPFFGASPVLLDAEGRviEGP-GE-------GSLCFDRAW 501
Cdd:PRK13382 337 G--DV-IYNNYNATEAG--MIAT---ATPadlrAAPDTAGRPAEGTEIRILDQDFR--EVPtGEvgtifvrNDTQFDGYT 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 502 PGMMRGIYgdeqrfvktylapfNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAA 581
Cdd:PRK13382 407 SGSTKDFH--------------DGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGV 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71982997 582 PHDIKGSFPYAFVTLNVGERineKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILR 647
Cdd:PRK13382 473 DDEQYGQRLAAFVVLKPGAS---ATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
287-643 |
2.67e-19 |
|
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: 89.63 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 287 EDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYTFDAQEDDVYWCTADCGWITGHSYLLYGPLMNGLKGIWYEgvpt 366
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 367 YPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSsrKTLKVIGTVGE-PINPAAWMWLYKQvglsNVSIVDTYW 445
Cdd:cd17635 77 NTTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATV--PSLRLIGYGGSrAIAADVRFIEATG----LTNTAQVYG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 446 QTETGghMITCLP-GATPMKPGAAAMPFFGASPVLLDAEGRVIEGPGEGSLCFDRAWpgMMRGIYGDEQRFVKTYLapfN 524
Cdd:cd17635 151 LSETG--TALCLPtDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPA--NMLGYWNNPERTAEVLI---D 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 525 GYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTlnVGERINE 604
Cdd:cd17635 224 GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVV--ASAELDE 301
|
330 340 350
....*....|....*....|....*....|....*....
gi 71982997 605 KLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTR 643
Cdd:cd17635 302 NAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
288-648 |
3.08e-19 |
|
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: 90.81 E-value: 3.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 288 DPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYtfdaqeddvyWctadcGWiTGHSYLLYG-PL------MNGLKGIW 360
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDA----------W-----RW-TEDDVLLHVlPLhhvhglVNALLCPL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 361 YEGVP----TYPTPSRMWDVTDKYGVTKLYTSPT------AARALMALGNQWLESSSRKTLK--VIGTVGEPInP--AAW 426
Cdd:cd05941 154 FAGASveflPKFDPKEVAISRLMPSITVFMGVPTiytrllQYYEAHFTDPQFARAAAAERLRlmVSGSAALPV-PtlEEW 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 427 MWLYKQVglsnvsIVDTYWQTETGghMITCLPGATPMKPGAAAMPFFGASPVLLDAEGRVIEGPGE-GSLCFdrAWPGMM 505
Cdd:cd05941 233 EAITGHT------LLERYGMTEIG--MALSNPLDGERRPGTVGMPLPGVQARIVDEETGEPLPRGEvGEIQV--RGPSVF 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 506 RGIYGDEQRFVKTYLApfNGYYFTGDGARRDEDGYLWITGRV-DDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHD 584
Cdd:cd05941 303 KEYWNKPEATKEEFTD--DGWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDP 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71982997 585 IKGSFPYAFVTLNVGErinEKLVAE-LKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRK 648
Cdd:cd05941 381 DWGERVVAVVVLRAGA---AALSLEeLKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
126-646 |
5.03e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 92.33 E-value: 5.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 126 TWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARcrvlvta 205
Cdd:PRK12316 536 TLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSG------- 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 206 dgvfrgakpiglksiadaAAVLASQEdvkveaiimveHLKRVTkPDGVELPKVDYTDITVIYDSEmlkcaGVDSPVEWMD 285
Cdd:PRK12316 609 ------------------VQLLLSQS-----------HLGRKL-PLAAGVQVLDLDRPAAWLEGY-----SEENPGTELN 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 286 SEDPLFILYTSGSTGKPKGIQHTTAGYMTY-AYATTKYTFDAQeDDVYWCTADCGWITghSYLLYGPLMNGLKGIwYEGV 364
Cdd:PRK12316 654 PENLAYVIYTSGSTGKPKGAGNRHRALSNRlCWMQQAYGLGVG-DTVLQKTPFSFDVS--VWEFFWPLMSGARLV-VAAP 729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 365 PTYPTPSRMWDVTDKYGVTKLYTSPTAARALMalgnQWLESSSRKTLKVIGTVGEPINPAAWMWLYKQvgLSNVSIVDTY 444
Cdd:PRK12316 730 GDHRDPAKLVELINREGVDTLHFVPSMLQAFL----QDEDVASCTSLRRIVCSGEALPADAQEQVFAK--LPQAGLYNLY 803
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 445 WQTETGGHmITClpgATPMKPGAAAM----PFFGASPVLLDAEGRVIEGPGEGSLCFdrAWPGMMRGIYG----DEQRFV 516
Cdd:PRK12316 804 GPTEAAID-VTH---WTCVEEGGDSVpigrPIANLACYILDANLEPVPVGVLGELYL--AGRGLARGYHGrpglTAERFV 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 517 KtylAPF-NG--YYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAaphdIKGSFPYAF 593
Cdd:PRK12316 878 P---SPFvAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGY 950
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 71982997 594 VTL-NVGERINEKLVAELKKLVREKIgalaVPDVIQEAPGLPKTRSGKVTRRIL 646
Cdd:PRK12316 951 VVLeSEGGDWREALKAHLAASLPEYM----VPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
128-646 |
1.11e-18 |
|
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: 89.49 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 128 TYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTADG 207
Cdd:cd05923 30 TYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAVD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 208 vfrgAKPIglKSIADAAA-VLASQEDVKVeaiimvehlkRVTKPDGVELPkvdytditviydsemlkcagvDSPVEwmdS 286
Cdd:cd05923 110 ----AQVM--DAIFQSGVrVLALSDLVGL----------GEPESAGPLIE---------------------DPPRE---P 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 287 EDPLFILYTSGSTGKPKG--IQHTTAGYMTYAYAT-TKYTFDAQED-----DVYWctadcgwITGHSYLLYGPLMngLKG 358
Cdd:cd05923 150 EQPAFVFYTSGTTGLPKGavIPQRAAESRVLFMSTqAGLRHGRHNVvlglmPLYH-------VIGFFAVLVAALA--LDG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 359 IWYegVPTYPTPSRMWDVTDKYGVTKLYTSPTAARALMALgnqwLESSSRK--TLKVIGTVGEPINPAawmwLYKQVG-- 434
Cdd:cd05923 221 TYV--VVEEFDPADALKLIEQERVTSLFATPTHLDALAAA----AEFAGLKlsSLRHVTFAGATMPDA----VLERVNqh 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 435 LSNvSIVDTYWQTETGGHMITCLPGA-TPMKPGaaampFF--------GASPVLLDAEGRviEGPGEGSLCFDRAWPGMM 505
Cdd:cd05923 291 LPG-EKVNIYGTTEAMNSLYMRDARTgTEMRPG-----FFsevrivriGGSPDEALANGE--EGELIVAAAADAAFTGYL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 506 RgiygdeqRFVKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDI 585
Cdd:cd05923 363 N-------QPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADER 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71982997 586 KGSFPYAFVTLNVGERINEKL-----VAELKKLVREKigALAVPDviqeapGLPKTRSGKVTRRIL 646
Cdd:cd05923 436 WGQSVTACVVPREGTLSADELdqfcrASELADFKRPR--RYFFLD------ELPKNAMNKVLRRQL 493
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
100-651 |
1.61e-18 |
|
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: 89.26 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 100 LERNIKRGYGNKIAYIFEGNEPTdtsTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACarigamhs 179
Cdd:cd05906 16 LLRAAERGPTKGITYIDADGSEE---FQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWAC-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 180 vVFAGFSAESLAARVVDARCRVlvtadgvfRGAKPIGLKSIADAAAVLASQEdvkveaiiMVEHLKRVTKPDGVElpkvd 259
Cdd:cd05906 85 -VLAGFVPAPLTVPPTYDEPNA--------RLRKLRHIWQLLGSPVVLTDAE--------LVAEFAGLETLSGLP----- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 260 ytDITVIYDSEMLKCAGvDSPVEWMDSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKyTFDAQEDDVY--WCTAD 337
Cdd:cd05906 143 --GIRVLSIEELLDTAA-DHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQ-HNGLTPQDVFlnWVPLD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 338 cgwitgHsylLYGPLMNGLKGIWYEG----VPT---YPTPSRMWDVTDKYGVTklYT-SPTAARALMalgNQWLESSSRK 409
Cdd:cd05906 219 ------H---VGGLVELHLRAVYLGCqqvhVPTeeiLADPLRWLDLIDRYRVT--ITwAPNFAFALL---NDLLEEIEDG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 410 T-----LKVIGTVGEPINPA---AWMWLYKQVGLSNVSIVDTYWQTETGGHMITCLPGATPMKPGA-------AAMPffG 474
Cdd:cd05906 285 TwdlssLRYLVNAGEAVVAKtirRLLRLLEPYGLPPDAIRPAFGMTETCSGVIYSRSFPTYDHSQAlefvslgRPIP--G 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 475 ASPVLLDAEGRVIEGPGEGSLcfDRAWPGMMRGIYGDEQRFVKTYLApfNGYYFTGDGARRDeDGYLWITGRVDDLMNVS 554
Cdd:cd05906 363 VSMRIVDDEGQLLPEGEVGRL--QVRGPVVTKGYYNNPEANAEAFTE--DGWFRTGDLGFLD-NGNLTITGRTKDTIIVN 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 555 GHLLSTAEIESALVAHEkvaeaavvaaphDIKGSFPYAFVTLNVGERINE----------------KLVAELKKLVREKI 618
Cdd:cd05906 438 GVNYYSHEIEAAVEEVP------------GVEPSFTAAFAVRDPGAETEElaiffvpeydlqdalsETLRAIRSVVSREV 505
|
570 580 590
....*....|....*....|....*....|....
gi 71982997 619 GaLAVPDVIQEAPG-LPKTRSGKVTRRILRKIAE 651
Cdd:cd05906 506 G-VSPAYLIPLPKEeIPKTSLGKIQRSKLKAAFE 538
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
125-648 |
2.22e-18 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 89.04 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 125 STWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVT 204
Cdd:PRK06087 48 ASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 205 adgvfrgakPIGLKSIADAAAVLASQEDVKveaiimveHLKRVTKPDGVELPKVDYTDITVIYDSEMLKcagvdSPVEwM 284
Cdd:PRK06087 128 ---------PTLFKQTRPVDLILPLQNQLP--------QLQQIVGVDKLAPATSSLSLSQIIADYEPLT-----TAIT-T 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 285 DSEDPLFILYTSGSTGKPKGI--QHTTAGYMTYAYATTkytFDAQEDDVYWCTADCGWITGHSYLLYGPLMNGLKGIWYE 362
Cdd:PRK06087 185 HGDELAAVLFTSGTEGLPKGVmlTHNNILASERAYCAR---LNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 363 GVptypTPSRMWDVTDKYGVT-KLYTSPTAARALMALGNQWLESSsrkTLKVIGTVGEPInPAAwmwLYKQVGLSNVSIV 441
Cdd:PRK06087 262 IF----TPDACLALLEQQRCTcMLGATPFIYDLLNLLEKQPADLS---ALRFFLCGGTTI-PKK---VARECQQRGIKLL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 442 DTYWQTETGGHMITCLPGATPMKPGAAAMPFFGASPVLLDAEGRVIEGPGEGSLCfDRAwPGMMRGIYGDEQRFVKTYLA 521
Cdd:PRK06087 331 SVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEA-SRG-PNVFMGYLDEPELTARALDE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 522 pfNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGER 601
Cdd:PRK06087 409 --EGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHH 486
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 71982997 602 INEklVAELKK-LVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRK 648
Cdd:PRK06087 487 SLT--LEEVVAfFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
562-640 |
2.83e-18 |
|
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: 79.51 E-value: 2.83e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71982997 562 EIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGeriNEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGK 640
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPG---VELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
110-646 |
8.63e-18 |
|
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: 87.00 E-value: 8.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 110 NKIAYIFEGNeptdtsTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAES 189
Cdd:cd17655 12 DHTAVVFEDQ------TLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 190 LAARVVDARCRVLVTAdgvfrgaKPIGLKSIADAAAVLASQEDVKVEAiimVEHLKRVTKPDgvelpkvdytditviyds 269
Cdd:cd17655 86 IQYILEDSGADILLTQ-------SHLQPPIAFIGLIDLLDEDTIYHEE---SENLEPVSKSD------------------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 270 emlkcagvdspvewmdseDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYTFDAQEDDV-----YWCTADCGWItgh 344
Cdd:cd17655 138 ------------------DLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRValfasISFDASVTEI--- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 345 syllYGPLMNGLKGIWYEGVPTYPTPSRMwDVTDKYGVTKLYTSPTAARALMAlgNQWLESSSRKTLkVIGtvGEPINPA 424
Cdd:cd17655 197 ----FASLLSGNTLYIVRKETVLDGQALT-QYIRQNRITIIDLTPAHLKLLDA--ADDSEGLSLKHL-IVG--GEALSTE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 425 AWMWLYKQVGLsNVSIVDTYWQTETgghMITCLPG-ATPMKPGAAAMPFfgASPV------LLDAEGRVI-EG-PGEgsL 495
Cdd:cd17655 267 LAKKIIELFGT-NPTITNAYGPTET---TVDASIYqYEPETDQQVSVPI--GKPLgntriyILDQYGRPQpVGvAGE--L 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 496 CFdrAWPGMMRGIYG----DEQRFVKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHE 571
Cdd:cd17655 339 YI--GGEGVARGYLNrpelTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHP 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71982997 572 KVAEAAVVAAPHDIKGSFPYAFVTLNvgeriNEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRIL 646
Cdd:cd17655 417 DIKEAVVIARKDEQGQNYLCAYIVSE-----KELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
128-680 |
8.87e-18 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 87.78 E-value: 8.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 128 TYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTADG 207
Cdd:PRK06060 32 THGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 208 VFRGAKPiglKSIADAAAVLAsqedvkveaiimvehlkrvtkpDGVELPKVDYtditviydsemlkcagvdspvEWMDSE 287
Cdd:PRK06060 112 LRDRFQP---SRVAEAAELMS----------------------EAARVAPGGY---------------------EPMGGD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 288 DPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYTFDAQEDDVYWCTADCGWITGHSYLLYGPLMNGLKGIwYEGVPTY 367
Cdd:PRK06060 146 ALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAV-INSAPVT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 368 PTPSRMwdVTDKYGVTKLYTSPTA-ARALMALgnqwlESSSRKTLKVIGTVGEPINPAAWMWLYKQVGlsNVSIVDTYWQ 446
Cdd:PRK06060 225 PEAAAI--LSARFGPSVLYGVPNFfARVIDSC-----SPDSFRSLRCVVSAGEALELGLAERLMEFFG--GIPILDGIGS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 447 TETGGHMITclPGATPMKPGAAAmpffgasPVLLDAEGRVIE------GPG-EGSLcfdraW---PGMMRGIYGDEQRFV 516
Cdd:PRK06060 296 TEVGQTFVS--NRVDEWRLGTLG-------RVLPPYEIRVVApdgttaGPGvEGDL-----WvrgPAIAKGYWNRPDSPV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 517 KTylapfNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTL 596
Cdd:PRK06060 362 AN-----EGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVA 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 597 NVGERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRkiAEGSESGIGDTTTLVDESVIKQLISGR 676
Cdd:PRK06060 437 TSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR--KQSPTKPIWELSLTEPGSGVRAQRDDL 514
|
....
gi 71982997 677 SARA 680
Cdd:PRK06060 515 SASN 518
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
287-647 |
9.63e-18 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 85.02 E-value: 9.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 287 EDPLFILYTSGSTGKPKGIQHTTAGYMTYAYAT---TKYTfdaqEDDVYWCtadcgwitghSYLLY---GPLMNGLKGIW 360
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIgerLGLT----EQDRLCI----------PVPLFhcfGSVLGVLACLT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 361 YEGVPTYPTPSrmWDVTD------KYGVTKLYTSPTAARALMALGNQWLESSSRKTLKVIGtvGEPINPAAWMWLYKQVG 434
Cdd:cd05917 68 HGATMVFPSPS--FDPLAvleaieKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMA--GAPCPPELMKRVIEVMN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 435 LSNVSIVdtYWQTETGGHMITCLPGATPMKPGAA---AMPFFGASPVllDAEGRVIEGPGE-GSLCFdRAWpGMMRGIYG 510
Cdd:cd05917 144 MKDVTIA--YGMTETSPVSTQTRTDDSIEKRVNTvgrIMPHTEAKIV--DPEGGIVPPVGVpGELCI-RGY-SVMKGYWN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 511 DEQRFVKTYLApfNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFP 590
Cdd:cd05917 218 DPEKTAEAIDG--DGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEV 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 71982997 591 YAFVTLNVGERINEklvAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILR 647
Cdd:cd05917 296 CAWIRLKEGAELTE---EDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
128-646 |
1.31e-17 |
|
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: 85.77 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 128 TYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTadg 207
Cdd:cd17652 14 TYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLT--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 208 vfrgakpiglksiadaaavlasqedvkveaiimvehlkrvtkpdgvelpkvdytditviydsemlkcagvdspvewmDSE 287
Cdd:cd17652 91 -----------------------------------------------------------------------------TPD 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 288 DPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYtFDAQEDDVY--------------WCTAdcgWITGHSYLLygplm 353
Cdd:cd17652 94 NLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAA-FDVGPGSRVlqfaspsfdasvweLLMA---LLAGATLVL----- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 354 nglkgiwyegVPTYPT--PSRMWDVTDKYGVTKLyTSPTAARAlmalgnqWLESSSRKTLKVIGTVGEPINPAawmwLYK 431
Cdd:cd17652 165 ----------APAEELlpGEPLADLLREHRITHV-TLPPAALA-------ALPPDDLPDLRTLVVAGEACPAE----LVD 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 432 QVGLSNVsIVDTYWQTET--GGHMITCLPGATPMKPGAaamPFFGASPVLLDAEGRVIEgPGE-GSLCFdrAWPGMMRGi 508
Cdd:cd17652 223 RWAPGRR-MINAYGPTETtvCATMAGPLPGGGVPPIGR---PVPGTRVYVLDARLRPVP-PGVpGELYI--AGAGLARG- 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 509 YGDE-----QRFVktyLAPFNG----YYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVV 579
Cdd:cd17652 295 YLNRpgltaERFV---ADPFGApgsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVV 371
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71982997 580 AAPHDIKGSFPYAFVTLNVGERINeklVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRIL 646
Cdd:cd17652 372 VRDDRPGDKRLVAYVVPAPGAAPT---AAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
128-647 |
2.48e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 85.51 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 128 TYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTAdg 207
Cdd:PRK13391 26 TYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITS-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 208 vfrGAKpiglksiADAAAvLASQEDVKVEAIIMVEHLKRVTKPDGVELPKVDYTDiTVIYDsemlKCAGVDspvewmdse 287
Cdd:PRK13391 104 ---AAK-------LDVAR-ALLKQCPGVRHRLVLDGDGELEGFVGYAEAVAGLPA-TPIAD----ESLGTD--------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 288 dplfILYTSGSTGKPKGIQH--------TTAGYmtYAYATTKYTFDaqEDDVYWCTADcgwitghsylLY--GPLMNGLK 357
Cdd:PRK13391 159 ----MLYSSGTTGRPKGIKRplpeqppdTPLPL--TAFLQRLWGFR--SDMVYLSPAP----------LYhsAPQRAVML 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 358 GIWYEG---VPTYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSRKTLKVIGTVGEPINPA------AWmW 428
Cdd:PRK13391 221 VIRLGGtviVMEHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHAAAPCPPQvkeqmiDW-W 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 429 lykqvGlsnvSIVDTYWQTETGGHMITCLPGATPMKPGAAAMPFFGaSPVLLDAEGRVIEgPGE-GSLCFDRawpGMMRG 507
Cdd:PRK13391 300 -----G----PIIHEYYAATEGLGFTACDSEEWLAHPGTVGRAMFG-DLHILDDDGAELP-PGEpGTIWFEG---GRPFE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 508 IYGDEQrfvKTYLA--PFNGYYFTGDGARRDEDGYLWITGRVDDlMNVSGHL-LSTAEIESALVAHEKVAEAAVVAAPHD 584
Cdd:PRK13391 366 YLNDPA---KTAEArhPDGTWSTVGDIGYVDEDGYLYLTDRAAF-MIISGGVnIYPQEAENLLITHPKVADAAVFGVPNE 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71982997 585 IKGSFPYAFVTLNVGERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILR 647
Cdd:PRK13391 442 DLGEEVKAVVQPVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
126-646 |
3.08e-17 |
|
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: 85.02 E-value: 3.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 126 TWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTA 205
Cdd:cd12114 12 TLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 206 DGVFRGAKPIGLKSIADAAAVLASQEDVKVEAiimvehlkrvtkpdgvelpkvdytditviydsemlkcagvdspvewmD 285
Cdd:cd12114 92 GPDAQLDVAVFDVLILDLDALAAPAPPPPVDV-----------------------------------------------A 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 286 SEDPLFILYTSGSTGKPKGIQHTTAGYM-TYAYATTKYTFDAqeDDVYWCTADCgwitgH----SYLLYGPLMNGlkgiw 360
Cdd:cd12114 125 PDDLAYVIFTSGSTGTPKGVMISHRAALnTILDINRRFAVGP--DDRVLALSSL-----SfdlsVYDIFGALSAG----- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 361 yeGVPTYPT------PSRMWDVTDKYGVTKLYTSPtaarALMALGNQWLESSSRktlkvigtvgEPINPAAWMWLYKQVG 434
Cdd:cd12114 193 --ATLVLPDearrrdPAHWAELIERHGVTLWNSVP----ALLEMLLDVLEAAQA----------LLPSLRLVLLSGDWIP 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 435 LSnvsIVDTYWQTETGGHMITcLPGAT---------PMKPGAAA-------MPFFGASPVLLDAEGR-VIEG-PGEgslc 496
Cdd:cd12114 257 LD---LPARLRALAPDARLIS-LGGATeasiwsiyhPIDEVPPDwrsipygRPLANQRYRVLDPRGRdCPDWvPGE---- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 497 fdrAW---PGMMRGIYGDEQ----RFVKtyLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVA 569
Cdd:cd12114 329 ---LWiggRGVALGYLGDPEltaaRFVT--HPDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQA 403
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71982997 570 HEKVAEAAVVAAPHDIKGSFpYAFVTlnVGERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRIL 646
Cdd:cd12114 404 HPGVARAVVVVLGDPGGKRL-AAFVV--PDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
129-647 |
3.97e-17 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 84.75 E-value: 3.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 129 YNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTADGV 208
Cdd:PRK12406 14 FDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 209 FRGAKPIglksIADAAAVLASQEDVKVEAIIMVEHLKRVTKPDGVElpkvdytditviYDSEMLKCAGVDSPVewmdSED 288
Cdd:PRK12406 94 LHGLASA----LPAGVTVLSVPTPPEIAAAYRISPALLTPPAGAID------------WEGWLAQQEPYDGPP----VPQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 289 PLFILYTSGSTGKPKGIQHTtagymtyayATTKYTFDAQEDDVywcTADCGWITGHSYLLYGPLMN------GLKGIWYE 362
Cdd:PRK12406 154 PQSMIYTSGTTGHPKGVRRA---------APTPEQAAAAEQMR---ALIYGLKPGIRALLTGPLYHsapnayGLRAGRLG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 363 GV----PTYpTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSRKTLKVIGTVGEPInPA-------AWmWlyk 431
Cdd:PRK12406 222 GVlvlqPRF-DPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAPC-PAdvkramiEW-W--- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 432 qvglsNVSIVDTYWQTETGGhMITCLPGATPMKPGAAAMPFFGASPVLLDAEGRVIeGPGEGSLCFDRAwPGMMRGIY-G 510
Cdd:PRK12406 296 -----GPVIYEYYGSTESGA-VTFATSEDALSHPGTVGKAAPGAELRFVDEDGRPL-PQGEIGEIYSRI-AGNPDFTYhN 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 511 DEQRFVKTYLApfnGYYFTGDGARRDEDGYLWITGRVDDlMNVSGHL-LSTAEIESALVAHEKVAEAAVVAAPHDIKGSF 589
Cdd:PRK12406 368 KPEKRAEIDRG---GFITSGDVGYLDADGYLFLCDRKRD-MVISGGVnIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEA 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 71982997 590 PYAFVTLNVGERINEklvAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILR 647
Cdd:PRK12406 444 LMAVVEPQPGATLDE---ADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
124-657 |
5.00e-17 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 84.67 E-value: 5.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 124 TSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAmhsvvfagfsaeslaarvvdarcrVLV 203
Cdd:PRK05857 39 TSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGA------------------------IAV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 204 TADGVFRGAKPIGLKSIADAAAVLASQEDvKVEAiimvehlkrVTKPDGVELPKVDYTDITViyDSEMLKCAG-VDSPVE 282
Cdd:PRK05857 95 MADGNLPIAAIERFCQITDPAAALVAPGS-KMAS---------SAVPEALHSIPVIAVDIAA--VTRESEHSLdAASLAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 283 WMDS--EDPLFILYTSGSTGKPKgiqhttagymtyAYATTKYTFDA-----QEDDVYWCTadcgWITGHSylLYGPL-MN 354
Cdd:PRK05857 163 NADQgsEDPLAMIFTSGTTGEPK------------AVLLANRTFFAvpdilQKEGLNWVT----WVVGET--TYSPLpAT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 355 GLKGIWY------EGVPTYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQW-LESSSRKTLKVIGTVGEPINPAAwm 427
Cdd:PRK05857 225 HIGGLWWiltclmHGGLCVTGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELkSANATVPSLRLVGYGGSRAIAAD-- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 428 wlYKQVGLSNVSIVDTYWQTETGGHMItCLP----GATPMKPGAAAMPFFGASPVLLDAEGRVIEGPGEG-SLCFDRAW- 501
Cdd:PRK05857 303 --VRFIEATGVRTAQVYGLSETGCTAL-CLPtddgSIVKIEAGAVGRPYPGVDVYLAATDGIGPTAPGAGpSASFGTLWi 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 502 --PGMMRGIYGDEQRfvkTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVV 579
Cdd:PRK05857 380 ksPANMLGYWNNPER---TAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACY 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 580 AAPHDIKGsfpyAFVTLNV--GERINEKLVAELKKLV----REKIGALAVPDVIQEAPGLPKTRSGKVTRRILRKIAEGS 653
Cdd:PRK05857 457 EIPDEEFG----ALVGLAVvaSAELDESAARALKHTIaarfRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAATAD 532
|
....
gi 71982997 654 ESGI 657
Cdd:PRK05857 533 KARV 536
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
128-648 |
5.72e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 85.78 E-value: 5.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 128 TYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTAdg 207
Cdd:PRK12316 3084 SYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQ-- 3161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 208 vfrgakpiglksiadaaavlasqedvkveaiimvEHLkRVTKPDGVELPKVDYTDitviydsemlKCAGVDSPVEWMDSE 287
Cdd:PRK12316 3162 ----------------------------------SHL-RLPLAQGVQVLDLDRGD----------ENYAEANPAIRTMPE 3196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 288 DPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYTFDAQEDDVYWCTADCgwITGHSYLLYGPLMNGLKgIWYEGVPTY 367
Cdd:PRK12316 3197 NLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFS--FDVFVEELFWPLMSGAR-VVLAGPEDW 3273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 368 PTPSRMWDVTDKYGVTKLYTSPTAARALMalgnQWLESSSRKTLKVIGTVGEPINPA------AWMWLYKQVGLSNVSIV 441
Cdd:PRK12316 3274 RDPALLVELINSEGVDVLHAYPSMLQAFL----EEEDAHRCTSLKRIVCGGEALPADlqqqvfAGLPLYNLYGPTEATIT 3349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 442 DTYWQTETGGhmITCLPGATPMKPGAAAMPFFGASPVLLDAEGRVIEGpGEGSLCFDRAWPGMmrgiygDEQRFVKTYLA 521
Cdd:PRK12316 3350 VTHWQCVEEG--KDAVPIGRPIANRACYILDGSLEPVPVGALGELYLG-GEGLARGYHNRPGL------TAERFVPDPFV 3420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 522 PFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVaaphDIKGSFPYAFVtlnVGER 601
Cdd:PRK12316 3421 PGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYV---VPED 3493
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 71982997 602 INEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRK 648
Cdd:PRK12316 3494 EAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPR 3540
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
112-654 |
7.78e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 85.21 E-value: 7.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 112 IAYIFEGNEptdtstWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLA 191
Cdd:PRK12467 3112 PALVFGDQQ------LSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLA 3185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 192 ARVVDARCRVLVTAdgvfrgakpiglksiadaAAVLasqedvkvEAIIMVEHLKRVTKPDGVELPKVDytditviydsem 271
Cdd:PRK12467 3186 YMIEDSGVKLLLTQ------------------AHLL--------EQLPAPAGDTALTLDRLDLNGYSE------------ 3227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 272 lkcagvDSPVEWMDSEDPLFILYTSGSTGKPKG--IQHTTAGYMTYAYAT-------------TKYTFDAQEDDVYWcta 336
Cdd:PRK12467 3228 ------NNPSTRVMGENLAYVIYTSGSTGKPKGvgVRHGALANHLCWIAEayeldandrvllfMSFSFDGAQERFLW--- 3298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 337 dcgwitghsyllygPLMNGLKGIWYEGvpTYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGnqwlESSSRKTLKVIGT 416
Cdd:PRK12467 3299 --------------TLICGGCLVVRDN--DLWDPEELWQAIHAHRISIACFPPAYLQQFAEDA----GGADCASLDIYVF 3358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 417 VGEPINPAAWMWLYKQvgLSNVSIVDTYWQTETgghMITCLPGATPM--KPGAAAMPF----FGASPVLLDAEGrvieGP 490
Cdd:PRK12467 3359 GGEAVPPAAFEQVKRK--LKPRGLTNGYGPTEA---VVTVTLWKCGGdaVCEAPYAPIgrpvAGRSIYVLDGQL----NP 3429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 491 ------GE---GSLCFDRAW---PGMMrgiygdEQRFVKTylaPFNG----YYFTGDGARRDEDGYLWITGRVDDLMNVS 554
Cdd:PRK12467 3430 vpvgvaGElyiGGVGLARGYhqrPSLT------AERFVAD---PFSGsggrLYRTGDLARYRADGVIEYLGRIDHQVKIR 3500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 555 GHLLSTAEIESALVAHEKVAEAAVVAAPHDiKGSFPYAFVTLNVgerINEKLVAELKKLVREKIGALAVPDVIQEAPGLP 634
Cdd:PRK12467 3501 GFRIELGEIEARLLQHPSVREAVVLARDGA-GGKQLVAYVVPAD---PQGDWRETLRDHLAASLPDYMVPAQLLVLAAMP 3576
|
570 580
....*....|....*....|.
gi 71982997 635 KTRSGKVTRRILRKI-AEGSE 654
Cdd:PRK12467 3577 LGPNGKVDRKALPDPdAKGSR 3597
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
127-648 |
1.15e-16 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 83.25 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 127 WTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLvtad 206
Cdd:cd05915 25 TTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVL---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 207 gvfrgakpiglksIADAAAVLASQEDVKVeaiimvehLKRVTKPDGVELPKVDYTDITVIYDSEMlkcagvdSPVEWMDS 286
Cdd:cd05915 101 -------------LFDPNLLPLVEAIRGE--------LKTVQHFVVMDEKAPEGYLAYEEALGEE-------ADPVRVPE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 287 EDPLFILYTSGSTGKPKGIQHTTAG-YMTYAYATTKYTFDAQEDDVYWCTAD----CGWITGHSYLLYGPLMNGLKGIWY 361
Cdd:cd05915 153 RAACGMAYTTGTTGLPKGVVYSHRAlVLHSLAASLVDGTALSEKDVVLPVVPmfhvNAWCLPYAATLVGAKQVLPGPRLD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 362 EGVptyptpsrMWDVTDKYGVTKLYTSPTAARaLMALGNQWLESSSRKTLKVIGTVGEPinPAAWMWLYKqvgLSNVSIV 441
Cdd:cd05915 233 PAS--------LVELFDGEGVTFTAGVPTVWL-ALADYLESTGHRLKTLRRLVVGGSAA--PRSLIARFE---RMGVEVR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 442 DTYWQTETGGHMITCL--------PGATPMKPGAA-AMPFFGASPVLLDAEGRVIEGPGEGSLCFDRAWPGMMRGIYGDE 512
Cdd:cd05915 299 QGYGLTETSPVVVQNFvkshleslSEEEKLTLKAKtGLPIPLVRLRVADEEGRPVPKDGKALGEVQLKGPWITGGYYGNE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 513 QrfVKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYA 592
Cdd:cd05915 379 E--ATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLA 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 71982997 593 FVTLNVGERINEKLVaelkKLVREKIGALA-VPDVIQEAPGLPKTRSGKVTRRILRK 648
Cdd:cd05915 457 VVVPRGEKPTPEELN----EHLLKAGFAKWqLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
123-648 |
1.37e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 84.62 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 123 DTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVL 202
Cdd:PRK12316 4573 DEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALL 4652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 203 VTADGVfrgakpiglksiadaaavlasqedvkveaiimvehLKRVTKPDGVELPKVDYTDITVIYDSEmlkcagvdSPVE 282
Cdd:PRK12316 4653 LTQSHL-----------------------------------LQRLPIPDGLASLALDRDEDWEGFPAH--------DPAV 4689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 283 WMDSEDPLFILYTSGSTGKPKGIQ--------HTTAgyMTYAYATT---------KYTFDAQEDDVYWctadcGWITGHS 345
Cdd:PRK12316 4690 RLHPDNLAYVIYTSGSTGRPKGVAvshgslvnHLHA--TGERYELTpddrvlqfmSFSFDGSHEGLYH-----PLINGAS 4762
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 346 YLLYGPlmnglkGIWyegvptypTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSrktLKVIGTVGEPINPAA 425
Cdd:PRK12316 4763 VVIRDD------SLW--------DPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPS---LRVYCFGGEAVAQAS 4825
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 426 WMWLYKQvgLSNVSIVDTYWQTETGgHMITCLPGATPMKPGAAAMP----FFGASPVLLDAEGRVIEGPGEGSLCFdrAW 501
Cdd:PRK12316 4826 YDLAWRA--LKPVYLFNGYGPTETT-VTVLLWKARDGDACGAAYMPigtpLGNRSGYVLDGQLNPLPVGVAGELYL--GG 4900
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 502 PGMMRGIYG----DEQRFVKT-YLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEA 576
Cdd:PRK12316 4901 EGVARGYLErpalTAERFVPDpFGAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREA 4980
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71982997 577 AVVAAPHDIkGSFPYAFVT-----LNVGERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRK 648
Cdd:PRK12316 4981 VVIAQEGAV-GKQLVGYVVpqdpaLADADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQ 5056
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
108-659 |
2.63e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 82.30 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 108 YGNKIAYIFEGNEptdtstWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSA 187
Cdd:PRK08162 31 YPDRPAVIHGDRR------RTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 188 ESLAARVVDARCRVLVTaDGVFrgakpiglKSIADAAAVLASQEDVKVEAIIMVEHlkrvtkPDGVELPKVDYTDITviy 267
Cdd:PRK08162 105 ASIAFMLRHGEAKVLIV-DTEF--------AEVAREALALLPGPKPLVIDVDDPEY------PGGRFIGALDYEAFL--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 268 dsemlkcAGVDSPVEWM---DSEDPLFILYTSGSTGKPKGI--QHTTAGYMTYAYATTkytfdaqeddvywctadcgWIT 342
Cdd:PRK08162 167 -------ASGDPDFAWTlpaDEWDAIALNYTSGTTGNPKGVvyHHRGAYLNALSNILA-------------------WGM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 343 GH--SYLLYGPLM--NGlkgiWyegvpTYP----------------TPSRMWDVTDKYGVTKLYTSPTAARALMALGNQW 402
Cdd:PRK08162 221 PKhpVYLWTLPMFhcNG----W-----CFPwtvaaragtnvclrkvDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEW 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 403 LESSSRKtlkVIGTVGEPINPAAWMWLYKQVGLSnvsIVDTYWQTETGGHMITC--------LPGAT------------P 462
Cdd:PRK08162 292 RAGIDHP---VHAMVAGAAPPAAVIAKMEEIGFD---LTHVYGLTETYGPATVCawqpewdaLPLDEraqlkarqgvryP 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 463 MKPGAAAMPFFGASPVllDAEGRVIegpGE----GSLCfdrawpgmMRGIYGDEQrfvKTYLAPFNGYYFTGDGARRDED 538
Cdd:PRK08162 366 LQEGVTVLDPDTMQPV--PADGETI---GEimfrGNIV--------MKGYLKNPK---ATEEAFAGGWFHTGDLAVLHPD 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 539 GYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEklvAELKKLVREKI 618
Cdd:PRK08162 430 GYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATE---EEIIAHCREHL 506
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 71982997 619 GALAVPDVIQEAPgLPKTRSGKVTRRILRKIAeGSESGIGD 659
Cdd:PRK08162 507 AGFKVPKAVVFGE-LPKTSTGKIQKFVLREQA-KSLKAIDL 545
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
128-644 |
3.50e-16 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 81.86 E-value: 3.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 128 TYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCR-VLVTAD 206
Cdd:PRK05852 45 SYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARvVLIDAD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 207 GVFRGAK------PIGLKSIADAAAVLASqedVKVEAIIMVEHLKRVTKPDGVElpkvdytditviydsemlkcagvdsp 280
Cdd:PRK05852 125 GPHDRAEpttrwwPLTVNVGGDSGPSGGT---LSVHLDAATEPTPATSTPEGLR-------------------------- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 281 vewmdsEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYA-TTKYTFDAQEDDVywctADCGWITGHSylLYGPLMNGLKGi 359
Cdd:PRK05852 176 ------PDDAMIMFTGGTTGLPKMVPWTHANIASSVRAiITGYRLSPRDATV----AVMPLYHGHG--LIAALLATLAS- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 360 wyEGVPTYPTPSRM-----WDVTDKYGVTKLYTSPTAARALMALGNQWLESSSRKTLKVIGTVGEPINPAAWMWLYKQVG 434
Cdd:PRK05852 243 --GGAVLLPARGRFsahtfWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 435 lsnVSIVDTYWQTETgGHMITclpgaTPMKPGAAAMPFFGASPVLLDAEGRV---IEGPGEGSLCFD---RAW---PGMM 505
Cdd:PRK05852 321 ---APVVCAFGMTEA-THQVT-----TTQIEGIGQTENPVVSTGLVGRSTGAqirIVGSDGLPLPAGavgEVWlrgTTVV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 506 RGIYGDEQrfvKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDI 585
Cdd:PRK05852 392 RGYLGDPT---ITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQL 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 71982997 586 KGSFPYAFVtlnVGERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRR 644
Cdd:PRK05852 469 YGEAVAAVI---VPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
288-655 |
7.24e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 80.98 E-value: 7.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 288 DPLFILYTSGSTGKPKGIQHTTAGYMTyAYATTKYTFDAQEDDVYWctadcgwITG---HSYLLYGPLMNGLKGIWYEGV 364
Cdd:PRK07638 144 APFYMGFTSGSTGKPKAFLRAQQSWLH-SFDCNVHDFHMKREDSVL-------IAGtlvHSLFLYGAISTLYVGQTVHLM 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 365 PTYpTPSRMWDVTDKYGVTKLYTSPTAARALMAL-------------GNQWlESSSRKTLKVIgtvgepiNPAAWmwLYK 431
Cdd:PRK07638 216 RKF-IPNQVLDKLETENISVMYTVPTMLESLYKEnrvienkmkiissGAKW-EAEAKEKIKNI-------FPYAK--LYE 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 432 QVGLSNVSIVdTYWQTETgghmitclpgaTPMKPGAAAMPFFGASPVLLDAEGRVIEgPGEGSLCFDRAwPGMMRGIYGD 511
Cdd:PRK07638 285 FYGASELSFV-TALVDEE-----------SERRPNSVGRPFHNVQVRICNEAGEEVQ-KGEIGTVYVKS-PQFFMGYIIG 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 512 EqrfVKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPY 591
Cdd:PRK07638 351 G---VLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPV 427
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71982997 592 AFVTLNVGERineklvaELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRKIAEGSES 655
Cdd:PRK07638 428 AIIKGSATKQ-------QLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQEK 484
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
100-335 |
2.01e-15 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 79.92 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 100 LERNIKRgYGNKIAYIFEGneptdtSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHS 179
Cdd:PRK08279 43 FEEAAAR-HPDRPALLFED------QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 180 VVFAGFSAESLA--ARVVDArcRVLVTADgvfrgakpiglksiADAAAVLASQEDVKVEAIIMVEHLKRVTKPDGVElpk 257
Cdd:PRK08279 116 LLNTQQRGAVLAhsLNLVDA--KHLIVGE--------------ELVEAFEEARADLARPPRLWVAGGDTLDDPEGYE--- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 258 vdytditvIYDSEMLKCAGVDSPV-EWMDSEDPLFILYTSGSTGKPKgiqhttAGYMTYAYATTKY-----TFDAQEDDV 331
Cdd:PRK08279 177 --------DLAAAAAGAPTTNPASrSGVTAKDTAFYIYTSGTTGLPK------AAVMSHMRWLKAMggfggLLRLTPDDV 242
|
....
gi 71982997 332 YWCT 335
Cdd:PRK08279 243 LYCC 246
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
126-646 |
2.15e-15 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 80.47 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 126 TWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTA 205
Cdd:PRK10252 483 QFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITT 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 206 DGVF-RGAKPIGLKSIADAAAVLASQedvkveaiimvehlkrvTKPDGVELPkvdytditviydsemlkcagvdspvewm 284
Cdd:PRK10252 563 ADQLpRFADVPDLTSLCYNAPLAPQG-----------------AAPLQLSQP---------------------------- 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 285 dsEDPLFILYTSGSTGKPKG--IQHTTAG----YMTYAYATTkytfdaqEDDVYW----CTADCG-WitghsyLLYGPLM 353
Cdd:PRK10252 598 --HHTAYIIFTSGSTGRPKGvmVGQTAIVnrllWMQNHYPLT-------ADDVVLqktpCSFDVSvW------EFFWPFI 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 354 NGLKGIWYEgvP-TYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSRKTLKVIGTVGEPInPAA----WMW 428
Cdd:PRK10252 663 AGAKLVMAE--PeAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVFCSGEAL-PADlcreWQQ 739
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 429 LYkQVGLSNV-----SIVD-TYWqtETGGHMITCLPGAT-PMkpgaaAMPFFGASPVLLDAEGRVIEgPG-EGSLCFdrA 500
Cdd:PRK10252 740 LT-GAPLHNLygpteAAVDvSWY--PAFGEELAAVRGSSvPI-----GYPVWNTGLRILDARMRPVP-PGvAGDLYL--T 808
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 501 WPGMMRGIYG----DEQRFVKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESAL--------- 567
Cdd:PRK10252 809 GIQLAQGYLGrpdlTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMqalpdveqa 888
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71982997 568 VAHEkvaEAAVVAAPHDIKGSFPYAFVTLNVGERINeklVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRIL 646
Cdd:PRK10252 889 VTHA---CVINQAAATGGDARQLVGYLVSQSGLPLD---TSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
287-646 |
2.94e-15 |
|
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: 78.63 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 287 EDPLFILYTSGSTGKPKG--IQHT-----TAGYMTYAYATTK--------YTFDAQEDDVYWCtadcgWITGHSYLLYGP 351
Cdd:cd17644 106 ENLAYVIYTSGSTGKPKGvmIEHQslvnlSHGLIKEYGITSSdrvlqfasIAFDVAAEEIYVT-----LLSGATLVLRPE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 352 LMnglkgiwyegvptYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSrKTLKVIGTVGEPINPAAWMWLYK 431
Cdd:cd17644 181 EM-------------RSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLP-SSLRLVIVGGEAVQPELVRQWQK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 432 QVGlSNVSIVDTYWQTE----TGGHMITCLPGATPMKPgAAAMPFFGASPVLLDAEGRV--IEGPGEGSLCfdraWPGMM 505
Cdd:cd17644 247 NVG-NFIQLINVYGPTEatiaATVCRLTQLTERNITSV-PIGRPIANTQVYILDENLQPvpVGVPGELHIG----GVGLA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 506 RGIYG-DE---QRFVKTYLA--PFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHE--KVAEAA 577
Cdd:cd17644 321 RGYLNrPEltaEKFISHPFNssESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNdvKTAVVI 400
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71982997 578 VVAAPHDIKGSFPYAfvtlnVGERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRIL 646
Cdd:cd17644 401 VREDQPGNKRLVAYI-----VPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
128-570 |
6.73e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 79.05 E-value: 6.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 128 TYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTAdg 207
Cdd:PRK12467 1601 TYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQ-- 1678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 208 vfrgakpiglksiadaAAVLAsqedvkveaiimvehlkRVTKPDGVELPKVDYTDitviydsEMLKCAGVDSPVEWMDSE 287
Cdd:PRK12467 1679 ----------------SHLQA-----------------RLPLPDGLRSLVLDQED-------DWLEGYSDSNPAVNLAPQ 1718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 288 DPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTK-YTFDAqeddvywctADCgWITGHSYL-------LYGPLMNGLK-- 357
Cdd:PRK12467 1719 NLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEaYQLSA---------ADV-VLQFTSFAfdvsvweLFWPLINGARlv 1788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 358 ----GIWYEgvptyptPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSrktLKVIGTVGEPINPAA---WMWLY 430
Cdd:PRK12467 1789 iappGAHRD-------PEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLS---LRRVVCGGEALEVEAlrpWLERL 1858
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 431 KQVGLSNV-----SIVD-TYW----QTETGGhmiTCLPGATPMKpgaaampffGASPVLLDAE-----GRVIegpGEGSL 495
Cdd:PRK12467 1859 PDTGLFNLygpteTAVDvTHWtcrrKDLEGR---DSVPIGQPIA---------NLSTYILDASlnpvpIGVA---GELYL 1923
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 496 CFDrawpGMMRGIYG----DEQRFVKTylaPFNGY----YFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESAL 567
Cdd:PRK12467 1924 GGV----GLARGYLNrpalTAERFVAD---PFGTVgsrlYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARL 1996
|
...
gi 71982997 568 VAH 570
Cdd:PRK12467 1997 REQ 1999
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
285-572 |
7.46e-15 |
|
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: 77.89 E-value: 7.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 285 DSEDPLFILYTSGSTGKPKGIQHTTAGYmTYAYATTKYTFDAQEDDVYWCTADCGWITGHSYLLYGPLMNGLKGIWYEGV 364
Cdd:cd05932 135 FPEQLATLIYTSGTTGQPKGVMLTFGSF-AWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 365 PTYPT------PS------RMW-----DVTDKYGVTKL--------YTSPTAARALMALG-NQwlesssrktLKVIGTVG 418
Cdd:cd05932 214 DTFVEdvqrarPTlffsvpRLWtkfqqGVQDKIPQQKLnlllkipvVNSLVKRKVLKGLGlDQ---------CRLAGCGS 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 419 EPINPAAWMWlYKQVGLSnvsIVDTYWQTETGGHMITCLPGATpmKPGAAAMPFFGASpVLLDAEGRVIEGPgegslcfd 498
Cdd:cd05932 285 APVPPALLEW-YRSLGLN---ILEAYGMTENFAYSHLNYPGRD--KIGTVGNAGPGVE-VRISEDGEILVRS-------- 349
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71982997 499 rawPGMMRGIYGDEQRFVKTYLApfNGYYFTGDGARRDEDGYLWITGRVDDLMNVS-GHLLSTAEIESALVAHEK 572
Cdd:cd05932 350 ---PALMMGYYKDPEATAEAFTA--DGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDR 419
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
123-649 |
2.62e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 76.12 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 123 DTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALylpmipeLA-------VAMLACARIGAMHSVVFAGFSAESLAArvV 195
Cdd:PRK07788 71 ERGTLTYAELDEQSNALARGLLALGVRAGDGVAV-------LArnhrgfvLALYAAGKVGARIILLNTGFSGPQLAE--V 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 196 DARCRV-LVTADGVFrgakpiglksiadAAAVLASQEDV-KVEAIIMvehlkrvtKPDGVELPkvDYTDITViydsemlk 273
Cdd:PRK07788 142 AAREGVkALVYDDEF-------------TDLLSALPPDLgRLRAWGG--------NPDDDEPS--GSTDETL-------- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 274 cagvDSPVEWMDSEdPL--------FILYTSGSTGKPKGIQH-TTAGYMTYAYATTKYTFDAQEddVYWCTADCGWITGH 344
Cdd:PRK07788 191 ----DDLIAGSSTA-PLpkppkpggIVILTSGTTGTPKGAPRpEPSPLAPLAGLLSRVPFRAGE--TTLLPAPMFHATGW 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 345 SYLLYGpLMNGLKGIwyegVPTYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSRKTLKVIGTVGEPINPa 424
Cdd:PRK07788 264 AHLTLA-MALGSTVV----LRRRFDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSP- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 425 awmWLYKQV----G--LSNVsivdtYWQTETGGHMItclpgATP----MKPGAAAMPFFGASPVLLDAEGRVIEgPGEGS 494
Cdd:PRK07788 338 ---ELATRAleafGpvLYNL-----YGSTEVAFATI-----ATPedlaEAPGTVGRPPKGVTVKILDENGNEVP-RGVVG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 495 LCFDRAwpGM-MRGiY---GDEQRfvktylapFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAH 570
Cdd:PRK07788 404 RIFVGN--GFpFEG-YtdgRDKQI--------IDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGH 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 571 EKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEKlvaELKKLVREKIGALAVP-DVI--QEapgLPKTRSGKVTRRILR 647
Cdd:PRK07788 473 PDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDED---AIKDYVRDNLARYKVPrDVVflDE---LPRNPTGKVLKRELR 546
|
..
gi 71982997 648 KI 649
Cdd:PRK07788 547 EM 548
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
106-646 |
3.11e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 77.13 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 106 RGYGNKIAYIFEGneptdtSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGF 185
Cdd:PRK05691 1142 RQTPERIALVWDG------GSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDY 1215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 186 SAESLAARVVDARCRVLVTADGVfrgakpiglksiadaaavlasqedvkveaiimvehLKRVTKPDGVelpkvdytdITV 265
Cdd:PRK05691 1216 PAERLAYMLADSGVELLLTQSHL-----------------------------------LERLPQAEGV---------SAI 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 266 IYDSEMLKCAGVDSPVEWMDSEDPLFILYTSGSTGKPKGIQHTTAGyMTYAYATTKYTFDAQEDDVYWCTA--------- 336
Cdd:PRK05691 1252 ALDSLHLDSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAA-LAERLQWMQATYALDDSDVLMQKApisfdvsvw 1330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 337 DCGW--ITGHSYLLYGPlmnglkgiwyegvPTYPTPSRMWDVTDKYGVTKLYTSPtaarALMALGNQWLESSSRKTLKVI 414
Cdd:PRK05691 1331 ECFWplITGCRLVLAGP-------------GEHRDPQRIAELVQQYGVTTLHFVP----PLLQLFIDEPLAAACTSLRRL 1393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 415 GTVGEPINPA---------AWMWLYKQVGLSNVSIVDTYWQtetgghmitCLPGATPMKPgaAAMPFFGASPVLLDAEGR 485
Cdd:PRK05691 1394 FSGGEALPAElrnrvlqrlPQVQLHNRYGPTETAINVTHWQ---------CQAEDGERSP--IGRPLGNVLCRVLDAELN 1462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 486 VIEGPGEGSLCFDRAwpGMMRGIYG----DEQRFVKTYLA-PFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLST 560
Cdd:PRK05691 1463 LLPPGVAGELCIGGA--GLARGYLGrpalTAERFVPDPLGeDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEP 1540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 561 AEIESALVAHEKVAEAAVVAApHDIKGSFPYAFVTLNVGErinEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGK 640
Cdd:PRK05691 1541 EEIQARLLAQPGVAQAAVLVR-EGAAGAQLVGYYTGEAGQ---EAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGK 1616
|
....*.
gi 71982997 641 VTRRIL 646
Cdd:PRK05691 1617 LDRRAL 1622
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
126-647 |
4.64e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 75.05 E-value: 4.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 126 TWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTA 205
Cdd:PRK13390 24 QVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVAS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 206 ---DGVfrgakpiglksIADAAAvlasqedvkveaiimvehlkrvtkPDGVELPKVDYTDITVIYDSEMlkcAGVDSPVe 282
Cdd:PRK13390 104 aalDGL-----------AAKVGA------------------------DLPLRLSFGGEIDGFGSFEAAL---AGAGPRL- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 283 wmdSEDPL--FILYTSGSTGKPKGIQHTTAGYMTYA-----YATTKYTFDAQEDDVYWCTADcgwITGHSYLLYGPLMNG 355
Cdd:PRK13390 145 ---TEQPCgaVMLYSSGTTGFPKGIQPDLPGRDVDApgdpiVAIARAFYDISESDIYYSSAP---IYHAAPLRWCSMVHA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 356 LKGIwyegvptyPTPSRMWDVTD------KYGVTKLYTSPTAARALMALGNQWLESSSRKTLKVIGTVGEP----INPAA 425
Cdd:PRK13390 219 LGGT--------VVLAKRFDAQAtlghveRYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVIHAAAPcpvdVKHAM 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 426 WMWLykqvglsNVSIVDTYWQTETGGhMITCLPGATPMKPGAAAMPFFGASPVLlDAEGRVIEGPGEGSLCFDR-AWPgm 504
Cdd:PRK13390 291 IDWL-------GPIVYEYYSSTEAHG-MTFIDSPDWLAHPGSVGRSVLGDLHIC-DDDGNELPAGRIGTVYFERdRLP-- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 505 MRGIYGDEQRFVKTYLA-PFngYYFTGDGARRDEDGYLWITGRvDDLMNVSGHL-LSTAEIESALVAHEKVAEAAVVAAP 582
Cdd:PRK13390 360 FRYLNDPEKTAAAQHPAhPF--WTTVGDLGSVDEDGYLYLADR-KSFMIISGGVnIYPQETENALTMHPAVHDVAVIGVP 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71982997 583 HDIKGSFPYAFVTLNVGERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILR 647
Cdd:PRK13390 437 DPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
292-647 |
5.24e-14 |
|
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: 74.72 E-value: 5.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 292 ILYTSGSTGKPKGI-QHTTAGymtyayattkyTFDAqeDDVYWCTADCGWITGHSYLLYGPL---------MNGLK-GIW 360
Cdd:cd05929 130 MLYSGGTTGRPKGIkRGLPGG-----------PPDN--DTLMAAALGFGPGADSVYLSPAPLyhaapfrwsMTALFmGGT 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 361 YEGVPTYpTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSRKTLKVIGTVGEPINPA---AWMWLYKQVglsn 437
Cdd:cd05929 197 LVLMEKF-DPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPCPPWvkeQWIDWGGPI---- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 438 vsIVDTYWQTETGGhmITCLPGATPMK-PGAAAMPFFGASPVLlDAEGRVIEgPGEgslcfdrawPG--MMRGIYGDE-- 512
Cdd:cd05929 272 --IWEYYGGTEGQG--LTIINGEEWLThPGSVGRAVLGKVHIL-DEDGNEVP-PGE---------IGevYFANGPGFEyt 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 513 QRFVKTYLAPFNGYYFT-GDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPY 591
Cdd:cd05929 337 NDPEKTAAARNEGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVH 416
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 71982997 592 AFVTLNVGERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILR 647
Cdd:cd05929 417 AVVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
438-652 |
5.76e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 75.10 E-value: 5.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 438 VSIVDTYWQTEtGGHMITCLPGaTPmkPGAAAMPFFGASpvLLDAEGRVIEGPGE----GSLCFDRA--------WPGMM 505
Cdd:PRK07867 291 CVVVDGFGSTE-GGVAITRTPD-TP--PGALGPLPPGVA--IVDPDTGTECPPAEdadgRLLNADEAigelvntaGPGGF 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 506 RGIYGDEQ----RFVktylapfNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAA 581
Cdd:PRK07867 365 EGYYNDPEadaeRMR-------GGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAV 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71982997 582 PHDIKGSFPYAFVTLNVG-----ERINEKLVAelkklvREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRkiAEG 652
Cdd:PRK07867 438 PDPVVGDQVMAALVLAPGakfdpDAFAEFLAA------QPDLGPKQWPSYVRVCAELPRTATFKVLKRQLS--AEG 505
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
108-648 |
1.16e-13 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 74.25 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 108 YGNKIAYIfegnEPTDTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLAcarigamhsvvfagfsa 187
Cdd:PLN02330 41 YADKVAFV----EAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALG----------------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 188 eslaarvvdarcrvLVTADGVFRGAKPIGLKSIADAAAVLASqedvkveAIIMVEHLKRVTKPDGVELPKV---DYTDIT 264
Cdd:PLN02330 100 --------------IMAAGGVFSGANPTALESEIKKQAEAAG-------AKLIVTNDTNYGKVKGLGLPVIvlgEEKIEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 265 VIYDSEMLKCA---GVDSPVEWMDSEDPLFILYTSGSTGKPKGIQHTTAGYMtyayATTKYTFDAQEDDVYWCTADCGWI 341
Cdd:PLN02330 159 AVNWKELLEAAdraGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLV----ANLCSSLFSVGPEMIGQVVTLGLI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 342 TG-HSYllygplmnGLKGIWYEGVPTYPTPSRMWDVTDKYGVTKLYT-----SPTAARALMAL-GNQWLESS--SRKTLK 412
Cdd:PLN02330 235 PFfHIY--------GITGICCATLRNKGKVVVMSRFELRTFLNALITqevsfAPIVPPIILNLvKNPIVEEFdlSKLKLQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 413 VIGTVGEPINPAAWMWLYKQvgLSNVSIVDTYWQTEtggHMITCLPGATPMK-PGAAAMPFFGAspVLLDAEGRVIEgPG 491
Cdd:PLN02330 307 AIMTAAAPLAPELLTAFEAK--FPGVQVQEAYGLTE---HSCITLTHGDPEKgHGIAKKNSVGF--ILPNLEVKFID-PD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 492 EGsLCFDRAWPG--------MMRGIYGDEQRFVKTYLApfNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEI 563
Cdd:PLN02330 379 TG-RSLPKNTPGelcvrsqcVMQGYYNNKEETDRTIDE--DGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAEL 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 564 ESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEKlvaELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTR 643
Cdd:PLN02330 456 EAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEE---DILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMR 532
|
....*
gi 71982997 644 RILRK 648
Cdd:PLN02330 533 RLLKE 537
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
40-99 |
1.26e-13 |
|
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many acetyl-coenzyme A synthetase enzymes.
Pssm-ID: 465043 [Multi-domain] Cd Length: 55 Bit Score: 65.57 E-value: 1.26e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 40 YHDLYRSSINDADEFWRTVSSELHFEQGTSKGLEWNFDskagnVFVKFMDGAKTNISYNC 99
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKELDWFKPFDKVLDGSNG-----PFAKWFVGGKLNVCYNC 55
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
126-647 |
1.69e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 73.64 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 126 TWTYNELHAQVVQFSAVLRSH-GVKRGDVVALYLPMIPELAVAMLACARIGAMhsVVFAG--FSAESLAARVVDARCRVL 202
Cdd:PRK05677 49 TLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLI--VVNTNplYTAREMEHQFNDSGAKAL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 203 VT----ADGVFRGAKPIGLKS--IADAAAVLASQEDVKVEAIImvEHLKRVTKPdgVELPK-VDYTDITviydsemlkCA 275
Cdd:PRK05677 127 VClanmAHLAEKVLPKTGVKHviVTEVADMLPPLKRLLINAVV--KHVKKMVPA--YHLPQaVKFNDAL---------AK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 276 GVDSPVEWMD--SEDPLFILYTSGSTGKPKGIQHTTAGyMTYAYATTKYTFDAQEDD-------------VYWCTADCGW 340
Cdd:PRK05677 194 GAGQPVTEANpqADDVAVLQYTGGTTGVAKGAMLTHRN-LVANMLQCRALMGSNLNEgceiliaplplyhIYAFTFHCMA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 341 ---ITGHSYLLYGPlmnglkgiwyEGVPTYPTPSRMWDVTDKYGVTKLYtsptaaralMALGN----QWLESSSrktLKV 413
Cdd:PRK05677 273 mmlIGNHNILISNP----------RDLPAMVKELGKWKFSGFVGLNTLF---------VALCNneafRKLDFSA---LKL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 414 IGTVGEPINPA-AWMWlyKQVglSNVSIVDTYWQTETGGhmITCLPGATPMKPGAAAMPFFGASPVLLDAEGRviEGP-G 491
Cdd:PRK05677 331 TLSGGMALQLAtAERW--KEV--TGCAICEGYGMTETSP--VVSVNPSQAIQVGTIGIPVPSTLCKVIDDDGN--ELPlG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 492 E-GSLCFDRawPGMMRGIYGDEQRFVKTYLApfNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAH 570
Cdd:PRK05677 403 EvGELCVKG--PQVMKGYWQRPEATDEILDS--DGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAAL 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71982997 571 EKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEKlvaELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILR 647
Cdd:PRK05677 479 PGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKE---QVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
292-643 |
1.86e-13 |
|
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: 72.15 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 292 ILYTSGSTGKPKGIqhttagymTYAYATTKYTFDAqeddvyWCtaDCGWIT-GHSYLLYGPLMN--GLKGIWYEGVPTYP 368
Cdd:cd17638 5 IMFTSGTTGRSKGV--------MCAHRQTLRAAAA------WA--DCADLTeDDRYLIINPFFHtfGYKAGIVACLLTGA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 369 T--PSRMWDV------TDKYGVTKLYTSPTAARALmaLGNQWLESSSRKTLKVIGTVGEPINPAAWMWLYKQVGLSNVsi 440
Cdd:cd17638 69 TvvPVAVFDVdaileaIERERITVLPGPPTLFQSL--LDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETV-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 441 VDTYWQTETGGhmitclpgATPMKPGAAAMPFFGASPVLLDAEGRVIEGPGEGSLcfdRAwPGMMRGIYGDEQRFVKTYL 520
Cdd:cd17638 145 LTAYGLTEAGV--------ATMCRPGDDAETVATTCGRACPGFEVRIADDGEVLV---RG-YNVMQGYLDDPEATAEAID 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 521 ApfNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGE 600
Cdd:cd17638 213 A--DGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGV 290
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 71982997 601 RINEklvAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTR 643
Cdd:cd17638 291 TLTE---EDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
524-651 |
3.25e-13 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 72.57 E-value: 3.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 524 NGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVG-ERI 602
Cdd:PLN02479 429 NGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGvDKS 508
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 71982997 603 NE-KLVAELKKLVREKIGALAVPDVIQEAPgLPKTRSGKVTRRILRKIAE 651
Cdd:PLN02479 509 DEaALAEDIMKFCRERLPAYWVPKSVVFGP-LPKTATGKIQKHVLRAKAK 557
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
126-650 |
6.02e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 71.78 E-value: 6.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 126 TWTYNELHAQVVQFSAVLRSH-GVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVT 204
Cdd:PRK12492 49 TLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVY 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 205 ADgVFrGAKpiglksiadAAAVLAsqeDVKVEAII------------------MVEHLKRVTkPDgVELPKvdytdiTVI 266
Cdd:PRK12492 129 LN-MF-GKL---------VQEVLP---DTGIEYLIeakmgdllpaakgwlvntVVDKVKKMV-PA-YHLPQ------AVP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 267 YDSEMLKCAGVDSPVEWMDSEDPLFILYTSGSTGKPKGIQHTTAGY---MTYAYATTKYT--------FDAQE------- 328
Cdd:PRK12492 187 FKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLvanMLQVRACLSQLgpdgqplmKEGQEvmiaplp 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 329 -DDVYWCTADCG--WITG-HSYLLYGPlmnglkgiwyEGVPTYPTPSRMWDVTDKYGVTKLYTsptaarALMAlgNQWLE 404
Cdd:PRK12492 267 lYHIYAFTANCMcmMVSGnHNVLITNP----------RDIPGFIKELGKWRFSALLGLNTLFV------ALMD--HPGFK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 405 SSSRKTLKVIGTVGEPINPA-AWMWlykqVGLSNVSIVDTYWQTETGGhMITCLPGATPMKPGAAAMPFFGASPVLLDAE 483
Cdd:PRK12492 329 DLDFSALKLTNSGGTALVKAtAERW----EQLTGCTIVEGYGLTETSP-VASTNPYGELARLGTVGIPVPGTALKVIDDD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 484 GrvIEGP-GE-GSLCFDRawPGMMRGIYGDEQRFVKTYLApfNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTA 561
Cdd:PRK12492 404 G--NELPlGErGELCIKG--PQVMKGYWQQPEATAEALDA--EGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPN 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 562 EIESALVAHEKVAEAAVVAAPHDIKGSfpyaFVTLNVGERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKV 641
Cdd:PRK12492 478 EIEDVVMAHPKVANCAAIGVPDERSGE----AVKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKI 553
|
....*....
gi 71982997 642 TRRILRKIA 650
Cdd:PRK12492 554 LRRELRDIA 562
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
286-640 |
1.00e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 70.10 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 286 SEDPLFILYTSGSTGKPKGI---QH-------TTAGYMTYAYATTKYTFDAQEDDvywctadcgwiTGHSYLLYGPLMNG 355
Cdd:cd05924 2 SADDLYILYTGGTTGMPKGVmwrQEdifrmlmGGADFGTGEFTPSEDAHKAAAAA-----------AGTVMFPAPPLMHG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 356 lKGIW-YEGVPTYPT----------PSRMWDVTDKYGVTKLYTSPTA-AR----ALMALGNQWLESssrktLKVIGTVGE 419
Cdd:cd05924 71 -TGSWtAFGGLLGGQtvvlpddrfdPEEVWRTIEKHKVTSMTIVGDAmARplidALRDAGPYDLSS-----LFAISSGGA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 420 PINPAAWMWLykQVGLSNVSIVDTYWQTETGGHMITClpgATPMKPGAAAMPFFGASPVLLDAEGRVIEGPGEGslcfdR 499
Cdd:cd05924 145 LLSPEVKQGL--LELVPNITLVDAFGSSETGFTGSGH---SAGSGPETGPFTRANPDTVVLDDDGRVVPPGSGG-----V 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 500 AWPG----MMRGIYGDEQRFVKTYLApFNG--YYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKV 573
Cdd:cd05924 215 GWIArrghIPLGYYGDEAKTAETFPE-VDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAV 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71982997 574 AEAAVVAAPHDIKGSFPYAFVTLNVGERINEklvAELKKLVREKIGALAVPDVIQEAPGLPKTRSGK 640
Cdd:cd05924 294 YDVLVVGRPDERWGQEVVAVVQLREGAGVDL---EELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
126-650 |
1.43e-12 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 70.68 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 126 TWTYNELHAQVVQFSAVLRSH-GVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVT 204
Cdd:PRK08751 50 TITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 205 ADGVFRGAKPIglksIADA------AAVLASQEDVKVEAII--MVEHLKRVTKpdgvelpkvDYTDITVIYDSEMLKCAG 276
Cdd:PRK08751 130 IDNFGTTVQQV----IADTpvkqviTTGLGDMLGFPKAALVnfVVKYVKKLVP---------EYRINGAIRFREALALGR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 277 VDS-PVEWMDSEDPLFILYTSGSTGKPKGiqhttagymtyAYATTKYTFDAQEDDVYWCTADCGWITGHS--------YL 347
Cdd:PRK08751 197 KHSmPTLQIEPDDIAFLQYTGGTTGVAKG-----------AMLTHRNLVANMQQAHQWLAGTGKLEEGCEvvitalplYH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 348 LYGPLMNGLKGIWYEG----------VPTYPTPSRMWDVTDKYGVTKLYTSptaarALMALGNQWLESSSrktLKVIGTV 417
Cdd:PRK08751 266 IFALTANGLVFMKIGGcnhlisnprdMPGFVKELKKTRFTAFTGVNTLFNG-----LLNTPGFDQIDFSS---LKMTLGG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 418 GEPINPA-AWMWlyKQVglSNVSIVDTYWQTETGghmitclPGA--TPMK----PGAAAMPFFGASPVLLDAEGRVIEGP 490
Cdd:PRK08751 338 GMAVQRSvAERW--KQV--TGLTLVEAYGLTETS-------PAAciNPLTlkeyNGSIGLPIPSTDACIKDDAGTVLAIG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 491 GEGSLCFDRawPGMMRGIYGDEQRFVKTYLApfNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAH 570
Cdd:PRK08751 407 EIGELCIKG--PQVMKGYWKRPEETAKVMDA--DGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMM 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 571 EKVAEAAVVAAPHDIKGSFPYAFVTlnvgeRINEKLVAE-LKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRKI 649
Cdd:PRK08751 483 PGVLEVAAVGVPDEKSGEIVKVVIV-----KKDPALTAEdVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDA 557
|
.
gi 71982997 650 A 650
Cdd:PRK08751 558 A 558
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
434-647 |
1.51e-12 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 70.47 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 434 GLSNVSIVDTYWQTETGGHMITCLpGATPMKPGAAAMPF----FGAS---PV------LLDAEGRVIEgPGEGSLCFDRA 500
Cdd:PRK08974 334 GMAVQQAVAERWVKLTGQYLLEGY-GLTECSPLVSVNPYdldyYSGSiglPVpsteikLVDDDGNEVP-PGEPGELWVKG 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 501 wPGMMRGIYgdeQRFVKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVA 580
Cdd:PRK08974 412 -PQVMLGYW---QRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVG 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71982997 581 APHDIKGSFPYAFVTlnvgeRINEKLVA-ELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILR 647
Cdd:PRK08974 488 VPSEVSGEAVKIFVV-----KKDPSLTEeELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
122-655 |
3.06e-12 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 69.49 E-value: 3.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 122 TDTST---WTYNELHAQVVQFSAVLRSH-GVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDA 197
Cdd:PLN02574 59 IDSSTgfsISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDC 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 198 RCRVLVTADGVFRGAKPIGLKSIADAAAVlaSQEDVKVEAIIMVEHLKrvTKPDGVELPKVDYTDITVIydsemlkcagv 277
Cdd:PLN02574 139 SVGLAFTSPENVEKLSPLGVPVIGVPENY--DFDSKRIEFPKFYELIK--EDFDFVPKPVIKQDDVAAI----------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 278 dspvewmdsedplfiLYTSGSTGKPKGIQHTTAGYMtyAYATTKYTFDAQE------DDVYWCTADCGWITGHSYLLYGP 351
Cdd:PLN02574 204 ---------------MYSSGTTGASKGVVLTHRNLI--AMVELFVRFEASQyeypgsDNVYLAALPMFHIYGLSLFVVGL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 352 LMNGLKGIwyegVPTYPTPSRMWDVTDKYGVTKLytsPTAARALMAL--GNQWLESSSRKTLKVIGTVGEPINpAAWMWL 429
Cdd:PLN02574 267 LSLGSTIV----VMRRFDASDMVKVIDRFKVTHF---PVVPPILMALtkKAKGVCGEVLKSLKQVSCGAAPLS-GKFIQD 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 430 YKQVgLSNVSIVDTYWQTETGGHMITCLPGATPMKPGAAAM--PFFGASPVLLDAeGRVIEGPGEGSLcfdraW---PGM 504
Cdd:PLN02574 339 FVQT-LPHVDFIQGYGMTESTAVGTRGFNTEKLSKYSSVGLlaPNMQAKVVDWST-GCLLPPGNCGEL-----WiqgPGV 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 505 MRGIYGDEQRFVKTYLApfNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHD 584
Cdd:PLN02574 412 MKGYLNNPKATQSTIDK--DGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDK 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71982997 585 IKGSFPYAFV------TLNVGERIN--EKLVAELKKlVREkigalavpdVIQEAPgLPKTRSGKVTRRILRKIAEGSES 655
Cdd:PLN02574 490 ECGEIPVAFVvrrqgsTLSQEAVINyvAKQVAPYKK-VRK---------VVFVQS-IPKSPAGKILRRELKRSLTNSVS 557
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
101-646 |
3.80e-12 |
|
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: 68.74 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 101 ERNIKRgYGNKIAYIFEGNeptdtsTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSV 180
Cdd:cd17645 5 EEQVER-TPDHVAVVDRGQ------SLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 181 VFAGFSAESLAARVVDARCRVLVTadgvfrgakpiglksiadaaavlasqedvkveaiimvehlkrvtkpdgvelpkvdy 260
Cdd:cd17645 78 IDPDYPGERIAYMLADSSAKILLT-------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 261 tditviydsemlkcagvdspvewmDSEDPLFILYTSGSTGKPKGIQ------------HTTAGYMTYAYATTKY---TFD 325
Cdd:cd17645 102 ------------------------NPDDLAYVIYTSGSTGLPKGVMiehhnlvnlcewHRPYFGVTPADKSLVYasfSFD 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 326 AQEDDVYwctadcgwitghSYLLYGPLMNGL-KGIWYEGVptyptpsRMWDVTDKYGVTKLYTSPTAARALMALGNQwle 404
Cdd:cd17645 158 ASAWEIF------------PHLTAGAALHVVpSERRLDLD-------ALNDYFNQEGITISFLPTGAAEQFMQLDNQ--- 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 405 sssrkTLKVIGTVGEPINPAAwmwlykqvgLSNVSIVDTYWQTETgghmiTCLPGATPMKPGAAAMPFFGA---SPVLLD 481
Cdd:cd17645 216 -----SLRVLLTGGDKLKKIE---------RKGYKLVNNYGPTEN-----TVVATSFEIDKPYANIPIGKPidnTRVYIL 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 482 AEGRVIEGPG-EGSLCFdrAWPGMMRGIYGDE----QRFVKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGH 556
Cdd:cd17645 277 DEALQLQPIGvAGELCI--AGEGLARGYLNRPeltaEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGY 354
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 557 LLSTAEIESALVAHEKVAEAAVVAAPHdiKGSFPYAFVTLNVGERINeklVAELKKLVREKIGALAVPDVIQEAPGLPKT 636
Cdd:cd17645 355 RIEPGEIEPFLMNHPLIELAAVLAKED--ADGRKYLVAYVTAPEEIP---HEELREWLKNDLPDYMIPTYFVHLKALPLT 429
|
570
....*....|
gi 71982997 637 RSGKVTRRIL 646
Cdd:cd17645 430 ANGKVDRKAL 439
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
291-646 |
2.12e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 67.89 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 291 FILYTSGSTGKPKGIQHTTAGYMTYAYATTKYtFDAQEDDVYWCTADCGWITGHSYLLYGPLMNGLKGIwyegVPTYPT- 369
Cdd:PRK05691 3873 YVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPY-LALSEADVIAQTASQSFDISVWQFLAAPLFGARVEI----VPNAIAh 3947
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 370 -PSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESssrktLKVIGTVGEPINP---AAWMWLYKQVGLSN-------- 437
Cdd:PRK05691 3948 dPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQALDG-----LRWMLPTGEAMPPelaRQWLQRYPQIGLVNaygpaecs 4022
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 438 --VSIVDTYWQTETGGHmitcLPGATPMKPGAAampffgaspVLLDAEGRVIEGPGEGSLCFdrAWPGMMRGIYGDEQRF 515
Cdd:PRK05691 4023 ddVAFFRVDLASTRGSY----LPIGSPTDNNRL---------YLLDEALELVPLGAVGELCV--AGTGVGRGYVGDPLRT 4087
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 516 VKTYL-----APFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALvaHEKVAEAAVVAAPHD-IKGSF 589
Cdd:PRK05691 4088 ALAFVphpfgAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARL--HEQAEVREAAVAVQEgVNGKH 4165
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 71982997 590 PYAFVTLNVGERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRIL 646
Cdd:PRK05691 4166 LVGYLVPHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
285-652 |
3.27e-11 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 66.87 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 285 DSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKyTFDAQEDDVywctadcgwITG-----HSY----LLYGPLMNG 355
Cdd:PRK08633 780 KPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISD-VFNLRNDDV---------ILSslpffHSFgltvTLWLPLLEG 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 356 LKGIWYegvpTYPTPSRM-WDVTDKYGVTKLYTSPTAARALMAlgNQWLESSSRKTLKVIGTVGEPINPaawmwlykQVG 434
Cdd:PRK08633 850 IKVVYH----PDPTDALGiAKLVAKHRATILLGTPTFLRLYLR--NKKLHPLMFASLRLVVAGAEKLKP--------EVA 915
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 435 LS-----NVSIVDTYWQTETGGhMITC-LPGA--------TPMKPGAAAMPFFGASPVLLDAEGRVIEGPGEgslcfdra 500
Cdd:PRK08633 916 DAfeekfGIRILEGYGATETSP-VASVnLPDVlaadfkrqTGSKEGSVGMPLPGVAVRIVDPETFEELPPGE-------- 986
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 501 wPGM--------MRGIYGDEQR---FVKTYLAPfnGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALva 569
Cdd:PRK08633 987 -DGLiliggpqvMKGYLGDPEKtaeVIKDIDGI--GWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEEL-- 1061
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 570 hekvaeaavvaapHDIKGSFPYAFVTLNV-----GERI------NEKLVAELKKLVRE-KIGALAVPDVIQEAPGLPKTR 637
Cdd:PRK08633 1062 -------------AKALGGEEVVFAVTAVpdekkGEKLvvlhtcGAEDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLG 1128
|
410
....*....|....*
gi 71982997 638 SGKVTRRILRKIAEG 652
Cdd:PRK08633 1129 SGKLDLKGLKELALA 1143
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
124-648 |
3.91e-11 |
|
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: 65.91 E-value: 3.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 124 TSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLV 203
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 204 TadgvfrgakpiglksiadaaavlasqedvkveaiimvEHLKRVTKPDGVELPKVDYTDITviydsemlkcagvdspvew 283
Cdd:cd05939 81 F-------------------------------------NLLDPLLTQSSTEPPSQDDVNFR------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 284 mdseDPLFILYTSGSTGKPKGIQHTTAGYMTYAyATTKYTFDAQEDDV-YWC-----TAdcGWITG-HSYLLYGPLMNGL 356
Cdd:cd05939 105 ----DKLFYIYTSGTTGLPKAAVIVHSRYYRIA-AGAYYAFGMRPEDVvYDClplyhSA--GGIMGvGQALLHGSTVVIR 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 357 KGIwyegvptypTPSRMWDVTDKYGVTKLYTSPTAARALMAlgNQWLESSSRKTLKVIgtVGEPINPAAWMWLYKQVGLS 436
Cdd:cd05939 178 KKF---------SASNFWDDCVKYNCTIVQYIGEICRYLLA--QPPSEEEQKHNVRLA--VGNGLRPQIWEQFVRRFGIP 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 437 NVSivDTYWQTETgghmiTCLPGATPMKPGAAA-MPFFGAS--PVLL----DAEGRVIEG---------PGEgslcfdra 500
Cdd:cd05939 245 QIG--EFYGATEG-----NSSLVNIDNHVGACGfNSRILPSvyPIRLikvdEDTGELIRDsdglcipcqPGE-------- 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 501 wPGMMRGI------------YGDE----QRFVKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIE 564
Cdd:cd05939 310 -PGLLVGKiiqndplrrfdgYVNEgatnKKIARDVFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVE 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 565 SAL--VAHEKVAEAAVVAAPHdIKGSFPYAFVTLNVGERINEKLVAELKKlvreKIGALAVPDVIQEAPGLPKTRSGKVT 642
Cdd:cd05939 389 GILsnVLGLEDVVVYGVEVPG-VEGRAGMAAIVDPERKVDLDRFSAVLAK----SLPPYARPQFIRLLPEVDKTGTFKLQ 463
|
....*.
gi 71982997 643 RRILRK 648
Cdd:cd05939 464 KTDLQK 469
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
126-571 |
3.92e-11 |
|
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: 65.84 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 126 TWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVvdarcrvlvta 205
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCL----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 206 dgvfrgakpiglkSIADAAAVLAsqedvkveaiimvehlkrvtkpdgvelpkvdytditviydsemlkcagvdspvewmd 285
Cdd:cd05940 72 -------------NVSSAKHLVV--------------------------------------------------------- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 286 seDPLFILYTSGSTGKPKG--IQHTTAGYMTYAYAttkYTFDAQEDDVYWCTADCGWITGHSYLLYGPLMNGLKGIWYEG 363
Cdd:cd05940 82 --DAALYIYTSGTTGLPKAaiISHRRAWRGGAFFA---GSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKK 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 364 VptypTPSRMWDVTDKYGVTKLYTSPTAARALMalgNQWLESSSRKTlKVIGTVGEPINPAAWMWLYKQVGLSNvsIVDT 443
Cdd:cd05940 157 F----SASNFWDDIRKYQATIFQYIGELCRYLL---NQPPKPTERKH-KVRMIFGNGLRPDIWEEFKERFGVPR--IAEF 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 444 YWQTEtGGHMITCLPGatpmKPGAAampffGASPVLL--------------------DAEGRVIE-GPGEGSLCFDRAWP 502
Cdd:cd05940 227 YAATE-GNSGFINFFG----KPGAI-----GRNPSLLrkvaplalvkydlesgepirDAEGRCIKvPRGEPGLLISRINP 296
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71982997 503 GMMRGIYGD----EQRFVKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHE 571
Cdd:cd05940 297 LEPFDGYTDpaatEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFP 369
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
285-647 |
7.29e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 65.01 E-value: 7.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 285 DSEDPLFILYTSGSTGKPKGIQHTTAgymtyAYATTkytFDAQEDDVYWCTADcgwITGHSYLLY----------GPLMN 354
Cdd:PRK07787 126 DPDAPALIVYTSGTTGPPKGVVLSRR-----AIAAD---LDALAEAWQWTADD---VLVHGLPLFhvhglvlgvlGPLRI 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 355 G-------------------LKGIWYEGVPTyptpsrMWdvtdkygvTKLYTSPTAARALmalgnqwleSSSRktLKVIG 415
Cdd:PRK07787 195 GnrfvhtgrptpeayaqalsEGGTLYFGVPT------VW--------SRIAADPEAARAL---------RGAR--LLVSG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 416 TVGEPINPAAwmwlyKQVGLSNVSIVDTYWQTETgghMITCLPGAT-PMKPGAAAMPFFGASPVLLDAEGRVIEGPGE-- 492
Cdd:PRK07787 250 SAALPVPVFD-----RLAALTGHRPVERYGMTET---LITLSTRADgERRPGWVGLPLAGVETRLVDEDGGPVPHDGEtv 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 493 GSLCFdRAwPGMMRGIYGDEQRFVKTYLApfNGYYFTGDGARRDEDGYLWITGRVD-DLMNVSGHLLSTAEIESALVAHE 571
Cdd:PRK07787 322 GELQV-RG-PTLFDGYLNRPDATAAAFTA--DGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHP 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 572 KVAEAAVVAAPHDikgsfpyafvtlNVGERINEKLVA-------ELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRR 644
Cdd:PRK07787 398 GVREAAVVGVPDD------------DLGQRIVAYVVGaddvaadELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKK 465
|
...
gi 71982997 645 ILR 647
Cdd:PRK07787 466 QLL 468
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
126-651 |
8.90e-11 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 65.01 E-value: 8.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 126 TWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAmhSVVFAGFSAESLAarvVDARCRVLvta 205
Cdd:PRK10946 48 QFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGV--APVNALFSHQRSE---LNAYASQI--- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 206 dgvfrgaKPIGLksIADAAAVLASQEDvkveaiiMVEHLKRVTKPDGVELPKVDYTDITViydSEMLKCAGVDSPVEWMD 285
Cdd:PRK10946 120 -------EPALL--IADRQHALFSDDD-------FLNTLVAEHSSLRVVLLLNDDGEHSL---DDAINHPAEDFTATPSP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 286 SEDPLFILYTSGSTGKPKGIQHTtagYMTYAYATTKYT----FDAQEddVYWCTADcgwiTGHSYLLYGPlmnGLKGIWY 361
Cdd:PRK10946 181 ADEVAFFQLSGGSTGTPKLIPRT---HNDYYYSVRRSVeicgFTPQT--RYLCALP----AAHNYPMSSP---GALGVFL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 362 EG----VPTYPTPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSRKTLKVIGTVGEPIN-------PAAWMWLY 430
Cdd:PRK10946 249 AGgtvvLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKLLQVGGARLSetlarriPAELGCQL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 431 KQV-----GLSNVSIVDtywqtETGGHMITClpGATPMKPgaaampffgaspvllDAEGRVI--EG----PGE-GSLcfd 498
Cdd:PRK10946 329 QQVfgmaeGLVNYTRLD-----DSDERIFTT--QGRPMSP---------------DDEVWVAdaDGnplpQGEvGRL--- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 499 rawpgMMRGIYgdeqRFVKTYLAP------F--NGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAH 570
Cdd:PRK10946 384 -----MTRGPY----TFRGYYKSPqhnasaFdaNGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRH 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 571 EKVAEAAVVAAPHDIKGSFPYAFVTLnvgeriNEKLVA-ELKKLVREK-IGALAVPDVIQEAPGLPKTRSGKVTRRILRK 648
Cdd:PRK10946 455 PAVIHAALVSMEDELMGEKSCAFLVV------KEPLKAvQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQ 528
|
...
gi 71982997 649 IAE 651
Cdd:PRK10946 529 WLA 531
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
125-308 |
1.71e-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: 64.01 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 125 STWTYNELHAQVVQFSAVLRS-HGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVL- 202
Cdd:cd17632 66 ETITYAELWERVGAVAAAHDPeQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLa 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 203 VTADGVfrgakPIGLKSIADAAAVlasqedvkvEAIIMVEHLKRV-TKPDGVE-----LPKVDYTDITVIYDSEMLKCAG 276
Cdd:cd17632 146 VSAEHL-----DLAVEAVLEGGTP---------PRLVVFDHRPEVdAHRAALEsarerLAAVGIPVTTLTLIAVRGRDLP 211
|
170 180 190
....*....|....*....|....*....|...
gi 71982997 277 VDSPVEWMDSEDPL-FILYTSGSTGKPKGIQHT 308
Cdd:cd17632 212 PAPLFRPEPDDDPLaLLIYTSGSTGTPKGAMYT 244
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
127-304 |
2.36e-10 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 63.68 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 127 WTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTAD 206
Cdd:PRK08315 44 WTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAAD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 207 GvFRGAKPIGLksIADAAAVLASQEDVKVEAiIMVEHLKRVTKPDGVELPKVDYTDiTVIYDSEMLKCAGVDSPVEWMDS 286
Cdd:PRK08315 124 G-FKDSDYVAM--LYELAPELATCEPGQLQS-ARLPELRRVIFLGDEKHPGMLNFD-ELLALGRAVDDAELAARQATLDP 198
|
170
....*....|....*...
gi 71982997 287 EDPLFILYTSGSTGKPKG 304
Cdd:PRK08315 199 DDPINIQYTSGTTGFPKG 216
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
112-646 |
2.58e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 64.03 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 112 IAYIFEGneptdtSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLA 191
Cdd:PRK05691 2205 PALTFAG------QTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLH 2278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 192 ARVVDARCRVLVTADGVFR--GAKPIGLK--SIADAAAVLASQEDVKVEAIIMVEHLKrvtkpdgvelpkvdytditviy 267
Cdd:PRK05691 2279 YMIEDSGIGLLLSDRALFEalGELPAGVArwCLEDDAAALAAYSDAPLPFLSLPQHQA---------------------- 2336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 268 dsemlkcagvdspvewmdsedplFILYTSGSTGKPKGIQHTTAGYMTYAYATTKyTFDAQEDDV----YWCTADCGwitg 343
Cdd:PRK05691 2337 -----------------------YLIYTSGSTGKPKGVVVSHGEIAMHCQAVIE-RFGMRADDCelhfYSINFDAA---- 2388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 344 hSYLLYGPLMNGLK------GIWyeGVPTYPTPSRMWDVTdKYGVTKLYTSPTAaralmalgnQWLESSSRK-TLKVIGT 416
Cdd:PRK05691 2389 -SERLLVPLLCGARvvlraqGQW--GAEEICQLIREQQVS-ILGFTPSYGSQLA---------QWLAGQGEQlPVRMCIT 2455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 417 VGEPINPAAWMWLykQVGLSNVSIVDTYWQTETGGHMITCLPGATpMKPGAAAMPF---FGA-SPVLLDAEGRVIEGPGE 492
Cdd:PRK05691 2456 GGEALTGEHLQRI--RQAFAPQLFFNAYGPTETVVMPLACLAPEQ-LEEGAASVPIgrvVGArVAYILDADLALVPQGAT 2532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 493 GSLCFDRAwpGMMRGIYG----DEQRFVKTYLAPFNG-YYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESAL 567
Cdd:PRK05691 2533 GELYVGGA--GLAQGYHDrpglTAERFVADPFAADGGrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRL 2610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 568 VAHEKVAEAAVVAapHDIKGSFPYA-FVTLNVGERINEK---LVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTR 643
Cdd:PRK05691 2611 LEHPAVREAVVLA--LDTPSGKQLAgYLVSAVAGQDDEAqaaLREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDR 2688
|
...
gi 71982997 644 RIL 646
Cdd:PRK05691 2689 RAL 2691
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
126-567 |
3.78e-10 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 62.83 E-value: 3.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 126 TWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMhSVvfaGFSAESLAARVVDarcrvlvta 205
Cdd:cd17641 11 EFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGAL-SL---GIYQDSMAEEVAY--------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 206 dgvfrgakpigLKSIADAAAVLASQEDvKVEAIImvEHLKRVtkpdgvelPKVDYtditVIY----------DSEMLKCA 275
Cdd:cd17641 78 -----------LLNYTGARVVIAEDEE-QVDKLL--EIADRI--------PSVRY----VIYcdprgmrkydDPRLISFE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 276 GVDSPVEWMDSEDP-LF--------------ILYTSGSTGKPKG--IQHTTAGYMTYAYATtkytFDAQE-DDVYWCTAD 337
Cdd:cd17641 132 DVVALGRALDRRDPgLYerevaagkgedvavLCTTSGTTGKPKLamLSHGNFLGHCAAYLA----ADPLGpGDEYVSVLP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 338 CGWITGHSYLLYGPL---------------MNGLKGIWyegvPTYP-TPSRMWDVTDKYGVTKLYTSPTAARAL----MA 397
Cdd:cd17641 208 LPWIGEQMYSVGQALvcgfivnfpeepetmMEDLREIG----PTFVlLPPRVWEGIAADVRARMMDATPFKRFMfelgMK 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 398 LGNQWLESSSRKTlkvigTVGEPINPAAWMW-------LYKQVGLSNVSIVDT-----------------------YWQT 447
Cdd:cd17641 284 LGLRALDRGKRGR-----PVSLWLRLASWLAdallfrpLRDRLGFSRLRSAATggaalgpdtfrffhaigvplkqlYGQT 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 448 ETGGhmITCLPGATPMKPGAAAMPFFGASpVLLDAEGRViegpgegslcFDRAwPGMMRGIYGDEQRFVKTYLApfNGYY 527
Cdd:cd17641 359 ELAG--AYTVHRDGDVDPDTVGVPFPGTE-VRIDEVGEI----------LVRS-PGVFVGYYKNPEATAEDFDE--DGWL 422
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 71982997 528 FTGDGARRDEDGYLWITGRVDDLMNVS-GHLLSTAEIESAL 567
Cdd:cd17641 423 HTGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSPQFIENKL 463
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
120-647 |
7.51e-10 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 61.82 E-value: 7.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 120 EPTDTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAmhsvVF-----AGFSAEsLAARV 194
Cdd:PRK07514 22 ETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGA----VFlplntAYTLAE-LDYFI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 195 VDARCRVLVTADGVFRGAKPI---------------GLKSIADAAAVLASQ-EDVKVEAiimvehlkrvtkpdgvelpkv 258
Cdd:PRK07514 97 GDAEPALVVCDPANFAWLSKIaaaagaphvetldadGTGSLLEAAAAAPDDfETVPRGA--------------------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 259 dytditviydsemlkcagvdspvewmdsEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYtFDAQEDDV------- 331
Cdd:PRK07514 156 ----------------------------DDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDY-WRFTPDDVlihalpi 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 332 YwctadcgwitgHSYLLY----GPLMNGLKGIWYEGVPTYPTPSRMWDVTDKYGVTKLYTSptaaralmALGNQWL--ES 405
Cdd:PRK07514 207 F-----------HTHGLFvatnVALLAGASMIFLPKFDPDAVLALMPRATVMMGVPTFYTR--------LLQEPRLtrEA 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 406 SSRKTLKVIGTVgePINP---AAWmwlYKQVGLSnvsIVDTYWQTETGghMITCLPGATPMKPGAAAMPFFGASPVLLDA 482
Cdd:PRK07514 268 AAHMRLFISGSA--PLLAethREF---QERTGHA---ILERYGMTETN--MNTSNPYDGERRAGTVGFPLPGVSLRVTDP 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 483 E-GRVIeGPGE-------GSLCFDRAW--PGmmrgiygdeqrfvKTyLAPF--NGYYFTGDGARRDEDGYLWITGRVDDL 550
Cdd:PRK07514 338 EtGAEL-PPGEigmievkGPNVFKGYWrmPE-------------KT-AEEFraDGFFITGDLGKIDERGYVHIVGRGKDL 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 551 MNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEK-LVAELKklvrekiGALA---VPDV 626
Cdd:PRK07514 403 IISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAaILAALK-------GRLArfkQPKR 475
|
570 580
....*....|....*....|.
gi 71982997 627 IQEAPGLPKTRSGKVTRRILR 647
Cdd:PRK07514 476 VFFVDELPRNTMGKVQKNLLR 496
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
285-643 |
1.32e-09 |
|
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: 60.92 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 285 DSEDPLFILYTSGSTGKPKGIQHT---TAGYMTYAYATTKYTfdaqEDDVYWCTADCGWITGHSYLLYGPLMNG------ 355
Cdd:cd05914 87 DEDDVALINYTSGTTGNSKGVMLTyrnIVSNVDGVKEVVLLG----KGDKILSILPLHHIYPLTFTLLLPLLNGahvvfl 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 356 --------LKGIWYEGVPTYPTPsRMWDVTDKYGVTKLyTSPTAARALMALGNQWLESSSRKTLK--------------V 413
Cdd:cd05914 163 dkipsakiIALAFAQVTPTLGVP-VPLVIEKIFKMDII-PKLTLKKFKFKLAKKINNRKIRKLAFkkvheafggnikefV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 414 IGtvGEPINPAAWMWLYKqvglSNVSIVDTYWQTETGGhmITCLPGATPMKPGAAAMPFFG-----ASPVLLDAEGRVI- 487
Cdd:cd05914 241 IG--GAKINPDVEEFLRT----IGFPYTIGYGMTETAP--IISYSPPNRIRLGSAGKVIDGvevriDSPDPATGEGEIIv 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 488 EGPGegslcfdrawpgMMRGIYGDEQRFVKTYLApfNGYYFTGDGARRDEDGYLWITGRVDDLM-NVSGHLLSTAEIESA 566
Cdd:cd05914 313 RGPN------------VMKGYYKNPEATAEAFDK--DGWFHTGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAK 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 567 L-----------VAHEKVAEAAVVAAPHDIKGSfpyafvTLNVGERInEKLVAELKKLVREKIGALA-VPDVIQEAPGLP 634
Cdd:cd05914 379 InnmpfvleslvVVQEKKLVALAYIDPDFLDVK------ALKQRNII-DAIKWEVRDKVNQKVPNYKkISKVKIVKEEFE 451
|
....*....
gi 71982997 635 KTRSGKVTR 643
Cdd:cd05914 452 KTPKGKIKR 460
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
288-643 |
1.85e-09 |
|
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: 59.59 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 288 DPLFILYTSGSTGKPKG--IQHTTagyMTYAYATTKYTFDAQEDDVYWCTADCGWITGHSYLLYGpLMNGLKGIwyegVP 365
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGavLSHGN---LIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALAT-FHAGGANV----VM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 366 TYPTPSRMWDVTDKYGVTKLYT-SPTAARALMALGNQWLESSSrktLKVIGTVGEPINPAAWMwlykqvGLSNVSIVDTY 444
Cdd:cd17637 73 EKFDPAEALELIEEEKVTLMGSfPPILSNLLDAAEKSGVDLSS---LRHVLGLDAPETIQRFE------ETTGATFWSLY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 445 WQTETGGhMITCLPGATpmKPGAAAMPFFGASPVLLDAEGR-VIEG-PGE----GSLCFDRAWpgmmRGIYGDEQRFVkt 518
Cdd:cd17637 144 GQTETSG-LVTLSPYRE--RPGSAGRPGPLVRVRIVDDNDRpVPAGeTGEivvrGPLVFQGYW----NLPELTAYTFR-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 519 ylapfNGYYFTGDGARRDEDGYLWITGRV--DDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPhDIK-GSFPYAFVT 595
Cdd:cd17637 215 -----NGWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVP-DPKwGEGIKAVCV 288
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 71982997 596 LNVGERINEKlvaELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTR 643
Cdd:cd17637 289 LKPGATLTAD---ELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
123-332 |
1.98e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 60.76 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 123 DTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVL 202
Cdd:PTZ00216 118 ETRYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 203 VTadgvfrgakpiGLKSIADAAAVLASQEdVKVEAIIMVEHLkrvtkPDGVELPKVD---YTDItVIYDSEMLKCAGVDS 279
Cdd:PTZ00216 198 VC-----------NGKNVPNLLRLMKSGG-MPNTTIIYLDSL-----PASVDTEGCRlvaWTDV-VAKGHSAGSHHPLNI 259
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 71982997 280 PvewMDSEDPLFILYTSGSTGKPKGIQHT----TAGYMTYAYATTKYTFDAQEDDVY 332
Cdd:PTZ00216 260 P---ENNDDLALIMYTSGTTGDPKGVMHThgslTAGILALEDRLNDLIGPPEEDETY 313
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
128-648 |
1.04e-08 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 58.22 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 128 TYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTaDG 207
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVIT-DL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 208 VFrgaKPIgLKSIADAAAvlasqedvKVEAIIMV---EHLKRVTKPDGVElpkvdYTDITviydsemlkcAGVDSPVEW- 283
Cdd:PRK06018 120 TF---VPI-LEKIADKLP--------SVERYVVLtdaAHMPQTTLKNAVA-----YEEWI----------AEADGDFAWk 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 284 -MDSEDPLFILYTSGSTGKPKG--------IQHTTAGYMTYAYATTKY--------TFDAQEddvyWCTADCGWITGHSY 346
Cdd:PRK06018 173 tFDENTAAGMCYTSGTTGDPKGvlyshrsnVLHALMANNGDALGTSAAdtmlpvvpLFHANS----WGIAFSAPSMGTKL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 347 LLYGPLMNGlkgiwyegvptyptpSRMWDVTDKYGVTKLYTSPTAAraLMALgnQWLESSSRK--TLKVIGTVGEPInPA 424
Cdd:PRK06018 249 VMPGAKLDG---------------ASVYELLDTEKVTFTAGVPTVW--LMLL--QYMEKEGLKlpHLKMVVCGGSAM-PR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 425 AWMWLYKQVGlsnVSIVDTYWQTETGGHMITC-LPGATPMKPGAAAM--------PFFGASPVLLDAEGRVIEGPGEGSL 495
Cdd:PRK06018 309 SMIKAFEDMG---VEVRHAWGMTEMSPLGTLAaLKPPFSKLPGDARLdvlqkqgyPPFGVEMKITDDAGKELPWDGKTFG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 496 CFDRAWPGMMRGIYGDEQRFVKTylapfNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAE 575
Cdd:PRK06018 386 RLKVRGPAVAAAYYRVDGEILDD-----DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAE 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71982997 576 AAVVAAPHDIKGSFPYAFVTLNVGERINEklvAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRK 648
Cdd:PRK06018 461 AAVIGVYHPKWDERPLLIVQLKPGETATR---EEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
126-648 |
3.22e-08 |
|
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: 56.67 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 126 TWTYNELHAQVVQFSAVLRS-HGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVt 204
Cdd:cd05937 5 TWTYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVI- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 205 adgvfrgakpiglksiadaaavlasqedvkveaiimvehlkrvtkpdgvelpkvdytditviydsemlkcagvdspvewM 284
Cdd:cd05937 84 -------------------------------------------------------------------------------V 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 285 DSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYTFDAQEDDVYWC----------TADCGWITGHSYLLYGPLMn 354
Cdd:cd05937 85 DPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCmplyhgtaafLGACNCLMSGGTLALSRKF- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 355 glkgiwyegvptypTPSRMWDVTDKYGVTKLYTSPTAARALMALGnqwlESSSRKTLKVIGTVGEPINPAAWMWLYKQVG 434
Cdd:cd05937 164 --------------SASQFWKDVRDSGATIIQYVGELCRYLLSTP----PSPYDRDHKVRVAWGNGLRPDIWERFRERFN 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 435 LSnvSIVDTYWQTETGGHMITCLPGATpmkpGAAAMPFFGA----------SPVLLDAE-GRVI-------------EGP 490
Cdd:cd05937 226 VP--EIGEFYAATEGVFALTNHNVGDF----GAGAIGHHGLirrwkfenqvVLVKMDPEtDDPIrdpktgfcvrapvGEP 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 491 GE--GSLCFD--RAWPGMMRGIYGDEQRFVKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESA 566
Cdd:cd05937 300 GEmlGRVPFKnrEAFQGYLHNEDATESKLVRDVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADV 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 567 LVAHEKVAEAAV--VAAP-HDikGSFPYAFVTL-NVGERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVT 642
Cdd:cd05937 380 LGAHPDIAEANVygVKVPgHD--GRAGCAAITLeESSAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQ 457
|
....*.
gi 71982997 643 RRILRK 648
Cdd:cd05937 458 KGVLRD 463
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
286-648 |
1.02e-07 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 55.19 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 286 SEDPLFILYTSGSTGKPKG--IQHTTAGYMTYA-YATTKYTfdaqEDDVYWCTADCGWITGHSYLLyGPLMNGLKGIWye 362
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGvtISHSALIVQSLAkIAIVGYG----EDDVYLHTAPLCHIGGLSSAL-AMLMVGACHVL-- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 363 gVPTYPTpSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSRKTLKVIGTVGEPInPAAWMWLYKQVgLSNVSIVD 442
Cdd:PLN02860 244 -LPKFDA-KAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRKILNGGGSL-SSRLLPDAKKL-FPNAKLFS 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 443 TYWQTETGGHMiTCLPGATPMKPGAAAMPFFGASPVLLDAegrvieGPGEGSlCFDRAWPGMMRGIYGDE---------- 512
Cdd:PLN02860 320 AYGMTEACSSL-TFMTLHDPTLESPKQTLQTVNQTKSSSV------HQPQGV-CVGKPAPHVELKIGLDEssrvgriltr 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 513 ----------QRFVKTYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAP 582
Cdd:PLN02860 392 gphvmlgywgQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVP 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 583 HDIKGSFPYAFVTLNVG---------ERINEKLVAE--LKKLVREK-IGALAVPD--VIQEAPgLPKTRSGKVTRRILRK 648
Cdd:PLN02860 472 DSRLTEMVVACVRLRDGwiwsdnekeNAKKNLTLSSetLRHHCREKnLSRFKIPKlfVQWRKP-FPLTTTGKIRRDEVRR 550
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
128-568 |
1.15e-07 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 54.67 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 128 TYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAmhsvvfagfsaeslaarvVDarcrvlvtadg 207
Cdd:cd17640 7 TYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGA------------------VD----------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 208 VFRGAKpiglKSIADAAAVLASQEDVkveaIIMVEHlkrvtkpdgvelpkvdytditviydsemlkcagvdspvewmDSE 287
Cdd:cd17640 58 VVRGSD----SSVEELLYILNHSESV----ALVVEN-----------------------------------------DSD 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 288 DPLFILYTSGSTGKPKGIQHTTAGYM-----TYAYATTKYtfdaqeddvywctadcgwitGHSYLLYGPlmnglkgIW-- 360
Cdd:cd17640 89 DLATIIYTSGTTGNPKGVMLTHANLLhqirsLSDIVPPQP--------------------GDRFLSILP-------IWhs 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 361 YEGVPTYPTPSRmwdvtdkyGVTKLYTSPTAARALMALGNQ---------W----------LESSSR------KTLKVIG 415
Cdd:cd17640 142 YERSAEYFIFAC--------GCSQAYTSIRTLKDDLKRVKPhyivsvprlWeslysgiqkqVSKSSPikqflfLFFLSGG 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 416 TVGEPINPAAWM-----WLYKQVGlsnVSIVDTYWQTETGghmitclPGATPMKP-----GAAAMPFFGASPVLLDAEGR 485
Cdd:cd17640 214 IFKFGISGGGALpphvdTFFEAIG---IEVLNGYGLTETS-------PVVSARRLkcnvrGSVGRPLPGTEIKIVDPEGN 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 486 VIEGPGEGSLCFDRAwPGMMRGIYGDEQRFVKTyLAPfNGYYFTGDGARRDEDGYLWITGRVDDLMNVS-GHLLSTAEIE 564
Cdd:cd17640 284 VVLPPGEKGIVWVRG-PQVMKGYYKNPEATSKV-LDS-DGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIE 360
|
....
gi 71982997 565 SALV 568
Cdd:cd17640 361 EALM 364
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
282-647 |
1.72e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 54.33 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 282 EWMDSED-----PLF-------ILYTSGSTGKPKGIQHTTAGYMTYAYAttkytfdAQEDDVYWCTA-DC---------- 338
Cdd:PRK07008 159 TLVGAQDgdydwPRFdenqassLCYTSGTTGNPKGALYSHRSTVLHAYG-------AALPDAMGLSArDAvlpvvpmfhv 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 339 -GW-------ITGHSYLLYGPLMNGlKGIwYE-----------GVPTyptpsrMWdvtdkygvtklytsptaaraLMALG 399
Cdd:PRK07008 232 nAWglpysapLTGAKLVLPGPDLDG-KSL-YElieaervtfsaGVPT------VW--------------------LGLLN 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 400 ----NQWLESSSRKTlkVIGtvGEPINPAAWMWLYKQVGlsnVSIVDTYWQTETGGHMITC-LPGATPMKPGAAAMPffg 474
Cdd:PRK07008 284 hmreAGLRFSTLRRT--VIG--GSACPPAMIRTFEDEYG---VEVIHAWGMTEMSPLGTLCkLKWKHSQLPLDEQRK--- 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 475 aspvLLDAEGRVIEG------PGEGSlcfDRAWPGMMrgiYGDEQ--------RFVKTYLAPF-NGYYFTGDGARRDEDG 539
Cdd:PRK07008 354 ----LLEKQGRVIYGvdmkivGDDGR---ELPWDGKA---FGDLQvrgpwvidRYFRGDASPLvDGWFPTGDVATIDADG 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 540 YLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEKlvaELKKLVREKIG 619
Cdd:PRK07008 424 FMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTRE---ELLAFYEGKVA 500
|
410 420
....*....|....*....|....*...
gi 71982997 620 ALAVPDVIQEAPGLPKTRSGKVTRRILR 647
Cdd:PRK07008 501 KWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
110-653 |
2.64e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.40 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 110 NKIAYIFEGNEPTDTSTWTYNELHAQVVQFSAVLRSHGVKrGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSA-- 187
Cdd:PRK05691 24 DRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARASF-GDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESArr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 188 ---ESLAARVVDARCRVLVTADGVFRGAKPIGLKSIADAAAVLAsqedvkveaiimVEHLKRVTKPDGVElPKVDYTDIT 264
Cdd:PRK05691 103 hhqERLLSIIADAEPRLLLTVADLRDSLLQMEELAAANAPELLC------------VDTLDPALAEAWQE-PALQPDDIA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 265 viydsemlkcagvdspvewmdsedplFILYTSGSTGKPKGIQHTTAGYMTYAYATTK-YTFDAQEDDVY--WCTA--DCG 339
Cdd:PRK05691 170 --------------------------FLQYTSGSTALPKGVQVSHGNLVANEQLIRHgFGIDLNPDDVIvsWLPLyhDMG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 340 WITGhsylLYGPLMNGLKGIWYEgvPTY--PTPSRMWDVTDKYGVTkLYTSPTAARALMA--LGNQWLESSSRKTLKVIG 415
Cdd:PRK05691 224 LIGG----LLQPIFSGVPCVLMS--PAYflERPLRWLEAISEYGGT-ISGGPDFAYRLCSerVSESALERLDLSRWRVAY 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 416 TVGEPINP---AAWMWLYKQVGLSNVSIVDTYWQTE-----TG---GHMITCL-------------PGATPM-------K 464
Cdd:PRK05691 297 SGSEPIRQdslERFAEKFAACGFDPDSFFASYGLAEatlfvSGgrrGQGIPALeldaealarnraePGTGSVlmscgrsQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 465 PGAAAMPffgASPVLLD--AEGRVIE----GPGEGSlcfdrawpGMMRGIYGDEQRFV----KTYLApfngyyfTGD-GA 533
Cdd:PRK05691 377 PGHAVLI---VDPQSLEvlGDNRVGEiwasGPSIAH--------GYWRNPEASAKTFVehdgRTWLR-------TGDlGF 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 534 RRDedGYLWITGRVDDLMNVSGHLLSTAEIESALvahEKVAEAAVvaaphdiKGSFPYAFVTLNVGERINekLVAELKKL 613
Cdd:PRK05691 439 LRD--GELFVTGRLKDMLIVRGHNLYPQDIEKTV---EREVEVVR-------KGRVAAFAVNHQGEEGIG--IAAEISRS 504
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 71982997 614 VR------EKIGAL--AVPDVIQEAP---------GLPKTRSGKVTRRILR-KIAEGS 653
Cdd:PRK05691 505 VQkilppqALIKSIrqAVAEACQEAPsvvlllnpgALPKTSSGKLQRSACRlRLADGS 562
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
292-646 |
2.92e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 53.46 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 292 ILYTSGSTGKPKGIQHttAGYMTYAYATTKYTFDAQEddvywctadcgWITGHSYLLYGPLMNGLK-GIWYEGVPTYPT- 369
Cdd:PRK13383 179 VLLTSGTTGKPKGVPR--APQLRSAVGVWVTILDRTR-----------LRTGSRISVAMPMFHGLGlGMLMLTIALGGTv 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 370 -PSRMWDVTDKYGVTKLYTS------PTAARALMALGNQWLESSSRKTLKVIGTVGEPINPA---AWMWLYKQVglsnvs 439
Cdd:PRK13383 246 lTHRHFDAEAALAQASLHRAdaftavPVVLARILELPPRVRARNPLPQLRVVMSSGDRLDPTlgqRFMDTYGDI------ 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 440 IVDTYWQTETGghmITCLpgATPMK----PGAAAMPFFGASPVLLDAEGRVIeGP---GE----GSLCFDRAWPGMMRGI 508
Cdd:PRK13383 320 LYNGYGSTEVG---IGAL--ATPADlrdaPETVGKPVAGCPVRILDRNNRPV-GPrvtGRifvgGELAGTRYTDGGGKAV 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 509 ygdeqrfvktylapFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGS 588
Cdd:PRK13383 394 --------------VDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGH 459
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 71982997 589 FPYAFVTLNVGERINeklVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRIL 646
Cdd:PRK13383 460 RLAAFVVLHPGSGVD---AAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
128-426 |
3.81e-07 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 53.36 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 128 TYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAarvvdaRCrvlvtadg 207
Cdd:PRK09274 43 SFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPGMGIKNLK------QC-------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 208 vFRGAKPIGLKSIADAaavlasqedvkveaiimveHLKRVT---KPDGVElpkvdyTDITV---------IYDSEMLKCA 275
Cdd:PRK09274 109 -LAEAQPDAFIGIPKA-------------------HLARRLfgwGKPSVR------RLVTVggrllwggtTLATLLRDGA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 276 GVDSPVEWMDSEDPLFILYTSGSTGKPKGIQHTTAgymtyayattkyTFDAQeddVYWCTADCGWITGHSYL-------L 348
Cdd:PRK09274 163 AAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHG------------MFEAQ---IEALREDYGIEPGEIDLptfplfaL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 349 YGPLMnGLKGIWYEGVPTYPT---PSRMWDVTDKYGVTKLYTSPtaarALM-ALGnQWLESSSRK--TLKVIGTVGEPIN 422
Cdd:PRK09274 228 FGPAL-GMTSVIPDMDPTRPAtvdPAKLFAAIERYGVTNLFGSP----ALLeRLG-RYGEANGIKlpSLRRVISAGAPVP 301
|
....
gi 71982997 423 PAAW 426
Cdd:PRK09274 302 IAVI 305
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
285-652 |
5.20e-07 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 53.05 E-value: 5.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 285 DSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAY-ATTKYTFDAQeDDVYWCTAdcgwiTGHSYLLYG----PLMNGLKgi 359
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAqVAARIDFSPE-DKVFNALP-----VFHSFGLTGglvlPLLSGVK-- 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 360 wyegVPTYPT-------PSRMWDVtdkyGVTKLYTSPT--AARALMAlgnqwlESSSRKTLKVIGTVGEPINPAA---WM 427
Cdd:PRK06814 863 ----VFLYPSplhyriiPELIYDT----NATILFGTDTflNGYARYA------HPYDFRSLRYVFAGAEKVKEETrqtWM 928
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 428 WLYkqvglsNVSIVDTYWQTETGGhMITClpgATPM--KPGAA--AMPffGASPVLLDAEGrvIEgpgEGSLCFDRAwPG 503
Cdd:PRK06814 929 EKF------GIRILEGYGVTETAP-VIAL---NTPMhnKAGTVgrLLP--GIEYRLEPVPG--ID---EGGRLFVRG-PN 990
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 504 MMRGIYGDEQRFVktYLAPFNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPH 583
Cdd:PRK06814 991 VMLGYLRAENPGV--LEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPD 1068
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 584 DIKGSFPYAFVTLNVGERineklvAELKKLVREK-IGALAVPDVIQEAPGLPKTRSGKVTRRILRKIAEG 652
Cdd:PRK06814 1069 ARKGERIILLTTASDATR------AAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKIDYVAVTKLAEE 1132
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
528-651 |
7.89e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 51.96 E-value: 7.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 528 FTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHdikgsfPYAfvtlnvGERINEKLV 607
Cdd:PRK08308 294 FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKD------PVA------GERVKAKVI 361
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 71982997 608 AE-------LKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRiLRKIAE 651
Cdd:PRK08308 362 SHeeidpvqLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRK-LLELGE 411
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
226-570 |
2.52e-06 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 50.58 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 226 VLASQEDVKVEAII----MVEHLkRVTKPDGVELP-KVDYTDITVIYDSEMLKCA---GVDSPVEWM---------DSED 288
Cdd:PRK06334 106 VTACANLVGVTHVLtskqLMQHL-AQTHGEDAEYPfSLIYMEEVRKELSFWEKCRigiYMSIPFEWLmrwfgvsdkDPED 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 289 PLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYtFDAQEDDVYWctadcgwitghSYL----LYG-------PLMNGLK 357
Cdd:PRK06334 185 VAVILFTSGTEKLPKGVPLTHANLLANQRACLKF-FSPKEDDVMM-----------SFLppfhAYGfnsctlfPLLSGVP 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 358 gIWYEGVPTYptPSRMWDVTDKYGVTKLYTSPTAARALMALGNQWLESSSRKTLKVIGtvGEPINPAawmwLYKQV--GL 435
Cdd:PRK06334 253 -VVFAYNPLY--PKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIG--GDAFKDS----LYQEAlkTF 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 436 SNVSIVDTYWQTETGGhMITCLPGATPMKPGAAAMPFFGASPVLLDAEGRVIEGPGEGSLCFDRAwPGMMRGIYGDE--Q 513
Cdd:PRK06334 324 PHIQLRQGYGTTECSP-VITINTVNSPKHESCVGMPIRGMDVLIVSEETKVPVSSGETGLVLTRG-TSLFSGYLGEDfgQ 401
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 71982997 514 RFVKtyLAPFNgYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAH 570
Cdd:PRK06334 402 GFVE--LGGET-WYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
110-306 |
3.82e-06 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 49.89 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 110 NKIAYIFEGneptdtSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGamHSVVfagfsaes 189
Cdd:PRK04813 17 DFPAYDYLG------EKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAG--HAYI-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 190 laarvvdarcrvlvtadgvfrgakPIGLKSIADAaaVLASQEDVKVEAIIMVEhlkrvtkpdgvELPkVDYTDITVI--Y 267
Cdd:PRK04813 81 ------------------------PVDVSSPAER--IEMIIEVAKPSLIIATE-----------ELP-LEILGIPVItlD 122
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 71982997 268 DSEMLKCAGVDSPVE-WMDSEDPLFILYTSGSTGKPKGIQ 306
Cdd:PRK04813 123 ELKDIFATGNPYDFDhAVKGDDNYYIIFTSGTTGKPKGVQ 162
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
127-314 |
6.76e-06 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 49.34 E-value: 6.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 127 W-TYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTa 205
Cdd:PLN02387 106 WiTYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVIC- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 206 dgvfrGAKPigLKSIADaaavLASQEDVKVEAIIMVEhlkrvtKPDGVELPKVDYTDITVIYDSEMLKcAGVDSPVE--W 283
Cdd:PLN02387 185 -----DSKQ--LKKLID----ISSQLETVKRVIYMDD------EGVDSDSSLSGSSNWTVSSFSEVEK-LGKENPVDpdL 246
|
170 180 190
....*....|....*....|....*....|....*...
gi 71982997 284 MDSEDPLFILYTSGSTGKPKG--IQH-----TTAGYMT 314
Cdd:PLN02387 247 PSPNDIAVIMYTSGSTGLPKGvmMTHgnivaTVAGVMT 284
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
423-647 |
2.86e-05 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 47.32 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 423 PAAWMWlYKQVGlsnVSIVDTYWQTETGGhMITCLPGATPMKPGAAAMPFFGASPVLLDAEGRVIEgPGE-GSLCFdRAw 501
Cdd:PRK07059 342 PVAERW-LEMTG---CPITEGYGLSETSP-VATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLP-LGEpGEICI-RG- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 502 PGMMRGIYG--DEQRFVKTYlapfNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVV 579
Cdd:PRK07059 414 PQVMAGYWNrpDETAKVMTA----DGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAV 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71982997 580 AAPHDIKGSFPYAFVTlnvgeRINEKLV-AELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILR 647
Cdd:PRK07059 490 GVPDEHSGEAVKLFVV-----KKDPALTeEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
108-652 |
3.60e-05 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 47.08 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 108 YGNKIAYIFEGNEPTDTstwTYNELHAQVVQFSAVLRSH-GVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFS 186
Cdd:PRK05620 23 HGDTTVTTWGGAEQEQT---TFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 187 AESLAARVVDARCRVLVtADGvfRGAKPIG--LKSIADAAAVL-ASQEDVKVEAIIMVEHLKrvtkpdgvelpkvdytdi 263
Cdd:PRK05620 100 NDQIVHIINHAEDEVIV-ADP--RLAEQLGeiLKECPCVRAVVfIGPSDADSAAAHMPEGIK------------------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 264 tvIYDSEML---KCAGVDSPVewMDSEDPLFILYTSGSTGKPKGIqhttagymtyAYATTKYTFDAQEddvyWCTADCGW 340
Cdd:PRK05620 159 --VYSYEALldgRSTVYDWPE--LDETTAAAICYSTGTTGAPKGV----------VYSHRSLYLQSLS----LRTTDSLA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 341 IT-GHSYLLYGPLMNGLK-----GIWYEGVP-TYP----TPSRMWDVTDKygvtklyTSPTAARALMALGNQWL-----E 404
Cdd:PRK05620 221 VThGESFLCCVPIYHVLSwgvplAAFMSGTPlVFPgpdlSAPTLAKIIAT-------AMPRVAHGVPTLWIQLMvhylkN 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 405 SSSRKTLKVIGTVGEPINPA---AWMWLYkqvglsNVSIVDTYWQTETGghmitclPGATPMKP-----GAAAMPFF--- 473
Cdd:PRK05620 294 PPERMSLQEIYVGGSAVPPIlikAWEERY------GVDVVHVWGMTETS-------PVGTVARPpsgvsGEARWAYRvsq 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 474 GASPVLLD----AEGRVIEGP--GEGSLCFDRAW----------------PGMMRGIYGDE--QRFVKtylapfNGYYFT 529
Cdd:PRK05620 361 GRFPASLEyrivNDGQVMESTdrNEGEIQVRGNWvtasyyhspteegggaASTFRGEDVEDanDRFTA------DGWLRT 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 530 GDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEKLVAE 609
Cdd:PRK05620 435 GDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAER 514
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 71982997 610 LKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRK-IAEG 652
Cdd:PRK05620 515 LRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQhLADG 558
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
128-308 |
8.67e-05 |
|
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: 45.67 E-value: 8.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 128 TYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAMHSVVFAGFSAESLAARVVDARCRVLVTadg 207
Cdd:cd17639 7 SYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIFT--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 208 vfrgakpiglksiadaaavlasqedvkveaiimvehlkrvtkpDGvelpkvdytditviydsemlkcagvdspvewmDSE 287
Cdd:cd17639 84 -------------------------------------------DG--------------------------------KPD 88
|
170 180
....*....|....*....|.
gi 71982997 288 DPLFILYTSGSTGKPKGIQHT 308
Cdd:cd17639 89 DLACIMYTSGSTGNPKGVMLT 109
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
285-646 |
8.73e-05 |
|
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: 45.47 E-value: 8.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 285 DSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYTFDAQEDDvywctadcgwitgHSYLLYG-------------P 351
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGD-------------EAVLFFSnyvfdffveqmtlA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 352 LMNGLKGIWYEGvPTYPTPSRMWDVTDKYGVTKLYTSPTAAralmalgnQWLESSSRKTLKVIGTVGEPINPAAWMWLYK 431
Cdd:cd17648 159 LLNGQKLVVPPD-EMRFDPDRFYAYINREKVTYLSGTPSVL--------QQYDLARLPHLKRVDAAGEEFTAPVFEKLRS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 432 QV-GLsnvsIVDTYWQTETGghmITCLpgATPMKPGAAAMPFFGA------SPVLLDAEGRV-IEGPGE---GSLCFDRA 500
Cdd:cd17648 230 RFaGL----IINAYGPTETT---VTNH--KRFFPGDQRFDKSLGRpvrntkCYVLNDAMKRVpVGAVGElylGGDGVARG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 501 W---PGMMRgiygdeQRFVKTylaPF----------NG-YYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESA 566
Cdd:cd17648 301 YlnrPELTA------ERFLPN---PFqteqerargrNArLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAA 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 567 L-----------VAHEKVAEAAVVAAPHDIkgsfpyAFVTLNVGErINEklvAELKKLVREKIGALAVPDVIQEAPGLPK 635
Cdd:cd17648 372 LasypgvrecavVAKEDASQAQSRIQKYLV------GYYLPEPGH-VPE---SDLLSFLRAKLPRYMVPARLVRLEGIPV 441
|
410
....*....|.
gi 71982997 636 TRSGKVTRRIL 646
Cdd:cd17648 442 TINGKLDVRAL 452
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
291-654 |
8.82e-05 |
|
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: 45.56 E-value: 8.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 291 FILYTSGSTGKPKGIQHTTAGYMTYAYATTKYTfDAQEDDVY--W--CTADCGWITGHsyllYGPLmnglkgiwYEGVPT 366
Cdd:cd05908 110 FIQFSSGSTGDPKGVMLTHENLVHNMFAILNST-EWKTKDRIlsWmpLTHDMGLIAFH----LAPL--------IAGMNQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 367 YPTPSRMWDV--------TDKYGVTKLyTSPTAARALM------ALGNQWLESSsrktLKVIGTVGEPINPAAWMWLYKQ 432
Cdd:cd05908 177 YLMPTRLFIRrpilwlkkASEHKATIV-SSPNFGYKYFlktlkpEKANDWDLSS----IRMILNGAEPIDYELCHEFLDH 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 433 V---GLSNVSIVDTYWQTETGghMITCLPgatpmkpgAAAMPFFgasPVLLDAEG-----RVIEGPGEGSLCF------- 497
Cdd:cd05908 252 MskyGLKRNAILPVYGLAEAS--VGASLP--------KAQSPFK---TITLGRRHvthgePEPEVDKKDSECLtfvevgk 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 498 ----------DRAWPGMMRGIYGDEQRFVKTYLApfnGYY---------FTGDGARRDED------GYLWITGRVDDLMN 552
Cdd:cd05908 319 pidetdiricDEDNKILPDGYIGHIQIRGKNVTP---GYYnnpeatakvFTDDGWLKTGDlgfirnGRLVITGREKDIIF 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 553 VSGHLLSTAEIESalVAHEKVAEAAVVAAP---HDIKGSFPYAFVTLNVGERINE--KLVAELKKLVREKiGALAVPDV- 626
Cdd:cd05908 396 VNGQNVYPHDIER--IAEELEGVELGRVVAcgvNNSNTRNEEIFCFIEHRKSEDDfyPLGKKIKKHLNKR-GGWQINEVl 472
|
410 420
....*....|....*....|....*....
gi 71982997 627 -IQEapgLPKTRSGKVTRRILRKIAEGSE 654
Cdd:cd05908 473 pIRR---IPKTTSGKVKRYELAQRYQSGE 498
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
126-333 |
1.93e-04 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 44.83 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 126 TW-TYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIG----------AMHSVVFAGFSAESLAARV 194
Cdd:PLN02861 76 VWlTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGityvplydtlGANAVEFIINHAEVSIAFV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 195 VDARCRVLVTadgVFRGAKPiGLKSIADAAAVLASQedvKVEA------IIMVEHLKRVTKPDgVELPKVDYTDItviyd 268
Cdd:PLN02861 156 QESKISSILS---CLPKCSS-NLKTIVSFGDVSSEQ---KEEAeelgvsCFSWEEFSLMGSLD-CELPPKQKTDI----- 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71982997 269 semlkCAgvdspvewmdsedplfILYTSGSTGKPKGIQHTTAGYMTYAYATTKYTFD----AQEDDVYW 333
Cdd:PLN02861 223 -----CT----------------IMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKVtdrvATEEDSYF 270
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
295-648 |
5.01e-04 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 42.72 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 295 TSGSTGKPKGIQHTTAGYMTYAYATtkytfdaqeddvywctadcgwitgHSYLlygplmnGLKGIWYEGVPTY------- 367
Cdd:PRK07824 43 TSGTTGTPKGAMLTAAALTASADAT------------------------HDRL-------GGPGQWLLALPAHhiaglqv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 368 ----------PTpsrMWDVTDKYGVTKL------------YTSPTAARALMALGNqwLESS-SRKTLKVIGTVGEPInPA 424
Cdd:PRK07824 92 lvrsviagsePV---ELDVSAGFDPTALpravaelgggrrYTSLVPMQLAKALDD--PAATaALAELDAVLVGGGPA-PA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 425 AWMWLYKQVGlsnVSIVDTYWQTETGGhmiTCLPGATPMkPGAaampffgaspvlldaEGRVIEGpgegslcfdRAW--- 501
Cdd:PRK07824 166 PVLDAAAAAG---INVVRTYGMSETSG---GCVYDGVPL-DGV---------------RVRVEDG---------RIAlgg 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 502 PGMMRGIYGDEQRfvktylAPFN--GYYFTGDGARRDeDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVV 579
Cdd:PRK07824 215 PTLAKGYRNPVDP------DPFAepGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVF 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71982997 580 AAPHDIKGSfpyAFVTLNVGERINEKLVAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKVTRRILRK 648
Cdd:PRK07824 288 GLPDDRLGQ---RVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
108-308 |
1.07e-03 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 42.17 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 108 YGNKIAYIfegnepTDTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGAmhsvvfagfsa 187
Cdd:PRK09029 16 RPQAIALR------LNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGA----------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 188 eslaarvvdarcRVLvtadgvfrgakPIGLKSIADAAAVLAsqEDVKVEAIIMVEHLKRVTKPDGVELPKVDYTDitviy 267
Cdd:PRK09029 79 ------------RVL-----------PLNPQLPQPLLEELL--PSLTLDFALVLEGENTFSALTSLHLQLVEGAH----- 128
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 71982997 268 dsemlkcagvdsPVEWMDSEDPLFILyTSGSTGKPKGIQHT 308
Cdd:PRK09029 129 ------------AVAWQPQRLATMTL-TSGSTGLPKAAVHT 156
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
120-644 |
1.54e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 41.52 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 120 EPTDTSTWTYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIGA---M-----HSVVFAGFSAESLa 191
Cdd:PRK07768 23 EPDAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGAsltMlhqptPRTDLAVWAEDTL- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 192 aRVVDArcrvlVTADGVFRGAkPIglksiaDAAAVLASQEDVKVEAIimvehlkrvtkpdgvelpkvdytditviydSEM 271
Cdd:PRK07768 102 -RVIGM-----IGAKAVVVGE-PF------LAAAPVLEEKGIRVLTV------------------------------ADL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 272 LKCAGVDsPVEwMDSEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYA-TTKYTFDAqEDDVY--W--CTADCGWITGhsy 346
Cdd:PRK07768 139 LAADPID-PVE-TGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAmFVAAEFDV-ETDVMvsWlpLFHDMGMVGF--- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 347 lLYGPLMNGLkgiwyEGVPTYPT-----PSRMWDVTDKYGVTkLYTSPTAARALMA--LGNQWLESS-SRKTLKVIGTVG 418
Cdd:PRK07768 213 -LTVPMYFGA-----ELVKVTPMdflrdPLLWAELISKYRGT-MTAAPNFAYALLArrLRRQAKPGAfDLSSLRFALNGA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 419 EPINPAAWMWLY---KQVGLSNVSIVDTYWQTET---------GGHMITCLPGATPM----------KPGAAAMPFFGas 476
Cdd:PRK07768 286 EPIDPADVEDLLdagARFGLRPEAILPAYGMAEAtlavsfspcGAGLVVDEVDADLLaalrravpatKGNTRRLATLG-- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 477 PVLLDAEGRVI---------EGPGEGSLCFDRAWPGmmrgiYGDEQRFVKTYLApfNGYYFTGDGARRDEDGYLWITGRV 547
Cdd:PRK07768 364 PPLPGLEVRVVdedgqvlppRGVGVIELRGESVTPG-----YLTMDGFIPAQDA--DGWLDTGDLGYLTEEGEVVVCGRV 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 548 DDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERINEKLVAELKKLVREKI-GALAV-P- 624
Cdd:PRK07768 437 KDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRLDAGHSREGFAVAVESNAFEDPAEVRRIRHQVAHEVvAEVGVrPr 516
|
570 580
....*....|....*....|.
gi 71982997 625 DVIQEAPG-LPKTRSGKVTRR 644
Cdd:PRK07768 517 NVVVLGPGsIPKTPSGKLRRA 537
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
525-655 |
3.72e-03 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 40.46 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 525 GYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERinE 604
Cdd:PRK08043 591 GWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEALVLFTTDSELTR--E 668
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 71982997 605 KLVAELKKLvreKIGALAVPDVIQEAPGLPKTRSGKVTRRILRKIAEGSES 655
Cdd:PRK08043 669 KLQQYAREH---GVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSMVDEPEQ 716
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
129-643 |
3.88e-03 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 40.37 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 129 YNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACarigamhsvVFAGFSAESLAarvvdarcrvLVTADGV 208
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFAC---------QYAGLVPVPLP----------LPMGFGG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 209 FRG--AKPIGLKSIADAAAVLASQEDVK-VEAIIMVEHLKRVTKPDGVELPKVDYTDITVIydsemlkcagvdSPvewmd 285
Cdd:PRK09192 113 RESyiAQLRGMLASAQPAAIITPDELLPwVNEATHGNPLLHVLSHAWFKALPEADVALPRP------------TP----- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 286 sEDPLFILYTSGSTGKPKGIQHTTAGYMTYAYATTKYTFDAQEDD--VYWCT--ADCGWITghsyLLYGPLMNGLKgiwy 361
Cdd:PRK09192 176 -DDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDGLKVRPGDrcVSWLPfyHDMGLVG----FLLTPVATQLS---- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 362 egVPTYPT------PSRMWDVTDKYGVTKLYtSPTAARALMALGnqwLESSSRKTL-----KVIGTVGEPI--------- 421
Cdd:PRK09192 247 --VDYLPTrdfarrPLQWLDLISRNRGTISY-SPPFGYELCARR---VNSKDLAELdlscwRVAGIGADMIrpdvlhqfa 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 422 --------NPAAWMWLYkqvGLSN----VSIVD--TYWQTET-------GGHMitclpGATPMKPGAAAMPFFGASPVLL 480
Cdd:PRK09192 321 eafapagfDDKAFMPSY---GLAEatlaVSFSPlgSGIVVEEvdrdrleYQGK-----AVAPGAETRRVRTFVNCGKALP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 481 DAEGRVIEGPGE-------GSLCFdrAWPGMMRGIYGDE--QRFVKTylapfNGYYFTGDGARRdEDGYLWITGRVDDLM 551
Cdd:PRK09192 393 GHEIEIRNEAGMplpervvGHICV--RGPSLMSGYFRDEesQDVLAA-----DGWLDTGDLGYL-LDGYLYITGRAKDLI 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 552 NVSGHLLSTAEIESALVAHEKvaeaavvaaphdIKGSFPYAFVTLN-VGERI-------------NEKLVAELKKLVREK 617
Cdd:PRK09192 465 IINGRNIWPQDIEWIAEQEPE------------LRSGDAAAFSIAQeNGEKIvllvqcrisdeerRGQLIHALAALVRSE 532
|
570 580
....*....|....*....|....*...
gi 71982997 618 IGalaVPDVIQEAP--GLPKTRSGKVTR 643
Cdd:PRK09192 533 FG---VEAAVELVPphSLPRTSSGKLSR 557
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
524-651 |
4.70e-03 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 39.98 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 524 NGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFVTLNVGERIN 603
Cdd:PRK07445 323 QGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISL 402
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 71982997 604 EKLVAELK-KLVREKIGA--LAVpdviqeaPGLPKTRSGKVTRRILRKIAE 651
Cdd:PRK07445 403 EELKTAIKdQLSPFKQPKhwIPV-------PQLPRNPQGKINRQQLQQIAV 446
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
444-641 |
5.09e-03 |
|
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: 39.59 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 444 YWQTETGGhmITCLPGATPMKPGAAAMPffgaSPVL----LDAEGRVIeGPGE-GSLCFDRawPGMMRGIYG-DE---QR 514
Cdd:cd17636 143 YGQTEVMG--LATFAALGGGAIGGAGRP----SPLVqvriLDEDGREV-PDGEvGEIVARG--PTVMAGYWNrPEvnaRR 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982997 515 FVktylapfNGYYFTGDGARRDEDGYLWITGRVDDLMNVSGHLLSTAEIESALVAHEKVAEAAVVAAPHDIKGSFPYAFV 594
Cdd:cd17636 214 TR-------GGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIV 286
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 71982997 595 TLNVGERINEklvAELKKLVREKIGALAVPDVIQEAPGLPKTRSGKV 641
Cdd:cd17636 287 VLKPGASVTE---AELIEHCRARIASYKKPKSVEFADALPRTAGGAD 330
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
128-175 |
5.53e-03 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 40.00 E-value: 5.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 71982997 128 TYNELHAQVVQFSAVLRSHGVKRGDVVALYLPMIPELAVAMLACARIG 175
Cdd:PRK07059 50 TYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAG 97
|
|
| |
