|
Name |
Accession |
Description |
Interval |
E-value |
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
45-660 |
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: 1134.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 45 QRYRELHRRSLEEPREFWGDIAKEFYWKTPCPGPFlqynfDVTKGKIFIEWMKGATTNICYNVLDRivHEKKLGDKVAFY 124
Cdd:cd05966 1 EQYKELYKQSIEDPEEFWGEIAKELDWFKPWDKVL-----DWSKGPPFIKWFEGGKLNISYNCLDR--HLKERGDKVAII 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 125 WEGNEPEETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERIL 204
Cdd:cd05966 74 WEGDEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRIN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 205 DSNCSLLITTDAFYRGEKLVNLKELADEALEKCqekgFPVKCCIVVKHLGRAelvtgdspsqsppikrpcpdvqISWNEG 284
Cdd:cd05966 154 DAQCKLVITADGGYRGGKVIPLKEIVDEALEKC----PSVEKVLVVKRTGGE----------------------VPMTEG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 285 VDLWWHELMQKAGDECEPEWCDAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITG 364
Cdd:cd05966 208 RDLWWHDLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 365 HSYVTYGPLANGATSVLFEGIPTYPDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINP 444
Cdd:cd05966 288 HSYIVYGPLANGATTVMFEGTPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINP 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 445 EAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGAIPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPG 524
Cdd:cd05966 368 EAWMWYYEVIGKERCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPWPG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 525 IMRTVYGNHERFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPH 604
Cdd:cd05966 448 MARTIYGDHERYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPH 527
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387203675 605 PVKGECLYCFVTLCDGHIFSPALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:cd05966 528 DIKGEAIYAFVTLKDGEEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSG 583
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
31-660 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 1058.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 31 PPPEVSRSAHVpSLQRYRELHRRSLEEPREFWGDIAKEFYWKTPcpgpflqYNFDVTKGKIFIEWMKGATTNICYNVLDR 110
Cdd:PRK00174 4 PPAEFAANALI-DMEQYKALYQESVEDPEGFWAEQAKRLDWFKP-------FDTVLDWNAPFIKWFEDGELNVSYNCLDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 111 ivHEKKLGDKVAFYWEGNEPEETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIV 190
Cdd:PRK00174 76 --HLKTRGDKVAIIWEGDDPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 191 FAGFSSESLCERILDSNCSLLITTDAFYRGEKLVNLKELADEALEKCQekgfPVKCCIVVKHLGraelvtGDspsqsppi 270
Cdd:PRK00174 154 FGGFSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALANCP----SVEKVIVVRRTG------GD-------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 271 krpcpdvqISWNEGVDLWWHELMQKAGDECEPEWCDAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKYVFDFHAE 350
Cdd:PRK00174 216 --------VDWVEGRDLWWHELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 351 DVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRA 430
Cdd:PRK00174 288 DVYWCTADVGWVTGHSYIVYGPLANGATTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLS 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 431 SLQVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGAIPMKPGSATFPFFGVAPAILNESGEELEG 510
Cdd:PRK00174 368 SLRLLGSVGEPINPEAWEWYYKVVGGERCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPLPGIQPAVVDEEGNPLEG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 511 EAEGYLVFKQPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVE 590
Cdd:PRK00174 448 GEGGNLVIKDPWPGMMRTIYGDHERFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVA 527
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 591 HKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSPALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:PRK00174 528 HPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSG 597
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
43-660 |
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: 979.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 43 SLQRYRELHRRSLEEPREFWGDIAKE-FYWKTPcPGPFLQYNFDVtkgkiFIEWMKGATTNICYNVLDRivHEKKLGDKV 121
Cdd:TIGR02188 3 NLEQYKELYEESIEDPDKFWAKLARElLDWFKP-FTKVLDWSFPP-----FYKWFVGGELNVSYNCVDR--HLEARPDKV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 122 AFYWEGNEPEETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCE 201
Cdd:TIGR02188 75 AIIWEGDEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALAD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 202 RILDSNCSLLITTDAFYRGEKLVNLKELADEALEKCQEKgfpVKCCIVVKHLGraelvtgdspsqsppikrpcpDVQISW 281
Cdd:TIGR02188 155 RINDAGAKLVITADEGLRGGKVIPLKAIVDEALEKCPVS---VEHVLVVRRTG---------------------NPVVPW 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 282 NEGVDLWWHELMQKAGDECEPEWCDAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGW 361
Cdd:TIGR02188 211 VEGRDVWWHDLMAKASAYCEPEPMDSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGW 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 362 ITGHSYVTYGPLANGATSVLFEGIPTYPDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEP 441
Cdd:TIGR02188 291 ITGHSYIVYGPLANGATTVMFEGVPTYPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSVGEP 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 442 INPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGAIPMKPGSATFPFFGVAPAILNES-GEELEGEAEGYLVFKQ 520
Cdd:TIGR02188 371 INPEAWMWYYKVVGKERCPIVDTWWQTETGGIMITPLPGATPTKPGSATLPFFGIEPAVVDEEgNPVEGPGEGGYLVIKQ 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 521 PWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVV 600
Cdd:TIGR02188 451 PWPGMLRTIYGDHERFVDTYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVV 530
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 601 GHPHPVKGECLYCFVTLCDGHIFSPALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:TIGR02188 531 GIPDDIKGQAIYAFVTLKDGYEPDDELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSG 590
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
31-664 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 845.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 31 PPPEVSRSAHVPSLQRYRELHRRSLEEPREFWGDIAKEFYWKTP-CPGPFLQYNFDVTKGKIFIEWMKGATTNICYNVLD 109
Cdd:PLN02654 16 PSKDFSAQALVSSPQQYMEMYKRSVDDPAGFWSDIASQFYWKQKwEGDEVCSENLDVRKGPISIEWFKGGKTNICYNCLD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 110 RIVhEKKLGDKVAFYWEGNEPEETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSI 189
Cdd:PLN02654 96 RNV-EAGNGDKIAIYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 190 VFAGFSSESLCERILDSNCSLLITTDAFYRGEKLVNLKELADEALEKCQEKGFPVKCCIVVKHlgraelvtgdspsqSPP 269
Cdd:PLN02654 175 VFAGFSAESLAQRIVDCKPKVVITCNAVKRGPKTINLKDIVDAALDESAKNGVSVGICLTYEN--------------QLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 270 IKRpcpdVQISWNEGVDLWWHELMQKAGDECEPEWCDAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKYVFDFHA 349
Cdd:PLN02654 241 MKR----EDTKWQEGRDVWWQDVVPNYPTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 350 EDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSR 429
Cdd:PLN02654 317 TDVYWCTADCGWITGHSYVTYGPMLNGATVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 430 ASLQVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGAIPMKPGSATFPFFGVAPAILNESGEELE 509
Cdd:PLN02654 397 KSLRVLGSVGEPINPSAWRWFFNVVGDSRCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGKEIE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 510 GEAEGYLVFKQPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALV 589
Cdd:PLN02654 477 GECSGYLCVKKSWPGAFRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALV 556
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387203675 590 EHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSPALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGNQKR 664
Cdd:PLN02654 557 SHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMR 631
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
94-660 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 825.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 94 EWMKGATTNICYNVLDRivHEKKLGDKVAFYWEGnEPEETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPEL 173
Cdd:COG0365 1 RWFVGGRLNIAYNCLDR--HAEGRGDKVALIWEG-EDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 174 VVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLITTDAFYRGEKLVNLKELADEALEKCQEkgfpVKCCIVVKHL 253
Cdd:COG0365 78 VIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPS----LEHVIVVGRT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 254 GRAELVTGDspsqsppikrpcpdvqiswnegvdLWWHELMQKAGDECEPEWCDAEDPLFILYTSGSTGKPKGVLHTVGGY 333
Cdd:COG0365 154 GADVPMEGD------------------------LDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGY 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 334 MLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVSRLWNIVEKYKVTKFYTAPTAI 413
Cdd:COG0365 210 LVHAATTAKYVLDLKPGDVFWCTADIGWATGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAI 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 414 RLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETGGHMLTPLPGaIPMKPGSATFPF 493
Cdd:COG0365 290 RALMKAGDEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLPG-LPVKPGSMGKPV 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 494 FGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLN 573
Cdd:COG0365 366 PGYDVAVVDEDGNPVPPGEEGELVIKGPWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVIN 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 574 VSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSPALTEELKKQIREKIGPIATPDYIQNAPG 653
Cdd:COG0365 446 VSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDE 525
|
....*..
gi 1387203675 654 LPKTRSG 660
Cdd:COG0365 526 LPKTRSG 532
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
47-660 |
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: 707.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 47 YRELHRRSLEEPREFWGDIAKEFYWKTPCPGpflQYNFDVTKGKIFIEWMKGATTNICYNVLDRivHEKKLGDKVAFYWE 126
Cdd:cd17634 1 YETKYRQSINDPDTFWGEAGKILDWITPYQK---VKNTSFAPGAPSIKWFEDATLNLAANALDR--HLRENGDRTAIIYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 127 GNEPEETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDS 206
Cdd:cd17634 76 GDDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 207 NCSLLITTDAFYRGEKLVNLKELADEALEKcqeKGFPVKCCIVVKHLGraelvtgdspsqsppikrpcpdVQISWNEGVD 286
Cdd:cd17634 156 SSRLLITADGGVRAGRSVPLKKNVDDALNP---NVTSVEHVIVLKRTG----------------------SDIDWQEGRD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 287 LWWHELMQKAGDECEPEWCDAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHS 366
Cdd:cd17634 211 LWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHS 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 367 YVTYGPLANGATSVLFEGIPTYPDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEA 446
Cdd:cd17634 291 YLLYGPLACGATTLLYEGVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 447 WLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGAIPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIM 526
Cdd:cd17634 371 YEWYWKKIGKEKCPVVDTWWQTETGGFMITPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWPGQT 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 527 RTVYGNHERFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPV 606
Cdd:cd17634 451 RTLFGDHERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAI 530
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1387203675 607 KGECLYCFVTLCDGHIFSPALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:cd17634 531 KGQAPYAYVVLNHGVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSG 584
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
47-660 |
0e+00 |
|
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: 567.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 47 YRELHRRSLEEPREFWGDIAKEFYWKTPcpgpfLQYNFDVTKGKiFIEWMKGATTNICYNVLDRIVhEKKLGDKVAFYWE 126
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARLIDWFKP-----PEKILDNSNPP-FTRWFVGGRLNTCYNALDRHV-EAGRGDQIALIYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 127 GNEPEETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDS 206
Cdd:cd05967 74 SPVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 207 NCSLLITTDAFYRGEKLVNLKELADEALEKCQEKgfPVKCCIVVKHLGRAELVTGdspsqsppikrpcpdvqiswneGVD 286
Cdd:cd05967 154 KPKLIVTASCGIEPGKVVPYKPLLDKALELSGHK--PHHVLVLNRPQVPADLTKP----------------------GRD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 287 LWWHELMQKAGdECEPEWCDAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHS 366
Cdd:cd05967 210 LDWSELLAKAE-PVDCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHS 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 367 YVTYGPLANGATSVLFEGIPT-YPDVSRLWNIVEKYKVTKFYTAPTAIRLLMKF--GDEPVTKHSRASLQVLGTVGEPIN 443
Cdd:cd05967 289 YIVYGPLLHGATTVLYEGKPVgTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKEdpDGKYIKKYDLSSLRTLFLAGERLD 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 444 PEAWLWYHRVVGAqrcPIVDTFWQTETGGHMLTPLPG--AIPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQP 521
Cdd:cd05967 369 PPTLEWAENTLGV---PVIDHWWQTETGWPITANPVGlePLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLP 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 522 W-PGIMRTVYGNHERFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVV 600
Cdd:cd05967 446 LpPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVV 525
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387203675 601 GHPHPVKGECLYCFVTLCDGHIFSPA-LTEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:cd05967 526 GVRDELKGQVPLGLVVLKEGVKITAEeLEKELVALVREQIGPVAAFRLVIFVKRLPKTRSG 586
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
45-660 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 549.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 45 QRYRELHRRSLEEPREFWGDIAKEFYWKTPcPGPFLQYNfdvtkGKIFIEWMKGATTNICYNVLDRivHEKKLGDKVAFY 124
Cdd:PRK10524 2 MSYSEFYQRSIDDPEAFWAEQARRIDWQTP-FTQVLDYS-----NPPFARWFVGGRTNLCHNAVDR--HLAKRPEQLALI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 125 WEGNEPEETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERIL 204
Cdd:PRK10524 74 AVSTETDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARID 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 205 DSNCSLLITTDAFYRGEKLVNLKELADEALEKCQEKgfPVKCCIVVKHLGRAELVtgdspsqsppikrpcpdvqiswnEG 284
Cdd:PRK10524 154 DAKPVLIVSADAGSRGGKVVPYKPLLDEAIALAQHK--PRHVLLVDRGLAPMARV-----------------------AG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 285 VDLWWHELMQKAGDECEP-EWCDAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWIT 363
Cdd:PRK10524 209 RDVDYATLRAQHLGARVPvEWLESNEPSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVV 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 364 GHSYVTYGPLANGATSVLFEGIPTYPDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPIN 443
Cdd:PRK10524 289 GHSYIVYAPLLAGMATIMYEGLPTRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLD 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 444 PEAWLWYHRVVGAqrcPIVDTFWQTETGGHMLTPLPG--AIPMKPGSATFPFFGVAPAILNESGEELEGEAEG-YLVFKQ 520
Cdd:PRK10524 369 EPTASWISEALGV---PVIDNYWQTETGWPILAIARGveDRPTRLGSPGVPMYGYNVKLLNEVTGEPCGPNEKgVLVIEG 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 521 PW-PGIMRTVYGNHERFETTYFKKF-PGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAA 598
Cdd:PRK10524 446 PLpPGCMQTVWGDDDRFVKTYWSLFgRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVA 525
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387203675 599 VVGHPHPVKGECLYCFVTLCDGHIFS-----PALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:PRK10524 526 VVGVKDALKGQVAVAFVVPKDSDSLAdrearLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSG 592
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
93-660 |
8.00e-170 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 497.50 E-value: 8.00e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 93 IEWMKGATTNICYNVLDRIVHEKkLGDKVAFYWEGNEPEETtqITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPE 172
Cdd:PRK04319 34 FSWLETGKVNIAYEAIDRHADGG-RKDKVALRYLDASRKEK--YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 173 LVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLITTDAFYRGEKLVNLKELadealekcqekgfpvkccivvKH 252
Cdd:PRK04319 111 LYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERKPADDLPSL---------------------KH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 253 LgraeLVTGDSPSQSPPIkrpcpdvqiswnegVDLWwhELMQKAGDECEPEWCDAEDPLFILYTSGSTGKPKGVLHtVGG 332
Cdd:PRK04319 170 V----LLVGEDVEEGPGT--------------LDFN--ALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLH-VHN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 333 YMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGiptYPDVSRLWNIVEKYKVTKFYTAPTA 412
Cdd:PRK04319 229 AMLQHYQTGKYVLDLHEDDVYWCTADPGWVTGTSYGIFAPWLNGATNVIDGG---RFSPERWYRILEDYKVTVWYTAPTA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 413 IRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTETGGHMLTPLPgAIPMKPGSATFP 492
Cdd:PRK04319 306 IRMLMGAGDDLVKKYDLSSLRHILSVGEPLNPEVVRWGMKVFGL---PIHDNWWMTETGGIMIANYP-AMDIKPGSMGKP 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 493 FFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFETtYFKkfPGYYVTGDGCRRDKDGYYWITGRIDDML 572
Cdd:PRK04319 382 LPGIEAAIVDDQGNELPPNRMGNLAIKKGWPSMMRGIWNNPEKYES-YFA--GDWYVSGDSAYMDEDGYFWFQGRVDDVI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 573 NVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSPALTEELKKQIREKIGPIATPDYIQNAP 652
Cdd:PRK04319 459 KTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFKD 538
|
....*...
gi 1387203675 653 GLPKTRSG 660
Cdd:PRK04319 539 KLPKTRSG 546
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
44-658 |
3.01e-166 |
|
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: 489.69 E-value: 3.01e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 44 LQRYRELHRRSLEEPREFWGDIAKEF-YWKTPCPGPFLqynfDVTKGKIFIEWMKGATTNICYNVLDRivHEKKLGDKVA 122
Cdd:cd05968 6 IPDLEAFLERSAEDNAWFWGEFVKDVgIEWYEPPYQTL----DLSGGKPWAAWFVGGRMNIVEQLLDK--WLADTRTRPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 123 FYWEGnEPEETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCER 202
Cdd:cd05968 80 LRWEG-EDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 203 ILDSNCSLLITTDAFYRGEKLVNLKELADEALEKCqekgFPVKCCIVVKHLGRAELvtgdspsqsppikrpcpdvqisWN 282
Cdd:cd05968 159 LQDAEAKALITADGFTRRGREVNLKEEADKACAQC----PTVEKVVVVRHLGNDFT----------------------PA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 283 EGVDLWWHELMQKAGDECEPewCDAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKYVFDFHAED-VFWCTaDIGW 361
Cdd:cd05968 213 KGRDLSYDEEKETAGDGAER--TESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDlLTWFT-DLGW 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 362 ITGhSYVTYGPLANGATSVLFEGIPTYPDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEP 441
Cdd:cd05968 290 MMG-PWLIFGGLILGATMVLYDGAPDHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEP 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 442 INPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPgAIPMKPGSATFPFFGVAPAILNESGEELEGEAEGyLVFKQP 521
Cdd:cd05968 369 WNPEPWNWLFETVGKGRNPIINYSGGTEISGGILGNVL-IKPIKPSSFNGPVPGMKADVLDESGKPARPEVGE-LVLLAP 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 522 WPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVG 601
Cdd:cd05968 447 WPGMTRGFWRDEDRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIG 526
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1387203675 602 HPHPVKGECLYCFVTLCDGHIFSPALTEELKKQIREKIGPIATPDYIQNAPGLPKTR 658
Cdd:cd05968 527 VPHPVKGEAIVCFVVLKPGVTPTEALAEELMERVADELGKPLSPERILFVKDLPKTR 583
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
137-664 |
2.38e-130 |
|
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: 391.87 E-value: 2.38e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 137 TYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLITTDA 216
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 217 FYRgeklvnlkeladealekcqekgfpvkccivvkhlgraelvtgdspsqsppiKRpcpdvqiswnegvdlwwhelmqka 296
Cdd:cd05969 82 LYE---------------------------------------------------RT------------------------ 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 297 gdecepewcDAEDPLFILYTSGSTGKPKGVLHtVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANG 376
Cdd:cd05969 87 ---------DPEDPTLLHYTSGTTGTPKGVLH-VHDAMIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNG 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 377 ATSVLFEGiptYPDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGA 456
Cdd:cd05969 157 VTNVVYEG---RFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGV 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 457 qrcPIVDTFWQTETGGHMLTPLPGaIPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERF 536
Cdd:cd05969 234 ---PIHDTWWQTETGSIMIANYPC-MPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPGWPSMFRGIWNDEERY 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 537 ETtYFKKfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVT 616
Cdd:cd05969 310 KN-SFID--GWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFIS 386
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1387203675 617 LCDGHIFSPALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGNQKR 664
Cdd:cd05969 387 LKEGFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMR 434
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
115-575 |
1.40e-106 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 329.66 E-value: 1.40e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 115 KKLGDKVAFywegnEPEETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGF 194
Cdd:pfam00501 6 ARTPDKTAL-----EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 195 SSESLCERILDSNCSLLITTDAFYrgeklvnlkelaDEALEKCQEKGFPVKCCIVVKHLGRAELvtgdspsqsppikrpc 274
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALK------------LEELLEALGKLEVVKLVLVLDRDPVLKE---------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 275 pdvqiswnegvDLWWHELMQKAGDECEPEWCDAEDPLFILYTSGSTGKPKGVLHTVgGYMLYVATTFKYV----FDFHAE 350
Cdd:pfam00501 133 -----------EPLPEEAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTH-RNLVANVLSIKRVrprgFGLGPD 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 351 DVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTyPDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSra 430
Cdd:pfam00501 201 DRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLS-- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 431 SLQVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETGGHMLTPLPGAIPM-KPGSATFPFFGVAPAILNESGEELE 509
Cdd:pfam00501 278 SLRLVLSGGAPLPPELARRFRELFG---GALVNGYGLTETTGVVTTPLPLDEDLrSLGSVGRPLPGTEVKIVDDETGEPV 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387203675 510 GEAEG-YLVFKQpwPGIMRTVYGNHERFETTYFKKfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVS 575
Cdd:pfam00501 355 PPGEPgELCVRG--PGVMKGYLNDPELTAEAFDED--GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
137-665 |
2.36e-103 |
|
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: 321.59 E-value: 2.36e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 137 TYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLIttda 216
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 217 fyrgeklvnlkeladealekcqekgfpvkccivvkhlgraelvtgdspsqsppikrpcpdvqiswnegvdlwwhelmqka 296
Cdd:cd05972 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 297 gdecepewCDAEDPLFILYTSGSTGKPKGVLHTVGgYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANG 376
Cdd:cd05972 78 --------TDAEDPALIYFTSGTTGLPKGVLHTHS-YPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLG 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 377 ATSVLFEGIPTypDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEpvtKHSRASLQVLGTVGEPINPEAWLWYHRVVGA 456
Cdd:cd05972 149 ATVFVYEGPRF--DAERILELLERYGVTSFCGPPTAYRMLIKQDLS---SYKFSHLRLVVSAGEPLNPEVIEWWRAATGL 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 457 qrcPIVDTFWQTETGgHMLTPLPGaIPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERF 536
Cdd:cd05972 224 ---PIRDGYGQTETG-LTVGNFPD-MPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPPPGLFLGYVGDPEKT 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 537 ETTYFKkfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVT 616
Cdd:cd05972 299 EASIRG---DYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVV 375
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1387203675 617 LCDGHIFSPALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGNQKRV 665
Cdd:cd05972 376 LTSGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRV 424
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
309-660 |
3.70e-84 |
|
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: 268.38 E-value: 3.70e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 309 DPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKYvFDFHAEDVFWCTADIGWItGHSYVTYGPLANGATSVLFEGipty 388
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS-GGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 389 PDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPvtKHSRASLQVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQT 468
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKAPESA--GYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 469 ETGGHMLTPLPGAIPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPgiMRtVYGNHErfETTYFKKFPGYY 548
Cdd:cd04433 150 ETGGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSV--MK-GYWNNP--EATAAVDEDGWY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 549 VTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHifsPALT 628
Cdd:cd04433 225 RTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGA---DLDA 301
|
330 340 350
....*....|....*....|....*....|..
gi 1387203675 629 EELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:cd04433 302 EELRAHVRERLAPYKVPRRVVFVDALPRTASG 333
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
40-665 |
1.59e-83 |
|
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: 275.69 E-value: 1.59e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 40 HVPSLQRYRELHRRSLEEPREFWGDIAKefYWKTPCPGPflqYNFDVTKGKIF--IEWMKGATTNICYNVLDRIVHEkkl 117
Cdd:cd05943 12 HGLSLADYAALHRWSVDDPGAFWAAVWD--FSGVRGSKP---YDVVVVSGRIMpgARWFPGARLNYAENLLRHADAD--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 118 gDKVAFYweGNEPEETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSE 197
Cdd:cd05943 84 -DPAAIY--AAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 198 SLCERILDSNCSLLITTDAFYRGEKLVNLkeladeaLEKCQE--KGFPVKCCIVVKHLGRAElvtgdspsqsPPIKRPCP 275
Cdd:cd05943 161 GVLDRFGQIEPKVLFAVDAYTYNGKRHDV-------REKVAElvKGLPSLLAVVVVPYTVAA----------GQPDLSKI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 276 DVQISWNEGvdlwwheLMQKAGDECEPEWCDAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKYVFDFHAEDVFWC 355
Cdd:cd05943 224 AKALTLEDF-------LATGAAGELEFEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRLFY 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 356 TADIGWITGHSYVTYgpLANGATSVLFEGIPTYPDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVL 435
Cdd:cd05943 297 YTTCGWMMWNWLVSG--LAVGATIVLYDGSPFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 436 GTVGEPINPEAWLWYHRVVGAqrcpivDTFWQTETGGhmlTPLPGA-------IPMKPGSATFPFFGVAPAILNESGEEL 508
Cdd:cd05943 375 LSTGSPLKPESFDYVYDHIKP------DVLLASISGG---TDIISCfvggnplLPVYRGEIQCRGLGMAVEAFDEEGKPV 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 509 EGEAEGyLVFKQPWPGiMRTVYGNHE---RFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVE 585
Cdd:cd05943 446 WGEKGE-LVCTKPFPS-MPVGFWNDPdgsRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIY 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 586 SALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSPALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGnqKRV 665
Cdd:cd05943 524 RVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSG--KKV 601
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
136-664 |
1.18e-77 |
|
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: 254.75 E-value: 1.18e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 136 ITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERiLDSNCSLLITTD 215
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHR-LRTSGARLVVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 216 AFYRgeklvnlkeladealekcqekgfpvkccivvkhlgraelvtgdspsqsppikrpcpdvqiswnegvdlwwHELmqk 295
Cdd:cd05973 80 AANR----------------------------------------------------------------------HKL--- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 296 agdecepewcdAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATtFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLAN 375
Cdd:cd05973 87 -----------DSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAY-LRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLAL 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 376 GATSVLFEGIPTYPDVsrlWNIVEKYKVTKFYTAPTAIRLLMKFGdEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVG 455
Cdd:cd05973 155 GHPTILLEGGFSVEST---WRVIERLGVTNLAGSPTAYRLLMAAG-AEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALG 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 456 AqrcPIVDTFWQTETGGHMLTPLPGAIPMKPGSATFPFFGVAPAILNESGeelegeaegylvfKQPWPGIMRTVYGNHER 535
Cdd:cd05973 231 V---PIHDHYGQTELGMVLANHHALEHPVHAGSAGRAMPGWRVAVLDDDG-------------DELGPGEPGRLAIDIAN 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 536 FETTYFKKFP---------GYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPV 606
Cdd:cd05973 295 SPLMWFRGYQlpdtpaidgGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPE 374
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387203675 607 KGECLYCFVTLCDGHIFSPALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGNQKR 664
Cdd:cd05973 375 RTEVVKAFVVLRGGHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQR 432
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
118-660 |
9.57e-77 |
|
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: 252.81 E-value: 9.57e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 118 GDKVAFYWEGnepeetTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSE 197
Cdd:COG0318 13 PDRPALVFGG------RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 198 SLcERIL-DSNCSLLITtdafyrgeklvnlkeladealekcqekgfpvkccivvkhlgraelvtgdspsqsppikrpcpd 276
Cdd:COG0318 87 EL-AYILeDSGARALVT--------------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 277 vqiswnegvdlwwhelmqkagdecepewcdaedpLFILYTSGSTGKPKGVLHTVGGyMLYVATTFKYVFDFHAEDVFWCT 356
Cdd:COG0318 103 ----------------------------------ALILYTSGTTGRPKGVMLTHRN-LLANAAAIAAALGLTPGDVVLVA 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 357 ADIGWITGHSYVTYGPLANGATSVLfegiPTYPDVSRLWNIVEKYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLG 436
Cdd:COG0318 148 LPLFHVFGLTVGLLAPLLAGATLVL----LPRFDPERVLELIERERVTVLFGVPTMLARLLR--HPEFARYDLSSLRLVV 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 437 TVGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETGGHMLTPLPGAIPMKPGSATFPFFGVAPAILNESGEELEGEAEGYL 516
Cdd:COG0318 222 SGGAPLPPELLERFEERFG---VRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEI 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 517 VFKQPWpgIMRTVYGNHERFEttyfKKFP-GYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVA 595
Cdd:COG0318 299 VVRGPN--VMKGYWNDPEATA----EAFRdGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVA 372
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387203675 596 EAAVVGHPHPVKGECLYCFVTLCDGHIFSPaltEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:COG0318 373 EAAVVGVPDEKWGERVVAFVVLRPGAELDA---EELRAFLRERLARYKVPRRVEFVDELPRTASG 434
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
57-664 |
3.52e-76 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 256.59 E-value: 3.52e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 57 EPREFWGDIAKEF-YWKTpcpgpflQYNFDVTKGKIFIEWMKGATTNICYNVLDRIVHEKKLGDKVAFYWEGNEPEETTQ 135
Cdd:PTZ00237 20 NPESFWDEVAKKYvHWDK-------MYDKVYSGDEIYPDWFKGGELNTCYNVLDIHVKNPLKRDQDALIYECPYLKKTIK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 136 ITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLITTD 215
Cdd:PTZ00237 93 LTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTN 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 216 AFYRGEKLVNLKELADEALEKCQEKgfPVKcciVVKHLgRAElVTGDSPSQSPPIKRPCPDVqISWNEGVDLWwHELMQK 295
Cdd:PTZ00237 173 YGILNDEIITFTPNLKEAIELSTFK--PSN---VITLF-RND-ITSESDLKKIETIPTIPNT-LSWYDEIKKI-KENNQS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 296 AGDECEPewCDAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVtYGPLAN 375
Cdd:PTZ00237 244 PFYEYVP--VESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFL-YGSLSL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 376 GATSVLFEGIPTYPDVSR--LWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSR---ASLQVLGTVGEPINPEAWLWY 450
Cdd:PTZ00237 321 GNTFVMFEGGIIKNKHIEddLWNTIEKHKVTHTLTLPKTIRYLIKTDPEATIIRSKydlSNLKEIWCGGEVIEESIPEYI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 451 HRVVGAqRCPIVdtFWQTETGghMLTPLPGAIPMKPGSAT-FPFFGVAPAILNESGEELEGEAEGYLVFKQPWP-GIMRT 528
Cdd:PTZ00237 401 ENKLKI-KSSRG--YGQTEIG--ITYLYCYGHINIPYNATgVPSIFIKPSILSEDGKELNVNEIGEVAFKLPMPpSFATT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 529 VYGNHERFETTyFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKG 608
Cdd:PTZ00237 476 FYKNDEKFKQL-FSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCY 554
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 609 ECLYCFVTL----CDGHIFSPALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGNQKR 664
Cdd:PTZ00237 555 NVPIGLLVLkqdqSNQSIDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
29-665 |
2.81e-71 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 243.55 E-value: 2.81e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 29 WSPPPEVSRSAHVPSLQR------------YRELHRRSLEEPREFWGDIAkEFY---WKTPCPgpflqynfDVTKGKIFI 93
Cdd:PRK03584 6 WTPSAERIAASRMTAFIRwlaarrglsfddYAALWRWSVEDLEAFWQSVW-DFFgviGSTPYT--------VVLAGRRMP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 94 --EWMKGATTNICYNVLdrivhEKKLGDKVAFYWEGnEPEETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIP 171
Cdd:PRK03584 77 gaRWFPGARLNYAENLL-----RHRRDDRPAIIFRG-EDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 172 ELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLITTDAFYRGEKLVN----LKELADE--ALEKcqekgfpvk 245
Cdd:PRK03584 151 ETVVAMLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDGYRYGGKAFDrrakVAELRAAlpSLEH--------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 246 cCIVVKHLGraelvtgdspsqSPPIKRPCPDVQIswnegvdlwWHELMQKAGD-ECEPEWCDAEDPLFILYTSGSTGKPK 324
Cdd:PRK03584 222 -VVVVPYLG------------PAAAAAALPGALL---------WEDFLAPAEAaELEFEPVPFDHPLWILYSSGTTGLPK 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 325 GVLHTVGGYMLYVATTFKYVFDFHAED-VFWCTAdIGWITGHSYVtyGPLANGATSVLFEGIPTYPDVSRLWNIVEKYKV 403
Cdd:PRK03584 280 CIVHGHGGILLEHLKELGLHCDLGPGDrFFWYTT-CGWMMWNWLV--SGLLVGATLVLYDGSPFYPDPNVLWDLAAEEGV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 404 TKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcpivDTFWQTETGG-HMLTPLPGAI 482
Cdd:PRK03584 357 TVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPLPPEGFDWVYEHVKA------DVWLASISGGtDICSCFVGGN 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 483 PMKP---GSATFPFFGVAPAILNESGEELEGEAEGyLVFKQPWPGiMrTVY----GNHERFETTYFKKFPGYYVTGDGCR 555
Cdd:PRK03584 431 PLLPvyrGEIQCRGLGMAVEAWDEDGRPVVGEVGE-LVCTKPFPS-M-PLGfwndPDGSRYRDAYFDTFPGVWRHGDWIE 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 556 RDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSPALTEELKKQI 635
Cdd:PRK03584 508 ITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDDALRARIRTTI 587
|
650 660 670
....*....|....*....|....*....|
gi 1387203675 636 REKIGPIATPDYIQNAPGLPKTRSGnqKRV 665
Cdd:PRK03584 588 RTNLSPRHVPDKIIAVPDIPRTLSG--KKV 615
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
39-666 |
7.58e-64 |
|
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of IPP biosynthesis. Most bacteria do not use this pathway, but rather the deoxyxylulose pathway. [Central intermediary metabolism, Other]
Pssm-ID: 273507 [Multi-domain] Cd Length: 652 Bit Score: 223.60 E-value: 7.58e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 39 AHVPSLQRYRELHRRSLEEPREFWGDIAKEFywKTPCPGPFLQYnFDVTKGkIFIEWMKGATTNICYNVLdrivhEKKLG 118
Cdd:TIGR01217 29 HHGAAEGGYDALHRWSVDELDTFWKAVWEWF--DVRFSTPCARV-VDDRTM-PGAQWFPGARLNYAENLL-----RAAGT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 119 DKVAFYWegNEPEETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSES 198
Cdd:TIGR01217 100 EPALLYV--DETHEPAPVTWAELRRQVASLAAALRALGVRPGDRVSGYLPNIPQAVVAMLATASVGAIWSSCSPDFGARG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 199 LCERILDSNCSLLITTDAFYRGEKlvnlkelADEALEKCQEkgfpvkcciVVKHLGRAELVT-----GDSPSQSPPIkrp 273
Cdd:TIGR01217 178 VLDRFQQIEPKLLFTVDGYRYNGK-------EHDRRDKVAE---------VRKELPTLRAVVhipylGPRETEAPKI--- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 274 cpdvqiswnEGvDLWWHELMQKAGD-ECEPEWCDAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKYVFDFHAEDV 352
Cdd:TIGR01217 239 ---------DG-ALDLEDFTAAAQAaELVFEQLPFDHPLWILFSSGTTGLPKCIVHSAGGTLVQHLKEHGLHCDLGPGDR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 353 FWCTADIGWITGHSYVTygPLANGATSVLFEGIPTYPDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASL 432
Cdd:TIGR01217 309 LFYYTTTGWMMWNWLVS--GLATGATLVLYDGSPGFPATNVLWDIAERTGATLFGTSAKYVMACRKAGVHPARTHDLSAL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 433 QVLGTVGEPINPEAWLWYHRVVGAqrcpivDTFWQTETGG-HMLTPLPGAIPMKP---GSATFPFFGVAPAILNESGEEL 508
Cdd:TIGR01217 387 QCVASTGSPLPPDGFRWVYDEIKA------DVWLASISGGtDICSCFAGANPTLPvhiGEIQAPGLGTAVQSWDPEGKPV 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 509 EGEAEGyLVFKQPWPGiMRTVYGNHE---RFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVE 585
Cdd:TIGR01217 461 TGEVGE-LVCTNPMPS-MPIRFWNDPdgsKYRDAYFDTYPGVWRHGDWITLTPRGGIVIHGRSDSTLNPQGVRMGSAEIY 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 586 SALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSPALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGnqKRV 665
Cdd:TIGR01217 539 NAVERLDEVRESLCIGQEQPDGGYRVVLFVHLAPGATLDDALLDRIKRTIRAGLSPRHVPDEIIEVPGIPHTLTG--KRV 616
|
.
gi 1387203675 666 D 666
Cdd:TIGR01217 617 E 617
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
133-664 |
1.19e-60 |
|
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: 209.60 E-value: 1.19e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 133 TTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLI 212
Cdd:cd05971 4 PEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 213 Ttdafyrgeklvnlkeladealekcqekgfpvkccivvkhlgraelvtgdspsqsppikrpcpdvqiswnegvdlwwhel 292
Cdd:cd05971 84 T------------------------------------------------------------------------------- 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 293 mqkagDEcepewcdAEDPLFILYTSGSTGKPKGVLHT-------VGGYMLYvattfkyvFDF--HAEDVFWCTADIGWIt 363
Cdd:cd05971 85 -----DG-------SDDPALIIYTSGTTGPPKGALHAhrvllghLPGVQFP--------FNLfpRDGDLYWTPADWAWI- 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 364 ghsyvtyGPLANGATSVLFEGIP------TYPDVSRLWNIVEKYKVTKFYTAPTAIRLlMKFGDEPVtKHSRASLQVLGT 437
Cdd:cd05971 144 -------GGLLDVLLPSLYFGVPvlahrmTKFDPKAALDLMSRYGVTTAFLPPTALKM-MRQQGEQL-KHAQVKLRAIAT 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 438 VGEPINPEAWLWYHRVVGAqrcPIVDTFWQTEtGGHMLTPLPGAIPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLV 517
Cdd:cd05971 215 GGESLGEELLGWAREQFGV---EVNEFYGQTE-CNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIA 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 518 FKQPWPGIMRTVYGNHERFEttyfKKFPG-YYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAE 596
Cdd:cd05971 291 VELPDPVAFLGYWNNPSATE----KKMAGdWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLM 366
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387203675 597 AAVVGHPHPVKGECLYCFVTLCDGHIFSPALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGNQKR 664
Cdd:cd05971 367 AAVVGIPDPIRGEIVKAFVVLNPGETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRR 434
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
102-665 |
1.01e-57 |
|
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: 203.85 E-value: 1.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 102 NICYNVLDRIVHEKKLGDKV---AFYWEGNEPEETtQITYRELLVQVCRFSNVLRKQ-GICKGDRVAIYMPMIPELVVAM 177
Cdd:cd05928 6 NFASDVLDQWADKEKAGKRPpnpALWWVNGKGDEV-KWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 178 LACARLGAlhsivfagfsseslcerILDSNCSLLITTDAFYRgeklvnlkeladeaLEKCQEKgfpvkcCIVvkhlgrae 257
Cdd:cd05928 85 VACIRTGL-----------------VFIPGTIQLTAKDILYR--------------LQASKAK------CIV-------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 258 lvTGDSPSQS-PPIKRPCPDVQI-------SWNEGVDLwwHELMQKAGDECEPEWCDAEDPLFILYTSGSTGKPKGVLHT 329
Cdd:cd05928 120 --TSDELAPEvDSVASECPSLKTkllvsekSRDGWLNF--KELLNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHS 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 330 VGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATsVLFEGIPTYpDVSRLWNIVEKYKVTKFYTA 409
Cdd:cd05928 196 HSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGAC-VFVHHLPRF-DPLVILKTLSSYPITTFCGA 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 410 PTAIRLLMKfgdEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQrcpIVDTFWQTETGghMLTPLPGAIPMKPGS- 488
Cdd:cd05928 274 PTVYRMLVQ---QDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLD---IYEGYGQTETG--LICANFKGMKIKPGSm 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 489 -ATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVY-GNHERFETTYFKKFpgyYVTGDGCRRDKDGYYWITG 566
Cdd:cd05928 346 gKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYvDNPEKTAATIRGDF---YLTGDRGIMDEDGYFWFMG 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 567 RIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFS--PALTEELKKQIREKIGPIAT 644
Cdd:cd05928 423 RADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSHdpEQLTKELQQHVKSVTAPYKY 502
|
570 580
....*....|....*....|.
gi 1387203675 645 PDYIQNAPGLPKTRSGNQKRV 665
Cdd:cd05928 503 PRKVEFVQELPKTVTGKIQRN 523
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
114-664 |
1.28e-57 |
|
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: 202.98 E-value: 1.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 114 EKKLGDKVAFYwegnepEETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALhSIVFAG 193
Cdd:cd05959 14 NEGRGDKTAFI------DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIV-PVPVNT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 194 FSSESLCERIL-DSNCSLLITTDAFYrgeklvnlkELADEALEKcqekgfpvkccivVKHLGRAELVTGDSPSQSPpikr 272
Cdd:cd05959 87 LLTPDDYAYYLeDSRARVVVVSGELA---------PVLAAALTK-------------SEHTLVVLIVSGGAGPEAG---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 273 pcpdvqiswnegvDLWWHELMQKAGDECEPEWCDAEDPLFILYTSGSTGKPKGVLHTVGGyMLYVATTF-KYVFDFHAED 351
Cdd:cd05959 141 -------------ALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHAD-IYWTAELYaRNVLGIREDD 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 352 VFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTyPDvsRLWNIVEKYKVTKFYTAPTAIRLLMKfgDEPVTKHSRAS 431
Cdd:cd05959 207 VCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERPT-PA--AVFKRIRRYRPTVFFGVPTLYAAMLA--APNLPSRDLSS 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 432 LQVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETGGHMLTPLPGAIpmKPGSATFPFFGVAPAILNESGEELEGE 511
Cdd:cd05959 282 LRLCVSAGEALPAEVGERWKARFG---LDILDGIGSTEMLHIFLSNRPGRV--RYGTTGKPVPGYEVELRDEDGGDVADG 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 512 AEGYLVFKQPWPGIMrtVYGNHERFETTyfkkFPGYYV-TGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVE 590
Cdd:cd05959 357 EPGELYVRGPSSATM--YWNNRDKTRDT----FQGEWTrTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQ 430
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387203675 591 HKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSPALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGNQKR 664
Cdd:cd05959 431 HPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQR 504
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
102-666 |
1.68e-56 |
|
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: 200.80 E-value: 1.68e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 102 NICYNVLDRIVHEKKlgDKVAFYWeGNEPEETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACA 181
Cdd:cd05970 17 NFAYDVVDAMAKEYP--DKLALVW-CDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 182 RLGALHSIVFAGFSSESLCERILDSNCSLLITTDafyrgEKlvNLKELADEALEKCQEKGFPVKCcivvkhlgraelvtG 261
Cdd:cd05970 94 KLGAIAIPATHQLTAKDIVYRIESADIKMIVAIA-----ED--NIPEEIEKAAPECPSKPKLVWV--------------G 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 262 DspsqsppikrPCPDVQISWNEgvdlwwhELMQKAGDECEPEWCDA---EDPLFILYTSGSTGKPKGVLHtVGGYMLYVA 338
Cdd:cd05970 153 D----------PVPEGWIDFRK-------LIKNASPDFERPTANSYpcgEDILLVYFSSGTTGMPKMVEH-DFTYPLGHI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 339 TTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDvsRLWNIVEKYKVTKFYTAPTAIRLLMK 418
Cdd:cd05970 215 VTAKYWQNVREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDPK--ALLEKLSKYGVTTFCAPPTIYRFLIR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 419 fgdEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQrcpIVDTFWQTETGGHMLTpLPGAIPmKPGSATFPFFGVAP 498
Cdd:cd05970 293 ---EDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIK---LMEGFGQTETTLTIAT-FPWMEP-KPGSMGKPAPGYEI 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 499 AILNESGEELEGEAEGYLVF----KQPWpGIMRTVYGNHERFETTYFKkfpGYYVTGDGCRRDKDGYYWITGRIDDMLNV 574
Cdd:cd05970 365 DLIDREGRSCEAGEEGEIVIrtskGKPV-GLFGGYYKDAEKTAEVWHD---GYYHTGDAAWMDEDGYLWFVGRTDDLIKS 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 575 SGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSPALTEELKKQIREKIGPIATPDYIQNAPGL 654
Cdd:cd05970 441 SGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDEL 520
|
570
....*....|..
gi 1387203675 655 PKTRSGNQKRVD 666
Cdd:cd05970 521 PKTISGKIRRVE 532
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
136-664 |
4.43e-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: 186.13 E-value: 4.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 136 ITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLITtd 215
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVT-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 216 afyrgeklvnlkeladealekcqekgfpvkccivvkhlgraelvtgdspsqsppikrpcpdvqiswnegvdlwwhelmqk 295
Cdd:cd05919 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 296 agdecepewcDAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKYVFDFHAEDVFWCTADI--GWITGHSyvTYGPL 373
Cdd:cd05919 89 ----------SADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNS--LWFPL 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 374 ANGATSVLFegiPTYPDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPvtKHSRASLQVLGTVGEPInPEAwLWYhRV 453
Cdd:cd05919 157 AVGASAVLN---PGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGS--PDALRSLRLCVSAGEAL-PRG-LGE-RW 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 454 VGAQRCPIVDTFWQTETGGHMLTPLPGAIpmKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMrtvYGNh 533
Cdd:cd05919 229 MEHFGGPILDGIGATEVGHIFLSNRPGAW--RLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVG---YWN- 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 534 eRFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYC 613
Cdd:cd05919 303 -NPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTA 381
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1387203675 614 FVTLCDGHIFSPALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGNQKR 664
Cdd:cd05919 382 FVVLKSPAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQR 432
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
118-660 |
1.33e-51 |
|
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: 184.74 E-value: 1.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 118 GDKVAFYWEGNEpeettqITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSE 197
Cdd:cd17631 9 PDRTALVFGGRS------LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 198 SLCERILDSNCSLLIttdafyrgeklvnlkeladealekcqekgfpvkccivvkhlgraelvtgdspsqsppikrpcpdv 277
Cdd:cd17631 83 EVAYILADSGAKVLF----------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 278 qiswnegvdlwwhelmqkagdecepewcdaEDPLFILYTSGSTGKPKGVLHTVGGyMLYVATTFKYVFDFHAEDVFWCTA 357
Cdd:cd17631 98 ------------------------------DDLALLMYTSGTTGRPKGAMLTHRN-LLWNAVNALAALDLGPDDVLLVVA 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 358 DIGWITGHSYVTYGPLANGATSVLFEGiptyPDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSraSLQVLGT 437
Cdd:cd17631 147 PLFHIGGLGVFTLPTLLRGGTVVILRK----FDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLS--SLRAVIY 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 438 VGEPInPEAWLwyhRVVGAQRCPIVDTFWQTETGGHMLTPLPGAIPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLV 517
Cdd:cd17631 221 GGAPM-PERLL---RALQARGVKFVQGYGMTETSPGVTFLSPEDHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIV 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 518 FKQPwpGIMRTVYGNHERFETTYFKkfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEA 597
Cdd:cd17631 297 VRGP--HVMAGYWNRPEATAAAFRD---GWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEV 371
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387203675 598 AVVGHPHPVKGECLYCFVTLCDGHIFSPaltEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:cd17631 372 AVIGVPDEKWGEAVVAVVVPRPGAELDE---DELIAHCRERLARYKIPKSVEFVDALPRNATG 431
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
130-664 |
9.18e-51 |
|
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: 183.67 E-value: 9.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 130 PEETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLcERILDSNCS 209
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEF-EFYLADLGS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 210 LLITTDAFYRGEKLVNLKELADEALEKcqekGFPVKCCIVVkhlGRAELVTGDSPSQSPPIKRPCPDvqiswnegvdlww 289
Cdd:cd05926 88 KLVLTPKGELGPASRAASKLGLAILEL----ALDVGVLIRA---PSAESLSNLLADKKNAKSEGVPL------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 290 helmqkagdecepewcdAEDPLFILYTSGSTGKPKGVLHT---VGGYMLYVATTFKYVFD---------FHaedvfwcta 357
Cdd:cd05926 148 -----------------PDDLALILHTSGTTGRPKGVPLThrnLAASATNITNTYKLTPDdrtlvvmplFH--------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 358 digwITGHSYVTYGPLANGATSVlfegIPTYPDVSRLWNIVEKYKVTkFYTA-PTAIRLLMKFgDEPVTKHSRASLQVLG 436
Cdd:cd05926 202 ----VHGLVASLLSTLAAGGSVV----LPPRFSASTFWPDVRDYNAT-WYTAvPTIHQILLNR-PEPNPESPPPKLRFIR 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 437 TVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTETGGHM-LTPLPgAIPMKPGSATFPFfGVAPAILNESGEELEGEAEGY 515
Cdd:cd05926 272 SCSASLPPAVLEALEATFGA---PVLEAYGMTEAAHQMtSNPLP-PGPRKPGSVGKPV-GVEVRILDEDGEILPPGVVGE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 516 LVFKQPwpGIMRTVYGNHE-RFEttYFKKFpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAV 594
Cdd:cd05926 347 ICLRGP--NVTRGYLNNPEaNAE--AAFKD-GWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAV 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 595 AEAAVVGHPHPVKGECLYCFVTLCDGHifsPALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGNQKR 664
Cdd:cd05926 422 LEAVAFGVPDEKYGEEVAAAVVLREGA---SVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQR 488
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
105-665 |
1.33e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 183.85 E-value: 1.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 105 YNVLDRIV--HEKKLGDKVAFYWEGNEpeettqITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACAR 182
Cdd:PRK06187 5 PLTIGRILrhGARKHPDKEAVYFDGRR------TTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 183 LGA-LHSI-VFagFSSESLcerildsncsLLITTDAfyrGEKLVnlkeLADEALEKcqekgfpvkccIVVKHLGRAE--- 257
Cdd:PRK06187 79 IGAvLHPInIR--LKPEEI----------AYILNDA---EDRVV----LVDSEFVP-----------LLAAILPQLPtvr 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 258 --LVTGDSPSQSPPikrpcPDVQIswnegvdlwWHELMQKAGDEcePEWCDAE--DPLFILYTSGSTGKPKGV------- 326
Cdd:PRK06187 129 tvIVEGDGPAAPLA-----PEVGE---------YEELLAAASDT--FDFPDIDenDAAAMLYTSGTTGHPKGVvlshrnl 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 327 -LHTVGGymlyvattfKYVFDFHAEDVF-----------WctadiGWitghsyvTYGPLANGATSVlfegIPTYPDVSRL 394
Cdd:PRK06187 193 fLHSLAV---------CAWLKLSRDDVYlvivpmfhvhaW-----GL-------PYLALMAGAKQV----IPRRFDPENL 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 395 WNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGtvGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETGG-- 472
Cdd:PRK06187 248 LDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYG--GAALPPALLREFKEKFG---IDLVQGYGMTETSPvv 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 473 HMLTP---LPGAIPmKPGSATFPFFGVAPAILNESGEELEGEAEGY--LVFKQPWpgIMRTVYGNHERFETTYFKkfpGY 547
Cdd:PRK06187 323 SVLPPedqLPGQWT-KRRSAGRPLPGVEARIVDDDGDELPPDGGEVgeIIVRGPW--LMQGYWNRPEATAETIDG---GW 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 548 YVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSPal 627
Cdd:PRK06187 397 LHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDA-- 474
|
570 580 590
....*....|....*....|....*....|....*....
gi 1387203675 628 tEELKKQIREKIGPIATPDYIQNAPGLPKTRSGN-QKRV 665
Cdd:PRK06187 475 -KELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKiLKRV 512
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
105-660 |
2.18e-46 |
|
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: 171.21 E-value: 2.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 105 YNVLDRIVheKKLGDKVAFYWEGnepeetTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLG 184
Cdd:cd05936 2 ADLLEEAA--RRFPDKTALIFMG------RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 185 AlhsIVFagfsseslcerildsNCSLLITtdafyrgeklvnLKELAdEALEKCQekgfpvkccivvkhlgrAELVTgdsp 264
Cdd:cd05936 74 A---VVV---------------PLNPLYT------------PRELE-HILNDSG-----------------AKALI---- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 265 sqsppikrpcpdvqiswnegVDLWWHELMQKAGDECEPEWCDAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKYV 344
Cdd:cd05936 102 --------------------VAVSFTDLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWL 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 345 FDFH-AEDVFWCTADIgwitghsYVTYG-------PLANGATSVLfegIPTyPDVSRLWNIVEKYKVTKFYTAPTAIRLL 416
Cdd:cd05936 162 EDLLeGDDVVLAALPL-------FHVFGltvalllPLALGATIVL---IPR-FRPIGVLKEIRKHRVTIFPGVPTMYIAL 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 417 MKFGDepVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETG--GHmLTPLPGaiPMKPGSATFPFF 494
Cdd:cd05936 231 LNAPE--FKKRDFSSLRLCISGGAPLPVEVAERFEELTG---VPIVEGYGLTETSpvVA-VNPLDG--PRKPGSIGIPLP 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 495 GVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHERFETTyFKKfpGYYVTGDGCRRDKDGYYWITGRIDDMLNV 574
Cdd:cd05936 303 GTEVKIVDDDGEELPPGEVGELWVRGP--QVMKGYWNRPEETAEA-FVD--GWLRTGDIGYMDEDGYFFIVDRKKDMIIV 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 575 SGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSPaltEELKKQIREKIGPIATPDYIQNAPGL 654
Cdd:cd05936 378 GGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTE---EEIIAFCREQLAGYKVPRQVEFRDEL 454
|
....*.
gi 1387203675 655 PKTRSG 660
Cdd:cd05936 455 PKSAVG 460
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
307-664 |
2.24e-45 |
|
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: 167.66 E-value: 2.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 307 AEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGip 386
Cdd:cd05958 96 SDDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEE-- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 387 TYPDvsRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEpvTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFW 466
Cdd:cd05958 174 ATPD--LLLSAIARYKPTVLFTAPTAYRAMLAHPDA--AGPDLSSLRKCVSAGEALPAALHRAWKEATGI---PIIDGIG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 467 QTETGGHMLTPLPGAIpmKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpgimrTVY-GNHERFETTYFKKfp 545
Cdd:cd05958 247 STEMFHIFISARPGDA--RPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP------TGCrYLADKRQRTYVQG-- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 546 GYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSP 625
Cdd:cd05958 317 GWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGP 396
|
330 340 350
....*....|....*....|....*....|....*....
gi 1387203675 626 ALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGNQKR 664
Cdd:cd05958 397 VLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQR 435
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
136-666 |
2.48e-45 |
|
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: 167.36 E-value: 2.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 136 ITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGAlhsIVFAGfsseslcerildsncSLLITTD 215
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGA---VVIPA---------------TTLLTPD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 216 afyrgeklvnlkELADEAlekcqEKGFPVKCcivvkhlgRAELVTGdspsqsppikrpcpdvqiswnegvdlwwhelmqk 295
Cdd:cd05974 63 ------------DLRDRV-----DRGGAVYA--------AVDENTH---------------------------------- 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 296 agdecepewcdAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFkYVFDFHAEDVFWCTADIGWiTGHSYVT-YGPLA 374
Cdd:cd05974 84 -----------ADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTM-YWIGLKPGDVHWNISSPGW-AKHAWSCfFAPWN 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 375 NGATSVLFegipTYP--DVSRLWNIVEKYKVTKFYTAPTAIRLLMKfgdEPVTKHSRASLQVLGTvGEPINPEAwlwYHR 452
Cdd:cd05974 151 AGATVFLF----NYArfDAKRVLAALVRYGVTTLCAPPTVWRMLIQ---QDLASFDVKLREVVGA-GEPLNPEV---IEQ 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 453 VVGAQRCPIVDTFWQTETGGhMLTPLPGAiPMKPGSATFPFFGVAPAILNESGEELEGEAEGyLVFKQPWP-GIMRTVYG 531
Cdd:cd05974 220 VRRAWGLTIRDGYGQTETTA-LVGNSPGQ-PVKAGSMGRPLPGYRVALLDPDGAPATEGEVA-LDLGDTRPvGLMKGYAG 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 532 NHERfetTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECL 611
Cdd:cd05974 297 DPDK---TAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVP 373
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1387203675 612 YCFVTLCDGHIFSPALTEELKKQIREKIGPIATPDYIQNAPgLPKTRSGNQKRVD 666
Cdd:cd05974 374 KAFIVLRAGYEPSPETALEIFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRRVE 427
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
134-660 |
2.98e-45 |
|
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: 166.70 E-value: 2.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 134 TQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALhsivfagfsseslcerildsncslLIT 213
Cdd:cd05934 2 RRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAV------------------------LVP 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 214 TDAFYRGEklvnlkELADealekcqekgfpvkcciVVKHLGRAELVTgdspsqsppikrpcpdvqiswnegvdlwwhelm 293
Cdd:cd05934 58 INTALRGD------ELAY-----------------IIDHSGAQLVVV--------------------------------- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 294 qkagdecepewcdaeDPLFILYTSGSTGKPKGVL--HTvggYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYG 371
Cdd:cd05934 82 ---------------DPASILYTSGTTGPPKGVVitHA---NLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLA 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 372 PLANGATSVLfegIPTYpDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLqvlgTVGEPINPEAWLWYH 451
Cdd:cd05934 144 ALSVGATLVL---LPRF-SASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRA----AYGAPNPPELHEEFE 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 452 RVVGaqrCPIVDTFWQTETGGHMLTPLPGAIPmkPGSATFPFFGVAPAILNESGEELEGEAEGYLVFK-QPWPGIMRTVY 530
Cdd:cd05934 216 ERFG---VRLLEGYGMTETIVGVIGPRDEPRR--PGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRgLRGWGFFKGYY 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 531 GNHErfETTyfKKFP-GYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGE 609
Cdd:cd05934 291 NMPE--ATA--EAMRnGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGED 366
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1387203675 610 CLYCFVTLCDGHIFSPaltEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:cd05934 367 EVKAVVVLRPGETLDP---EELFAFCEGQLAYFKVPRYIRFVDDLPKTPTE 414
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
131-660 |
5.22e-43 |
|
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: 162.00 E-value: 5.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 131 EETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSL 210
Cdd:cd05911 6 DTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 211 LITTDAFYrgeklvnlkeladealEKCQEKgfpVKCCIVVKHLgraeLVTGDSPSQSPPIKRPcpdvqISWNEGVDLWWH 290
Cdd:cd05911 86 IFTDPDGL----------------EKVKEA---AKELGPKDKI----IVLDDKPDGVLSIEDL-----LSPTLGEEDEDL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 291 ELMQKAGDEcepewcdaeDPLFILYTSGSTGKPKGVL--HTVGGYMLYVATTFKYVfDFHAEDVFWCTADIGWITG-HSY 367
Cdd:cd05911 138 PPPLKDGKD---------DTAAILYSSGTTGLPKGVClsHRNLIANLSQVQTFLYG-NDGSNDVILGFLPLYHIYGlFTT 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 368 VTYgpLANGATSVLFEGiptyPDVSRLWNIVEKYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLGTVGEPINPEAw 447
Cdd:cd05911 208 LAS--LLNGATVIIMPK----FDSELFLDLIEKYKITFLYLVPPIAAALAK--SPLLDKYDLSSLRVILSGGAPLSKEL- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 448 lwYHRV-VGAQRCPIVDTFWQTETGGHMLTPLPGaiPMKPGSATFPFFGVAPAILNESGEELEGEaegylvfKQP---W- 522
Cdd:cd05911 279 --QELLaKRFPNATIKQGYGMTETGGILTVNPDG--DDKPGSVGRLLPNVEAKIVDDDGKDSLGP-------NEPgeiCv 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 523 --PGIMRTVYGNHERFETTYFKKfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVV 600
Cdd:cd05911 348 rgPQVMKGYYNNPEATKETFDED--GWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVI 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387203675 601 GHPHPVKGECLYCFVTLCDGhifsPALTE-ELKKQIREKIgpiatPDY------IQNAPGLPKTRSG 660
Cdd:cd05911 426 GIPDEVSGELPRAYVVRKPG----EKLTEkEVKDYVAKKV-----ASYkqlrggVVFVDEIPKSASG 483
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
102-664 |
1.72e-42 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 160.77 E-value: 1.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 102 NICYNVLDRIVHEKKlGDKVAFYwegnepEETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACA 181
Cdd:TIGR02262 4 NAAEDLLDRNVVEGR-GGKTAFI------DDISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 182 RLGALHSIVFAGFSSESLCERILDSNCSLLITTDAFYrgeklvnlkELADEALEKcqekgfpvkccivVKHLgRAELVTG 261
Cdd:TIGR02262 77 RAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALL---------PVIKAALGK-------------SPHL-EHRVVVG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 262 DSPSqsppikrpcPDVQISwnegvdlwwhELMQKAGDECEPEWCDAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTF 341
Cdd:TIGR02262 134 RPEA---------GEVQLA----------ELLATESEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 342 KYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVSRLWNiveKYKVTKFYTAPTAIRLLMkfGD 421
Cdd:TIGR02262 195 RNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGERPTPDAVFDRLR---RHQPTIFYGVPTLYAAML--AD 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 422 EPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQrcpIVDTFWQTETGGHMLTPLPGAIpmKPGSATFPFFGVAPAIL 501
Cdd:TIGR02262 270 PNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVD---IVDGIGSTEMLHIFLSNLPGDV--RYGTSGKPVPGYRLRLV 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 502 NESGEELEGEAEGYLVFKQPWPGIMrtVYGNHERFETTYFKkfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLST 581
Cdd:TIGR02262 345 GDGGQDVADGEPGELLISGPSSATM--YWNNRAKSRDTFQG---EWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSP 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 582 AEVESALVEHKAVAEAAVVGHPHP---VKGEclyCFVTLCDGHifsPALTEELKKQIREKIGPIATPDYIQNAPGLPKTR 658
Cdd:TIGR02262 420 FEIESALIQHPAVLEAAVVGVADEdglIKPK---AFVVLRPGQ---TALETELKEHVKDRLAPYKYPRWIVFVDDLPKTA 493
|
....*.
gi 1387203675 659 SGNQKR 664
Cdd:TIGR02262 494 TGKIQR 499
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
119-660 |
2.96e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 160.48 E-value: 2.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 119 DKVAFYWEGnepeetTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSES 198
Cdd:PRK08316 26 DKTALVFGD------RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 199 LCERILDSNCSLLITTDAFYrgeklvnlkELADEALEKCQEKGFpvkccivvkhlgRAELVTGDSPSqsppikrpcPDVQ 278
Cdd:PRK08316 100 LAYILDHSGARAFLVDPALA---------PTAEAALALLPVDTL------------ILSLVLGGREA---------PGGW 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 279 ISWNEgvdlwwhelMQKAGDECEPE-WCDAEDPLFILYTSGSTGKPKGVLHT----VGGYMLYVATTfkyvfDFHAEDVF 353
Cdd:PRK08316 150 LDFAD---------WAEAGSVAEPDvELADDDLAQILYTSGTESLPKGAMLThralIAEYVSCIVAG-----DMSADDIP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 354 WCTADIGwitgHS---YVTYGP-LANGATSVLFEGiptyPDVSRLWNIVEKYKVTKFYTAPTA-IRLLmkfgdepvtKH- 427
Cdd:PRK08316 216 LHALPLY----HCaqlDVFLGPyLYVGATNVILDA----PDPELILRTIEAERITSFFAPPTVwISLL---------RHp 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 428 --SRASLQVL--GTVGEPINPEAWLwyHRVvgAQRCPIVdTFW----QTETGghmltPL-----PGAIPMKPGSATFPFF 494
Cdd:PRK08316 279 dfDTRDLSSLrkGYYGASIMPVEVL--KEL--RERLPGL-RFYncygQTEIA-----PLatvlgPEEHLRRPGSAGRPVL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 495 GVAPAILNESGEELEgeaegylvfkqpwPGIMRTVYGNHERFETTYFKKfP---------GYYVTGDGCRRDKDGYYWIT 565
Cdd:PRK08316 349 NVETRVVDDDGNDVA-------------PGEVGEIVHRSPQLMLGYWDD-PektaeafrgGWFHSGDLGVMDEEGYITVV 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 566 GRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSPaltEELKKQIREKIGPIATP 645
Cdd:PRK08316 415 DRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTE---DELIAHCRARLAGFKVP 491
|
570
....*....|....*
gi 1387203675 646 DYIQNAPGLPKTRSG 660
Cdd:PRK08316 492 KRVIFVDELPRNPSG 506
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
132-660 |
1.20e-38 |
|
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: 148.44 E-value: 1.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 132 ETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGAlhsiVFAGFSSESLCERIL----DSN 207
Cdd:cd05930 9 GDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGA----AYVPLDPSYPAERLAyileDSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 208 CSLLITtdafyrgeklvnlkeladealekcqekgfpvkccivvkhlgraelvtgdspsqsppikrpcpdvqiswnegvdl 287
Cdd:cd05930 85 AKLVLT-------------------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 288 wwhelmqkagdecepewcDAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATtFKYVFDFHAEDVFWCTADIGWItGHSY 367
Cdd:cd05930 91 ------------------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW-MQEAYPLTPGDRVLQFTSFSFD-VSVW 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 368 VTYGPLANGATSVLfegIP--TYPDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVtkhsRASLQVLGTVGEPINPE 445
Cdd:cd05930 151 EIFGALLAGATLVV---LPeeVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAA----LPSLRLVLVGGEALPPD 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 446 AW-LWYHRVVGAQrcpIVDTFWQTETGGHMLTplpGAIPMKPGSATF-----PFFGVAPAILNESGeelegeaegylvfk 519
Cdd:cd05930 224 LVrRWRELLPGAR---LVNLYGPTEATVDATY---YRVPPDDEEDGRvpigrPIPNTRVYVLDENL-------------- 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 520 QPWP------------GIMRTVYGNHE----RFETTYFkkFPG--YYVTGDGCRRDKDG--YYwiTGRIDDMLNVSGHLL 579
Cdd:cd05930 284 RPVPpgvpgelyiggaGLARGYLNRPEltaeRFVPNPF--GPGerMYRTGDLVRWLPDGnlEF--LGRIDDQVKIRGYRI 359
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 580 STAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHifsPALTEELKKQIREKIGPIATPDYIQNAPGLPKTRS 659
Cdd:cd05930 360 ELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGG---ELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPN 436
|
.
gi 1387203675 660 G 660
Cdd:cd05930 437 G 437
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
121-657 |
2.80e-36 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 144.71 E-value: 2.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 121 VAFYWEGNEPEETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLAcarlGALHSIVFA---GFSSE 197
Cdd:PRK07529 44 LSFLLDADPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG----GEAAGIANPinpLLEPE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 198 SLCERILDSNCSLLITtdafYRGEKLVNLKELADEALEKCQEkgfpVKCCIVVkHLGRAelVTGDSPSQSPPIKRPCPDV 277
Cdd:PRK07529 120 QIAELLRAAGAKVLVT----LGPFPGTDIWQKVAEVLAALPE----LRTVVEV-DLARY--LPGPKRLAVPLIRRKAHAR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 278 QISWNEgvdlwwhELMQKAGDECE-PEWCDAEDPLFILYTSGSTGKPKGVLHTVGGyMLYVATTFKYVFDFHAEDVFWCT 356
Cdd:PRK07529 189 ILDFDA-------ELARQPGDRLFsGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDTVFCG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 357 ADIGWITGhSYVT-YGPLANGAtSVLFEGIPTYPD---VSRLWNIVEKYKVTKFYTAPTAIRLLMkfgDEPVTKHSRASL 432
Cdd:PRK07529 261 LPLFHVNA-LLVTgLAPLARGA-HVVLATPQGYRGpgvIANFWKIVERYRINFLSGVPTVYAALL---QVPVDGHDISSL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 433 QVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTE-TGGHMLTPLPGaiPMKPGSA--TFPFFGVAPAILNESGEELE 509
Cdd:PRK07529 336 RYALCGAAPLPVEVFRRFEAATGV---RIVEGYGLTEaTCVSSVNPPDG--ERRIGSVglRLPYQRVRVVILDDAGRYLR 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 510 GEAEG---YLVFKQP--WPGIMRTVYGNHERFEttyfkkfPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEV 584
Cdd:PRK07529 411 DCAVDevgVLCIAGPnvFSGYLEAAHNKGLWLE-------DGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAI 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387203675 585 ESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSPA-LTEELKKQIREkigPIATPDYIQNAPGLPKT 657
Cdd:PRK07529 484 EEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAeLLAFARDHIAE---RAAVPKHVRILDALPKT 554
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
115-660 |
6.64e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 141.97 E-value: 6.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 115 KKLGDKVAfYWEGNEpeettQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGF 194
Cdd:PRK07656 16 RRFGDKEA-YVFGDQ-----RLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 195 SSESLCERILDSNCSLLITTDAFyrgeklVNLKELADEALEkcqekgfpvkccivvkHLGRAELVTGDSPSQSPPIKRPC 274
Cdd:PRK07656 90 TADEAAYILARGDAKALFVLGLF------LGVDYSATTRLP----------------ALEHVVICETEEDDPHTEKMKTF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 275 PDVqiswnegvdlwwheLMQKAGDECEPEwCDAEDPLFILYTSGSTGKPKGVLHTVGG-YMLY--VATTFKYVFD----- 346
Cdd:PRK07656 148 TDF--------------LAAGDPAERAPE-VDPDDVADILFTSGTTGRPKGAMLTHRQlLSNAadWAEYLGLTEGdryla 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 347 ----FHaedVFWCTAdiGWITghsyvtygPLANGATSVLfegIPTYpDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDE 422
Cdd:PRK07656 213 anpfFH---VFGYKA--GVNA--------PLMRGATILP---LPVF-DPDEVFRLIETERITVLPGPPTMYNSLLQHPDR 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 423 pvTKHSRASLQVLGTVGEPInPEAWLwyHRVVGAQRCPIVDT-FWQTETGGHM-LTPLPGAIPMKPGSATFPFFGVAPAI 500
Cdd:PRK07656 276 --SAEDLSSLRLAVTGAASM-PVALL--ERFESELGVDIVLTgYGLSEASGVTtFNRLDDDRKTVAGTIGTAIAGVENKI 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 501 LNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHErfETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLS 580
Cdd:PRK07656 351 VNELGEEVPVGEVGELLVRGP--NVMKGYYDDPE--ATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVY 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 581 TAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGhifsPALTEE-LKKQIREKIGPIATPDYIQNAPGLPKTRS 659
Cdd:PRK07656 427 PAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPG----AELTEEeLIAYCREHLAKYKVPRSIEFLDELPKNAT 502
|
.
gi 1387203675 660 G 660
Cdd:PRK07656 503 G 503
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
132-660 |
8.71e-35 |
|
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: 137.44 E-value: 8.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 132 ETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLAcarlgalhsIVFAGfsseslcerildsncsll 211
Cdd:cd17643 9 EDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLA---------ILKAG------------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 212 ittdAFYrgeklVNLkeladealekcqEKGFPVKccivvkhlgRAELVTGDSPsqsppikrpcPDVQISwnegvdlwwhe 291
Cdd:cd17643 62 ----GAY-----VPI------------DPAYPVE---------RIAFILADSG----------PSLLLT----------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 292 lmqkagdecepewcDAEDPLFILYTSGSTGKPKGVLHTVGGYM-LYVATTfkYVFDFHAEDVfwctadigWITGHSYV-- 368
Cdd:cd17643 91 --------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLaLFAATQ--RWFGFNEDDV--------WTLFHSYAfd 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 369 -----TYGPLANGATSVlfegIPTYpDVSR----LWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGtvG 439
Cdd:cd17643 147 fsvweIWGALLHGGRLV----VVPY-EVARspedFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFG--G 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 440 EPINPeAWL--WYHRVvGAQRCPIVDTFWQTETGGHM----LTP--LPGAiPMKPGSATFPFFGVAPAILNESGEELEGE 511
Cdd:cd17643 220 EALEA-AMLrpWAGRF-GLDRPQLVNMYGITETTVHVtfrpLDAadLPAA-AASPIGRPLPGLRVYVLDADGRPVPPGVV 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 512 AEGYLVFKQPWPGIMRTVYGNHERFETTYFKKfPG--YYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALV 589
Cdd:cd17643 297 GELYVSGAGVARGYLGRPELTAERFVANPFGG-PGsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALA 375
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387203675 590 EHKAVAEAAVVGHPHPVKGECLYCFVTLCDGhifSPALTEELKKQIREKIgpiatPDYIQNA-----PGLPKTRSG 660
Cdd:cd17643 376 THPSVRDAAVIVREDEPGDTRLVAYVVADDG---AAADIAELRALLKELL-----PDYMVPAryvplDALPLTVNG 443
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
119-660 |
1.30e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 135.86 E-value: 1.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 119 DKVAFYWEGNEpeettqITYRELLVQVCRFSNVL-RKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSE 197
Cdd:PRK08314 25 DKTAIVFYGRA------ISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 198 SLCERILDSNCSLLITTDAFY-RGEKLVNLKELAdealekcqekgfpvkcCIVVKHLGRAelVTGDSPSQSPPIKRPCPD 276
Cdd:PRK08314 99 ELAHYVTDSGARVAIVGSELApKVAPAVGNLRLR----------------HVIVAQYSDY--LPAEPEIAVPAWLRAEPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 277 VQISWNEGVDLWwhELMQKAGDECEPEWCDAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKYvFDFHAEDVFWCT 356
Cdd:PRK08314 161 LQALAPGGVVAW--KEALAAGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLW-SNSTPESVVLAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 357 ADIGWITGHSYVTYGPLANGATSVLfegiptypdVSRlWN------IVEKYKVTKFYTAPT-AIRLLMKFGdepVTKHSR 429
Cdd:PRK08314 238 LPLFHVTGMVHSMNAPIYAGATVVL---------MPR-WDreaaarLIERYRVTHWTNIPTmVVDFLASPG---LAERDL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 430 ASLQVLGTVGEPInPEAWlwyhrvvgAQR------CPIVDTFWQTETGGHMLTPLPGAiPmKPGSATFPFFGVAPAILNE 503
Cdd:PRK08314 305 SSLRYIGGGGAAM-PEAV--------AERlkeltgLDYVEGYGLTETMAQTHSNPPDR-P-KLQCLGIPTFGVDARVIDP 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 504 SGEELEGEAEG--YLVFKqpwPGIMRTVYGNHERFETTyFKKFPG--YYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLL 579
Cdd:PRK08314 374 ETLEELPPGEVgeIVVHG---PQVFKGYWNRPEATAEA-FIEIDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKV 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 580 STAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSPAlTEELKKQIREKIGPIATPDYIQNAPGLPKTRS 659
Cdd:PRK08314 450 WPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTT-EEEIIAWAREHMAAYKYPRIVEFVDSLPKSGS 528
|
.
gi 1387203675 660 G 660
Cdd:PRK08314 529 G 529
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
137-599 |
1.76e-33 |
|
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: 133.16 E-value: 1.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 137 TYRELLVQVCRFSNVLRKQ-GICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLcERIL-DSNCSLLITT 214
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERL-AFILeDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 215 DAFyrgeklvnlkeladealekCQEKGFPVKCCIVVkhLGRAELVTGDSPSQSPPIKRPCPDvqiswnegvdlwwhelmq 294
Cdd:TIGR01733 80 SAL-------------------ASRLAGLVLPVILL--DPLELAALDDAPAPPPPDAPSGPD------------------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 295 kagdecepewcdaeDPLFILYTSGSTGKPKGVLHTVGGyMLYVATTFKYVFDFHAEDVfwctadigWITGHSYV------ 368
Cdd:TIGR01733 121 --------------DLAYVIYTSGSTGRPKGVVVTHRS-LVNLLAWLARRYGLDPDDR--------VLQFASLSfdasve 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 369 -TYGPLANGATSVLFEGIPTYPDVSRLWNIVEKYKVTKFYTAPTAIRLLMkfgDEPVTkhSRASLQVLGTVGEPINPEAW 447
Cdd:TIGR01733 178 eIFGALLAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALLA---AALPP--ALASLRLVILGGEALTPALV 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 448 LWYHRVVGAQRcpIVDTFWQTETGGH-MLTPLPGAIPMKPGSATF--PFFGVAPAILNESGeelegeaegylvfkQPWP- 523
Cdd:TIGR01733 253 DRWRARGPGAR--LINLYGPTETTVWsTATLVDPDDAPRESPVPIgrPLANTRLYVLDDDL--------------RPVPv 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 524 -----------GIMRtvyGNHERFETT--YFKKFPGY-------YVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAE 583
Cdd:TIGR01733 317 gvvgelyiggpGVAR---GYLNRPELTaeRFVPDPFAggdgarlYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGE 393
|
490
....*....|....*.
gi 1387203675 584 VESALVEHKAVAEAAV 599
Cdd:TIGR01733 394 IEAALLRHPGVREAVV 409
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
135-660 |
9.75e-33 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 132.96 E-value: 9.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 135 QITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHsiVFAGFS---SE--SLCERildSNCS 209
Cdd:COG1021 50 RLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIP--VFALPAhrrAEisHFAEQ---SEAV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 210 LLITTDAfYRGeklVNLKELADEALEKCQEkgfpvkccivVKHLgraeLVTGDspsqsppikrpcPDVQISWNEgvdlww 289
Cdd:COG1021 125 AYIIPDR-HRG---FDYRALARELQAEVPS----------LRHV----LVVGD------------AGEFTSLDA------ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 290 heLMQKAGDECEPEwCDAEDPLFILYTSGSTGKPKGVLHTVGGYmLYVATTFKYVFDFHAEDVFWCTADIGwitgHSY-- 367
Cdd:COG1021 169 --LLAAPADLSEPR-PDPDDVAFFQLSGGTTGLPKLIPRTHDDY-LYSVRASAEICGLDADTVYLAALPAA----HNFpl 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 368 ---VTYGPLANGATSVLFEGipTYPDVsrLWNIVEKYKVTkfYTA--PTAIRLLMKFGDEpvTKHSRASLQVLGTVGEPI 442
Cdd:COG1021 241 sspGVLGVLYAGGTVVLAPD--PSPDT--AFPLIERERVT--VTAlvPPLALLWLDAAER--SRYDLSSLRVLQVGGAKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 443 NPEA----------WLW-----------Y-------HRVVGAQRCP--------IVDtfwqtETGghmlTPLPgaipmkP 486
Cdd:COG1021 313 SPELarrvrpalgcTLQqvfgmaeglvnYtrlddpeEVILTTQGRPispddevrIVD-----EDG----NPVP------P 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 487 GSAtfpffGVapailnesgeelegeaegyLVFKQPWpgimrTVYGnherfettYFKKfP----------GYYVTGDGCRR 556
Cdd:COG1021 378 GEV-----GE-------------------LLTRGPY-----TIRG--------YYRA-PehnaraftpdGFYRTGDLVRR 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 557 DKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGE--CLycFVTLcDGHIFSPAlteELKKQ 634
Cdd:COG1021 420 TPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGErsCA--FVVP-RGEPLTLA---ELRRF 493
|
570 580
....*....|....*....|....*....
gi 1387203675 635 IREKiGpIAT---PDYIQNAPGLPKTRSG 660
Cdd:COG1021 494 LRER-G-LAAfklPDRLEFVDALPLTAVG 520
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
22-659 |
2.91e-32 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 133.28 E-value: 2.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 22 ARSPTRSWSPPPEVSRSAHVPSLQRYR-----------------ELHRRSLEEPREFWGDIAKEF--YWKTPcPGPFLQY 82
Cdd:PLN03052 80 TLGPPPAWFPSPEIAKLTNLGRLLEARgkellgskykdpissfsEFQRFSVENPEVYWSIVLDELslVFSVP-PRCILDT 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 83 NFDVTKGKifiEWMKGATTNICYNVLdrIVHEKKLGDKVAFYW--EGNEPEETTQITYRELLVQVCRFSNVLRKQGICKG 160
Cdd:PLN03052 159 SDESNPGG---QWLPGAVLNVAECCL--TPKPSKTDDSIAIIWrdEGSDDLPVNRMTLSELRSQVSRVANALDALGFEKG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 161 DRVAIYMPMIPELVVAMLAcarlgalhsIVFAG---------FSSESLCERILDSNCSLLITTDAFYRGEKlvnlkelad 231
Cdd:PLN03052 234 DAIAIDMPMNVHAVIIYLA---------IILAGcvvvsiadsFAPSEIATRLKISKAKAIFTQDVIVRGGK--------- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 232 ealekcqekGFPVKCCIVVKHLGRAELVTGDSPSqsppikrpcpdVQISWNEGvDLWWHELMQKA-----GDECEPEWCD 306
Cdd:PLN03052 296 ---------SIPLYSRVVEAKAPKAIVLPADGKS-----------VRVKLREG-DMSWDDFLARAnglrrPDEYKAVEQP 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 307 AEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKYVfDFHAEDVF-WCTaDIGWITGHsYVTYGPLANGATSVLFEGI 385
Cdd:PLN03052 355 VEAFTNILFSSGTTGEPKAIPWTQLTPLRAAADAWAHL-DIRKGDIVcWPT-NLGWMMGP-WLVYASLLNGATLALYNGS 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 386 PTYPDVSRLwniVEKYKVTKFYTAPTAIRLLMKFGdePVTKHSRASLQVLGTVGEPINPEAWLWYhrVVGAQRCPIVDTF 465
Cdd:PLN03052 432 PLGRGFAKF---VQDAKVTMLGTVPSIVKTWKNTN--CMAGLDWSSIRCFGSTGEASSVDDYLWL--MSRAGYKPIIEYC 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 466 WQTETGGHMLT-----------------------------PLPGAIPMKPGSATFP-FFGVAPAILNesgeelegeaegy 515
Cdd:PLN03052 505 GGTELGGGFVTgsllqpqafaafstpamgcklfilddsgnPYPDDAPCTGELALFPlMFGASSTLLN------------- 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 516 lvfkqpwpgimrtvyGNHERfetTYFKKFPGYYVT-----GDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVE----S 586
Cdd:PLN03052 572 ---------------ADHYK---VYFKGMPVFNGKilrrhGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIErvcnA 633
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387203675 587 AlveHKAVAEAAVVGHPHPVKG-ECLYCFVTLCDGHIFSPALtEELKK----QIREKIGPIATPDYIQNAPGLPKTRS 659
Cdd:PLN03052 634 A---DESVLETAAIGVPPPGGGpEQLVIAAVLKDPPGSNPDL-NELKKifnsAIQKKLNPLFKVSAVVIVPSFPRTAS 707
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
167-659 |
2.78e-31 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 128.01 E-value: 2.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 167 MPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLITTDAFYRGEKLVnlkELADEALEKCQEKgfpvkc 246
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRAL---PLYSKVVEAAPAK------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 247 CIVVKHLGRaelvtgdspSQSPPIKrpcPDVQiSWNE--GVDLWWHelmQKAGDECEPEWCDAEDPLFILYTSGSTGKPK 324
Cdd:PLN03051 72 AIVLPAAGE---------PVAVPLR---EQDL-SWCDflGVAAAQG---SVGGNEYSPVYAPVESVTNILFSSGTTGEPK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 325 GV-------LHTVGGYMLYVattfkyvfDFHAEDVFWCTADIGWITGhSYVTYGPLANGATSVLFEGIPTYPDVSRLwni 397
Cdd:PLN03051 136 AIpwthlspLRCASDGWAHM--------DIQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGAPLGRGFGKF--- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 398 VEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQRcPIVDTFWQTETGGHML-- 475
Cdd:PLN03051 204 VQDAGVTVLGLVPSIVKAWRHTGAFAMEGLDWSKLRVFASTGEASAVDDVLWLSSVRGYYK-PVIEYCGGTELASGYIss 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 476 TPLpgaIPMKPGSATFPFFGVAPAILNESGEELEGEAEGY--LVFKQPWPGIM-RTVYGNHERfetTYFKKFPGYYVTGD 552
Cdd:PLN03051 283 TLL---QPQAPGAFSTASLGTRFVLLNDNGVPYPDDQPCVgeVALAPPMLGASdRLLNADHDK---VYYKGMPMYGSKGM 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 553 GCRRDKD-------GYYWITGRIDDMLNVSGHLLSTAEVESALVE-HKAVAEAAVVGHPHPVKG-ECLYCFVTLCD-GHI 622
Cdd:PLN03051 357 PLRRHGDimkrtpgGYFCVQGRADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGpELLVIFLVLGEeKKG 436
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1387203675 623 FSPALTEELKKQ----IREKIGPIATPDYIQNAPGLPKTRS 659
Cdd:PLN03051 437 FDQARPEALQKKfqeaIQTNLNPLFKVSRVKIVPELPRNAS 477
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
137-665 |
3.00e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 128.00 E-value: 3.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 137 TYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLITTDA 216
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDDA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 217 FYRGEklvnlkeladealekcqekgfpvkcCIVVKHLGRAELVTGDSPSQSPPIkrpcpdvqiswnegvdlwwhelmqka 296
Cdd:PRK09088 104 VAAGR-------------------------TDVEDLAAFIASADALEPADTPSI-------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 297 gdecepewcDAEDPLFILYTSGSTGKPKGVLHTVGGyMLYVATTFKYVFDFHAEDVFWCTAD----IGWITGHSYVtygp 372
Cdd:PRK09088 133 ---------PPERVSLILFTSGTSGQPKGVMLSERN-LQQTAHNFGVLGRVDAHSSFLCDAPmfhiIGLITSVRPV---- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 373 LANGATSVLFEGIPTYPDVSRLWNivEKYKVTKFYTAPtaiRLLMKFGDEPVTKHSR-ASLQVLGTVGEPiNPE----AW 447
Cdd:PRK09088 199 LAVGGSILVSNGFEPKRTLGRLGD--PALGITHYFCVP---QMAQAFRAQPGFDAAAlRHLTALFTGGAP-HAAedilGW 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 448 LwyhrvvgAQRCPIVDTFWQTETGGHMLTPL-PGAIPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQP--WPG 524
Cdd:PRK09088 273 L-------DDGIPMVDGFGMSEAGTVFGMSVdCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPnlSPG 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 525 IMRTVYGNHERFETTyfkkfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPH 604
Cdd:PRK09088 346 YWRRPQATARAFTGD------GWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMAD 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387203675 605 PVKGECLYCFVTLCDGhifSPALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGN-QKRV 665
Cdd:PRK09088 420 AQWGEVGYLAIVPADG---APLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKlQKAR 478
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
119-660 |
3.69e-30 |
|
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: 124.76 E-value: 3.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 119 DKVAFYWEGnepeetTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSES 198
Cdd:cd17651 10 DAPALVAEG------RRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 199 LCERILDSNCSLLITTDAFyrgeklvnLKELADEAlekcqekgfpvkccIVVKHLGRAELVTGDSPSQSPPIkrpcpdvq 278
Cdd:cd17651 84 LAFMLADAGPVLVLTHPAL--------AGELAVEL--------------VAVTLLDQPGAAAGADAEPDPAL-------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 279 iswnegvdlwwhelmqkagdecepewcDAEDPLFILYTSGSTGKPKGVL------------HTVGGYMLYVATTFKYV-- 344
Cdd:cd17651 134 ---------------------------DADDLAYVIYTSGSTGRPKGVVmphrslanlvawQARASSLGPGARTLQFAgl 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 345 -FDFHAEDVFwctadigwitghsyvtyGPLANGATSVLfegIPTY--PDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGD 421
Cdd:cd17651 187 gFDVSVQEIF-----------------STLCAGATLVL---PPEEvrTDPPALAAWLDEQRISRVFLPTVALRALAEHGR 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 422 EPVTKHsrASLQVLGTVGEPINPEAWL--WYHRVVGAQrcpIVDTFWQTET---GGHMLTPLPGAIPMKPGSATfPFFGV 496
Cdd:cd17651 247 PLGVRL--AALRYLLTGGEQLVLTEDLreFCAGLPGLR---LHNHYGPTEThvvTALSLPGDPAAWPAPPPIGR-PIDNT 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 497 APAILNEsgeelegeaegylvFKQPWP------------GIMRTVYGN----HERFETTYFKKFPGYYVTGDGCRRDKDG 560
Cdd:cd17651 321 RVYVLDA--------------ALRPVPpgvpgelyiggaGLARGYLNRpeltAERFVPDPFVPGARMYRTGDLARWLPDG 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 561 YYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHifsPALTEELKKQIREKIG 640
Cdd:cd17651 387 ELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEA---PVDAAELRAALATHLP 463
|
570 580
....*....|....*....|
gi 1387203675 641 PIATPDYIQNAPGLPKTRSG 660
Cdd:cd17651 464 EYMVPSAFVLLDALPLTPNG 483
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
115-663 |
1.50e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 123.23 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 115 KKLGDKVAFYWEGNepeettQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGAlhsiVFAGf 194
Cdd:PRK07470 18 RRFPDRIALVWGDR------SWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGA----VWVP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 195 sseslcerildsncsllittdafyrgeklVNLKELADEALEKCQEKGfpvkccivvkhlGRAELVTGDSPSQSPPIKRPC 274
Cdd:PRK07470 87 -----------------------------TNFRQTPDEVAYLAEASG------------ARAMICHADFPEHAAAVRAAS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 275 PD----VQISWNEGVDLWWHELMQKAGDECEPEWCDAEDPLFILYTSGSTGKPK-GVL-HtvgGYMLYVATTfkyvfdfH 348
Cdd:PRK07470 126 PDlthvVAIGGARAGLDYEALVARHLGARVANAAVDHDDPCWFFFTSGTTGRPKaAVLtH---GQMAFVITN-------H 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 349 AEDVFWCTadigwiTGH--SYVTyGPL------------ANGATSVLfegIPTYP-DVSRLWNIVEKYKVTKFYTAPTAI 413
Cdd:PRK07470 196 LADLMPGT------TEQdaSLVV-APLshgagihqlcqvARGAATVL---LPSERfDPAEVWALVERHRVTNLFTVPTIL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 414 RLLMKfgDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQrcpIVDTFWQTETGGHMlTPLPGAI------PM-KP 486
Cdd:PRK07470 266 KMLVE--HPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKV---LVQYFGLGEVTGNI-TVLPPALhdaedgPDaRI 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 487 GSATFPFFGVAPAILNESGEELEGEAEGYLVFKQP--WPGIMRTVYGNHERFETTYFKkfpgyyvTGDGCRRDKDGYYWI 564
Cdd:PRK07470 340 GTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPavFAGYYNNPEANAKAFRDGWFR-------TGDLGHLDARGFLYI 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 565 TGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSPaltEELKKQIREKIGPIAT 644
Cdd:PRK07470 413 TGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDE---AELLAWLDGKVARYKL 489
|
570
....*....|....*....
gi 1387203675 645 PDYIQNAPGLPKtrSGNQK 663
Cdd:PRK07470 490 PKRFFFWDALPK--SGYGK 506
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
119-666 |
1.51e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 123.61 E-value: 1.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 119 DKVAFYWEGnepeetTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSES 198
Cdd:PRK06178 48 QRPAIIFYG------HVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 199 LCERILDSNCSLLITTDAFYrgeKLVNlKELADEALEKcqekgfpvkccivVKHLGRAELVTgDSPSQSPPIKRPCPDVQ 278
Cdd:PRK06178 122 LSYELNDAGAEVLLALDQLA---PVVE-QVRAETSLRH-------------VIVTSLADVLP-AEPTLPLPDSLRAPRLA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 279 ISWnegvdlwWHELMQKAGDECEP---EWCDAEDPLFILYTSGSTGKPKGVLHTvGGYMLYVATTFKYVFDFHAED-VFW 354
Cdd:PRK06178 184 AAG-------AIDLLPALRACTAPvplPPPALDALAALNYTGGTTGMPKGCEHT-QRDMVYTAAAAYAVAVVGGEDsVFL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 355 CTADIGWITGHSYVTYGPLANGATSVLFegipTYPDVSRLWNIVEKYKVTK-FYTAPTAIRLLmkfgDEP-VTKHSRASL 432
Cdd:PRK06178 256 SFLPEFWIAGENFGLLFPLFSGATLVLL----ARWDAVAFMAAVERYRVTRtVMLVDNAVELM----DHPrFAEYDLSSL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 433 QVLGTVG--EPINPEAWLWYHRVVGaqrCPIVDTFW-QTET------------GGHMLT--------PLPGA---IPMKP 486
Cdd:PRK06178 328 RQVRVVSfvKKLNPDYRQRWRALTG---SVLAEAAWgMTEThtcdtftagfqdDDFDLLsqpvfvglPVPGTefkICDFE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 487 GSATFPFfGV-------APAILnesgeelegeaegylvfkqpwpgimrTVYGNHERFETTYFKKfpGYYVTGDGCRRDKD 559
Cdd:PRK06178 405 TGELLPL-GAegeivvrTPSLL--------------------------KGYWNKPEATAEALRD--GWLHTGDIGKIDEQ 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 560 GYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSPAlteELKKQIREKI 639
Cdd:PRK06178 456 GFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAA---ALQAWCRENM 532
|
570 580
....*....|....*....|....*...
gi 1387203675 640 GPIATPD-YIQNApgLPKTRSGNQKRVD 666
Cdd:PRK06178 533 AVYKVPEiRIVDA--LPMTATGKVRKQD 558
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
119-657 |
1.69e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 123.17 E-value: 1.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 119 DKVAFYWEGnepeetTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLG----ALHSIVfagf 194
Cdd:PRK06188 27 DRPALVLGD------TRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGlrrtALHPLG---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 195 SSESLCERILDSNCSLLITTDAFYRgeklvnlkELADEALEKCQEkgfpvkccivVKHLgraeLVTGDSPsqsppikrpc 274
Cdd:PRK06188 97 SLDDHAYVLEDAGISTLIVDPAPFV--------ERALALLARVPS----------LKHV----LTLGPVP---------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 275 pdvqiswnEGVDLWwhELMQKAGDECEPEWCDAEDPLFILYTSGSTGKPKGVLHTVGGYmlyvaTTFkyvfdfhaedVFW 354
Cdd:PRK06188 145 --------DGVDLL--AAAAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSI-----ATM----------AQI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 355 CTADIGWITGHSYVTYGPLANGATS----VLFEGIPTYP----DVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDepVTK 426
Cdd:PRK06188 200 QLAEWEWPADPRFLMCTPLSHAGGAfflpTLLRGGTVIVlakfDPAEVLRAIEEQRITATFLVPTMIYALLDHPD--LRT 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 427 HSRASLQVLGTVGEPINP----EAwlwyHRVVGaqrcPI-VDTFWQTETGgHMLTPLP-----GAIPMKPGSATFPFFGV 496
Cdd:PRK06188 278 RDLSSLETVYYGASPMSPvrlaEA----IERFG----PIfAQYYGQTEAP-MVITYLRkrdhdPDDPKRLTSCGRPTPGL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 497 APAILNESGEELEGEAEGYLVFKQPwpGIMRtvyGNHERFETT--YFKKfpGYYVTGDGCRRDKDGYYWITGRIDDMLNV 574
Cdd:PRK06188 349 RVALLDEDGREVAQGEVGEICVRGP--LVMD---GYWNRPEETaeAFRD--GWLHTGDVAREDEDGFYYIVDRKKDMIVT 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 575 SGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGhifSPALTEELKKQIREKIGPIATPDYIQNAPGL 654
Cdd:PRK06188 422 GGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPG---AAVDAAELQAHVKERKGSVHAPKQVDFVDSL 498
|
...
gi 1387203675 655 PKT 657
Cdd:PRK06188 499 PLT 501
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
136-609 |
1.83e-29 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 122.73 E-value: 1.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 136 ITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLITTD 215
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 216 AFYrgeklvnlkeladealEKCQEKGFPVKCC---IVVKHLGRAELVTGDSPSqsppikrpCPDVQISwnegvdlwwhel 292
Cdd:cd05904 113 ELA----------------EKLASLALPVVLLdsaEFDSLSFSDLLFEADEAE--------PPVVVIK------------ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 293 mqkagdecepewcdAEDPLFILYTSGSTGKPKGVLHTVGGYmlyVATTFKYVFDF----HAEDVFWCTADIGWITGHSYV 368
Cdd:cd05904 157 --------------QDDVAALLYSSGTTGRSKGVMLTHRNL---IAMVAQFVAGEgsnsDSEDVFLCVLPMFHIYGLSSF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 369 TYGPLANGATSVLfegIPTYpDVSRLWNIVEKYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLGTVGEPINPEAwl 448
Cdd:cd05904 220 ALGLLRLGATVVV---MPRF-DLEELLAAIERYKVTHLPVVPPIVLALVK--SPIVDKYDLSSLRQIMSGAAPLGKEL-- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 449 wYHRVvgAQRCPIVDtFWQ----TETGG--HMlTPLPGAIPMKPGSATFPFFGVAPAILNESGEELegeaegyLVFKQP- 521
Cdd:cd05904 292 -IEAF--RAKFPNVD-LGQgygmTESTGvvAM-CFAPEKDRAKYGSVGRLVPNVEAKIVDPETGES-------LPPNQTg 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 522 --W---PGIMRTVYGNHERFETTYFKKfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAE 596
Cdd:cd05904 360 elWirgPSIMKGYLNNPEATAATIDKE--GWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILD 437
|
490
....*....|...
gi 1387203675 597 AAVVGHPHPVKGE 609
Cdd:cd05904 438 AAVIPYPDEEAGE 450
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
136-665 |
5.78e-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: 121.43 E-value: 5.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 136 ITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLITTD 215
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTSS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 216 AFYRgeklvnlkeLADEALEKCqekgfpvkccivvkHLGRAELVTGDsPSQSPPiKRPCPDVqISWNEgvdlwwhelMQK 295
Cdd:TIGR03098 106 ERLD---------LLHPALPGC--------------HDLRTLIIVGD-PAHASE-GHPGEEP-ASWPK---------LLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 296 AGDECEPEWCDAEDPLFILYTSGSTGKPKGVLHT----VGGymlyvATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYG 371
Cdd:TIGR03098 151 LGDADPPHPVIDSDMAAILYTSGSTGRPKGVVLShrnlVAG-----AQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 372 pLANGATSVLFEGIpTYPDVSRLwniVEKYKVTKFYTAPTairLLMKFGDEPVTKHSRASLQVLGTVGEPInPEAWLWYH 451
Cdd:TIGR03098 226 -FYVGATVVLHDYL-LPRDVLKA---LEKHGITGLAAVPP---LWAQLAQLDWPESAAPSLRYLTNSGGAM-PRATLSRL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 452 RvvgaQRCPIVDTFWQ---TETGGHMLTPlPGAIPMKPGS--ATFPFFGVapAILNESGEELEGEAEGYLVFKQP----- 521
Cdd:TIGR03098 297 R----SFLPNARLFLMyglTEAFRSTYLP-PEEVDRRPDSigKAIPNAEV--LVLREDGSECAPGEEGELVHRGAlvamg 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 522 -WPGIMRTVygnhERFE-TTYFK---KFPGYYV-TGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVA 595
Cdd:TIGR03098 370 yWNDPEKTA----ERFRpLPPFPgelHLPELAVwSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVA 445
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 596 EAAVVGHPHPVKGECLYCFVTLCDGHIFSPAlteELKKQIREKIGPIATPDYIQNAPGLPKTRSGNQKRV 665
Cdd:TIGR03098 446 EAVAFGVPDPTLGQAIVLVVTPPGGEELDRA---ALLAECRARLPNYMVPALIHVRQALPRNANGKIDRK 512
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
315-660 |
9.44e-29 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 117.97 E-value: 9.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 315 YTSGSTGKPKGVLHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIGWITGhSYVTYG-PLANGAtSVLFEGIPTYPD--- 390
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNG-SVVTLLtPLASGA-HVVLAGPAGYRNpgl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 391 VSRLWNIVEKYKVTKFYTAPTAIRLLMKfgdEPVTKhSRASLQVLGTVGEPINPEAwlwYHRVVGAQRCPIVDTFWQTE- 469
Cdd:cd05944 86 FDNFWKLVERYRITSLSTVPTVYAALLQ---VPVNA-DISSLRFAMSGAAPLPVEL---RARFEDATGLPVVEGYGLTEa 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 470 TGGHMLTPLPGaiPMKPGSA--TFPFFGVAPAILNESGEELEGEAEGYLvfkqpWPGIM--RTVYGNH---ERFETTYFK 542
Cdd:cd05944 159 TCLVAVNPPDG--PKRPGSVglRLPYARVRIKVLDGVGRLLRDCAPDEV-----GEICVagPGVFGGYlytEGNKNAFVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 543 kfPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHI 622
Cdd:cd05944 232 --DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAV 309
|
330 340 350
....*....|....*....|....*....|....*....
gi 1387203675 623 FSPA-LTEELKKQIREKigpIATPDYIQNAPGLPKTRSG 660
Cdd:cd05944 310 VEEEeLLAWARDHVPER---AAVPKHIEVLEELPVTAVG 345
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
135-660 |
2.26e-28 |
|
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: 118.93 E-value: 2.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 135 QITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLcERIL-DSNCSLLIT 213
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRL-RYILeDAEPALVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 214 TDAfyrgeklvnlkeLADealekcqekGFPVkCCIVVKHLGRAELVTGDSPSQSPPikrpcPDvqiswnegvdlwwhelm 293
Cdd:cd12116 91 DDA------------LPD---------RLPA-GLPVLLLALAAAAAAPAAPRTPVS-----PD----------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 294 qkagdecepewcdaeDPLFILYTSGSTGKPKGV----------LHTVGG--------YMLYVATtfkYVFDFHAEDVFWc 355
Cdd:cd12116 127 ---------------DLAYVIYTSGSTGRPKGVvvshrnlvnfLHSMRErlglgpgdRLLAVTT---YAFDISLLELLL- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 356 tadigwitghsyvtygPLANGATSVLFEGIPTYpDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPvtkhsRASLQVL 435
Cdd:cd12116 188 ----------------PLLAGARVVIAPRETQR-DPEALARLIEAHSITVMQATPATWRMLLDAGWQG-----RAGLTAL 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 436 -GtvGEPINPEawlwyhrvVGAQRCPIVDTFWQ----TET----GGHMLTPLPGAIPM-KPGSATFpfFGVAPAILnesg 505
Cdd:cd12116 246 cG--GEALPPD--------LAARLLSRVGSLWNlygpTETtiwsTAARVTAAAGPIPIgRPLANTQ--VYVLDAAL---- 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 506 eelegeaegylvfkQPWP-GIMRTVY--------GNHERFETTyFKKF-------PG--YYVTGDGCRRDKDGYYWITGR 567
Cdd:cd12116 310 --------------RPVPpGVPGELYiggdgvaqGYLGRPALT-AERFvpdpfagPGsrLYRTGDLVRRRADGRLEYLGR 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 568 IDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGEcLYCFVTLCDGHIFSpalTEELKKQIREKIGPIATPDY 647
Cdd:cd12116 375 ADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRR-LVAYVVLKAGAAPD---AAALRAHLRATLPAYMVPSA 450
|
570
....*....|...
gi 1387203675 648 IQNAPGLPKTRSG 660
Cdd:cd12116 451 FVRLDALPLTANG 463
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
145-660 |
4.15e-28 |
|
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: 117.93 E-value: 4.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 145 VCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFagfsseslceriLDSNcSLLITTDAFYrgeklv 224
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVF------------VPLN-PTLKESVLRY------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 225 nLKELADEALEKCQEKGfpvkccivVKHLGRAELVTGDspsqsppikrpcPDVQISwnegVDLWWHELMQKAGDECEPEw 304
Cdd:cd05922 64 -LVADAGGRIVLADAGA--------ADRLRDALPASPD------------PGTVLD----ADGIRAARASAPAHEVSHE- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 305 cdaeDPLFILYTSGSTGKPKGVL--HTvggYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGpLANGATSVLF 382
Cdd:cd05922 118 ----DLALLLYTSGSTGSPKLVRlsHQ---NLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTH-LLRGATLVLT 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 383 EGipTYPDVSrLWNIVEKYKVTKFYTAPTAIRLL--MKFGDEPVtkhsrASLQVLGTVGEPInPEAWLWYHR--VVGAQr 458
Cdd:cd05922 190 ND--GVLDDA-FWEDLREHGATGLAGVPSTYAMLtrLGFDPAKL-----PSLRYLTQAGGRL-PQETIARLRelLPGAQ- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 459 cpIVDTFWQTETGGHMLTPLPGAIPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWpgIMRTvYGNHERFET 538
Cdd:cd05922 260 --VYVMYGQTEATRRMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPN--VMKG-YWNDPPYRR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 539 TYfKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVkGECLYCFVTLC 618
Cdd:cd05922 335 KE-GRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAP 412
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1387203675 619 DGHIFSPALteelkKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:cd05922 413 DKIDPKDVL-----RSLAERLPPYKVPATVRVVDELPLTASG 449
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
137-663 |
5.39e-28 |
|
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: 117.48 E-value: 5.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 137 TYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALhsivfagfsseslCERILdsncsllittdA 216
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAV-------------TNPIL-----------P 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 217 FYRGEKLVNLkeladeaLEKCQEKGFPVkccivvkhlgrAELVTGDSPSQSPpikrpcpdvqiswnegvdlwwhelmqka 296
Cdd:cd05903 59 FFREHELAFI-------LRRAKAKVFVV-----------PERFRQFDPAAMP---------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 297 gdecepewcdaEDPLFILYTSGSTGKPKGVLHTVGGYMlyvATTFKYV--FDFHAEDVFWCTADIGWITGHSYVTYGPLA 374
Cdd:cd05903 93 -----------DAVALLLFTSGTTGEPKGVMHSHNTLS---ASIRQYAerLGLGPGDVFLVASPMAHQTGFVYGFTLPLL 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 375 NGATSVLfegiptypdvSRLWN------IVEKYKVTKFYTAPTAIRLLMK---FGDEPVtkhsrASLQVLGTVGEPINP- 444
Cdd:cd05903 159 LGAPVVL----------QDIWDpdkalaLMREHGVTFMMGATPFLTDLLNaveEAGEPL-----SRLRTFVCGGATVPRs 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 445 ---EAWlwyhRVVGAQRCPIvdtFWQTETGGHMLTPLPGAIPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQP 521
Cdd:cd05903 224 larRAA----ELLGAKVCSA---YGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGP 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 522 wpgimRTVYGNHERFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVG 601
Cdd:cd05903 297 -----SVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVA 371
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387203675 602 HPHPVKGECLYCFVTLCDGHIFS-PALTEELKKQ--IREKIgpiatPDYIQNAPGLPKTRSGN-QK 663
Cdd:cd05903 372 LPDERLGERACAVVVTKSGALLTfDELVAYLDRQgvAKQYW-----PERLVHVDDLPRTPSGKvQK 432
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
119-663 |
8.65e-28 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 118.23 E-value: 8.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 119 DKVAFYWEGNEPEETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALhsivfagfsses 198
Cdd:PRK13295 39 DKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAV------------ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 199 lcerildSNCSLLIttdafYRGEKLVNLKELADEalekcqekgfpvKCCIVVKHL---GRAELVTGdspsqsppIKRPCP 275
Cdd:PRK13295 107 -------LNPLMPI-----FRERELSFMLKHAES------------KVLVVPKTFrgfDHAAMARR--------LRPELP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 276 DVQ---ISWNEGVDLWWHELmqkagdeCEPEWCDAEDPLFIL--------------YTSGSTGKPKGVLHT----VGGYM 334
Cdd:PRK13295 155 ALRhvvVVGGDGADSFEALL-------ITPAWEQEPDAPAILarlrpgpddvtqliYTSGTTGEPKGVMHTantlMANIV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 335 LYVATtfkyvFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEgiptYPDVSRLWNIVEKYKVTkFYTAPTAir 414
Cdd:PRK13295 228 PYAER-----LGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQD----IWDPARAAELIRTEGVT-FTMASTP-- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 415 LLMKFGDepVTKHSR---ASLQVLGTVGEPINP----EAWlwyhRVVGAQrcpIVDTFWQTETGGHMLTpLPGAiPMKPG 487
Cdd:PRK13295 296 FLTDLTR--AVKESGrpvSSLRTFLCAGAPIPGalveRAR----AALGAK---IVSAWGMTENGAVTLT-KLDD-PDERA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 488 SAT--FPFFGVAPAILNESGEELEGEAEGYLVFKQPwpgimrTVYGNHERFETTYFKKFPGYYVTGDGCRRDKDGYYWIT 565
Cdd:PRK13295 365 STTdgCPLPGVEVRVVDADGAPLPAGQIGRLQVRGC------SNFGGYLKRPQLNGTDADGWFDTGDLARIDADGYIRIS 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 566 GRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFS-PALTEELKKQireKIGPIAT 644
Cdd:PRK13295 439 GRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDfEEMVEFLKAQ---KVAKQYI 515
|
570 580
....*....|....*....|
gi 1387203675 645 PDYIQNAPGLPKTRSGN-QK 663
Cdd:PRK13295 516 PERLVVRDALPRTPSGKiQK 535
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
583-660 |
1.95e-27 |
|
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: 105.70 E-value: 1.95e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387203675 583 EVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGhifSPALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPG---VELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSG 75
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
132-667 |
2.10e-27 |
|
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: 118.81 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 132 ETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGAlhsivfA------GFSSESLcERIL- 204
Cdd:COG1020 498 GDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGA------AyvpldpAYPAERL-AYMLe 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 205 DSNCSLLITTDAFyrgeklvnLKELADEALEkcqekgfpvkcCIVVkhlgrAELVTGDSPSQSPPIKRpcpdvqiswneg 284
Cdd:COG1020 571 DAGARLVLTQSAL--------AARLPELGVP-----------VLAL-----DALALAAEPATNPPVPV------------ 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 285 vdlwwhelmqkagdecepewcDAEDPLFILYTSGSTGKPKGVLHTVGG---YMLYVATTFK------------YVFDFHA 349
Cdd:COG1020 615 ---------------------TPDDLAYVIYTSGSTGRPKGVMVEHRAlvnLLAWMQRRYGlgpgdrvlqfasLSFDASV 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 350 EDVFWctadigwitghsyvtygPLANGATSVLF--EGIptyPDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVtkh 427
Cdd:COG1020 674 WEIFG-----------------ALLSGATLVLAppEAR---RDPAALAELLARHRVTVLNLTPSLLRALLDAAPEAL--- 730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 428 srASLQVLGTVGEPINPEAWLWYHRVVGAQR---------CPIVDTFWQTETGGHMLTPLP--GAIP----------MKP 486
Cdd:COG1020 731 --PSLRLVLVGGEALPPELVRRWRARLPGARlvnlygpteTTVDSTYYEVTPPDADGGSVPigRPIAntrvyvldahLQP 808
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 487 -----------GSAtfpffGVAPAILNEsgeelegeaegylvfkqpwPGimRTVygnhERFETTYFkKFPG--YYVTGDG 553
Cdd:COG1020 809 vpvgvpgelyiGGA-----GLARGYLNR-------------------PE--LTA----ERFVADPF-GFPGarLYRTGDL 857
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 554 CRRDKDG---YywiTGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGhifSPALTEE 630
Cdd:COG1020 858 ARWLPDGnleF---LGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAG---AAAAAAL 931
|
570 580 590
....*....|....*....|....*....|....*..
gi 1387203675 631 LKKQIREKIGPIATPDYIQNAPGLPKTRSGNQKRVDP 667
Cdd:COG1020 932 LRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLAL 968
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
119-664 |
1.01e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 114.29 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 119 DKVAFYWEGnepeetTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGAlhSIVFAG--FSS 196
Cdd:PRK03640 17 DRTAIEFEE------KKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGA--VAVLLNtrLSR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 197 ESLCERILDSNCSLLITTDAFyrgeklvnlkelADEALEKCQEKgfpvkccivvkhlgraelvtgdspsqsppikrpcpd 276
Cdd:PRK03640 89 EELLWQLDDAEVKCLITDDDF------------EAKLIPGISVK------------------------------------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 277 vqiswnegvdlwWHELMQKAGDECEP-EWCDAEDPLFILYTSGSTGKPKGVLHTVGGYmLYVATTFKYVFDFHAEDVFWC 355
Cdd:PRK03640 121 ------------FAELMNGPKEEAEIqEEFDLDEVATIMYTSGTTGKPKGVIQTYGNH-WWSAVGSALNLGLTEDDCWLA 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 356 TADIGWITGHSYVTygplangaTSVLFeGIPTYP----DVSRLWNIVEKYKVTKFYTAPTAI-RLLMKFGDEPVTKHSRA 430
Cdd:PRK03640 188 AVPIFHISGLSILM--------RSVIY-GMRVVLvekfDAEKINKLLQTGGVTIISVVSTMLqRLLERLGEGTYPSSFRC 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 431 SLqvLGtvGEPInPEAWLwyhrvvgaQRC-----PIVDTFWQTETGGHMLTPLPGAIPMKPGSATFPFFGVAPAILNESG 505
Cdd:PRK03640 259 ML--LG--GGPA-PKPLL--------EQCkekgiPVYQSYGMTETASQIVTLSPEDALTKLGSAGKPLFPCELKIEKDGV 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 506 EELEGEAEGYLVfKQP--WPGIMRTVYGNHERFETTYFKkfpgyyvTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAE 583
Cdd:PRK03640 326 VVPPFEEGEIVV-KGPnvTKGYLNREDATRETFQDGWFK-------TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAE 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 584 VESALVEHKAVAEAAVVGHPHPVKGECLYCFVtLCDGHIFSpaltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGNQK 663
Cdd:PRK03640 398 IEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFV-VKSGEVTE----EELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLL 472
|
.
gi 1387203675 664 R 664
Cdd:PRK03640 473 R 473
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
136-660 |
3.52e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 113.20 E-value: 3.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 136 ITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLITTD 215
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 216 AFYrgEKLVNLKelADEALEKcqekgfpvkccIVVKHLgrAELVTGDSPSQSPPIKRPCPD--VQISWNEGVDLWwhELM 293
Cdd:PRK06710 130 LVF--PRVTNVQ--SATKIEH-----------VIVTRI--ADFLPFPKNLLYPFVQKKQSNlvVKVSESETIHLW--NSV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 294 QKAGDECEPEWCDAEDPLFIL-YTSGSTGKPKGVLHTVGGYMLYVATTFKYVFD-FHAEDVFWCTADIGWITGHSYVTYG 371
Cdd:PRK06710 191 EKEVNTGVEVPCDPENDLALLqYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNcKEGEEVVLGVLPFFHVYGMTAVMNL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 372 PLANGATSVLfegIPTYpDVSRLWNIVEKYKVTKFYTAPTAIRLLMkfgDEPVTK-HSRASLQVLGTVGEPINPEAWLWY 450
Cdd:PRK06710 271 SIMQGYKMVL---IPKF-DMKMVFEAIKKHKVTLFPGAPTIYIALL---NSPLLKeYDISSIRACISGSAPLPVEVQEKF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 451 HRVVGA---------QRCPIVDT--FWQTETGGHMLTPLPGA----IPMKPGSATFPffgvapailnesgeelegEAEGY 515
Cdd:PRK06710 344 ETVTGGklvegygltESSPVTHSnfLWEKRVPGSIGVPWPDTeamiMSLETGEALPP------------------GEIGE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 516 LVFKQPwpGIMRTVYGNHErfETTYFKKfPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVA 595
Cdd:PRK06710 406 IVVKGP--QIMKGYWNKPE--ETAAVLQ-DGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQ 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387203675 596 EAAVVGHPHPVKGECLYCFVTLCDGHIFSpalTEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:PRK06710 481 EVVTIGVPDPYRGETVKAFVVLKEGTECS---EEELNQFARKYLAAYKVPKVYEFRDELPKTTVG 542
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
118-660 |
7.47e-26 |
|
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: 111.95 E-value: 7.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 118 GDKVAFYWEGNEPEETTqiTYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGA-LHSI---VFAg 193
Cdd:cd12119 10 GDREIVSRTHEGEVHRY--TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAvLHTInprLFP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 194 fsseslcERILdsncslLITTDAfyrGEKLVnlkeLADEALEKCQEKGFPVkcCIVVKHLgraeLVTGDSPSQSPPIkrp 273
Cdd:cd12119 87 -------EQIA------YIINHA---EDRVV----FVDRDFLPLLEAIAPR--LPTVEHV----VVMTDDAAMPEPA--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 274 cpdvqiswNEGVDLWWHELMQKAGDECEPEWcDAEDPLFILYTSGSTGKPKGV--------LHTVGGYMlyvattfKYVF 345
Cdd:cd12119 138 --------GVGVLAYEELLAAESPEYDWPDF-DENTAAAICYTSGTTGNPKGVvyshrslvLHAMAALL-------TDGL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 346 DFHAEDVF-----------WCTADIGWITGHSYVTYGPLANGATsvlfegiptypdvsrLWNIVEKYKVTKFYTAPTAIR 414
Cdd:cd12119 202 GLSESDVVlpvvpmfhvnaWGLPYAAAMVGAKLVLPGPYLDPAS---------------LAELIEREGVTFAAGVPTVWQ 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 415 LLMKFGDEpvTKHSRASLQVLgtvgepinpeawlwyhrVVGAQRCP----------IVDTF--W-QTETG--GHMLTPLP 479
Cdd:cd12119 267 GLLDHLEA--NGRDLSSLRRV-----------------VIGGSAVPrslieafeerGVRVIhaWgMTETSplGTVARPPS 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 480 GAIPMKPG-------SATFPFFGVAPAILNESGEELEGEAEGY--LVFKQPWpgIMRTVYGNHErfeTTYFKKFPGYYVT 550
Cdd:cd12119 328 EHSNLSEDeqlalraKQGRPVPGVELRIVDDDGRELPWDGKAVgeLQVRGPW--VTKSYYKNDE---ESEALTEDGWLRT 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 551 GDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSPaltEE 630
Cdd:cd12119 403 GDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTA---EE 479
|
570 580 590
....*....|....*....|....*....|
gi 1387203675 631 LKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:cd12119 480 LLEFLADKVAKWWLPDDVVFVDEIPKTSTG 509
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
119-660 |
9.99e-26 |
|
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: 110.80 E-value: 9.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 119 DKVAFYWEGnepeetTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSES 198
Cdd:cd05945 6 DRPAVVEGG------RTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 199 LcERILD-SNCSLLITTDAfyrgeklvnlkeladealekcqekgfpvkccivvkhlgraelvtgdspsqsppikrpcpdv 277
Cdd:cd05945 80 I-REILDaAKPALLIADGD------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 278 qiswnegvdlwwhelmqkagdecepewcdaeDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKYvFDFHAEDVFWCTA 357
Cdd:cd05945 98 -------------------------------DNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSD-FPLGPGDVFLNQA 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 358 ---------DIgwitghsyvtYGPLANGATSV------------LFEGIPTYPdvsrlwnivekykVTKFYTAPTAIRLL 416
Cdd:cd05945 146 pfsfdlsvmDL----------YPALASGATLVpvprdatadpkqLFRFLAEHG-------------ITVWVSTPSFAAMC 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 417 MkfGDEPVTKHSRASL-QVLgTVGEPI-NPEAWLWYHRvvgAQRCPIVDTFWQTET----GGHMLTPLPGAiPMKPGSAT 490
Cdd:cd05945 203 L--LSPTFTPESLPSLrHFL-FCGEVLpHKTARALQQR---FPDARIYNTYGPTEAtvavTYIEVTPEVLD-GYDRLPIG 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 491 FPFFGVAPAILNESGEELEGEAEGYLVFKQP--WPGIMRtVYGNHERFettyFKKFPGY--YVTGDGCRRDKDGYYWITG 566
Cdd:cd05945 276 YAKPGAKLVILDEDGRPVPPGEKGELVISGPsvSKGYLN-NPEKTAAA----FFPDEGQraYRTGDLVRLEADGLLFYRG 350
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 567 RIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGhiFSPALTEELKKQIREKIGPIATPD 646
Cdd:cd05945 351 RLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPG--AEAGLTKAIKAELAERLPPYMIPR 428
|
570
....*....|....
gi 1387203675 647 YIQNAPGLPKTRSG 660
Cdd:cd05945 429 RFVYLDELPLNANG 442
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
115-660 |
2.68e-25 |
|
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: 109.98 E-value: 2.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 115 KKLGDKVAFYWEGnepeetTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGAlhsiVFAGF 194
Cdd:cd12117 8 ARTPDAVAVVYGD------RSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGA----AYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 195 SSESLCERIL----DSNCSLLITtdafyrgeklvnLKELADEALEkcqekgfpvkccivvkhlGRAELVTGDSPSQSPPI 270
Cdd:cd12117 78 DPELPAERLAfmlaDAGAKVLLT------------DRSLAGRAGG------------------LEVAVVIDEALDAGPAG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 271 KRPCPdvqiswnegvdlwwhelmqkagdecepewCDAEDPLFILYTSGSTGKPKGVLHTVGGyMLYVATTFKYVfDFHAE 350
Cdd:cd12117 128 NPAVP-----------------------------VSPDDLAYVMYTSGSTGRPKGVAVTHRG-VVRLVKNTNYV-TLGPD 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 351 DVFWCTADIGWiTGHSYVTYGPLANGATSVLFEGiPTYPDVSRLWNIVEKYKVTK-FYTAPTaIRLLMKFGDEpvtkhSR 429
Cdd:cd12117 177 DRVLQTSPLAF-DASTFEIWGALLNGARLVLAPK-GTLLDPDALGALIAEEGVTVlWLTAAL-FNQLADEDPE-----CF 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 430 ASLQVLGTVGEPINPEawlWYHRVVgaQRCP---IVDTFWQTETGG----HMLTPL---PGAIPMkpGSatfPFFGVAPA 499
Cdd:cd12117 249 AGLRELLTGGEVVSPP---HVRRVL--AACPglrLVNGYGPTENTTfttsHVVTELdevAGSIPI--GR---PIANTRVY 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 500 ILNesgeelegeaegylVFKQPWP------------GIMRTvYGNH-----ERFETTYFkkFPG--YYVTGDGCRRDKDG 560
Cdd:cd12117 319 VLD--------------EDGRPVPpgvpgelyvggdGLALG-YLNRpaltaERFVADPF--GPGerLYRTGDLARWLPDG 381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 561 YYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTlcdghiFSPALT-EELKKQIREKI 639
Cdd:cd12117 382 RLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVV------AEGALDaAELRAFLRERL 455
|
570 580
....*....|....*....|.
gi 1387203675 640 GPIATPDYIQNAPGLPKTRSG 660
Cdd:cd12117 456 PAYMVPAAFVVLDELPLTANG 476
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
130-629 |
3.19e-25 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 109.91 E-value: 3.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 130 PEETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSN-C 208
Cdd:cd05923 23 PARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEmT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 209 SLLITTDAF-YRGEKLVNLKELADEALEKcqekgfpvkccivvkhlgraelvTGDSPSQSPPIKRPcpdvqiswnegvdl 287
Cdd:cd05923 103 AAVIAVDAQvMDAIFQSGVRVLALSDLVG-----------------------LGEPESAGPLIEDP-------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 288 wwhelmqkagdECEPEwcdaeDPLFILYTSGSTGKPKGVL---HTVGGYMLYVATTFKYVFDFHaeDVFWCTADIGWITG 364
Cdd:cd05923 146 -----------PREPE-----QPAFVFYTSGTTGLPKGAVipqRAAESRVLFMSTQAGLRHGRH--NVVLGLMPLYHVIG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 365 HSYVTYGPLANGATSVLfegiPTYPDVSRLWNIVEKYKVTKFYTAPTAIRLLMkfGDEPVTKHSRASLQVLGTVGEPInP 444
Cdd:cd05923 208 FFAVLVAALALDGTYVV----VEEFDPADALKLIEQERVTSLFATPTHLDALA--AAAEFAGLKLSSLRHVTFAGATM-P 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 445 EAWLwyHRVVGAQRCPIVDTFWQTE--TGGHMLTPLPGAIpMKPGsatfpFFG---VAPaILNESGEELEGEAEGYLVFK 519
Cdd:cd05923 281 DAVL--ERVNQHLPGEKVNIYGTTEamNSLYMRDARTGTE-MRPG-----FFSevrIVR-IGGSPDEALANGEEGELIVA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 520 QP----WPGIMRtvygnheRFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVA 595
Cdd:cd05923 352 AAadaaFTGYLN-------QPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVT 424
|
490 500 510
....*....|....*....|....*....|....
gi 1387203675 596 EAAVVGHPHPVKGECLYCFVTLCDGHIFSPALTE 629
Cdd:cd05923 425 EVVVIGVADERWGQSVTACVVPREGTLSADELDQ 458
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
131-661 |
3.98e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 109.83 E-value: 3.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 131 EETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSL 210
Cdd:PRK06164 31 DEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARW 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 211 LITTDAFyRGEKLVN-LKELADEALEkcqekgfPVKCCIVVkhlgraelvtgDSPSQSPPIKRPCPDVQIswnegVDLWW 289
Cdd:PRK06164 111 LVVWPGF-KGIDFAAiLAAVPPDALP-------PLRAIAVV-----------DDAADATPAPAPGARVQL-----FALPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 290 HELMQKAGDECEPewcdaEDPLFILY-TSGSTGKPKGVLHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYV 368
Cdd:PRK06164 167 PAPPAAAGERAAD-----PDAGALLFtTSGTTSGPKLVLHRQAT-LLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 369 TyGPLANGATSVLfegIPTYpDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPvtkHSRASLQVLGTVGepINPeAWL 448
Cdd:PRK06164 241 L-GALAGGAPLVC---EPVF-DAARTARALRRHRVTHTFGNDEMLRRILDTAGER---ADFPSARLFGFAS--FAP-ALG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 449 WYHRVVGAQRCPIVDTFWQTE-----TGGHMLTP-----LPGAIPMKPGSATFPFFGVAPAILNESGEELEGEAEgylvf 518
Cdd:PRK06164 310 ELAALARARGVPLTGLYGSSEvqalvALQPATDPvsvriEGGGRPASPEARVRARDPQDGALLPDGESGEIEIRA----- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 519 kqpwPGIMRTVYGNHErfETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAA 598
Cdd:PRK06164 385 ----PSLMRGYLDNPD--ATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQ 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387203675 599 VVGHPHPVKGEClYCFVTLCDGhifSPALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGN 661
Cdd:PRK06164 459 VVGATRDGKTVP-VAFVIPTDG---ASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAN 517
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
118-660 |
9.66e-25 |
|
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: 108.13 E-value: 9.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 118 GDKVAFYWEGnepeetTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSE 197
Cdd:cd17646 12 PDAPAVVDEG------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 198 SLCERILDSNCSLLITT-DAFYRGEKLVNLKELADEALekcqekgfpvkccivvkhlgraelvtgDSPSQSPPIKRPCPD 276
Cdd:cd17646 86 RLAYMLADAGPAVVLTTaDLAARLPAGGDVALLGDEAL---------------------------AAPPATPPLVPPRPD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 277 vqiswnegvdlwwhelmqkagdecepewcdaeDPLFILYTSGSTGKPKGVLHTVGG---YMLYVATTFK----------- 342
Cdd:cd17646 139 --------------------------------NLAYVIYTSGSTGRPKGVMVTHAGivnRLLWMQDEYPlgpgdrvlqkt 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 343 -YVFDFHAEDVFWctadigwitghsyvtygPLANGATSVLFEgiP-TYPDVSRLWNIVEKYKVTKFYTAPTAIRLlmkFG 420
Cdd:cd17646 187 pLSFDVSVWELFW-----------------PLVAGARLVVAR--PgGHRDPAYLAALIREHGVTTCHFVPSMLRV---FL 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 421 DEPvTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTET----------GGHMLTPLPGAIPMkPGSAT 490
Cdd:cd17646 245 AEP-AAGSCASLRRVFCSGEALPPELAARFLALPGA---ELHNLYGPTEAaidvthwpvrGPAETPSVPIGRPV-PNTRL 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 491 FpffgVAPAILNEsgeelegeaegylvfkQPwPGIMRTVY--------GNH-------ERFETTYFKKFPGYYVTGDGCR 555
Cdd:cd17646 320 Y----VLDDALRP----------------VP-VGVPGELYlggvqlarGYLgrpaltaERFVPDPFGPGSRMYRTGDLAR 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 556 RDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHifSPALTEELKKQI 635
Cdd:cd17646 379 WRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGA--AGPDTAALRAHL 456
|
570 580
....*....|....*....|....*
gi 1387203675 636 REKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:cd17646 457 AERLPEYMVPAAFVVLDALPLTANG 481
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
96-602 |
1.12e-24 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 109.03 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 96 MKGATTNICYNVLDRIVHE--KKLGDKVAFYWEGNEPEETtqITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPEL 173
Cdd:COG1022 1 MSEFSDVPPADTLPDLLRRraARFPDRVALREKEDGIWQS--LTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 174 VVAMLACARLGALHSIVFAGfSSESLCERIL-DSNCSLLITTDAfyrgEKLVNLKELADE--ALEKcqekgfpvkccIVV 250
Cdd:COG1022 79 VIADLAILAAGAVTVPIYPT-SSAEEVAYILnDSGAKVLFVEDQ----EQLDKLLEVRDElpSLRH-----------IVV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 251 khlgraelVTGDSPSQSPPIkrpcpdvqISWNE----GVDLWWHELMQKAGDECEPewcdaEDPLFILYTSGSTGKPKGV 326
Cdd:COG1022 143 --------LDPRGLRDDPRL--------LSLDEllalGREVADPAELEARRAAVKP-----DDLATIIYTSGTTGRPKGV 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 327 LHTVGGyMLYVATTFKYVFDFHAEDVF-----WCtadigWITGHSyVTYGPLANGATSVLFEGIPTYPD----------- 390
Cdd:COG1022 202 MLTHRN-LLSNARALLERLPLGPGDRTlsflpLA-----HVFERT-VSYYALAAGATVAFAESPDTLAEdlrevkptfml 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 391 -VSRLWnivEKYK---VTKFYTAPTAIRLLMKFGDEPVTKHSRASLQ------------------VLGTV---------- 438
Cdd:COG1022 275 aVPRVW---EKVYagiQAKAEEAGGLKRKLFRWALAVGRRYARARLAgkspslllrlkhaladklVFSKLrealggrlrf 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 439 ----GEPINPEAWLWYHrVVGAqrcPIVDTFWQTETGGHMLTPLPGAIpmKPGSATFPFFGVAPAI-----Lnesgeele 509
Cdd:COG1022 352 avsgGAALGPELARFFR-ALGI---PVLEGYGLTETSPVITVNRPGDN--RIGTVGPPLPGVEVKIaedgeI-------- 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 510 geaegyLVfKQpwPGIMRTVYGNHErfETTyfKKFP--GYYVTGD-GcRRDKDGYYWITGRIDDMLNVS-GHLLSTAEVE 585
Cdd:COG1022 418 ------LV-RG--PNVMKGYYKNPE--ATA--EAFDadGWLHTGDiG-ELDEDGFLRITGRKKDLIVTSgGKNVAPQPIE 483
|
570
....*....|....*..
gi 1387203675 586 SALVEHKAVAEAAVVGH 602
Cdd:COG1022 484 NALKASPLIEQAVVVGD 500
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
119-664 |
1.52e-24 |
|
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: 107.07 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 119 DKVAFYWEGNEpeettqITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSES 198
Cdd:cd17649 2 DAVALVFGDQS------LSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 199 LCERILDSNCSLLITtdafyrgeklvnlkeladealekcqekgfpvkccivvkhlgraelvtgdspsQSPpikrpcpdvq 278
Cdd:cd17649 76 LRYMLEDSGAGLLLT----------------------------------------------------HHP---------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 279 iswnegvdlwwhelmqkagdecepewcdaEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKYvFDFHAEDVFWCTAD 358
Cdd:cd17649 94 -----------------------------RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGDRELQFAS 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 359 IGWITGHSYVtYGPLANGAtSVLFEGIPTYPDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEpVTKHSRASLQVLGTV 438
Cdd:cd17649 144 FNFDGAHEQL-LPPLICGA-CVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADR-TGDGRPPSLRLYIFG 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 439 GEPINPE-AWLWyhrvvGAQRCPIVDTFWQTETgghMLTPL-----------PGAIPMkpGSatfPFFGVAPAILNESGE 506
Cdd:cd17649 221 GEALSPElLRRW-----LKAPVRLFNAYGPTEA---TVTPLvwkceagaaraGASMPI--GR---PLGGRSAYILDADLN 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 507 ELEGEAEGYLVFKQPwpGIMRtvyGNHERFETTYfKKF-------PG--YYVTGDGCRRDKDGYYWITGRIDDMLNVSGH 577
Cdd:cd17649 288 PVPVGVTGELYIGGE--GLAR---GYLGRPELTA-ERFvpdpfgaPGsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGF 361
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 578 LLSTAEVESALVEHKAVAEAAVVGHPHPVkGECLYCFVTLCDGHIfSPALTEELKKQIREKIGPIATPDYIQNAPGLPKT 657
Cdd:cd17649 362 RIELGEIEAALLEHPGVREAAVVALDGAG-GKQLVAYVVLRAAAA-QPELRAQLRTALRASLPDYMVPAHLVFLARLPLT 439
|
....*..
gi 1387203675 658 RSGNQKR 664
Cdd:cd17649 440 PNGKLDR 446
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
135-660 |
1.68e-24 |
|
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: 106.79 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 135 QITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLITT 214
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 215 dafyrgeklvnlKELADEALekcqekgfpvkccivvkhlgraelvtgdspsqsppikrpcpdvqiswnegvdlwwhelmq 294
Cdd:cd05935 81 ------------SELDDLAL------------------------------------------------------------ 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 295 kagdecepewcdaedplfILYTSGSTGKPKGVLHTvGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLA 374
Cdd:cd05935 89 ------------------IPYTSGTTGLPKGCMHT-HFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVY 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 375 NGATSVLFegipTYPDVSRLWNIVEKYKVTKFYTAPTAIRLLMkfGDEPVTKHSRASLQVLGTVGEPInPEAWLwyHRVV 454
Cdd:cd05935 150 VGGTYVLM----ARWDRETALELIEKYKVTFWTNIPTMLVDLL--ATPEFKTRDLSSLKVLTGGGAPM-PPAVA--EKLL 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 455 GAQRCPIVDTFWQTETgghmLTPLPGAIPMKPGSATF--PFFGVAPAILNESGEELEGEAEG-YLVFKQPwpGIMRTvYG 531
Cdd:cd05935 221 KLTGLRFVEGYGLTET----MSQTHTNPPLRPKLQCLgiP*FGVDARVIDIETGRELPPNEVgEIVVRGP--QIFKG-YW 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 532 NHERFETTYFKKFPG--YYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGE 609
Cdd:cd05935 294 NRPEETEESFIEIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGE 373
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1387203675 610 CLYCFVTLcDGHIFSPALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:cd05935 374 EVKAFIVL-RPEYRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASG 423
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
119-660 |
2.24e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 107.56 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 119 DKVAFYWEGNEpeettqITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSES 198
Cdd:PRK07786 32 DAPALRFLGNT------TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 199 LCERILDSNCSLLITTDAfyrgekLVNLKELADEALEKCQekgfpvkccIVVkhlgraelVTGDSPsqsppikrpcpdvq 278
Cdd:PRK07786 106 IAFLVSDCGAHVVVTEAA------LAPVATAVRDIVPLLS---------TVV--------VAGGSS-------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 279 iswnEGVDLWWHELMQKAGDECEPEWCDAEDPLFILYTSGSTGKPKGVLHTvggYMLYVATTFKYVFDFHA---EDVFWC 355
Cdd:PRK07786 149 ----DDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLT---HANLTGQAMTCLRTNGAdinSDVGFV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 356 TADIGWITGhsyvtygpLANGATSVLFeGIPT--YP----DVSRLWNIVEKYKVTKFYTAPTAIRLLMkfgDEPVTKHSR 429
Cdd:PRK07786 222 GVPLFHIAG--------IGSMLPGLLL-GAPTviYPlgafDPGQLLDVLEAEKVTGIFLVPAQWQAVC---AEQQARPRD 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 430 ASLQVLGTVGEPiNPEAWL--WYHRVVGAQrcpIVDTFWQTEtgghmLTP----LPG--AIpMKPGSATFPFFGVAPAIL 501
Cdd:PRK07786 290 LALRVLSWGAAP-ASDTLLrqMAATFPEAQ---ILAAFGQTE-----MSPvtcmLLGedAI-RKLGSVGKVIPTVAARVV 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 502 NESGEELEGEAEGYLVFKQPwpGIMRTVYGN----HERFETtyfkkfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGH 577
Cdd:PRK07786 360 DENMNDVPVGEVGEIVYRAP--TLMSGYWNNpeatAEAFAG-------GWFHSGDLVRQDEEGYVWVVDRKKDMIISGGE 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 578 LLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGhifSPALT-EELKKQIREKIGPIATPDYIQNAPGLPK 656
Cdd:PRK07786 431 NIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRND---DAALTlEDLAEFLTDRLARYKHPKALEIVDALPR 507
|
....
gi 1387203675 657 TRSG 660
Cdd:PRK07786 508 NPAG 511
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
107-639 |
4.89e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 106.62 E-value: 4.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 107 VLDRIVHEkkLGDKVAFYWEGnepeetTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGA- 185
Cdd:PRK05605 37 LYDNAVAR--FGDRPALDFFG------ATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAv 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 186 --LHSIVFAGFSSESLCErilDSNCSLLITTD-AFYRGEKLVnlkelADEALEKcqekgfpvkccivvkhlgraeLVTGD 262
Cdd:PRK05605 109 vvEHNPLYTAHELEHPFE---DHGARVAIVWDkVAPTVERLR-----RTTPLET---------------------IVSVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 263 SPSQSPPIKR-------------------PCPDVqISWNEGVDlwwhELMQKAGDECEPEWCDAEDPLFILYTSGSTGKP 323
Cdd:PRK05605 160 MIAAMPLLQRlalrlpipalrkaraaltgPAPGT-VPWETLVD----AAIGGDGSDVSHPRPTPDDVALILYTSGTTGKP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 324 KGVLHTVGGYMLYVATTFKYVFD--------------FHAEDVFWCtadigwitghsyVTYGPLAnGATSVLFegiPTyP 389
Cdd:PRK05605 235 KGAQLTHRNLFANAAQGKAWVPGlgdgpervlaalpmFHAYGLTLC------------LTLAVSI-GGELVLL---PA-P 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 390 DVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEP-VTKHS-RASLQvlgtvgepinpeawlwyhrvvGAQRCPiVDTF-- 465
Cdd:PRK05605 298 DIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERgVDLSGvRNAFS---------------------GAMALP-VSTVel 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 466 WQTETGGHM-----LT---PLPGAIPM----KPGSATFPFFGVAPAILNESGEELEGEAEGY--LVFKQPwpgimRTVYG 531
Cdd:PRK05605 356 WEKLTGGLLvegygLTetsPIIVGNPMsddrRPGYVGVPFPDTEVRIVDPEDPDETMPDGEEgeLLVRGP-----QVFKG 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 532 NHERFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECL 611
Cdd:PRK05605 431 YWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEV 510
|
570 580
....*....|....*....|....*...
gi 1387203675 612 YCFVTLCDGHIFSPaltEELKKQIREKI 639
Cdd:PRK05605 511 VAAVVLEPGAALDP---EGLRAYCREHL 535
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
131-601 |
5.13e-24 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 105.76 E-value: 5.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 131 EETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESlCERIL-DSNCS 209
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQ-IAYILnDSEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 210 LLITTDAfyrgeklvnlkeladealekcqekgfpvkccivvkhlgraelvtgdspsqsppikrpcpdvqiswnegvdlww 289
Cdd:cd05907 80 ALFVEDP------------------------------------------------------------------------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 290 helmqkagdecepewcdaEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKYVfDFHAEDVFWCTADIGWITGHSYVT 369
Cdd:cd05907 87 ------------------DDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERL-PATEGDRHLSFLPLAHVFERRAGL 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 370 YGPLANGATSVLFEGIPTYPD------------VSRLWnivEK-YKVTKFYTAPTAIRLLMKFgdepvtkHSRASLQVLG 436
Cdd:cd05907 148 YVPLLAGARIYFASSAETLLDdlsevrptvflaVPRVW---EKvYAAIKVKAVPGLKRKLFDL-------AVGGRLRFAA 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 437 TVGEPINPEAWLWYHrvvgAQRCPIVDTFWQTETGGHMLTPLPGAIpmKPGSATFPFFGVAPAILNESGeelegeaegyL 516
Cdd:cd05907 218 SGGAPLPAELLHFFR----ALGIPVYEGYGLTETSAVVTLNPPGDN--RIGTVGKPLPGVEVRIADDGE----------I 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 517 VFKQpwPGIMRTVYGNHErfETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDML-NVSGHLLSTAEVESALVEHKAVA 595
Cdd:cd05907 282 LVRG--PNVMLGYYKNPE--ATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLIS 357
|
....*.
gi 1387203675 596 EAAVVG 601
Cdd:cd05907 358 QAVVIG 363
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
313-664 |
3.54e-23 |
|
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: 102.42 E-value: 3.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 313 ILYTSGSTGKPKGVLHTVGGYmLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGpLANGATSVLFEGIptypDVS 392
Cdd:cd05912 82 IMYTSGTTGKPKGVQQTFGNH-WWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRS-VIYGMTVYLVDKF----DAE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 393 RLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLqvLGtvGEPInPEAWLwyhrvvgaQRC-----PIVDTFWQ 467
Cdd:cd05912 156 QVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRCIL--LG--GGPA-PKPLL--------EQCkekgiPVYQSYGM 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 468 TETGGHMLTPLPGAIPMKPGSATFPFFGVAPAILNESGEELEGEAegyLVFKQPwpGIMRTVYGNHER----FETTYFKk 543
Cdd:cd05912 223 TETCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPPYEVGE---ILLKGP--NVTKGYLNRPDAteesFENGWFK- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 544 fpgyyvTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCdghif 623
Cdd:cd05912 297 ------TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE----- 365
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1387203675 624 SPALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGNQKR 664
Cdd:cd05912 366 RPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLR 406
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
132-660 |
4.13e-23 |
|
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: 102.78 E-value: 4.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 132 ETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLL 211
Cdd:cd12115 21 GDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 212 ITtdafyrgeklvnlkeladealekcqekgfpvkccivvkhlgraelvtgdspsqsppikrpcpdvqiswnegvdlwwhe 291
Cdd:cd12115 101 LT------------------------------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 292 lmqkagdecepewcDAEDPLFILYTSGSTGKPKGVL---HTVGGYMLYVATTF------------KYVFDFHAEDVFwct 356
Cdd:cd12115 103 --------------DPDDLAYVIYTSGSTGRPKGVAiehRNAAAFLQWAAAAFsaeelagvlastSICFDLSVFELF--- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 357 adigwitghsyvtyGPLANGATSVLFEGIPTYPDVSRLwnivekYKVTKFYTAPTAIRLLMKFGDEPvtkhsrASLQVLG 436
Cdd:cd12115 166 --------------GPLATGGKVVLADNVLALPDLPAA------AEVTLINTVPSAAAELLRHDALP------ASVRVVN 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 437 TVGEPINPEAWLWYHRVVGAQRcpIVDTFWQTETgghmlTPLPGAIPMKPGSATFPFFGVAPAilnesgeelegEAEGYL 516
Cdd:cd12115 220 LAGEPLPRDLVQRLYARLQVER--VVNLYGPSED-----TTYSTVAPVPPGASGEVSIGRPLA-----------NTQAYV 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 517 V--FKQPWP------------GIMRTVYGN----HERFETTYFkkFPG--YYVTGDGCRRDKDGYYWITGRIDDMLNVSG 576
Cdd:cd12115 282 LdrALQPVPlgvpgelyiggaGVARGYLGRpgltAERFLPDPF--GPGarLYRTGDLVRWRPDGLLEFLGRADNQVKVRG 359
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 577 HLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGhifSPALTEELKKQIREKIGPIATPDYIQNAPGLPK 656
Cdd:cd12115 360 FRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPG---AAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPL 436
|
....
gi 1387203675 657 TRSG 660
Cdd:cd12115 437 TPNG 440
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
108-660 |
4.78e-23 |
|
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: 103.18 E-value: 4.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 108 LDRIVHE--KKLGDKVAFYwEGNepeetTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGA 185
Cdd:cd05920 17 LGDLLARsaARHPDRIAVV-DGD-----RRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 186 LhsIVFAGFSseslcerildsncsllittdafYRGEKLVNLKELADealekcqekgfpVKCCIVvkhlgraelvtgdsps 265
Cdd:cd05920 91 V--PVLALPS----------------------HRRSELSAFCAHAE------------AVAYIV---------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 266 qsppikrpcPDVqiswNEGVDlwWHELMQKAGDECEpewcdaeDPLFILYTSGSTGKPKGVLHTVGGYmLYVATTFKYVF 345
Cdd:cd05920 119 ---------PDR----HAGFD--HRALARELAESIP-------EVALFLLSGGTTGTPKLIPRTHNDY-AYNVRASAEVC 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 346 DFHAEDVFWCTADIGwitgHSYVTYGP-----LANGATSVLfegiPTYPDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFG 420
Cdd:cd05920 176 GLDQDTVYLAVLPAA----HNFPLACPgvlgtLLAGGRVVL----APDPSPDAAFPLIEREGVTVTALVPALVSLWLDAA 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 421 DEPvtKHSRASLQVLGTVGEPINPEAwlwYHRVVGAQRCPIVDTFWQTEtGGHMLTPL--PGAI-------PMKPGSATF 491
Cdd:cd05920 248 ASR--RADLSSLRLLQVGGARLSPAL---ARRVPPVLGCTLQQVFGMAE-GLLNYTRLddPDEViihtqgrPMSPDDEIR 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 492 pffgvapaILNESGEELEGEAEGYLVFKQPWP--GIMRTVYGNHERFETTyfkkfpGYYVTGDGCRRDKDGYYWITGRID 569
Cdd:cd05920 322 --------VVDEEGNPVPPGEEGELLTRGPYTirGYYRAPEHNARAFTPD------GFYRTGDLVRRTPDGYLVVEGRIK 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 570 DMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDghifSPALTEELKKQIREKigPIAT---PD 646
Cdd:cd05920 388 DQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRD----PPPSAAQLRRFLRER--GLAAyklPD 461
|
570
....*....|....
gi 1387203675 647 YIQNAPGLPKTRSG 660
Cdd:cd05920 462 RIEFVDSLPLTAVG 475
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
134-660 |
8.91e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 102.46 E-value: 8.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 134 TQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLIT 213
Cdd:PRK13391 23 EVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALIT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 214 TDAFYrgeklvnlkELADEALEKCQEkgfpVKCCIVVkhlgraelvtgDSPSQSPPIKR------PCPDVQI-SWNEGVD 286
Cdd:PRK13391 103 SAAKL---------DVARALLKQCPG----VRHRLVL-----------DGDGELEGFVGyaeavaGLPATPIaDESLGTD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 287 LwwhelmqkagdecepewcdaedplfiLYTSGSTGKPKGVL----HTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGwi 362
Cdd:PRK13391 159 M--------------------------LYSSGTTGRPKGIKrplpEQPPDTPLPLTAFLQRLWGFRSDMVYLSPAPLY-- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 363 tgHSyvtyGPLA-------NGATSVLFEGIptypDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVL 435
Cdd:PRK13391 211 --HS----APQRavmlvirLGGTVIVMEHF----DAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEVA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 436 GTVGEPINPE------AWlWyhrvvgaqrCPIVDTFW-QTETGGHMLTPLPGAIPmKPGSATFPFFGVaPAILNESGeel 508
Cdd:PRK13391 281 IHAAAPCPPQvkeqmiDW-W---------GPIIHEYYaATEGLGFTACDSEEWLA-HPGTVGRAMFGD-LHILDDDG--- 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 509 egeaegylvfkQPWP-GIMRTVYGNHER-FEttYFK----------KFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSG 576
Cdd:PRK13391 346 -----------AELPpGEPGTIWFEGGRpFE--YLNdpaktaearhPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGG 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 577 HLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSPALTEELKKQIREKIGPIATPDYIQNAPGLPK 656
Cdd:PRK13391 413 VNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPR 492
|
....
gi 1387203675 657 TRSG 660
Cdd:PRK13391 493 LPTG 496
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
134-660 |
7.02e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 99.59 E-value: 7.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 134 TQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLIT 213
Cdd:PRK08276 10 EVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 214 TDAFyrgeklvnlKELADEALEKCQEkgfpvkccivvkHLGRAELVTGDSPsqsppikrpcpdvqiswneGVDLWWHELM 293
Cdd:PRK08276 90 SAAL---------ADTAAELAAELPA------------GVPLLLVVAGPVP-------------------GFRSYEEALA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 294 QKAGDECEPEWCDAEdplfILYTSGSTGKPKGVL--------HTVGGYMLYVATTFkyvFDFHAEDVFWCTADIGwitgH 365
Cdd:PRK08276 130 AQPDTPIADETAGAD----MLYSSGTTGRPKGIKrplpgldpDEAPGMMLALLGFG---MYGGPDSVYLSPAPLY----H 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 366 SYVT-YG--PLANGATSVLFEGIptypDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPI 442
Cdd:PRK08276 199 TAPLrFGmsALALGGTVVVMEKF----DAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYDVSSLRVAIHAAAPC 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 443 NPE------AWlWyhrvvGaqrcPIVD-TFWQTETGGHMLTPLPGAIPmKPGSATFPFFGVApAILNESGEELEGEAEGY 515
Cdd:PRK08276 275 PVEvkramiDW-W-----G----PIIHeYYASSEGGGVTVITSEDWLA-HPGSVGKAVLGEV-RILDEDGNELPPGEIGT 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 516 LVFKQPWPGImrTVYGNHERFETTYFKKfpGYYVTGDGCRRDKDGYYWITGRIDDMLnVSGHL-LSTAEVESALVEHKAV 594
Cdd:PRK08276 343 VYFEMDGYPF--EYHNDPEKTAAARNPH--GWVTVGDVGYLDEDGYLYLTDRKSDMI-ISGGVnIYPQEIENLLVTHPKV 417
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387203675 595 AEAAVVGHPHPVKGECLYCFVTLCDGHIFSPALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:PRK08276 418 ADVAVFGVPDEEMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTG 483
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
137-663 |
1.05e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 99.46 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 137 TYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLITTDA 216
Cdd:PRK12583 47 TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 217 FyRGEKLVN-----LKELADEALEKCQEKGFPvkccivvkHLGRAELVTGDSPsqsppikrpcpdvqiswnEGVdLWWHE 291
Cdd:PRK12583 127 F-KTSDYHAmlqelLPGLAEGQPGALACERLP--------ELRGVVSLAPAPP------------------PGF-LAWHE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 292 LmQKAGDECEPE-------WCDAEDPLFILYTSGSTGKPKGVL---HTV--GGYMLYVAttfkyvFDFHAEDVFWCTADI 359
Cdd:PRK12583 179 L-QARGETVSREalaerqaSLDRDDPINIQYTSGTTGFPKGATlshHNIlnNGYFVAES------LGLTEHDRLCVPVPL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 360 GWITGHSYVTYGPLANGATsVLFEGIPTYPDVSrlWNIVEKYKVTKFYTAPTairLLMKFGDEPvtKHSRASLQVLGT-- 437
Cdd:PRK12583 252 YHCFGMVLANLGCMTVGAC-LVYPNEAFDPLAT--LQAVEEERCTALYGVPT---MFIAELDHP--QRGNFDLSSLRTgi 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 438 -VGEPINPEAwlwYHRVVGAQRCP-IVDTFWQTETGG-HMLTPLPGAIPMKPGSA--TFPFFGVApaILNESGEELEGEA 512
Cdd:PRK12583 324 mAGAPCPIEV---MRRVMDEMHMAeVQIAYGMTETSPvSLQTTAADDLERRVETVgrTQPHLEVK--VVDPDGATVPRGE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 513 EGYLVFKqpwpG--IMRTVYGNHERFETTYFKKfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVE 590
Cdd:PRK12583 399 IGELCTR----GysVMKGYWNNPEATAESIDED--GWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFT 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387203675 591 HKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSpalTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGN-QK 663
Cdd:PRK12583 473 HPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAAS---EEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKvQK 543
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
116-660 |
1.45e-21 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 98.60 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 116 KLGDKVAFYWEgNEPEETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFS 195
Cdd:PRK08008 19 VYGHKTALIFE-SSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 196 SESlCERILDsNC--SLLITTDAFYRGEKLVNlkeladealekcQEKGFPVKccivvkHLgraeLVTGdspSQSPPIkrp 273
Cdd:PRK08008 98 REE-SAWILQ-NSqaSLLVTSAQFYPMYRQIQ------------QEDATPLR------HI----CLTR---VALPAD--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 274 cpdvqiswnEGVDLWWHELMQKAGDECEPEWCDAEDPLFILYTSGSTGKPKGVLHT-----VGGYmlY----VATTFKYV 344
Cdd:PRK08008 148 ---------DGVSSFTQLKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVIThynlrFAGY--YsawqCALRDDDV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 345 F-----DFHAEdvFWCTADIGWITGhsyvtygplanGATSVLFEgipTYpDVSRLWNIVEKYKVTKFYTAPTAIRLLMKf 419
Cdd:PRK08008 217 YltvmpAFHID--CQCTAAMAAFSA-----------GATFVLLE---KY-SARAFWGQVCKYRATITECIPMMIRTLMV- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 420 gdEPVTKHSRASL--QVLGTVgePINPEAWLWYHRVVGAQrcpIVDTFWQTETgghmltpLPGAIPMKPG------SATF 491
Cdd:PRK08008 279 --QPPSANDRQHClrEVMFYL--NLSDQEKDAFEERFGVR---LLTSYGMTET-------IVGIIGDRPGdkrrwpSIGR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 492 PFFGVAPAILNESGEELEGEAEGYLVFK-QPWPGIMRTVYGNHErfETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDD 570
Cdd:PRK08008 345 PGFCYEAEIRDDHNRPLPAGEIGEICIKgVPGKTIFKEYYLDPK--ATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCN 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 571 MLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSPaltEELKKQIREKIGPIATPDYIQN 650
Cdd:PRK08008 423 MIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSE---EEFFAFCEQNMAKFKVPSYLEI 499
|
570
....*....|
gi 1387203675 651 APGLPKTRSG 660
Cdd:PRK08008 500 RKDLPRNCSG 509
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
309-660 |
1.83e-21 |
|
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: 97.75 E-value: 1.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 309 DPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKYvFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFegipTY 388
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDA-WRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFL----PK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 389 PDVSRLWNIVEKYKVTKFYTAPTA-IRLL--MKFGDEPVTKHSRAS-----LQVLGTVGEPInP--EAWlwyhRVVGAQR 458
Cdd:cd05941 165 FDPKEVAISRLMPSITVFMGVPTIyTRLLqyYEAHFTDPQFARAAAaerlrLMVSGSAALPV-PtlEEW----EAITGHT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 459 cpIVDTFWQTETGGHMLTPLPGaiPMKPGSATFPFFGVAPAIL-NESGEELEGEAEGYLVFKQPwpGIMRTVYGNHERFE 537
Cdd:cd05941 240 --LLERYGMTEIGMALSNPLDG--ERRPGTVGMPLPGVQARIVdEETGEPLPRGEVGEIQVRGP--SVFKEYWNKPEATK 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 538 ttyfKKFP--GYYVTGDGCRRDKDGYYWITGRI-DDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCF 614
Cdd:cd05941 314 ----EEFTddGWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAV 389
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1387203675 615 VTLCDGhifSPALT-EELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:cd05941 390 VVLRAG---AAALSlEELKEWAKQRLAPYKRPRRLILVDELPRNAMG 433
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
119-660 |
7.11e-21 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 96.47 E-value: 7.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 119 DKVAFYweGNEPEettqITYRELLVQVCRFSNVLRKQ-GICKGDRVAIYMPMIPELVVAMLACARLGALhSIVFagfsse 197
Cdd:PRK06839 17 DRIAII--TEEEE----MTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECI-AVPL------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 198 slcerildsncsllittdafyrgeklvNLKELADEALEKCQEKGFPVKCCiVVKHLGRAELVTGDSpSQSPPIkrpcpdv 277
Cdd:PRK06839 84 ---------------------------NIRLTENELIFQLKDSGTTVLFV-EKTFQNMALSMQKVS-YVQRVI------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 278 qisWNEGVDlwwhELMQKAGDECEPEwcDAEDPLFILYTSGSTGKPKG-VLHTVGgyMLYVATTFKYVFDFHAEDVFWCT 356
Cdd:PRK06839 128 ---SITSLK----EIEDRKIDNFVEK--NESASFIICYTSGTTGKPKGaVLTQEN--MFWNALNNTFAIDLTMHDRSIVL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 357 ADIGWITGHSYVTYGPLANGATSVlfegIPTYPDVSRLWNIVEKYKVTKFYTAPT---AIRLLMKFgdepvTKHSRASLQ 433
Cdd:PRK06839 197 LPLFHIGGIGLFAFPTLFAGGVII----VPRKFEPTKALSMIEKHKVTVVMGVPTihqALINCSKF-----ETTNLQSVR 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 434 VLGTVGEPInPEAWLwyhRVVGAQRCPIVDTFWQTETGGHMLTPLPGAIPMKPGSATFPFFGVAPAILNESGEELEGEAE 513
Cdd:PRK06839 268 WFYNGGAPC-PEELM---REFIDRGFLFGQGFGMTETSPTVFMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 514 GYLVFKQPwpGIMRTVYGNHERFETTYFKkfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKA 593
Cdd:PRK06839 344 GELLIRGP--NVMKEYWNRPDATEETIQD---GWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSD 418
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387203675 594 VAEAAVVGHPHPVKGECLYCFVTLCDGHIFSpalTEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:PRK06839 419 VYEVAVVGRQHVKWGEIPIAFIVKKSSSVLI---EKDVIEHCRLFLAKYKIPKEIVFLKELPKNATG 482
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
133-665 |
5.41e-20 |
|
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: 93.52 E-value: 5.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 133 TTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALhsivfagfsseslcerildsNCSLLI 212
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAV--------------------LNALNT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 213 TTDAfyrgeklvnlkELADEALEKCQekgfpVKCCIVVKHLGRAELVTGDSPSqsppikrpcpdvqiswnegvdlwwhEL 292
Cdd:cd12118 87 RLDA-----------EEIAFILRHSE-----AKVLFVDREFEYEDLLAEGDPD-------------------------FE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 293 MQKAGDECepewcdaeDPLFILYTSGSTGKPKGVLHTVGGYMLyVATTFKYVFDFHAEDVFWCTADI----GWItghsyV 368
Cdd:cd12118 126 WIPPADEW--------DPIALNYTSGTTGRPKGVVYHHRGAYL-NALANILEWEMKQHPVYLWTLPMfhcnGWC-----F 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 369 TYGPLANGATSVLFEGIpTYPDVsrlWNIVEKYKVTKFYTAPTAIRLLMKfGDEPVTKHSRASLQVLgTVGEPiNPEAWL 448
Cdd:cd12118 192 PWTVAAVGGTNVCLRKV-DAKAI---YDLIEKHKVTHFCGAPTVLNMLAN-APPSDARPLPHRVHVM-TAGAP-PPAAVL 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 449 WYHRVVGAQrcpIVDTFWQTETGGhmltplPGAI-PMKPGSATFPffGVAPAILNESGEELEGEAEGYLVFKQ------P 521
Cdd:cd12118 265 AKMEELGFD---VTHVYGLTETYG------PATVcAWKPEWDELP--TEERARLKARQGVRYVGLEEVDVLDPetmkpvP 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 522 WPG------------IMRTVYGNHERFETTyFKKfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALV 589
Cdd:cd12118 334 RDGktigeivfrgniVMKGYLKNPEATAEA-FRG--GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLY 410
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387203675 590 EHKAVAEAAVVGHPHPVKGECLYCFVTLCDGhifSPALTEELKKQIREKIGPIATPDYIQNAPgLPKTRSGN-QKRV 665
Cdd:cd12118 411 KHPAVLEAAVVARPDEKWGEVPCAFVELKEG---AKVTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKiQKFV 483
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
313-660 |
6.19e-20 |
|
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: 93.21 E-value: 6.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 313 ILYTSGSTGKPKGVLHTVGGYMLYVAT--TFKYVFDFHAEDVFWCTADIGWITGHSyVTYGPLANGATSVLFEGIptypD 390
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLPGGPPDNDTlmAAALGFGPGADSVYLSPAPLYHAAPFR-WSMTALFMGGTLVLMEKF----D 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 391 VSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINP---EAWL-WYHrvvgaqrcPIVDTFW 466
Cdd:cd05929 205 PEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPCPPwvkEQWIdWGG--------PIIWEYY 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 467 Q-TETGGhmLTPLPGAIPMK-PGSATFPFFGVApAILNESGEelegeaegylvfKQPwPGIMRTVY--GN-----HERFE 537
Cdd:cd05929 277 GgTEGQG--LTIINGEEWLThPGSVGRAVLGKV-HILDEDGN------------EVP-PGEIGEVYfaNGpgfeyTNDPE 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 538 TTYFKKFPGYYVT-GDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVT 616
Cdd:cd05929 341 KTAAARNEGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQ 420
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1387203675 617 LCDGHIFSPALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:cd05929 421 PAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTG 464
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
137-664 |
7.50e-20 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 93.66 E-value: 7.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 137 TYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLITTDA 216
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 217 FYRGEKLVNLKELADEalekcqekgfpvkccivVKHLGRAELVTGDSPSQS-----------PPIKRPCPdvqiswnegv 285
Cdd:PRK06087 131 FKQTRPVDLILPLQNQ-----------------LPQLQQIVGVDKLAPATSslslsqiiadyEPLTTAIT---------- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 286 dlwwhelmqkagdecepewCDAEDPLFILYTSGSTGKPKGVLHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIGWITGH 365
Cdd:PRK06087 184 -------------------THGDELAAVLFTSGTEGLPKGVMLTHNN-ILASERAYCARLNLTWQDVFMMPAPLGHATGF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 366 SYVTYGPLANGATSVLFEGIPtyPDVSrlWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSraSLQVLGTVGEPInPE 445
Cdd:PRK06087 244 LHGVTAPFLIGARSVLLDIFT--PDAC--LALLEQQRCTCMLGATPFIYDLLNLLEKQPADLS--ALRFFLCGGTTI-PK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 446 awlwyhRVVgaQRC-----PIVDTFWQTETGGHMLTPLPGAIPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQ 520
Cdd:PRK06087 317 ------KVA--RECqqrgiKLLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 521 PwpGIMRTVYGNHERfeTTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVV 600
Cdd:PRK06087 389 P--NVFMGYLDEPEL--TARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVV 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387203675 601 GHPHPVKGECLYCFVTLCDGHiFSPALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGNQKR 664
Cdd:PRK06087 465 AMPDERLGERSCAYVVLKAPH-HSLTLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQK 527
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
118-666 |
8.17e-20 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 93.79 E-value: 8.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 118 GDKVAFYWEGnepeetTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSE 197
Cdd:PRK08279 51 PDRPALLFED------QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 198 SL--CERILDSncSLLITtdafyrGEKLVnlkeladEALEKCQEkgfpvkccivvkHLGRAELVTGDSpsqsppikrpcp 275
Cdd:PRK08279 125 VLahSLNLVDA--KHLIV------GEELV-------EAFEEARA------------DLARPPRLWVAG------------ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 276 DVQISWNEGVDlwwhELMQKAG--DECEPEWCD---AEDPLFILYTSGSTGKPKGVLHTVGGYMLYVAtTFKYVFDFHAE 350
Cdd:PRK08279 166 GDTLDDPEGYE----DLAAAAAgaPTTNPASRSgvtAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMG-GFGGLLRLTPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 351 DVFWCTADIGWITGHSYVTYGPLANGATSVL---FEgiptypdVSRLWNIVEKYKVTKFYtaptAI----RLLMkfgDEP 423
Cdd:PRK08279 241 DVLYCCLPLYHNTGGTVAWSSVLAAGATLALrrkFS-------ASRFWDDVRRYRATAFQ----YIgelcRYLL---NQP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 424 VTKHSRA-SLQVLgtVGEPINPEAW--------------LW--------------YHRVVGaqRCP--------IVDtfW 466
Cdd:PRK08279 307 PKPTDRDhRLRLM--IGNGLRPDIWdefqqrfgiprileFYaasegnvgfinvfnFDGTVG--RVPlwlahpyaIVK--Y 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 467 QTETGghmlTPLPGA----IPMKPGSAtfpffGVAPAILNEsgeelegeaegylvfKQPWPG----------IMRTVygn 532
Cdd:PRK08279 381 DVDTG----EPVRDAdgrcIKVKPGEV-----GLLIGRITD---------------RGPFDGytdpeasekkILRDV--- 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 533 herfettyFKKFPGYYVTGDGCRRDKDGYYWITGRIDDML-----NVsghllSTAEVESALVEHKAVAEAAVVGHPHP-V 606
Cdd:PRK08279 434 --------FKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFrwkgeNV-----ATTEVENALSGFPGVEEAVVYGVEVPgT 500
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 607 KGECLYCFVTLCDGHIFSPAlteELKKQIREKIGPIATPDYIQNAPGLPKTRSGNQKRVD 666
Cdd:PRK08279 501 DGRAGMAAIVLADGAEFDLA---ALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVD 557
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
289-660 |
1.75e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 92.40 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 289 WHELMQKAGDECEPEWCDAEDPLFILYTSGSTGKPKGVLHTVGgyMLYV---ATTFKYvfDFHAEDVFWCTADIGwitgH 365
Cdd:PRK13388 131 YAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHG--RLAFagrALTERF--GLTRDDVCYVSMPLF----H 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 366 S---YVTYGP-LANGATSVL---FEGIPTYPDVSRlwnivekYKVTKFYTAPTAIRLLMKFGDEPvtKHSRASLQV-LGT 437
Cdd:PRK13388 203 SnavMAGWAPaVASGAAVALpakFSASGFLDDVRR-------YGATYFNYVGKPLAYILATPERP--DDADNPLRVaFGN 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 438 VGEPINPEAWlwyhrvvgAQR--CPIVDTFWQTETGGhMLTPLPGAiPmkPGSATFPFFGVApaILNESGEelegeaegy 515
Cdd:PRK13388 274 EASPRDIAEF--------SRRfgCQVEDGYGSSEGAV-IVVREPGT-P--PGSIGRGAPGVA--IYNPETL--------- 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 516 lvfkQPWPgimRTVYGNH-----------ERFETTYFKKFPGYYV---------------TGDGCRRDKDGYYWITGRID 569
Cdd:PRK13388 331 ----TECA---VARFDAHgallnadeaigELVNTAGAGFFEGYYNnpeataermrhgmywSGDLAYRDADGWIYFAGRTA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 570 DMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSP-ALTEELKKQirEKIGPIATPDYI 648
Cdd:PRK13388 404 DWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPdAFAAFLAAQ--PDLGTKAWPRYV 481
|
410
....*....|..
gi 1387203675 649 QNAPGLPKTRSG 660
Cdd:PRK13388 482 RIAADLPSTATN 493
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
134-664 |
3.45e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 93.10 E-value: 3.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 134 TQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLIT 213
Cdd:PRK12316 535 ETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLS 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 214 TDAFyrGEKLvnlkeladealekcqekgfPVkccivvkhlgraelvtgdspsqSPPIKRPCPDVQISWNEGvdlWWHElm 293
Cdd:PRK12316 615 QSHL--GRKL-------------------PL----------------------AAGVQVLDLDRPAAWLEG---YSEE-- 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 294 qkagdecEPEWC-DAEDPLFILYTSGSTGKPKGVLHT------------------VGGYMLYVaTTFKyvFDFHAEDVFW 354
Cdd:PRK12316 647 -------NPGTElNPENLAYVIYTSGSTGKPKGAGNRhralsnrlcwmqqayglgVGDTVLQK-TPFS--FDVSVWEFFW 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 355 ctadigwitghsyvtygPLANGATSVLF-EGIPTYPDvsRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPvtkhSRASLQ 433
Cdd:PRK12316 717 -----------------PLMSGARLVVAaPGDHRDPA--KLVELINREGVDTLHFVPSMLQAFLQDEDVA----SCTSLR 773
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 434 VLGTVGEPI------NPEAWLWYHRVV---GAQRCPIVDTFWQ-TETGGhmltplpGAIPMKPgsatfPFFGVAPAILNE 503
Cdd:PRK12316 774 RIVCSGEALpadaqeQVFAKLPQAGLYnlyGPTEAAIDVTHWTcVEEGG-------DSVPIGR-----PIANLACYILDA 841
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 504 SGeelegeaegylvfkQPWP------------GIMRTVYG----NHERFETTYFKKFPGYYVTGDGCRRDKDGYYWITGR 567
Cdd:PRK12316 842 NL--------------EPVPvgvlgelylagrGLARGYHGrpglTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGR 907
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 568 IDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGhphpVKGECLYCFVTLCDGhifSPALTEELKKQIREKIGPIATPDY 647
Cdd:PRK12316 908 IDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLESE---GGDWREALKAHLAASLPEYMVPAQ 980
|
570
....*....|....*..
gi 1387203675 648 IQNAPGLPKTRSGNQKR 664
Cdd:PRK12316 981 WLALERLPLTPNGKLDR 997
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
131-664 |
5.90e-19 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 90.72 E-value: 5.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 131 EETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALhsivfagfsseslcerildsncsl 210
Cdd:PRK05852 39 ADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLV------------------------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 211 littdafyrgekLVNLkelaDEALEKCQEkgfpvkcCIVVKHLG-RAELVTGDSPSQSPPIKRPCPDVQISWNEGVDLWW 289
Cdd:PRK05852 95 ------------VVPL----DPALPIAEQ-------RVRSQAAGaRVVLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 290 HELMQKAGDECEPEWCDA------EDPLFILYTSGSTGKPKGVLHTVGGymlyVATTFKYV---FDFHAEDVfwCTADIG 360
Cdd:PRK05852 152 GTLSVHLDAATEPTPATStpeglrPDDAMIMFTGGTTGLPKMVPWTHAN----IASSVRAIitgYRLSPRDA--TVAVMP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 361 WITGHSYVT--YGPLANGATSVLfegiPTYPDVS--RLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLG 436
Cdd:PRK05852 226 LYHGHGLIAalLATLASGGAVLL----PARGRFSahTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 437 TVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTET---------GGHMLTPLPGAIPMKPGSATFPFFGVA--------PA 499
Cdd:PRK05852 302 SCSAPLTAETAQALQTEFAA---PVVCAFGMTEAthqvtttqiEGIGQTENPVVSTGLVGRSTGAQIRIVgsdglplpAG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 500 ILNesgeelegeaegylvfkQPW---PGIMRTVYGNHERFETTYFKkfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSG 576
Cdd:PRK05852 379 AVG-----------------EVWlrgTTVVRGYLGDPTITAANFTD---GWLRTGDLGSLSAAGDLSIRGRIKELINRGG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 577 HLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGhifSPALTEELKKQIREKIGPIATPDYIQNAPGLPK 656
Cdd:PRK05852 439 EKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRES---APPTAEELVQFCRERLAAFEIPASFQEASGLPH 515
|
....*...
gi 1387203675 657 TRSGNQKR 664
Cdd:PRK05852 516 TAKGSLDR 523
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
219-657 |
7.96e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 90.13 E-value: 7.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 219 RGEKLVnlkelADEALEKCQekgfpvkccIVVKHLGRAELVTGDSPsqsppikrpcpDVQISwNEGVDLWWHELMQKAGD 298
Cdd:PRK07867 89 RGAALA-----RDIAHADCQ---------LVLTESAHAELLDGLDP-----------GVRVI-NVDSPAWADELAAHRDA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 299 ECEPEWCDAEDPLFILYTSGSTGKPKGVLHTVG-----GYMLyvATTFkyvfDFHAEDVFWCTADI--------GWITGh 365
Cdd:PRK07867 143 EPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRkvasaGVML--AQRF----GLGPDDVCYVSMPLfhsnavmaGWAVA- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 366 syvtygpLANGATSVL---FEGIPTYPDVSRlwnivekYKVTKF--------YTAPTAIR-------LLMKFGDEpvtkh 427
Cdd:PRK07867 216 -------LAAGASIALrrkFSASGFLPDVRR-------YGATYAnyvgkplsYVLATPERpddadnpLRIVYGNE----- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 428 sraslqvlgtvGEPINPEAWlwyhrvvgAQR--CPIVDTFWQTEtGGHMLTPLPGAipmKPGSATFPFFGVA-------- 497
Cdd:PRK07867 277 -----------GAPGDIARF--------ARRfgCVVVDGFGSTE-GGVAITRTPDT---PPGALGPLPPGVAivdpdtgt 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 498 ---PAILNESGEELEGEAEGYLVFKQPwPGIMRTVYGNHErfeTTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNV 574
Cdd:PRK07867 334 ecpPAEDADGRLLNADEAIGELVNTAG-PGGFEGYYNDPE---ADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRV 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 575 SGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSP-ALTEELKKQirEKIGPIATPDYIQNAPG 653
Cdd:PRK07867 410 DGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPdAFAEFLAAQ--PDLGPKQWPSYVRVCAE 487
|
....
gi 1387203675 654 LPKT 657
Cdd:PRK07867 488 LPRT 491
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
117-660 |
1.41e-18 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 89.43 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 117 LGDKVAFYWEGnepeetTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSS 196
Cdd:PRK06155 34 YPDRPLLVFGG------TRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 197 ESLCERILDSNCSLLITTDAFYrgeklvnlkeladEALEKCQEKGFPVKCCIVVKHLGRAELVTGDSPSQSPPIKRPCPD 276
Cdd:PRK06155 108 PQLEHILRNSGARLLVVEAALL-------------AALEAADPGDLPLPAVWLLDAPASVSVPAGWSTAPLPPLDAPAPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 277 VQISwnegvdlwwhelmqkagdecepewcdAEDPLFILYTSGSTGKPKGVLHTvggymlyvattfkyvfdfHAEDVFW-- 354
Cdd:PRK06155 175 AAVQ--------------------------PGDTAAILYTSGTTGPSKGVCCP------------------HAQFYWWgr 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 355 -CTADIGWITGHSYVTYGPL-------------ANGATSVLFEGIptypDVSRLWNIVEKYKVTKFYTAPTAIRLLMKfg 420
Cdd:PRK06155 211 nSAEDLEIGADDVLYTTLPLfhtnalnaffqalLAGATYVLEPRF----SASGFWPAVRRHGATVTYLLGAMVSILLS-- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 421 dEPVTKHSRAS-LQVLGTVGEPINpeawlwYHRVVGAqRC--PIVDTFWQTETGGHMLTPLPGAipmKPGSATFPFFGVA 497
Cdd:PRK06155 285 -QPARESDRAHrVRVALGPGVPAA------LHAAFRE-RFgvDLLDGYGSTETNFVIAVTHGSQ---RPGSMGRLAPGFE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 498 PAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNH-----ERFETTYFKkfpgyyvTGDGCRRDKDGYYWITGRIDDML 572
Cdd:PRK06155 354 ARVVDEHDQELPDGEPGELLLRADEPFAFATGYFGMpektvEAWRNLWFH-------TGDRVVRDADGWFRFVDRIKDAI 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 573 NVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSPaltEELKKQIREKIGPIATPDYIQNAP 652
Cdd:PRK06155 427 RRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEP---VALVRHCEPRLAYFAVPRYVEFVA 503
|
....*...
gi 1387203675 653 GLPKTRSG 660
Cdd:PRK06155 504 ALPKTENG 511
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
308-664 |
1.23e-17 |
|
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: 84.62 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 308 EDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATsVLFEGIPT 387
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLC-VTGGENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 388 YpdvSRLWNIVEKYKVTKFYTAPTAIRLLMKfgdepVTKHSRA---SLQVLGTVGE-PINPEA--WLWYHRVvgaqrcPI 461
Cdd:cd17635 80 Y---KSLFKILTTNAVTTTCLVPTLLSKLVS-----ELKSANAtvpSLRLIGYGGSrAIAADVrfIEATGLT------NT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 462 VDTFWQTETGGHMLTPLpGAIPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWpgIMRTVYGNHERFETTYF 541
Cdd:cd17635 146 AQVYGLSETGTALCLPT-DDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPA--NMLGYWNNPERTAEVLI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 542 KkfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVT----L 617
Cdd:cd17635 223 D---GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVasaeL 299
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1387203675 618 CDGHIfspaltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGNQKR 664
Cdd:cd17635 300 DENAI------RALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
132-638 |
1.48e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 86.52 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 132 ETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLL 211
Cdd:PRK07788 71 ERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKAL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 212 ITTDAFyrgeklvnlkelaDEALEKCQEKgfpvkccivvkhLGRAeLVTGDSPSQSPPIKRPCPDVQiswnegvdlwwhE 291
Cdd:PRK07788 151 VYDDEF-------------TDLLSALPPD------------LGRL-RAWGGNPDDDEPSGSTDETLD------------D 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 292 LMQKAGDECEPEWcdAEDPLFILYTSGSTGKPKGVLH-------TVGGYMLYVAttfkyvfdFHAEDVFWCTADIGWITG 364
Cdd:PRK07788 193 LIAGSSTAPLPKP--PKPGGIVILTSGTTGTPKGAPRpepsplaPLAGLLSRVP--------FRAGETTLLPAPMFHATG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 365 HSYVTYGpLANGATSVL---FEGIPTYPDVsrlwnivEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEP 441
Cdd:PRK07788 263 WAHLTLA-MALGSTVVLrrrFDPEATLEDI-------AKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 442 INPEAWLWYHRVVGaqrcPIVDTFW-QTETG-GHMLTPLPGAIpmKPGSATFPFFGVAPAILNESGeelegeaegylvfk 519
Cdd:PRK07788 335 LSPELATRALEAFG----PVLYNLYgSTEVAfATIATPEDLAE--APGTVGRPPKGVTVKILDENG-------------- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 520 QPWPG--IMRTVYGNHERFETtYF-----KKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHK 592
Cdd:PRK07788 395 NEVPRgvVGRIFVGNGFPFEG-YTdgrdkQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHP 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1387203675 593 AVAEAAVVGHPHPVKGECLYCFVTLCDGHifspALTEE-LKKQIREK 638
Cdd:PRK07788 474 DVVEAAVIGVDDEEFGQRLRAFVVKAPGA----ALDEDaIKDYVRDN 516
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
137-634 |
1.70e-17 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 86.19 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 137 TYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLITTDA 216
Cdd:PLN02246 52 TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSC 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 217 FYrgEKLVNLKeladealekcQEKGFPVkccivvkhlgraelVTGDSPsqsppikrpcPDVQISWNegvdlwwhELMQKA 296
Cdd:PLN02246 132 YV--DKLKGLA----------EDDGVTV--------------VTIDDP----------PEGCLHFS--------ELTQAD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 297 GDECEPEWCDAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVAttfKYV------FDFHAEDVFWCTADIGWITGHSYVTY 370
Cdd:PLN02246 168 ENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVA---QQVdgenpnLYFHSDDVILCVLPMFHIYSLNSVLL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 371 GPLANGATSVLfegIPTYpDVSRLWNIVEKYKVTkfyTAPTAIRLLMKFGDEP-VTKHSRASLQVLGTVGEPINPEawlw 449
Cdd:PLN02246 245 CGLRVGAAILI---MPKF-EIGALLELIQRHKVT---IAPFVPPIVLAIAKSPvVEKYDLSSIRMVLSGAAPLGKE---- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 450 YHRVVGAqRCP---IVDTFWQTETGGHMLTPLPGA---IPMKPGSAtfpffgvAPAILNESGEELEGEAEGYLVFKQP-- 521
Cdd:PLN02246 314 LEDAFRA-KLPnavLGQGYGMTEAGPVLAMCLAFAkepFPVKSGSC-------GTVVRNAELKIVDPETGASLPRNQPge 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 522 ----WPGIMRTVYGNHERFETTYFKKfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEA 597
Cdd:PLN02246 386 icirGPQIMKGYLNDPEATANTIDKD--GWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADA 463
|
490 500 510
....*....|....*....|....*....|....*..
gi 1387203675 598 AVVGHPHPVKGECLYCFVTLCDGHifspALTEELKKQ 634
Cdd:PLN02246 464 AVVPMKDEVAGEVPVAFVVRSNGS----EITEDEIKQ 496
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
107-663 |
2.14e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 85.71 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 107 VLDRIVheKKLGDKVAFYWeGNEpeettQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGAL 186
Cdd:PRK07798 8 LFEAVA--DAVPDRVALVC-GDR-----RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 187 HSIVFAGFSSESLCERILDSNCSLLITTDAFyrGEKLVNLKEladeALEKcqekgfpvkccivVKHLgraeLVTGDSPSQ 266
Cdd:PRK07798 80 PVNVNYRYVEDELRYLLDDSDAVALVYEREF--APRVAEVLP----RLPK-------------LRTL----VVVEDGSGN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 267 SPPikrpcpdvqiswNEGVDlwWHELMQKAGDECEPEWCDAEDpLFILYTSGSTGKPKGVLHT--------VGGYMLYVA 338
Cdd:PRK07798 137 DLL------------PGAVD--YEDALAAGSPERDFGERSPDD-LYLLYTGGTTGMPKGVMWRqedifrvlLGGRDFATG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 339 TTFKYVFDfHAEDVFWCTADIGWITG---H---SYVTYGPLANGATSVLfegiptYPDVS----RLWNIVEKYKVTkfyt 408
Cdd:PRK07798 202 EPIEDEEE-LAKRAAAGPGMRRFPAPplmHgagQWAAFAALFSGQTVVL------LPDVRfdadEVWRTIEREKVN---- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 409 aptairLLMKFGD---EPVTKHSRA-------SLQVLGTVGEPINP---EAWLWY--HRVvgaqrcpIVDTFWQTETG-G 472
Cdd:PRK07798 271 ------VITIVGDamaRPLLDALEArgpydlsSLFAIASGGALFSPsvkEALLELlpNVV-------LTDSIGSSETGfG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 473 HMLTPLPGAIPmkPGSATF---PFFGVAPAILNEsgeelegeaegyLVFKQPWPG-IMRT------VYGNHERFETTyFK 542
Cdd:PRK07798 338 GSGTVAKGAVH--TGGPRFtigPRTVVLDEDGNP------------VEPGSGEIGwIARRghiplgYYKDPEKTAET-FP 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 543 KFPG--YYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDG 620
Cdd:PRK07798 403 TIDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREG 482
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1387203675 621 HIFSPaltEELKKQIREKIGPIATPDYIQNAPGLPktRSGNQK 663
Cdd:PRK07798 483 ARPDL---AELRAHCRSSLAGYKVPRAIWFVDEVQ--RSPAGK 520
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
135-664 |
4.29e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 86.37 E-value: 4.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 135 QITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLITT 214
Cdd:PRK12467 3120 QLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQ 3199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 215 DAFyrgeklvnlkeladeaLEKcqekgfpvkccIVVKHLGRAELVTGDSPSQSPPikrPCPDVQIswnegvdlwwhelmq 294
Cdd:PRK12467 3200 AHL----------------LEQ-----------LPAPAGDTALTLDRLDLNGYSE---NNPSTRV--------------- 3234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 295 kagdecepewcDAEDPLFILYTSGSTGKPKGVLHTVGG-----------YMLYVATT----FKYVFDFHAEDVFWctadi 359
Cdd:PRK12467 3235 -----------MGENLAYVIYTSGSTGKPKGVGVRHGAlanhlcwiaeaYELDANDRvllfMSFSFDGAQERFLW----- 3298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 360 gwitghsyvtygPLANGATSVLFEGIPTYPDvsRLWNIVEKYKVTKFYTAPTAIRLLMKFGDepvtKHSRASLQVLGTVG 439
Cdd:PRK12467 3299 ------------TLICGGCLVVRDNDLWDPE--ELWQAIHAHRISIACFPPAYLQQFAEDAG----GADCASLDIYVFGG 3360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 440 EPINPEAWLWYHRVV---------GAQRCPIVDTFWQTETGGhmlTPLPGAIPMKPGSAtfpffGVAPAILNESGeeleg 510
Cdd:PRK12467 3361 EAVPPAAFEQVKRKLkprgltngyGPTEAVVTVTLWKCGGDA---VCEAPYAPIGRPVA-----GRSIYVLDGQL----- 3427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 511 eaegylvfkQPWP-GIMRTVY--------GNH-------ERFETTYFKKFPG-YYVTGDGCRRDKDGYYWITGRIDDMLN 573
Cdd:PRK12467 3428 ---------NPVPvGVAGELYiggvglarGYHqrpsltaERFVADPFSGSGGrLYRTGDLARYRADGVIEYLGRIDHQVK 3498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 574 VSGHLLSTAEVESALVEHKAVAEAAVVGHPhPVKGECLYCFVTLcdgHIFSPALTEELKKQIREKIgpiatPDYIQNA-- 651
Cdd:PRK12467 3499 IRGFRIELGEIEARLLQHPSVREAVVLARD-GAGGKQLVAYVVP---ADPQGDWRETLRDHLAASL-----PDYMVPAql 3569
|
570
....*....|....*.
gi 1387203675 652 ---PGLPKTRSGNQKR 664
Cdd:PRK12467 3570 lvlAAMPLGPNGKVDR 3585
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
309-660 |
6.47e-17 |
|
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: 82.38 E-value: 6.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 309 DPLFILYTSGSTGKPKGVLHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLAnGATSVLFEGIPty 388
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAAN-LLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLA-GAELVLLERNQ-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 389 PDVSRLwnivEKYKVTKFYTAPTAIRLLMkfgDEPVTKHSRASLQVLGTVGEPINPEAwlwyHRVVGAQRCPIVDTFWQT 468
Cdd:cd17630 77 ALAEDL----APPGVTHVSLVPTQLQRLL---DSGQGPAALKSLRAVLLGGAPIPPEL----LERAADRGIPLYTTYGMT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 469 ETGGHMLTPLPGAipMKPGSATFPFFGVAPAILNESGEelegeaegylvfkqpWPGIMRTVYGNHERFETTYFKKfPGYY 548
Cdd:cd17630 146 ETASQVATKRPDG--FGRGGVGVLLPGRELRIVEDGEI---------------WVGGASLAMGYLRGQLVPEFNE-DGWF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 549 VTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLycfVTLCDGHifSPALT 628
Cdd:cd17630 208 TTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRP---VAVIVGR--GPADP 282
|
330 340 350
....*....|....*....|....*....|..
gi 1387203675 629 EELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:cd17630 283 AELRAWLKDKLARFKLPKRIYPVPELPRTGGG 314
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
306-660 |
7.84e-17 |
|
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: 83.92 E-value: 7.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 306 DAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKyVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGAtSVLFEGI 385
Cdd:cd05909 145 QPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITA-IFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGI-KVVFHPN 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 386 PTYPDvsRLWNIVEKYKVTKFYTAPTAIRLLMKFgdepVTKHSRASLQVLGTVGEPINPEAW-LWYHRvvgaQRCPIVDT 464
Cdd:cd05909 223 PLDYK--KIPELIYDKKATILLGTPTFLRGYARA----AHPEDFSSLRLVVAGAEKLKDTLRqEFQEK----FGIRILEG 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 465 FWQTETGGHMLTPLPGAiPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwPGIMRTVYGNHERFETTYFKkf 544
Cdd:cd05909 293 YGTTECSPVISVNTPQS-PNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRG-PNVMLGYLNEPELTSFAFGD-- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 545 pGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAV-AEAAVVGHPHPVKGECLYCFVTLCDGHIf 623
Cdd:cd05909 369 -GWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEdNEVAVVSVPDGRKGEKIVLLTTTTDTDP- 446
|
330 340 350
....*....|....*....|....*....|....*...
gi 1387203675 624 spaltEELKKQIRE-KIGPIATPDYIQNAPGLPKTRSG 660
Cdd:cd05909 447 -----SSLNDILKNaGISNLAKPSYIHQVEEIPLLGTG 479
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
47-107 |
1.40e-16 |
|
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: 74.05 E-value: 1.40e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387203675 47 YRELHRRSLEEPREFWGDIAKEFYWKTPCpgpflQYNFDVTKGkIFIEWMKGATTNICYNV 107
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKELDWFKPF-----DKVLDGSNG-PFAKWFVGGKLNVCYNC 55
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
309-660 |
1.43e-16 |
|
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: 81.30 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 309 DPLFILYTSGSTGKPKGVLHTVGGYM-LYVATtfKYVFDFHAEDvfwctadigwitghSYVTYGPLA-----NGATSVLF 382
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIeSFVCN--EDLFNISGED--------------AILAPGPLShslflYGAISALY 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 383 EG----IPTYPDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFgDEPVTKhsrasLQVLGTVGEPINPEAwlwyHRVVGAQ- 457
Cdd:cd17633 65 LGgtfiGQRKFNPKSWIRKINQYNATVIYLVPTMLQALART-LEPESK-----IKSIFSSGQKLFEST----KKKLKNIf 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 458 -RCPIVDTFWQTETGghMLTPLPGAIPMKPGSATFPFFGVAPAILNESGeelegeaegylvfkqpwpGIMRTVYGNHERF 536
Cdd:cd17633 135 pKANLIEFYGTSELS--FITYNFNQESRPPNSVGRPFPNVEIEIRNADG------------------GEIGKIFVKSEMV 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 537 ETTY----FKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGEcLY 612
Cdd:cd17633 195 FSGYvrggFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGE-IA 273
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1387203675 613 CFVTLCDGhIFSPALTEELKKQI-REKIgpiatPDYIQNAPGLPKTRSG 660
Cdd:cd17633 274 VALYSGDK-LTYKQLKRFLKQKLsRYEI-----PKKIIFVDSLPYTSSG 316
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
131-670 |
1.61e-16 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 82.88 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 131 EETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSL 210
Cdd:PRK13382 64 DELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 211 LITTDAFyrgeklvnlKELADEALEKCqekgfpvkccivvkhlgraelvtgdspsqsppikrPCPDVQISWNEGVDLWWH 290
Cdd:PRK13382 144 VIYDEEF---------SATVDRALADC-----------------------------------PQATRIVAWTDEDHDLTV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 291 ELMQKAGDECEPEWCDAEDPLfILYTSGSTGKPKGVLHT-VGGYMlyvatTFKYVFDfhaedvfwctaDIGWITGHSYVT 369
Cdd:PRK13382 180 EVLIAAHAGQRPEPTGRKGRV-ILLTSGTTGTPKGARRSgPGGIG-----TLKAILD-----------RTPWRAEEPTVI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 370 YGPL--ANGATSVLFEGIPTYPDVSR-------LWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGE 440
Cdd:PRK13382 243 VAPMfhAWGFSQLVLAASLACTIVTRrrfdpeaTLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 441 PINPEawlwyhrVVGA---QRCPIVDTFWQTETGGHMLTPLPGAIPMKPGSATFPFFGVAPAILNESgeelegeaegylv 517
Cdd:PRK13382 323 RMRPD-------VVIAfmdQFGDVIYNNYNATEAGMIATATPADLRAAPDTAGRPAEGTEIRILDQD------------- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 518 FKQPWPGIMRTVY-GNHERFE-----TTyfKKF-PGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVE 590
Cdd:PRK13382 383 FREVPTGEVGTIFvRNDTQFDgytsgST--KDFhDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLAT 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 591 HKAVAEAAVVGHPHPVKGECLYCFVTLCDGhifSPALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGNQKRVDPQGK 670
Cdd:PRK13382 461 HPDVAEAAVIGVDDEQYGQRLAAFVVLKPG---ASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
524-666 |
2.28e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 81.17 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 524 GIMRTVYGNHERFETTYFKKfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHP 603
Cdd:cd05917 210 SVMKGYWNDPEKTAEAIDGD--GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVP 287
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387203675 604 HPVKGECLYCFVTLCDGHIFSPaltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGNQKRVD 666
Cdd:cd05917 288 DERYGEEVCAWIRLKEGAELTE---EDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFK 347
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
131-664 |
2.45e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 82.13 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 131 EETTQITYRELLVQVCRFSNVLRKQGiCKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSL 210
Cdd:PRK07638 22 ENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 211 LITtDAFYrgeklvnLKELADEaleKCqekgfPVkccivvkhlgraelvtgdspsqsppikrpcpdvqISWNEgvdlwWH 290
Cdd:PRK07638 101 IVT-ERYK-------LNDLPDE---EG-----RV----------------------------------IEIDE-----WK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 291 ELMQKAGDECEPEwCDAE-DPLFILYTSGSTGKPKGVLHTVGGYMlyvattfkYVFDFHAEDVFWCTADIGWITG---HS 366
Cdd:PRK07638 126 RMIEKYLPTYAPI-ENVQnAPFYMGFTSGSTGKPKAFLRAQQSWL--------HSFDCNVHDFHMKREDSVLIAGtlvHS 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 367 YVTYGplangATSVLFEG-----IPTYPDVSRLWNIvEKYKVTKFYTAPTAIRLLMK---FGDEPVT------KHSRASL 432
Cdd:PRK07638 197 LFLYG-----AISTLYVGqtvhlMRKFIPNQVLDKL-ETENISVMYTVPTMLESLYKenrVIENKMKiissgaKWEAEAK 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 433 QVLGTvgepINPEAWLWyhRVVGAQRCPIVDTFWQTETgghmltplpgaiPMKPGSATFPFFGVAPAILNESGeelegea 512
Cdd:PRK07638 271 EKIKN----IFPYAKLY--EFYGASELSFVTALVDEES------------ERRPNSVGRPFHNVQVRICNEAG------- 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 513 egylvfKQPWPGIMRTVYGNHERFettyfkkFPGYYVTGDGCRR---------------DKDGYYWITGRIDDMLNVSGH 577
Cdd:PRK07638 326 ------EEVQKGEIGTVYVKSPQF-------FMGYIIGGVLARElnadgwmtvrdvgyeDEEGFIYIVGREKNMILFGGI 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 578 LLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLycfVTLCDGHifspALTEELKKQIREKIGPIATPDYIQNAPGLPKT 657
Cdd:PRK07638 393 NIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKP---VAIIKGS----ATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYT 465
|
....*..
gi 1387203675 658 RSGNQKR 664
Cdd:PRK07638 466 NSGKIAR 472
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
131-660 |
3.52e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 81.98 E-value: 3.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 131 EETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSL 210
Cdd:PRK13390 20 ETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 211 LIttdafyrgeklvnlkelADEALEkcqekgfpvkccivvkhlGRAELVTGDSPsqsppikrpcpdVQISWNEGVDLW-- 288
Cdd:PRK13390 100 LV-----------------ASAALD------------------GLAAKVGADLP------------LRLSFGGEIDGFgs 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 289 WHELMQKAGDECEPEWCDAedplFILYTSGSTGKPKGV--------LHTVGGYMLYVATTFkyvFDFHAEDVFWCTADIG 360
Cdd:PRK13390 133 FEAALAGAGPRLTEQPCGA----VMLYSSGTTGFPKGIqpdlpgrdVDAPGDPIVAIARAF---YDISESDIYYSSAPIY 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 361 witgHSyvtyGPL-------ANGATSVLFEGIptypDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQ 433
Cdd:PRK13390 206 ----HA----APLrwcsmvhALGGTVVLAKRF----DAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 434 VLGTVGEPINPEA------WLWyhrvvgaqrcPIVDTFWQ-TETGGHMLTPLPGAIPmKPGSATFPFFGVA--------- 497
Cdd:PRK13390 274 AVIHAAAPCPVDVkhamidWLG----------PIVYEYYSsTEAHGMTFIDSPDWLA-HPGSVGRSVLGDLhicdddgne 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 498 -PAilnesgeelegeaegylvfkqpwpGIMRTVYGNHERFETTYFKK-----------FPGYYVTGDGCRRDKDGYYWIT 565
Cdd:PRK13390 343 lPA------------------------GRIGTVYFERDRLPFRYLNDpektaaaqhpaHPFWTTVGDLGSVDEDGYLYLA 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 566 GRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSPALTEELKKQIREKIGPIATP 645
Cdd:PRK13390 399 DRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIAHYKAP 478
|
570
....*....|....*
gi 1387203675 646 DYIQNAPGLPKTRSG 660
Cdd:PRK13390 479 RSVEFVDELPRTPTG 493
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
135-648 |
5.49e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 82.70 E-value: 5.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 135 QITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLITT 214
Cdd:PRK12316 4576 KLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQ 4655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 215 DAFYrgEKLVNLKELADEALEKCQE-KGFPvkccivvkhlgraelvtgdspSQSPPIKrpcpdvqiswnegvdlwwhelm 293
Cdd:PRK12316 4656 SHLL--QRLPIPDGLASLALDRDEDwEGFP---------------------AHDPAVR---------------------- 4690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 294 qkagdecepewCDAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTfkyvfdfhaEDVFWCTADIGWITGHSYV----- 368
Cdd:PRK12316 4691 -----------LHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHAT---------GERYELTPDDRVLQFMSFSfdgsh 4750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 369 --TYGPLANGAtSVLFEGiPTYPDVSRLWNIVEKYKVTKFYTAPTAIRLLMKfGDEPVTKHSRASLQVLGtvGEPINPEA 446
Cdd:PRK12316 4751 egLYHPLINGA-SVVIRD-DSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAE-HAERDGEPPSLRVYCFG--GEAVAQAS 4825
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 447 W-LWY--------HRVVGAQRCPIVDTFWQTETGghmltPLPGAIPMKPGSatfPFFGVAPAILNESGEELEGEAEGYLV 517
Cdd:PRK12316 4826 YdLAWralkpvylFNGYGPTETTVTVLLWKARDG-----DACGAAYMPIGT---PLGNRSGYVLDGQLNPLPVGVAGELY 4897
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 518 FKQpwPGIMRtvyGNH-------ERFETTYFKKfPG--YYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESAL 588
Cdd:PRK12316 4898 LGG--EGVAR---GYLerpaltaERFVPDPFGA-PGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARL 4971
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387203675 589 VEHKAVAEAAVVGHPHPVkGECLYCFVTLCDGHIF-SPALTEELKKQIREKIGPiATPDYI 648
Cdd:PRK12316 4972 REHPAVREAVVIAQEGAV-GKQLVGYVVPQDPALAdADEAQAELRDELKAALRE-RLPEYM 5030
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
107-671 |
6.72e-16 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 81.62 E-value: 6.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 107 VLDRIVHEKKLGDKVAFYwegnEPEettQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGAL 186
Cdd:PRK06060 9 LLAEQASEAGWYDRPAFY----AAD---VVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 187 HSIVFAGFSSESLCERILDSNCSLLITTDAF---YRGEKLVNLKELADEAlekcqekgfpvkccivvkhlGRAElvtgds 263
Cdd:PRK06060 82 AFLANPELHRDDHALAARNTEPALVVTSDALrdrFQPSRVAEAAELMSEA--------------------ARVA------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 264 PSQSPPIkrpcpdvqiswnegvdlwwhelmqkAGDECEpewcdaedplFILYTSGSTGKPKGVLHTVggymlyvATTFKY 343
Cdd:PRK06060 136 PGGYEPM-------------------------GGDALA----------YATYTSGTTGPPKAAIHRH-------ADPLTF 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 344 VFDFHAEDVFWCTADIGWITGHSYVTYG-------PLANGATSVLfEGIPTYPDVSRLwnIVEKYKVTKFYTAPTAIRLL 416
Cdd:PRK06060 174 VDAMCRKALRLTPEDTGLCSARMYFAYGlgnsvwfPLATGGSAVI-NSAPVTPEAAAI--LSARFGPSVLYGVPNFFARV 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 417 MkfgdEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrCPIVD---------TF-------WQTETGGHMLTPLPG 480
Cdd:PRK06060 251 I----DSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGG--IPILDgigstevgqTFvsnrvdeWRLGTLGRVLPPYEI 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 481 AIPMKPGSATFPffGVAPAIlnesgeelegeaegylvfkqpW---PGIMRTVYGNHERFETTyfkkfPGYYVTGDGCRRD 557
Cdd:PRK06060 325 RVVAPDGTTAGP--GVEGDL---------------------WvrgPAIAKGYWNRPDSPVAN-----EGWLDTRDRVCID 376
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 558 KDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSPALTEELKKQIRE 637
Cdd:PRK06060 377 SDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLN 456
|
570 580 590
....*....|....*....|....*....|....
gi 1387203675 638 KIGPIATPDYIQNAPGLPKTRSGNQKRVDPQGKS 671
Cdd:PRK06060 457 RLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQS 490
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
136-664 |
9.73e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 81.93 E-value: 9.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 136 ITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLITTD 215
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR 2108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 216 AFYrgEKLVNLKELADEALEKcqekgfpvkccivvkhlgRAELvtgdspsQSPPIKRPCPDVqiswnegvdlwwhelmqk 295
Cdd:PRK12316 2109 HLL--ERLPLPAGVARLPLDR------------------DAEW-------ADYPDTAPAVQL------------------ 2143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 296 agdecepewcDAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKY---------------VFDFHAEDVFWctadig 360
Cdd:PRK12316 2144 ----------AGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERyelspadcelqfmsfSFDGAHEQWFH------ 2207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 361 witghsyvtygPLANGATSVLFEGipTYPDVSRLWNIVEKYKVTKFYTAPTairLLMKFGDEPVTKHSRASLQVLGTVGE 440
Cdd:PRK12316 2208 -----------PLLNGARVLIRDD--ELWDPEQLYDEMERHGVTILDFPPV---YLQQLAEHAERDGRPPAVRVYCFGGE 2271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 441 PINPEAWLWYHRVVGAQRcpIVDTFWQTETgghMLTPLP-GAIPMKPGSATFPFFGVAPA-----ILNESGEELEGEAEG 514
Cdd:PRK12316 2272 AVPAASLRLAWEALRPVY--LFNGYGPTEA---VVTPLLwKCRPQDPCGAAYVPIGRALGnrrayILDADLNLLAPGMAG 2346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 515 YLVFKQPwpGIMRTVYG----NHERFETTYFKKFPG-YYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALV 589
Cdd:PRK12316 2347 ELYLGGE--GLARGYLNrpglTAERFVPDPFSASGErLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQ 2424
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387203675 590 EHKAVAEAAVVGHPHPvKGECLYCFVTLCDGhifSPALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGNQKR 664
Cdd:PRK12316 2425 AHPAVREAVVVAQDGA-SGKQLVAYVVPDDA---AEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDR 2495
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
133-664 |
1.25e-15 |
|
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: 79.82 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 133 TTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLI 212
Cdd:cd17650 10 TRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 213 Ttdafyrgeklvnlkeladealekcqekgfpvkccivvkhlgraelvtgdspsqsppikrpcpdvqiswnegvdlwwhel 292
Cdd:cd17650 90 T------------------------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 293 mqkagdecepewcDAEDPLFILYTSGSTGKPKGVL-------HTVGGY------------MLYVATtfkYVFDFHAEDvf 353
Cdd:cd17650 91 -------------QPEDLAYVIYTSGTTGKPKGVMvehrnvaHAAHAWrreyeldsfpvrLLQMAS---FSFDVFAGD-- 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 354 WCTAdigwitghsyvtygpLANGATSVLfegIP--TYPDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRAS 431
Cdd:cd17650 153 FARS---------------LLNGGTLVI---CPdeVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMR 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 432 LQVLGTVGEPINPEAWLwYHRVvgAQRCPIVDTFWQTET--------GGhmLTPLPGAIPMKPGSatfPFFGVAPAILNE 503
Cdd:cd17650 215 LLIVGSDGCKAQDFKTL-AARF--GQGMRIINSYGVTEAtidstyyeEG--RDPLGDSANVPIGR---PLPNTAMYVLDE 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 504 SGeelegeaegylvfkQPWP------------GIMRTVYGN----HERFETTYFKKFPGYYVTGDGCRRDKDGYYWITGR 567
Cdd:cd17650 287 RL--------------QPQPvgvagelyiggaGVARGYLNRpeltAERFVENPFAPGERMYRTGDLARWRADGNVELLGR 352
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 568 IDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHpHPVKGECLYCfvtlcdGHIFSPAL--TEELKKQIREKIGPIATP 645
Cdd:cd17650 353 VDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVR-EDKGGEARLC------AYVVAAATlnTAELRAFLAKELPSYMIP 425
|
570
....*....|....*....
gi 1387203675 646 DYIQNAPGLPKTRSGNQKR 664
Cdd:cd17650 426 SYYVQLDALPLTPNGKVDR 444
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
119-664 |
1.65e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 81.16 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 119 DKVAFYWEGNEpeettqITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSES 198
Cdd:PRK12316 3072 DAVALAFGEQR------LSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEER 3145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 199 LCERILDSNCSLLITTDafyrgeklvnlkeladealekcqekgfpvkccivvkHLgraelvtgdSPSQSPPIKRPCPDVQ 278
Cdd:PRK12316 3146 LAYMLEDSGAQLLLSQS------------------------------------HL---------RLPLAQGVQVLDLDRG 3180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 279 iswnegvdlwwhelMQKAGDECEPEWCDAEDPLFILYTSGSTGKPKGVL--------HTVGGYMLYVATTFKYV------ 344
Cdd:PRK12316 3181 --------------DENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGirhsalsnHLCWMQQAYGLGVGDRVlqfttf 3246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 345 -FDFHAEDVFWctadigwitghsyvtygPLANGATSVLfEGIPTYPDVSRLWNIVEKYKVTKFYTAPTAIRLLMkfgdEP 423
Cdd:PRK12316 3247 sFDVFVEELFW-----------------PLMSGARVVL-AGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFL----EE 3304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 424 VTKHSRASLQVLGTVGEPINPEAwlwYHRVVGAQrcPIVDTFWQTETgghmlTPLPGAIPMKPGSATFPFFGVAPAILNE 503
Cdd:PRK12316 3305 EDAHRCTSLKRIVCGGEALPADL---QQQVFAGL--PLYNLYGPTEA-----TITVTHWQCVEEGKDAVPIGRPIANRAC 3374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 504 SGEELEGEAEGYLVFKQPWPGIMRTVYGNH-------ERFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSG 576
Cdd:PRK12316 3375 YILDGSLEPVPVGALGELYLGGEGLARGYHnrpgltaERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRG 3454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 577 HLLSTAEVESALVEHKAVAEAAVVGhphpVKGECLYCFVTLCDGhifSPALTEELKKQIREKIgpiatPDYIQNA----- 651
Cdd:PRK12316 3455 FRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVPEDE---AGDLREALKAHLKASL-----PEYMVPAhllfl 3522
|
570
....*....|...
gi 1387203675 652 PGLPKTRSGNQKR 664
Cdd:PRK12316 3523 ERMPLTPNGKLDR 3535
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
135-660 |
2.25e-15 |
|
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: 79.24 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 135 QITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLcERIL-DSNCSLLIT 213
Cdd:cd12114 12 TLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARR-EAILaDAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 214 TDAfyrgeklvnlkeladealekcqekgfpvkccIVVKHLGRAELVTGDSPSQSPPIKRPCPDVqiswnegvdlwwhelm 293
Cdd:cd12114 91 DGP-------------------------------DAQLDVAVFDVLILDLDALAAPAPPPPVDV---------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 294 qkagdecepewcDAEDPLFILYTSGSTGKPKGV-------LHTVGgymlyvATTFKYV--------------FDFHAEDV 352
Cdd:cd12114 124 ------------APDDLAYVIFTSGSTGTPKGVmishraaLNTIL------DINRRFAvgpddrvlalsslsFDLSVYDI 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 353 FwctadigwitghsyvtyGPLANGATSVLfegiPTY---PDVSRLWNIVEKYKVTKFYTAPTAIRLLMKF-GDEPVTKHS 428
Cdd:cd12114 186 F-----------------GALSAGATLVL----PDEarrRDPAHWAELIERHGVTLWNSVPALLEMLLDVlEAAQALLPS 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 429 -R--------------ASLQVLGTVGEPIN----PEAWLW--YHRVVGA---------------QRCPIVDTfwqtetgg 472
Cdd:cd12114 245 lRlvllsgdwipldlpARLRALAPDARLISlggaTEASIWsiYHPIDEVppdwrsipygrplanQRYRVLDP-------- 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 473 hMLTPLPGaipmkpgsatfpffGVAPAIlnesgeelegeaegylvfkqpW---PGIMRTVYGNHERFETTYFKKFPG--Y 547
Cdd:cd12114 317 -RGRDCPD--------------WVPGEL---------------------WiggRGVALGYLGDPELTAARFVTHPDGerL 360
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 548 YVTGD-GCRRDkDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPvKGECLYCFVTLCDGHifSPA 626
Cdd:cd12114 361 YRTGDlGRYRP-DGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDG--TPI 436
|
570 580 590
....*....|....*....|....*....|....
gi 1387203675 627 LTEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:cd12114 437 APDALRAFLAQTLPAYMIPSRVIALEALPLTANG 470
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
115-647 |
2.16e-14 |
|
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: 76.21 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 115 KKLGDKVAFYWEGNepeettQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGF 194
Cdd:cd17655 8 EKTPDHTAVVFEDQ------TLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 195 SSESLcERIL-DSNCSLLITTDAFYRGEKlvnlkeladealekcqekgfpvkccivvkHLGRAELVTGDspsqsppikrp 273
Cdd:cd17655 82 PEERI-QYILeDSGADILLTQSHLQPPIA-----------------------------FIGLIDLLDED----------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 274 cpdvQISWNEGVDLwwhelmqkagdecEPEwCDAEDPLFILYTSGSTGKPKGVLHT---------------VGGYMLYVA 338
Cdd:cd17655 121 ----TIYHEESENL-------------EPV-SKSDDLAYVIYTSGSTGKPKGVMIEhrgvvnlvewankviYQGEHLRVA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 339 TTFKYVFDFHAEDVFwctadigwitghsyvtyGPLANGATSVLFEGiPTYPDVSRLWNIVEKYKVTKFYTAPTAIRLLMK 418
Cdd:cd17655 183 LFASISFDASVTEIF-----------------ASLLSGNTLYIVRK-ETVLDGQALTQYIRQNRITIIDLTPAHLKLLDA 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 419 FGDEPvtkhsRASLQVLGTVGEPINPE-AWLWYHRVVGAqrCPIVDTFWQTETG-GHMLTPLpgaIPMKPGSATFPffgV 496
Cdd:cd17655 245 ADDSE-----GLSLKHLIVGGEALSTElAKKIIELFGTN--PTITNAYGPTETTvDASIYQY---EPETDQQVSVP---I 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 497 APAILNESGeelegeaegYLVFK--QPWP------------GIMRTvYGNHErfETTYfKKF------PG--YYVTGDGC 554
Cdd:cd17655 312 GKPLGNTRI---------YILDQygRPQPvgvagelyiggeGVARG-YLNRP--ELTA-EKFvddpfvPGerMYRTGDLA 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 555 RRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTlCDGHIFSPALTEELKKQ 634
Cdd:cd17655 379 RWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIV-SEKELPVAQLREFLARE 457
|
570
....*....|...
gi 1387203675 635 IrekigpiatPDY 647
Cdd:cd17655 458 L---------PDY 461
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
132-663 |
2.45e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 76.14 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 132 ETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGA-LH---------SIVFagfsseslce 201
Cdd:PRK08162 40 GDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAvLNtlntrldaaSIAF---------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 202 rILD-SNCSLLITTDAFyrgeklvnlKELADEALEKCqekgfPVKCCIVV----------KHLGRAE----LVTGDspsq 266
Cdd:PRK08162 110 -MLRhGEAKVLIVDTEF---------AEVAREALALL-----PGPKPLVIdvddpeypggRFIGALDyeafLASGD---- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 267 sppikrpcPDVQISWNEGvdlwwhelmqkagdecepEWcdaeDPLFILYTSGSTGKPKGVL-HTVGGYMLYVATTFKYVF 345
Cdd:PRK08162 171 --------PDFAWTLPAD------------------EW----DAIALNYTSGTTGNPKGVVyHHRGAYLNALSNILAWGM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 346 DFHAE-----DVFWCTadiGWitGHSY-VTygplANGATSVLFEGIptypDVSRLWNIVEKYKVTKFYTAPTAIRLLMkf 419
Cdd:PRK08162 221 PKHPVylwtlPMFHCN---GW--CFPWtVA----ARAGTNVCLRKV----DPKLIFDLIREHGVTHYCGAPIVLSALI-- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 420 gDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQrcpIVDTFWQTETGGhmltplPGAIPMK-PGSATFPFF---- 494
Cdd:PRK08162 286 -NAPAEWRAGIDHPVHAMVAGAAPPAAVIAKMEEIGFD---LTHVYGLTETYG------PATVCAWqPEWDALPLDeraq 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 495 -----GV------APAILNESGEELEgeaegylvfkqPWPG-----IMrtVYGN-------------HERFETtyfkkfp 545
Cdd:PRK08162 356 lkarqGVryplqeGVTVLDPDTMQPV-----------PADGetigeIM--FRGNivmkgylknpkatEEAFAG------- 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 546 GYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHifsP 625
Cdd:PRK08162 416 GWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGA---S 492
|
570 580 590
....*....|....*....|....*....|....*....
gi 1387203675 626 ALTEELKKQIREKIGPIATPDYIQNAPgLPKTRSGN-QK 663
Cdd:PRK08162 493 ATEEEIIAHCREHLAGFKVPKAVVFGE-LPKTSTGKiQK 530
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
135-648 |
2.46e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 77.12 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 135 QITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLITT 214
Cdd:PRK12467 1599 ELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQ 1678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 215 DA----FYRGEKLvnlkeladEALEKCQEKgfpvkccivvkhlgraELVTGDSPSQspPIKRPCPDvqiswnegvdlwwh 290
Cdd:PRK12467 1679 SHlqarLPLPDGL--------RSLVLDQED----------------DWLEGYSDSN--PAVNLAPQ-------------- 1718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 291 elmQKAgdecepewcdaedplFILYTSGSTGKPKGVLHTVGGYM-LYVATtfKYVFDFHAEDVfwctadigWITGHSYV- 368
Cdd:PRK12467 1719 ---NLA---------------YVIYTSGSTGRPKGAGNRHGALVnRLCAT--QEAYQLSAADV--------VLQFTSFAf 1770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 369 ------TYGPLANGAtSVLFEGIPTYPDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFgDEPVTKHSraSLQVLGTVGEPI 442
Cdd:PRK12467 1771 dvsvweLFWPLINGA-RLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQM-DEQVEHPL--SLRRVVCGGEAL 1846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 443 NPEAW-LWYHRVVGAQrcpIVDTFWQTETGGHML------------TPLPGAIPMkPGSATFpffgVAPAILNEsgeele 509
Cdd:PRK12467 1847 EVEALrPWLERLPDTG---LFNLYGPTETAVDVThwtcrrkdlegrDSVPIGQPI-ANLSTY----ILDASLNP------ 1912
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 510 geaegylvfkQPwPGIMRTVY--------GNH-------ERFETTYFKKFPG-YYVTGDGCRRDKDGYYWITGRIDDMLN 573
Cdd:PRK12467 1913 ----------VP-IGVAGELYlggvglarGYLnrpaltaERFVADPFGTVGSrLYRTGDLARYRADGVIEYLGRIDHQVK 1981
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 574 VSGHLLSTAEVESALVEHKAVAEAAVVGHPHPvKGECLYCFVT-----LCDGHIFSPALTEELKKQIREKIgpiatPDYI 648
Cdd:PRK12467 1982 IRGFRIELGEIEARLREQGGVREAVVIAQDGA-NGKQLVAYVVptdpgLVDDDEAQVALRAILKNHLKASL-----PEYM 2055
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
132-666 |
2.50e-14 |
|
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: 75.42 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 132 ETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLcERILD-SNCSL 210
Cdd:cd17653 19 LGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARI-QAILRtSGATL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 211 LITTDAfyrgeklvnlkeladealekcqekgfpvkccivvkhlgraelvtgdspsqsppikrpcpdvqiswnegvdlwwh 290
Cdd:cd17653 98 LLTTDS-------------------------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 291 elmqkagdecepewcdAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATT---------------FKYVFDFHAEDVFWC 355
Cdd:cd17653 104 ----------------PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPparldvgpgsrvaqvLSIAFDACIGEIFST 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 356 tadigwitghsyvtygpLANGATSVLFEGIPTYPDVSRlwnivekyKVTKFYTAPTAIRLLmkfgdepvtkhSRASLQVL 435
Cdd:cd17653 168 -----------------LCNGGTLVLADPSDPFAHVAR--------TVDALMSTPSILSTL-----------SPQDFPNL 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 436 GTV---GEPINP---EAWlWYHRVV----GAQRCPIVDTFWQTETGghmlTPLPGAIPMkPGSATFpffgvapaILNESg 505
Cdd:cd17653 212 KTIflgGEAVPPsllDRW-SPGRRLynayGPTECTISSTMTELLPG----QPVTIGKPI-PNSTCY--------ILDAD- 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 506 eelegeaegylvfKQPWP------------GIMRTVYGNHERfETTYFKKFPGY-----YVTGDGCRRDKDGYYWITGRI 568
Cdd:cd17653 277 -------------LQPVPegvvgeicisgvQVARGYLGNPAL-TASKFVPDPFWpgsrmYRTGDYGRWTEDGGLEFLGRE 342
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 569 DDMLNVSGHLLSTAEVES-ALVEHKAVAEAAVVGHphpvkGECLYCFVTlcdghifsPAL--TEELKKQIREKIGPIATP 645
Cdd:cd17653 343 DNQVKVRGFRINLEEIEEvVLQSQPEVTQAAAIVV-----NGRLVAFVT--------PETvdVDGLRSELAKHLPSYAVP 409
|
570 580
....*....|....*....|.
gi 1387203675 646 DYIQNAPGLPktRSGNQKrVD 666
Cdd:cd17653 410 DRIIALDSFP--LTANGK-VD 427
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
117-665 |
3.37e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 75.69 E-value: 3.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 117 LGDKVAFyWEGNEPEETT------QITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIV 190
Cdd:PRK06145 4 LSASIAF-HARRTPDRAAlvyrdqEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 191 FAGFSSESLCERILDSNCSLLittdafyrgeklvnlkeLADEALEkcqekgfpvkcciVVKHLGRAELVTGDSPSQSPPI 270
Cdd:PRK06145 83 NYRLAADEVAYILGDAGAKLL-----------------LVDEEFD-------------AIVALETPKIVIDAAAQADSRR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 271 krpcpdvqiswnegvdlwwhelMQKAGDECEPEWCDAEDPLF-ILYTSGSTGKPKGVLHTVGgymlyvattfkyvfdfha 349
Cdd:PRK06145 133 ----------------------LAQGGLEIPPQAAVAPTDLVrLMYTSGTTDRPKGVMHSYG------------------ 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 350 eDVFWCTAD----IGWITGHSYVTYGPLAN-GA-----TSVLFEG----IPTYPDVSRLWNIVEKYKVTKFYTAPTAIRL 415
Cdd:PRK06145 173 -NLHWKSIDhviaLGLTASERLLVVGPLYHvGAfdlpgIAVLWVGgtlrIHREFDPEAVLAAIERHRLTCAWMAPVMLSR 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 416 LMKFGDEpvTKHSRASLQVLGTVGEPiNPEAWLW-YHRVVGAQRcpIVDTFWQTET-GGHMLTPLPGAIPmKPGSATFPF 493
Cdd:PRK06145 252 VLTVPDR--DRFDLDSLAWCIGGGEK-TPESRIRdFTRVFTRAR--YIDAYGLTETcSGDTLMEAGREIE-KIGSTGRAL 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 494 FGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHERFETTYFKkfpGYYVTGDGCRRDKDGYYWITGRIDDMLN 573
Cdd:PRK06145 326 AHVEIRIADGAGRWLPPNMKGEICMRGP--KVTKGYWKDPEKTAEAFYG---DWFRSGDVGYLDEEGFLYLTDRKKDMII 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 574 VSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSpalTEELKKQIREKIGPIATPDYIQNAPG 653
Cdd:PRK06145 401 SGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLT---LEALDRHCRQRLASFKVPRQLKVRDE 477
|
570
....*....|...
gi 1387203675 654 LPKTRSGN-QKRV 665
Cdd:PRK06145 478 LPRNPSGKvLKRV 490
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
309-664 |
4.63e-14 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 73.84 E-value: 4.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 309 DPLFILYTSGSTGKPKGVLHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSyVTYGPLANGATSVLFEGIpty 388
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGN-LIAANLQLIHAMGLTEADVYLNMLPLFHIAGLN-LALATFHAGGANVVMEKF--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 389 pDVSRLWNIVEKYKVTKFYT-APTAIRLLMKFGDEPVtkhSRASLQVLGTVGEPINPEAWlwyHRVVGAqrcpivdTFW- 466
Cdd:cd17637 76 -DPAEALELIEEEKVTLMGSfPPILSNLLDAAEKSGV---DLSSLRHVLGLDAPETIQRF---EETTGA-------TFWs 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 467 ---QTETggHMLTPLpGAIPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpgimrTV---YGNHERFETTY 540
Cdd:cd17637 142 lygQTET--SGLVTL-SPYRERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGP------LVfqgYWNLPELTAYT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 541 FKKfpGYYVTGDGCRRDKDGYYWITGRI--DDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLC 618
Cdd:cd17637 213 FRN--GWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLK 290
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1387203675 619 DGHIFSPaltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGNQKR 664
Cdd:cd17637 291 PGATLTA---DELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
99-664 |
4.65e-14 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 75.43 E-value: 4.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 99 ATTNICYNVLDRIVHE-KKLGDKVAFywegNEPEETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAM 177
Cdd:PRK05857 8 AMPQLPSTVLDRVFEQaRQQPEAIAL----RRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 178 LACARLGALHSIVfagfsseslcerilDSNCSlLITTDAFyrgeklvnlKELADEAlekcqekgfpvkcCIVVKHLGRAe 257
Cdd:PRK05857 84 LACAKLGAIAVMA--------------DGNLP-IAAIERF---------CQITDPA-------------AALVAPGSKM- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 258 lvtgdSPSQSPPIKRPCPDVQISWNEGVDLWWHELmQKAGDECEPEWcDAEDPLFILYTSGSTGKPKGVlhtvggymLYV 337
Cdd:PRK05857 126 -----ASSAVPEALHSIPVIAVDIAAVTRESEHSL-DAASLAGNADQ-GSEDPLAMIFTSGTTGEPKAV--------LLA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 338 ATTFKYVFD-FHAEDVFWctadIGWITGHSyvTYGPLAngATSV---------LFEG---IPTYPDVSRLWNIVEKYKVT 404
Cdd:PRK05857 191 NRTFFAVPDiLQKEGLNW----VTWVVGET--TYSPLP--ATHIgglwwiltcLMHGglcVTGGENTTSLLEILTTNAVA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 405 KFYTAPTAIRLL---MKFGDEPVtkhsrASLQVLGTVG-EPINPEAwlwyhRVVGAQRCPIVDTFWQTETGGHMLTpLP- 479
Cdd:PRK05857 263 TTCLVPTLLSKLvseLKSANATV-----PSLRLVGYGGsRAIAADV-----RFIEATGVRTAQVYGLSETGCTALC-LPt 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 480 --GAIP-MKPGSATFPFFGV----APAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFETTYFKkfpGYYVTGD 552
Cdd:PRK05857 332 ddGSIVkIEAGAVGRPYPGVdvylAATDGIGPTAPGAGPSASFGTLWIKSPANMLGYWNNPERTAEVLID---GWVNTGD 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 553 GCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFV---TLCDGhifspALTE 629
Cdd:PRK05857 409 LLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVvasAELDE-----SAAR 483
|
570 580 590
....*....|....*....|....*....|....*....
gi 1387203675 630 ELKKQI----REKIGPIATPDYIQNAPGLPKTRSGNQKR 664
Cdd:PRK05857 484 ALKHTIaarfRRESEPMARPSTIVIVTDIPRTQSGKVMR 522
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
136-648 |
7.21e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 75.58 E-value: 7.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 136 ITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLITtd 215
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLT-- 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 216 afyrgeklvnlkeladealekcqekgfpvkccivvkhlgraelvtgdSPSQSPPIKRPCPDVQISWNEGVDLWWHelmqK 295
Cdd:PRK12467 616 -----------------------------------------------QSHLLAQLPVPAGLRSLCLDEPADLLCG----Y 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 296 AGDECEPewcdAEDP---LFILYTSGSTGKPKGVLHTVGGYMLYVATTFKYvFDFHAEDVFWCTADIGWITGHsYVTYGP 372
Cdd:PRK12467 645 SGHNPEV----ALDPdnlAYVIYTSGSTGQPKGVAISHGALANYVCVIAER-LQLAADDSMLMVSTFAFDLGV-TELFGA 718
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 373 LANGATsVLFEGIPTYPDVSRLWNIVEKYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLGtvGEpINPEAWLWYHR 452
Cdd:PRK12467 719 LASGAT-LHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQ--ASRVALPRPQRALVCG--GE-ALQVDLLARVR 792
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 453 VVGAQrCPIVDTFWQTETGGHMLT------PLP-GAIPMkpGSatfPFFGVAPAILNesgeelegeaeGYLvfkQPWP-- 523
Cdd:PRK12467 793 ALGPG-ARLINHYGPTETTVGVSTyelsdeERDfGNVPI--GQ---PLANLGLYILD-----------HYL---NPVPvg 852
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 524 ----------GIMRTVYG----NHERFETTYFKKfPG--YYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESA 587
Cdd:PRK12467 853 vvgelyiggaGLARGYHRrpalTAERFVPDPFGA-DGgrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEAR 931
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387203675 588 LVEHKAVAEAAVVGHPHPVKGECL-YCFVTLCDGHIFSPALTEELKKQIREKIgpiatPDYI 648
Cdd:PRK12467 932 LLAQPGVREAVVLAQPGDAGLQLVaYLVPAAVADGAEHQATRDELKAQLRQVL-----PDYM 988
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
135-664 |
1.42e-13 |
|
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: 73.62 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 135 QITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLITT 214
Cdd:cd05915 24 RTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 215 DAFYR--GEKLVNLKELADEALEKCQEKGFpvkccivvkhlgrAELVTGDSPSQSPpiKRPCpdvqiswnegvdlwwhel 292
Cdd:cd05915 104 PNLLPlvEAIRGELKTVQHFVVMDEKAPEG-------------YLAYEEALGEEAD--PVRV------------------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 293 mqkagDECepewcdaeDPLFILYTSGSTGKPKGVLHT-VGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYG 371
Cdd:cd05915 151 -----PER--------AACGMAYTTGTTGLPKGVVYShRALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 372 PLANGATSVLFEgiptYPDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEpVTKHSRASLQVLGTVGEPinPEAWL--- 448
Cdd:cd05915 218 TLVGAKQVLPGP----RLDPASLVELFDGEGVTFTAGVPTVWLALADYLES-TGHRLKTLRRLVVGGSAA--PRSLIarf 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 449 --WYHRVVGAQRCPIV-----DTFWQTEtggHMLTPLPGAIPMKPGSAtFPFFGVAPAILNESGEELEGEAEGYLVFKQP 521
Cdd:cd05915 291 erMGVEVRQGYGLTETspvvvQNFVKSH---LESLSEEEKLTLKAKTG-LPIPLVRLRVADEEGRPVPKDGKALGEVQLK 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 522 WPGIMRTVYGNHERFETTYFKKfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVG 601
Cdd:cd05915 367 GPWITGGYYGNEEATRSALTPD--GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVA 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387203675 602 HPHPVKGECLYCFVTLCDGHifspALTEELKKQIREKIGPIAT-PDYIQNAPGLPKTRSGNQKR 664
Cdd:cd05915 445 IPHPKWQERPLAVVVPRGEK----PTPEELNEHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLK 504
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
289-606 |
1.80e-13 |
|
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: 73.27 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 289 WHELMQKAGDECEPEWCDAEDPLFILYTSGSTGKPKGVLHTVGGYMlYVATTFKYVFDFHAEDVFWCTADIGWITGHSYV 368
Cdd:cd05932 118 WDDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFA-WAAQAGIEHIGTEENDRMLSYLPLAHVTERVFV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 369 TYGPLANGATSVLFEGIPTYPD------------VSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASL---- 432
Cdd:cd05932 197 EGGSLYGGVLVAFAESLDTFVEdvqrarptlffsVPRLWTKFQQGVQDKIPQQKLNLLLKIPVVNSLVKRKVLKGLgldq 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 433 -QVLGTVGEPINPEAWLWYHRVvgaqRCPIVDTFWQTETGGHMLTPLPGAipMKPGSATFPFFGVAPAIlnesgeelegE 511
Cdd:cd05932 277 cRLAGCGSAPVPPALLEWYRSL----GLNILEAYGMTENFAYSHLNYPGR--DKIGTVGNAGPGVEVRI----------S 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 512 AEGYLVFKQPwpGIMRTVYGNHERFETTYFKKfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVS-GHLLSTAEVESALVE 590
Cdd:cd05932 341 EDGEILVRSP--ALMMGYYKDPEATAEAFTAD--GFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAE 416
|
330
....*....|....*...
gi 1387203675 591 HKAVAEAAVVGH--PHPV 606
Cdd:cd05932 417 HDRVEMVCVIGSglPAPL 434
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
132-665 |
3.72e-13 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 72.57 E-value: 3.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 132 ETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLL 211
Cdd:PLN02479 42 GSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 212 ITTDAFYrgeklvnlkELADEALEKCQEKGfpvkccivVKHLGRAELVTGDSPSQSP-PIKRPCPDVQISWnegvdlwwh 290
Cdd:PLN02479 122 MVDQEFF---------TLAEEALKILAEKK--------KSSFKPPLLIVIGDPTCDPkSLQYALGKGAIEY--------- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 291 ELMQKAGDecePE--WCDAED---PLFILYTSGSTGKPKGV-LHTVGGYMLyvATTFKYVFDFHAEDVFWCTADIGWITG 364
Cdd:PLN02479 176 EKFLETGD---PEfaWKPPADewqSIALGYTSGTTASPKGVvLHHRGAYLM--ALSNALIWGMNEGAVYLWTLPMFHCNG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 365 HSYvTYGPLANGATSVLFEGIPTypdvSRLWNIVEKYKVTKFYTAPTAIRLL------------------MKFGDEP--- 423
Cdd:PLN02479 251 WCF-TWTLAALCGTNICLRQVTA----KAIYSAIANYGVTHFCAAPVVLNTIvnapksetilplprvvhvMTAGAAPpps 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 424 -VTKHSRASLQVLGTVG--EPINPE---AWL--WYH---------------RVVGAQRCPIVDTfwQTetgghmLTPLP- 479
Cdd:PLN02479 326 vLFAMSEKGFRVTHTYGlsETYGPStvcAWKpeWDSlppeeqarlnarqgvRYIGLEGLDVVDT--KT------MKPVPa 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 480 -----GAIPMKPGsatfpffgvapailnesgeelegeaegyLVFKqpwpGIMRTVYGNHERFETtyfkkfpGYYVTGDGC 554
Cdd:PLN02479 398 dgktmGEIVMRGN----------------------------MVMK----GYLKNPKANEEAFAN-------GWFHSGDLG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 555 RRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFS--PALTEELK 632
Cdd:PLN02479 439 VKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSdeAALAEDIM 518
|
570 580 590
....*....|....*....|....*....|....
gi 1387203675 633 KQIREKIGPIATPDYIQNAPgLPKTRSGN-QKRV 665
Cdd:PLN02479 519 KFCRERLPAYWVPKSVVFGP-LPKTATGKiQKHV 551
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
136-609 |
6.91e-13 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 71.45 E-value: 6.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 136 ITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGAlhsiVF----AGFSSESLCERILDSNCSLL 211
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGA----VFlplnTAYTLAELDYFIGDAEPALV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 212 ITTDAfyrgeklvnlkelADEALEKcqekgfpvkccIVVKHLGRAELVTGDSPSQSPPikrpcpdvqiswnegvdlwwhE 291
Cdd:PRK07514 105 VCDPA-------------NFAWLSK-----------IAAAAGAPHVETLDADGTGSLL---------------------E 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 292 LMQKAGDECEPEWCDAEDPLFILYTSGSTGKPKGVLHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYG 371
Cdd:PRK07514 140 AAAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGN-LLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 372 PLANGA------------------TSVLFEGIPTypdvsrlwnivekykvtkFYTaptaiRLLmkfgDEP-----VTKHS 428
Cdd:PRK07514 219 ALLAGAsmiflpkfdpdavlalmpRATVMMGVPT------------------FYT-----RLL----QEPrltreAAAHM 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 429 RasLQVLGTVgePINPE---AWlwyhrvvgAQRC--PIVDTFWQTETGghMLT--PLPGAipMKPGSATFPFFGVAPAIL 501
Cdd:PRK07514 272 R--LFISGSA--PLLAEthrEF--------QERTghAILERYGMTETN--MNTsnPYDGE--RRAGTVGFPLPGVSLRVT 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 502 NESGEELEGEAEGYL-------VFKQPW--PgimrtvygnherfETTY--FKKfPGYYVTGDGCRRDKDGYYWITGRIDD 570
Cdd:PRK07514 336 DPETGAELPPGEIGMievkgpnVFKGYWrmP-------------EKTAeeFRA-DGFFITGDLGKIDERGYVHIVGRGKD 401
|
490 500 510
....*....|....*....|....*....|....*....
gi 1387203675 571 MLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGE 609
Cdd:PRK07514 402 LIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGE 440
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
308-620 |
1.46e-12 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 70.63 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 308 EDPLFILYTSGSTGKPKGVLHT--------------VGGYMLYVATTFKYVFDFHaeDVFWCTADIGWITGhsyvtygpl 373
Cdd:cd17642 184 EQVALIMNSSGSTGLPKGVQLThknivarfshardpIFGNQIIPDTAILTVIPFH--HGFGMFTTLGYLIC--------- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 374 anGATSVLfegIPTYPDVSRLWNIvEKYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLGTVGEPINPEawlwyhrv 453
Cdd:cd17642 253 --GFRVVL---MYKFEEELFLRSL-QDYKVQSALLVPTLFAFFAK--STLVDKYDLSNLHEIASGGAPLSKE-------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 454 VGAQ-----RCPIV-DTFWQTETGGHMLTPLPGAIpmKPGSA--TFPFFGVAPAILNESGEELEGEAEGyLVFKQPwpGI 525
Cdd:cd17642 317 VGEAvakrfKLPGIrQGYGLTETTSAILITPEGDD--KPGAVgkVVPFFYAKVVDLDTGKTLGPNERGE-LCVKGP--MI 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 526 MRTVYGNHERFETTYFKKfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHP 605
Cdd:cd17642 392 MKGYVNNPEATKALIDKD--GWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDE 469
|
330
....*....|....*
gi 1387203675 606 VKGECLYCFVTLCDG 620
Cdd:cd17642 470 DAGELPAAVVVLEAG 484
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
135-669 |
1.80e-12 |
|
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: 69.97 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 135 QITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLITT 214
Cdd:cd17652 12 TLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLTT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 215 dafyrgeklvnlkeladealekcqekgfpvkccivvkhlgraelvtgdspsqsppikrpcpdvqiswnegvdlwwhelmq 294
Cdd:cd17652 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 295 kagdecepewcdAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKYvFDFHAEDVFWCTADIGWITGHSYVTYGPLA 374
Cdd:cd17652 92 ------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAA-FDVGPGSRVLQFASPSFDASVWELLMALLA 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 375 nGATSVLfegIPTYPDVS--RLWNIVEKYKVTkFYTAPTAIRLLMKFGDEPvtkhsraSLQVLGTVGEPINPE-AWLWyh 451
Cdd:cd17652 159 -GATLVL---APAEELLPgePLADLLREHRIT-HVTLPPAALAALPPDDLP-------DLRTLVVAGEACPAElVDRW-- 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 452 rvvgAQRCPIVDTFWQTET--GGHMLTPLPGAIPMKPGSatfPFFGVAPAILNESGeelegeaegylvfkQPWP------ 523
Cdd:cd17652 225 ----APGRRMINAYGPTETtvCATMAGPLPGGGVPPIGR---PVPGTRVYVLDARL--------------RPVPpgvpge 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 524 ------GIMRTvYGNH-----ERFETTYFKKfPG--YYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVE 590
Cdd:cd17652 284 lyiagaGLARG-YLNRpgltaERFVADPFGA-PGsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTE 361
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387203675 591 HKAVAEAAVVGHPHPVKGECLYCFVTLCDGhifSPALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGnqkRVDPQG 669
Cdd:cd17652 362 HPGVAEAVVVVRDDRPGDKRLVAYVVPAPG---AAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNG---KLDRRA 434
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
308-660 |
2.36e-12 |
|
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: 69.77 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 308 EDPLFILYTSGSTGKPKGVL--------HTVGGYMLYVATTFKYV-------FDFHAEDVF--WCTadigwitghsyvty 370
Cdd:cd17644 106 ENLAYVIYTSGSTGKPKGVMiehqslvnLSHGLIKEYGITSSDRVlqfasiaFDVAAEEIYvtLLS-------------- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 371 gplanGATSVLFEGiPTYPDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGdEPVTKHSRASLQVLGTVGEPINPEAWLWY 450
Cdd:cd17644 172 -----GATLVLRPE-EMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLEL-LLSTIDLPSSLRLVIVGGEAVQPELVRQW 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 451 HRVVGaQRCPIVDTFWQTE----TGGHMLTPLPGAIPMKPGSATfPFFGVAPAILNEsgeelegeaegylvFKQPWP-GI 525
Cdd:cd17644 245 QKNVG-NFIQLINVYGPTEatiaATVCRLTQLTERNITSVPIGR-PIANTQVYILDE--------------NLQPVPvGV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 526 MRTVY--G-------------NHERFETTYFKKFPG--YYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESAL 588
Cdd:cd17644 309 PGELHigGvglargylnrpelTAEKFISHPFNSSESerLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVL 388
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387203675 589 VEHKAVAEAAVVGHPHPVKGECLYCFVTlcdGHIFSPALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:cd17644 389 SQHNDVKTAVVIVREDQPGNKRLVAYIV---PHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNG 457
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
306-668 |
2.93e-12 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 69.66 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 306 DAEDPLFILYTSGSTGKPKGVL--HTvGGYMLYVATTFKY---VFDFH--AEDVFWCTadiGWItghsyVTYGPLANGAT 378
Cdd:PLN03102 184 DEHDPISLNYTSGTTADPKGVVisHR-GAYLSTLSAIIGWemgTCPVYlwTLPMFHCN---GWT-----FTWGTAARGGT 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 379 SVLFEGIpTYPDVSRlwNIvEKYKVTKFYTAPTAIRLLMKfGDEPVTKHSRASLQVLgTVGEPiNPEAWLWYHRVVGAQr 458
Cdd:PLN03102 255 SVCMRHV-TAPEIYK--NI-EMHNVTHMCCVPTVFNILLK-GNSLDLSPRSGPVHVL-TGGSP-PPAALVKKVQRLGFQ- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 459 cpIVDTFWQTETGGHML--------TPLPGAIPMK-PGSATFPFFGVAPAILNESGEELEG----EAEGYLVFKQPwpGI 525
Cdd:PLN03102 327 --VMHAYGLTEATGPVLfcewqdewNRLPENQQMElKARQGVSILGLADVDVKNKETQESVprdgKTMGEIVIKGS--SI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 526 MRTvYGNHERFETTYFKKfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHP 605
Cdd:PLN03102 403 MKG-YLKNPKATSEAFKH--GWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHP 479
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 606 VKGECLYCFVTLCDGH-----IFSPALTEE--LKKQIREKIGPIATPDYIQNAPGLPKtrSGNQKRVDPQ 668
Cdd:PLN03102 480 TWGETPCAFVVLEKGEttkedRVDKLVTRErdLIEYCRENLPHFMCPRKVVFLQELPK--NGNGKILKPK 547
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
546-660 |
3.34e-12 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 69.31 E-value: 3.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 546 GYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDghifsP 625
Cdd:PRK08974 432 GWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKD-----P 506
|
90 100 110
....*....|....*....|....*....|....*.
gi 1387203675 626 ALT-EELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:PRK08974 507 SLTeEELITHCRRHLTGYKVPKLVEFRDELPKSNVG 542
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
115-660 |
4.21e-12 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 69.14 E-value: 4.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 115 KKLGDKVAFYWEGnepeetTQITYRELLVQVCRF-SNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAG 193
Cdd:PRK08751 36 AKFADRPAYHSFG------KTITYREADQLVEQFaAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 194 FSSESLCERILDSNCSLLITTDAFYRGEKLVnlkeLADEALEKCQEK------GFPVKCCI--VVKHlgraelvtgdsps 265
Cdd:PRK08751 110 YTPRELKHQLIDSGASVLVVIDNFGTTVQQV----IADTPVKQVITTglgdmlGFPKAALVnfVVKY------------- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 266 qsppIKRPCPDVQISwneGVDLWWHELMQKAGDECEPEWCDAEDPLFILYTSGSTGKPKGVlhtvggyMLYVATTFKYVF 345
Cdd:PRK08751 173 ----VKKLVPEYRIN---GAIRFREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGA-------MLTHRNLVANMQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 346 DFHAedvfWCTADIGWITGHSYV-TYGPL-------ANGATSVLFEGIPTYPDVSR-LWNIVEKYKVTKFyTAPTAIRLL 416
Cdd:PRK08751 239 QAHQ----WLAGTGKLEEGCEVViTALPLyhifaltANGLVFMKIGGCNHLISNPRdMPGFVKELKKTRF-TAFTGVNTL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 417 M-KFGDEP-VTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTETG-GHMLTPLpgAIPMKPGSATFPF 493
Cdd:PRK08751 314 FnGLLNTPgFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGL---TLVEAYGLTETSpAACINPL--TLKEYNGSIGLPI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 494 FGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHErfETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLN 573
Cdd:PRK08751 389 PSTDACIKDDAGTVLAIGEIGELCIKGP--QVMKGYWKRPE--ETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMIL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 574 VSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDghifsPALT-EELKKQIREKIGPIATPDYIQNAP 652
Cdd:PRK08751 465 VSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKD-----PALTaEDVKAHARANLTGYKQPRIIEFRK 539
|
....*...
gi 1387203675 653 GLPKTRSG 660
Cdd:PRK08751 540 ELPKTNVG 547
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
136-615 |
8.12e-12 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 68.33 E-value: 8.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 136 ITYRELLVQVCRFSNVLRKQ-GICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLITt 214
Cdd:PLN02574 67 ISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFT- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 215 dafyrgeklvnlkelADEALEKCQEKGFPVkccivvkhLGRAELVTGDSPSQSPPIkrpcpdvqiswnegvdlwWHELMQ 294
Cdd:PLN02574 146 ---------------SPENVEKLSPLGVPV--------IGVPENYDFDSKRIEFPK------------------FYELIK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 295 KAGDECEPEWCDAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKYVFDFHA----EDVFWCTADIGWITGHSYVTY 370
Cdd:PLN02574 185 EDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEypgsDNVYLAALPMFHIYGLSLFVV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 371 GPLANGATSVLFEGIptypDVSRLWNIVEKYKVTKFYTAPTAIRLLMKfGDEPVTKHSRASLQVLGTVGEPINPEAWLWY 450
Cdd:PLN02574 265 GLLSLGSTIVVMRRF----DASDMVKVIDRFKVTHFPVVPPILMALTK-KAKGVCGEVLKSLKQVSCGAAPLSGKFIQDF 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 451 hrvvgAQRCPIVDtFWQtetgGHMLTPlPGAIPMKpGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQP------W-- 522
Cdd:PLN02574 340 -----VQTLPHVD-FIQ----GYGMTE-STAVGTR-GFNTEKLSKYSSVGLLAPNMQAKVVDWSTGCLLPPgncgelWiq 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 523 -PGIMRTVYGNHERFETTYFKKfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVG 601
Cdd:PLN02574 408 gPGVMKGYLNNPKATQSTIDKD--GWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTA 485
|
490
....*....|....
gi 1387203675 602 HPHPVKGECLYCFV 615
Cdd:PLN02574 486 VPDKECGEIPVAFV 499
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
119-609 |
1.04e-11 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 67.70 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 119 DKVAFYwegnEPEETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGAlhsiVFAGFSSES 198
Cdd:PLN02330 43 DKVAFV----EAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGG----VFSGANPTA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 199 LCERILD----SNCSLLITTDAFYrgeklvnlkeladealEKCQEKGFPVkccivvkhlgraeLVTGDSpsqsppikrpC 274
Cdd:PLN02330 115 LESEIKKqaeaAGAKLIVTNDTNY----------------GKVKGLGLPV-------------IVLGEE----------K 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 275 PDVQISWNEGVDLwwhelMQKAGDECEPEWCDAEDPLFILYTSGSTGKPKGVLHT--------------VGGYMLYVATT 340
Cdd:PLN02330 156 IEGAVNWKELLEA-----ADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLThrnlvanlcsslfsVGPEMIGQVVT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 341 FKYVFDFHaedvfwctadIGWITGHSYVTygpLANGATSVLFEGIptypDVSRLWNIVEKYKVTKFYTAPTAIRLLMKfg 420
Cdd:PLN02330 231 LGLIPFFH----------IYGITGICCAT---LRNKGKVVVMSRF----ELRTFLNALITQEVSFAPIVPPIILNLVK-- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 421 dEPVTKH---SRASLQVLGTVGEPINPEAWLWYH-RVVGAQrcpIVDTFWQTETGGHMLT---PLPGAIPMKPGSATFPF 493
Cdd:PLN02330 292 -NPIVEEfdlSKLKLQAIMTAAAPLAPELLTAFEaKFPGVQ---VQEAYGLTEHSCITLThgdPEKGHGIAKKNSVGFIL 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 494 FGVAPAILNESGEelegeaegyLVFKQPWPG--------IMRTVYGNHERFETTYFKKfpGYYVTGDGCRRDKDGYYWIT 565
Cdd:PLN02330 368 PNLEVKFIDPDTG---------RSLPKNTPGelcvrsqcVMQGYYNNKEETDRTIDED--GWLHTGDIGYIDDDGDIFIV 436
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1387203675 566 GRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGE 609
Cdd:PLN02330 437 DRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGE 480
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
115-382 |
1.13e-11 |
|
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: 67.65 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 115 KKLGDKVAFYWEGNEPEETTQITYRELLVQVCRFSNVLRKQGICkGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGF 194
Cdd:cd05931 4 AARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGKP-GDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 195 SSESLcERIL----DSNCSLLITTDAFyrgeklvnLKELADEALEKCQEKGFPVKCcivvkhlgrAELVTGDSPSQSPPI 270
Cdd:cd05931 83 PGRHA-ERLAailaDAGPRVVLTTAAA--------LAAVRAFAASRPAAGTPRLLV---------VDLLPDTSAADWPPP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 271 KrpcpdvqiswnegvdlwwhelmqkagdecepewCDAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKyVFDFHAE 350
Cdd:cd05931 145 S---------------------------------PDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRR-AYGLDPG 190
|
250 260 270
....*....|....*....|....*....|....*.
gi 1387203675 351 D--VFW--CTADIGWITGhsyvTYGPLANGATSVLF 382
Cdd:cd05931 191 DvvVSWlpLYHDMGLIGG----LLTPLYSGGPSVLM 222
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
134-664 |
1.33e-11 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 68.15 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 134 TQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLcERIL-DSNCSLLI 212
Cdd:PRK10252 482 YQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRL-KMMLeDARPSLLI 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 213 TTDAFyrgeklvnlkeladealekcQEKgFPvkccivvkHLGRAELVTGDSP---SQSPPIKRPCPDvqiswnegvdlww 289
Cdd:PRK10252 561 TTADQ--------------------LPR-FA--------DVPDLTSLCYNAPlapQGAAPLQLSQPH------------- 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 290 helmqkagdecepewcdaeDPLFILYTSGSTGKPKGVL--HT-VGGYMLYVATTFKyvfdFHAEDVFW----CTADIG-- 360
Cdd:PRK10252 599 -------------------HTAYIIFTSGSTGRPKGVMvgQTaIVNRLLWMQNHYP----LTADDVVLqktpCSFDVSvw 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 361 ---WitghsyvtygPLANGATSVLFEgiptyPDVSR----LWNIVEKYKVTKFYTAPTairLLMKFGDEPVTKHSRASLQ 433
Cdd:PRK10252 656 effW----------PFIAGAKLVMAE-----PEAHRdplaMQQFFAEYGVTTTHFVPS---MLAAFVASLTPEGARQSCA 717
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 434 VLGTV---GEPINPEAWLWYHRVVGAqrcPIVDTFWQTE---------TGGHMLTPLPGA-IPMKpgsatFPFFGVAPAI 500
Cdd:PRK10252 718 SLRQVfcsGEALPADLCREWQQLTGA---PLHNLYGPTEaavdvswypAFGEELAAVRGSsVPIG-----YPVWNTGLRI 789
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 501 LNESGeelegeaegylvfkQPWP-GIMRTVY--------GNH-------ERFETTYFKkfPG--YYVTGDGCRRDKDGYY 562
Cdd:PRK10252 790 LDARM--------------RPVPpGVAGDLYltgiqlaqGYLgrpdltaSRFIADPFA--PGerMYRTGDVARWLDDGAV 853
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 563 WITGRIDDMLNVSGHLLSTAEVESALVEH----KAVAEAAVVGHPHPVKGEC--LYCFVTLCDGhifSPALTEELKKQIR 636
Cdd:PRK10252 854 EYLGRSDDQLKIRGQRIELGEIDRAMQALpdveQAVTHACVINQAAATGGDArqLVGYLVSQSG---LPLDTSALQAQLR 930
|
570 580
....*....|....*....|....*...
gi 1387203675 637 EKIGPIATPDYIQNAPGLPKTRSGNQKR 664
Cdd:PRK10252 931 ERLPPHMVPVVLLQLDQLPLSANGKLDR 958
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
31-382 |
3.16e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 66.54 E-value: 3.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 31 PPPEVSRSAHVpslqrYReLHRRSLEEPREfwgdIAKEFYWKTPCPGPFLQynfdvtkgkifIEWMKGATTNICYNVLDR 110
Cdd:PTZ00216 37 PGTETENASAI-----YR-IAGVTDEEHER----LRNEWYYGPNFLQRLER-----------ICKERGDRRALAYRPVER 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 111 IVHEK-KLGDKVAFYWEGNEPEETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSI 189
Cdd:PTZ00216 96 VEKEVvKDADGKERTMEVTHFNETRYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAAT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 190 VFAGFSSESLCERILDSNCSLLITTdafyrGEKLVNLkeladeaLEKCQEKGFPvkCCIVVkHLGraelvtgdspsqSPP 269
Cdd:PTZ00216 176 VYANLGEDALAYALRETECKAIVCN-----GKNVPNL-------LRLMKSGGMP--NTTII-YLD------------SLP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 270 ikrpcPDVQIswnEGVDLW-WHELMQKAGDECE------PEWCDAEdpLFILYTSGSTGKPKGVLHTVGGYMLYVATTFK 342
Cdd:PTZ00216 229 -----ASVDT---EGCRLVaWTDVVAKGHSAGShhplniPENNDDL--ALIMYTSGTTGDPKGVMHTHGSLTAGILALED 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1387203675 343 YVFdfhaeDVFWCTADigwitGHSYVTYGPLAN----GATSVLF 382
Cdd:PTZ00216 299 RLN-----DLIGPPEE-----DETYCSYLPLAHimefGVTNIFL 332
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
135-668 |
3.53e-11 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 66.17 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 135 QITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGAlhSIVFAGFS---SEsLCERILDSNCSLL 211
Cdd:PRK10946 48 QFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGV--APVNALFShqrSE-LNAYASQIEPALL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 212 ITTdafyRGEKLVNLKELADEALEKCQEkgfpvkCCIVVKHlgraelvtGDSPSQSppikrpcpdvqiswnegVDLWwhe 291
Cdd:PRK10946 125 IAD----RQHALFSDDDFLNTLVAEHSS------LRVVLLL--------NDDGEHS-----------------LDDA--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 292 lMQKAGDECEPEWCDAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKyVFDFHAEDVFWCTADigwiTGHSYVTYG 371
Cdd:PRK10946 167 -INHPAEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVE-ICGFTPQTRYLCALP----AAHNYPMSS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 372 PlanGATSVLFEG----IPTYPDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINP--- 444
Cdd:PRK10946 241 P---GALGVFLAGgtvvLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKLLQVGGARLSEtla 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 445 ------------------EAWLWYHR-------VVGAQRCPIV--DTFWQTETGGHmltPLPGAIP---MKPGSATFPff 494
Cdd:PRK10946 318 rripaelgcqlqqvfgmaEGLVNYTRlddsderIFTTQGRPMSpdDEVWVADADGN---PLPQGEVgrlMTRGPYTFR-- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 495 gvapailnesgeelegeaegylvfkqpwpGIMRTVYGNHERFETTyfkkfpGYYVTGDGCRRDKDGYYWITGRIDDMLNV 574
Cdd:PRK10946 393 -----------------------------GYYKSPQHNASAFDAN------GFYCSGDLVSIDPDGYITVVGREKDQINR 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 575 SGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGE--CLYCFVTlcdghifSPALTEELKKQIREK-IGPIATPDYIQNA 651
Cdd:PRK10946 438 GGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEksCAFLVVK-------EPLKAVQLRRFLREQgIAEFKLPDRVECV 510
|
570
....*....|....*..
gi 1387203675 652 PGLPKTRSGnqkRVDPQ 668
Cdd:PRK10946 511 DSLPLTAVG---KVDKK 524
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
119-648 |
3.88e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 66.73 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 119 DKVAFYWEGNepeettQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSES 198
Cdd:PRK05691 1146 ERIALVWDGG------SLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAER 1219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 199 LCERILDSNCSLLITTDAFYrgEKLVNLKELADEALEKCqekgfpvkccivvkHLgraelvtgDS-PSQSPpikrpcpdv 277
Cdd:PRK05691 1220 LAYMLADSGVELLLTQSHLL--ERLPQAEGVSAIALDSL--------------HL--------DSwPSQAP--------- 1266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 278 qiswneGVDLWWHELMqkagdecepewcdaedplFILYTSGSTGKPKGVLHTVGGYMLYVA-TTFKYVFDfhAEDVFWCT 356
Cdd:PRK05691 1267 ------GLHLHGDNLA------------------YVIYTSGSTGQPKGVGNTHAALAERLQwMQATYALD--DSDVLMQK 1320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 357 ADIGWITGhSYVTYGPLANGATSVLfEGIPTYPDVSRLWNIVEKYKVTKFYTAPTairLLMKFGDEPVTKHSRaSLQVLG 436
Cdd:PRK05691 1321 APISFDVS-VWECFWPLITGCRLVL-AGPGEHRDPQRIAELVQQYGVTTLHFVPP---LLQLFIDEPLAAACT-SLRRLF 1394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 437 TVGEPINPE---------AWLWYHRVVGAQRCPIVDTFWQTET------------GGHM-------LTPLPGAIpmkPGS 488
Cdd:PRK05691 1395 SGGEALPAElrnrvlqrlPQVQLHNRYGPTETAINVTHWQCQAedgerspigrplGNVLcrvldaeLNLLPPGV---AGE 1471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 489 ATFPFFGVAPAILNEsgeelegeaegylvfkqpwPGImrtvygNHERFETTYFKKfPG--YYVTGDGCRRDKDGYYWITG 566
Cdd:PRK05691 1472 LCIGGAGLARGYLGR-------------------PAL------TAERFVPDPLGE-DGarLYRTGDRARWNADGALEYLG 1525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 567 RIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHpHPVKGECLYCFVTLCDGHifsPALTEELKKQIREKIgpiatPD 646
Cdd:PRK05691 1526 RLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVR-EGAAGAQLVGYYTGEAGQ---EAEAERLKAALAAEL-----PE 1596
|
..
gi 1387203675 647 YI 648
Cdd:PRK05691 1597 YM 1598
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
313-660 |
4.89e-11 |
|
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: 64.44 E-value: 4.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 313 ILYTSGSTGKPKGVL----HTVGgymLYVAttfkyvfdfhaedvfWCtaDIGWIT-GHSYVTYGPLAN------GATSVL 381
Cdd:cd17638 5 IMFTSGTTGRSKGVMcahrQTLR---AAAA---------------WA--DCADLTeDDRYLIINPFFHtfgykaGIVACL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 382 FEGIPTYP----DVSRLWNIVEKYKVTKFYTAPTAIRLLMkfgDEPVTKHSR-ASLQVLGTVGEPINPEAWLWYHRVVGA 456
Cdd:cd17638 65 LTGATVVPvavfDVDAILEAIERERITVLPGPPTLFQSLL---DHPGRKKFDlSSLRAAVTGAATVPVELVRRMRSELGF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 457 QRcpIVDTFWQTETG-GHMLTPLPGAIPMKPGSATfPFFGVAPAILNESGEELEGeaegylvfkqpwPGIMRTVYGNHER 535
Cdd:cd17638 142 ET--VLTAYGLTEAGvATMCRPGDDAETVATTCGR-ACPGFEVRIADDGEVLVRG------------YNVMQGYLDDPEA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 536 FETTYFKKfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFV 615
Cdd:cd17638 207 TAEAIDAD--GWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFV 284
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1387203675 616 TLCDGHifspALTEE-LKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:cd17638 285 VARPGV----TLTEEdVIAWCRERLANYKVPRFVRFLDELPRNASG 326
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
291-664 |
5.68e-11 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 65.59 E-value: 5.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 291 ELMQKAGDECEPEWCDA-EDPLFILYTSGSTGKPKGVlhTVGGYMLYVATTFKYVFDFHAE-DVFWCTADIGWITGHSYV 368
Cdd:PLN02860 154 MLKQRALGTTELDYAWApDDAVLICFTSGTTGRPKGV--TISHSALIVQSLAKIAIVGYGEdDVYLHTAPLCHIGGLSSA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 369 tygpLAN---GATSVLfegIPTYpDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVL----GTVGEP 441
Cdd:PLN02860 232 ----LAMlmvGACHVL---LPKF-DAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRKIlnggGSLSSR 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 442 INPEAWLWYhrvvgaQRCPIVDTFWQTETGGHMlTPLPGAIPmkpgsaTFPFFGVAPAILNESGEELEGEAEGYLVFKQP 521
Cdd:PLN02860 304 LLPDAKKLF------PNAKLFSAYGMTEACSSL-TFMTLHDP------TLESPKQTLQTVNQTKSSSVHQPQGVCVGKPA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 522 ---------------------WPGIMRTVYGNHErfETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLS 580
Cdd:PLN02860 371 phvelkigldessrvgriltrGPHVMLGYWGQNS--ETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVY 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 581 TAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSPALT-----------EELKKQIREK-IGPIATPD-Y 647
Cdd:PLN02860 449 PEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGWIWSDNEKenakknltlssETLRHHCREKnLSRFKIPKlF 528
|
410
....*....|....*..
gi 1387203675 648 IQNAPGLPKTRSGNQKR 664
Cdd:PLN02860 529 VQWRKPFPLTTTGKIRR 545
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
308-663 |
6.59e-11 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 64.33 E-value: 6.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 308 EDPLFILYTSGSTGKPKGVL---HTVGGYMLYVA--TTFKYVFDFHAEDVFWCTADIGW------ITGHSYVTYGPLANG 376
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGVMwrqEDIFRMLMGGAdfGTGEFTPSEDAHKAAAAAAGTVMfpapplMHGTGSWTAFGGLLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 377 ATSVLFEGIPTYPDvsRLWNIVEKYKVTKF------YTAPTaIRLLMKFGDEPVTkhsraSLQVLGTVGEPINPEawlwy 450
Cdd:cd05924 83 GQTVVLPDDRFDPE--EVWRTIEKHKVTSMtivgdaMARPL-IDALRDAGPYDLS-----SLFAISSGGALLSPE----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 451 hrvVGAQRCP------IVDTFWQTETGGHMlTPLPGaiPMKPGSATFPFFGVAPAILNESgeelegeaegyLVFKQPWPG 524
Cdd:cd05924 150 ---VKQGLLElvpnitLVDAFGSSETGFTG-SGHSA--GSGPETGPFTRANPDTVVLDDD-----------GRVVPPGSG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 525 IMRTV----------YGNHERFETTyFKKFPG--YYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHK 592
Cdd:cd05924 213 GVGWIarrghiplgyYGDEAKTAET-FPEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHP 291
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387203675 593 AVAEAAVVGHPHPVKGECLYCFVTLCDGHifSPALtEELKKQIREKIGPIATPDYIQNAPGLPktRSGNQK 663
Cdd:cd05924 292 AVYDVLVVGRPDERWGQEVVAVVQLREGA--GVDL-EELREHCRTRIARYKLPKQVVFVDEIE--RSPAGK 357
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
306-660 |
1.47e-10 |
|
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: 63.96 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 306 DAEDPLFILYTSGSTGKPKGVLHTVGGYM--------LY---------VATTFKYVFDFHAEDVFwctadIGWITGHSYV 368
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSVVnlrtslseRYfgrdngdeaVLFFSNYVFDFFVEQMT-----LALLNGQKLV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 369 tygplangatsVLFEGIPTYPDvsRLWNIVEKYKVTKFYTAPTAIRLLmKFGdepvtkhSRASLQVLGTVGEPINPEAwl 448
Cdd:cd17648 167 -----------VPPDEMRFDPD--RFYAYINREKVTYLSGTPSVLQQY-DLA-------RLPHLKRVDAAGEEFTAPV-- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 449 wYHRVVGAQRCPIVDTFWQTETGGHML-TPLPGAiPMKPGSATFPFFGVAPAILNESGeelegeaegylvfkQPWP---- 523
Cdd:cd17648 224 -FEKLRSRFAGLIINAYGPTETTVTNHkRFFPGD-QRFDKSLGRPVRNTKCYVLNDAM--------------KRVPvgav 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 524 --------GIMRTvYGNH-----ERFETTYFK--------KFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTA 582
Cdd:cd17648 288 gelylggdGVARG-YLNRpeltaERFLPNPFQteqerargRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 583 EVESALVEHKAVAEAAVVGHPHPVKGEC-----LYCFVTLCDGHIfsPAltEELKKQIREKIGPIATPDYIQNAPGLPKT 657
Cdd:cd17648 367 EVEAALASYPGVRECAVVAKEDASQAQSriqkyLVGYYLPEPGHV--PE--SDLLSFLRAKLPRYMVPARLVRLEGIPVT 442
|
...
gi 1387203675 658 RSG 660
Cdd:cd17648 443 ING 445
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
546-660 |
2.66e-10 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 63.23 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 546 GYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSP 625
Cdd:PRK06018 410 GFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATR 489
|
90 100 110
....*....|....*....|....*....|....*
gi 1387203675 626 altEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:PRK06018 490 ---EEILKYMDGKIAKWWMPDDVAFVDAIPHTATG 521
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
137-326 |
2.68e-10 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 63.29 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 137 TYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGA-LHSIVFAGFSSEslCERILD-SNCSLLITT 214
Cdd:PRK08315 45 TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAiLVTINPAYRLSE--LEYALNqSGCKALIAA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 215 DAF----YRG--EKLVnlKELADEALEKCQEKGFPvkccivvkHLgRAELVTGDSPsqsppikrpcPDVQISWNEGVDLw 288
Cdd:PRK08315 123 DGFkdsdYVAmlYELA--PELATCEPGQLQSARLP--------EL-RRVIFLGDEK----------HPGMLNFDELLAL- 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1387203675 289 whelmqkaGDECEPEWCDA-------EDPLFILYTSGSTGKPKGV 326
Cdd:PRK08315 181 --------GRAVDDAELAArqatldpDDPINIQYTSGTTGFPKGA 217
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
546-660 |
2.85e-10 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 63.12 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 546 GYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDghifsP 625
Cdd:PRK07059 435 GFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKD-----P 509
|
90 100 110
....*....|....*....|....*....|....*.
gi 1387203675 626 ALTEE-LKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:PRK07059 510 ALTEEdVKAFCKERLTNYKRPKFVEFRTELPKTNVG 545
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
140-660 |
2.96e-10 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 63.18 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 140 ELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLIT-TDAFy 218
Cdd:PRK12406 16 ELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAhADLL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 219 rgeklvnlkeladEALEKCQEKGFPVKCCivvkhlgraelvtgdspsQSPPikrpcpdvQISWNEGVDLwwHELMQKAGD 298
Cdd:PRK12406 95 -------------HGLASALPAGVTVLSV------------------PTPP--------EIAAAYRISP--ALLTPPAGA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 299 ECEPEWCDAEDPL---------FILYTSGSTGKPKGVLHTVG------GYMLYVATTFkyvfdfhaedvfwctadiGWIT 363
Cdd:PRK12406 134 IDWEGWLAQQEPYdgppvpqpqSMIYTSGTTGHPKGVRRAAPtpeqaaAAEQMRALIY------------------GLKP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 364 GHSYVTYGPLANGATSV-------LFEGIPTYP--DVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQv 434
Cdd:PRK12406 196 GIRALLTGPLYHSAPNAyglragrLGGVLVLQPrfDPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLR- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 435 lgtvgepinpeawlwyHRVVGAQRCP--------------IVDTFWQTETGGHMLTPLPGAIPmKPGSATFPFFGVAPAI 500
Cdd:PRK12406 275 ----------------HVIHAAAPCPadvkramiewwgpvIYEYYGSTESGAVTFATSEDALS-HPGTVGKAAPGAELRF 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 501 LNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHERFETTYFKKfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLS 580
Cdd:PRK12406 338 VDEDGRPLPQGEIGEIYSRIA--GNPDFTYHNKPEKRAEIDRG--GFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIY 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 581 TAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSPAlteELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:PRK12406 414 PAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEA---DIRAQLKARLAGYKVPKHIEIMAELPREDSG 490
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
136-664 |
6.36e-10 |
|
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: 62.07 E-value: 6.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 136 ITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLITTd 215
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 216 afyrgeklvnlkeladealekcqekgfpvkccivvkhlgraelvtgdspsqsppikrpcpdvqiswnegvdlwwhelmqk 295
Cdd:cd05914 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 296 agdecepewcDAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKYVFdFHAEDVFWCTADIGWITGHSYVTYGPLAN 375
Cdd:cd05914 87 ----------DEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVL-LGKGDKILSILPLHHIYPLTFTLLLPLLN 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 376 GATSVLFEGIPT-------------YPDVSRLWNIVEKYKVTKFYTAPTAI---RLLMKFGDEPVTKHSRASLQ------ 433
Cdd:cd05914 156 GAHVVFLDKIPSakiialafaqvtpTLGVPVPLVIEKIFKMDIIPKLTLKKfkfKLAKKINNRKIRKLAFKKVHeafggn 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 434 ----VLGtvGEPINPEAwLWYHRVVGAqrcPIVDTFWQTETGGHMLTPLPGAIpmKPGSATFPFFGVAPAILNESGEELE 509
Cdd:cd05914 236 ikefVIG--GAKINPDV-EEFLRTIGF---PYTIGYGMTETAPIISYSPPNRI--RLGSAGKVIDGVEVRIDSPDPATGE 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 510 GEaegyLVFKQpwPGIMRTVYGNHERFETTYFKKfpGYYVTGDGCRRDKDGYYWITGRIDDM-LNVSGHLLSTAEVESAL 588
Cdd:cd05914 308 GE----IIVRG--PNVMKGYYKNPEATAEAFDKD--GWFHTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKI 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 589 VEHKAVAEAAVV---------GHPHPVKGECLycfvtlcdgHIFSPALTEELKKQIREKIGpIATPDY-------IQNAP 652
Cdd:cd05914 380 NNMPFVLESLVVvqekklvalAYIDPDFLDVK---------ALKQRNIIDAIKWEVRDKVN-QKVPNYkkiskvkIVKEE 449
|
570
....*....|..
gi 1387203675 653 gLPKTRSGNQKR 664
Cdd:cd05914 450 -FEKTPKGKIKR 460
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
546-615 |
7.68e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 61.54 E-value: 7.68e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387203675 546 GYYVTGDGCRRDKDGYYWITGRID-DMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFV 615
Cdd:PRK07787 350 GWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYV 420
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
136-374 |
8.43e-10 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 62.06 E-value: 8.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 136 ITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLITtd 215
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVIC-- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 216 afyrGEKlvNLKELADealekCQEKGFPVKCCIVVKhlgraelvtgDSPSQSPPIKRPCPDVQISWNEGVdlwwhelmQK 295
Cdd:PLN02387 185 ----DSK--QLKKLID-----ISSQLETVKRVIYMD----------DEGVDSDSSLSGSSNWTVSSFSEV--------EK 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 296 AGDE--CEPEWCDAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKYVFDFHAEDVfwctadigwitghsYVTYGPL 373
Cdd:PLN02387 236 LGKEnpVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDV--------------YLAYLPL 301
|
.
gi 1387203675 374 A 374
Cdd:PLN02387 302 A 302
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
133-668 |
1.78e-09 |
|
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: 60.52 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 133 TTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLI 212
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 213 TtdafyrgEKLVNLKELADEALEKCQEKGFpvkccivvkhlgraelvtgdspsqsppikrpcpdvqiswnegvdlwwhel 292
Cdd:cd05939 81 F-------NLLDPLLTQSSTEPPSQDDVNF-------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 293 mqkagdecepewcdaEDPLFILYTSGSTGKPKGVLHTVGGYmLYVATTFKYVFDFHAEDVFWCTADIgWITGHSYVTYGP 372
Cdd:cd05939 104 ---------------RDKLFYIYTSGTTGLPKAAVIVHSRY-YRIAAGAYYAFGMRPEDVVYDCLPL-YHSAGGIMGVGQ 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 373 -LANGATSVLFEGIptypDVSRLWNIVEKYKVTKF-YTAPTAIRLLMKFGDEPVTKHsraslQVLGTVGEPINPEAWlwy 450
Cdd:cd05939 167 aLLHGSTVVIRKKF----SASNFWDDCVKYNCTIVqYIGEICRYLLAQPPSEEEQKH-----NVRLAVGNGLRPQIW--- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 451 HRVVGAQRCPIVDTFWQTETGGHMLTPLP---GAIPMKP--GSATFPffgVAPAILNESGEELEGEAEGYLVFKQPW-PG 524
Cdd:cd05939 235 EQFVRRFGIPQIGEFYGATEGNSSLVNIDnhvGACGFNSriLPSVYP---IRLIKVDEDTGELIRDSDGLCIPCQPGePG 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 525 IM----------RTVYG------NHERFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESAL 588
Cdd:cd05939 312 LLvgkiiqndplRRFDGyvnegaTNKKIARDVFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGIL 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 589 VEHKAVAEAAVVGHPHP-VKGEC----LYCFVTLCDGHIFSPALTEELKkqirekigPIATPDYIQNAPGLPKTRSGNQK 663
Cdd:cd05939 392 SNVLGLEDVVVYGVEVPgVEGRAgmaaIVDPERKVDLDRFSAVLAKSLP--------PYARPQFIRLLPEVDKTGTFKLQ 463
|
....*
gi 1387203675 664 RVDPQ 668
Cdd:cd05939 464 KTDLQ 468
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
132-648 |
2.60e-09 |
|
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: 60.18 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 132 ETTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGAlhsiVFAGFSSESLCERI----LDSN 207
Cdd:cd17656 10 ENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGG----AFVPIDPEYPEERRiyimLDSG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 208 CSLLITTdafyrgeklvnlkeladealekcqekgfpvkccivvKHLGraelvtgDSPSQSPPIkrpcpdVQISWnegvDL 287
Cdd:cd17656 86 VRVVLTQ------------------------------------RHLK-------SKLSFNKST------ILLED----PS 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 288 WWHELMQKAGDECEpewcdAEDPLFILYTSGSTGKPKGV----------LHTVGGYMLyvATTFKYVFDFHAEDVFWCTA 357
Cdd:cd17656 113 ISQEDTSNIDYINN-----SDDLLYIIYTSGTTGKPKGVqlehknmvnlLHFEREKTN--INFSDKVLQFATCSFDVCYQ 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 358 DIgwitghsyvtYGPLANGATSVLFEGiPTYPDVSRLWNIVEKYKVTKFYTaPTAIrLLMKFGDEPVTKHSRASLQVLGT 437
Cdd:cd17656 186 EI----------FSTLLSGGTLYIIRE-ETKRDVEQLFDLVKRHNIEVVFL-PVAF-LKFIFSEREFINRFPTCVKHIIT 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 438 VGEPI---NPeawlwYHRVVGAQRCPIVDTFWQTETggHMLT--------PLPGAIPM-KPGSATFPFfgvapaILNESg 505
Cdd:cd17656 253 AGEQLvitNE-----FKEMLHEHNVHLHNHYGPSET--HVVTtytinpeaEIPELPPIgKPISNTWIY------ILDQE- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 506 eelegeaegylvfKQPWP-GIMRTVY--------GNHERFETTYFKKFPG-------YYVTGDGCRRDKDGYYWITGRID 569
Cdd:cd17656 319 -------------QQLQPqGIVGELYisgasvarGYLNRQELTAEKFFPDpfdpnerMYRTGDLARYLPDGNIEFLGRAD 385
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387203675 570 DMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTlcdghifspALTEELKKQIREKIGPiATPDYI 648
Cdd:cd17656 386 HQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV---------MEQELNISQLREYLAK-QLPEYM 454
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
306-600 |
4.82e-09 |
|
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: 59.09 E-value: 4.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 306 DAEDPLFILYTSGSTGKPKGVL---HTVGGYMLYVATTFKY-----VFDF--HAEDVfwCTADIgwitghsyvtYGPLAN 375
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVViehRALSTSALAHGRALGLtsesrVLQFasYTFDV--SILEI----------FTTLAA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 376 GATSVlfegIPtyPDVSRLWNIVE---KYKVTkfyTA---PTAIRLLmkfGDEPVTkhsraSLQVLGTVGEPINPEAW-L 448
Cdd:cd05918 172 GGCLC----IP--SEEDRLNDLAGfinRLRVT---WAfltPSVARLL---DPEDVP-----SLRTLVLGGEALTQSDVdT 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 449 WYHRV------------VGAQRCPIVD-------------TFWQTETGGH-MLTPLpGAI-------PMkpgsatfpffg 495
Cdd:cd05918 235 WADRVrlinaygpaectIAATVSPVVPstdprnigrplgaTCWVVDPDNHdRLVPI-GAVgelliegPI----------- 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 496 VAPAILNESGEELEgeaegylVFKQPWPGIMRTVYGNHERFettyfkkfpgyYVTGDGCRRDKDG--YYwiTGRIDDMLN 573
Cdd:cd05918 303 LARGYLNDPEKTAA-------AFIEDPAWLKQEGSGRGRRL-----------YRTGDLVRYNPDGslEY--VGRKDTQVK 362
|
330 340
....*....|....*....|....*..
gi 1387203675 574 VSGHLLSTAEVESALVEHKAVAEAAVV 600
Cdd:cd05918 363 IRGQRVELGEIEHHLRQSLPGAKEVVV 389
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
137-601 |
7.65e-09 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 58.60 E-value: 7.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 137 TYRELLVQVCRFSNVLRKQ-GICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESL--CERIldSNCSLLIT 213
Cdd:cd05937 7 TYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLihCLKL--SGSRFVIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 214 TDafyrgeklvnlkeladealekcqekgfpvkccivvkhlgraelvtgdspsqsppikrpcpdvqiswnegvdlwwhelm 293
Cdd:cd05937 85 DP------------------------------------------------------------------------------ 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 294 qkagdecepewcdaEDPLFILYTSGSTGKPKGVLHTVGgyMLYV-ATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGP 372
Cdd:cd05937 87 --------------DDPAILIYTSGTTGLPKAAAISWR--RTLVtSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNC 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 373 LANGATSVL---FEgiptypdVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRaslqVLGTVGEPINPEAWLW 449
Cdd:cd05937 151 LMSGGTLALsrkFS-------ASQFWKDVRDSGATIIQYVGELCRYLLSTPPSPYDRDHK----VRVAWGNGLRPDIWER 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 450 YHRVVGAqrcPIVDTFWQ-TETGGHMLTPLPGAipmkpgsatfpfFGvAPAILNESGEELEGEAEGYLVFK------QPW 522
Cdd:cd05937 220 FRERFNV---PEIGEFYAaTEGVFALTNHNVGD------------FG-AGAIGHHGLIRRWKFENQVVLVKmdpetdDPI 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 523 ---------------PG--IMRTVYGNHERFETTY--------------FKKFPGYYVTGDGCRRDKDGYYWITGRIDDM 571
Cdd:cd05937 284 rdpktgfcvrapvgePGemLGRVPFKNREAFQGYLhnedatesklvrdvFRKGDIYFRTGDLLRQDADGRWYFLDRLGDT 363
|
490 500 510
....*....|....*....|....*....|
gi 1387203675 572 LNVSGHLLSTAEVESALVEHKAVAEAAVVG 601
Cdd:cd05937 364 FRWKSENVSTTEVADVLGAHPDIAEANVYG 393
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
118-647 |
9.64e-09 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 58.26 E-value: 9.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 118 GDKVAFYWEGNEPEETTqitYRELLVQVCRFSNVLRKQ-GICKGDRVAIYMPMIPELVVAMLACARLGAlhsiVFagfss 196
Cdd:PRK05620 24 GDTTVTTWGGAEQEQTT---FAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGA----VF----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 197 ESLCERILDSNCSLLITtdafYRGEKLVnlkeLADEALEKcqEKGFPVKCCIVVkhlgRAELVTGDSPSQSPPIKRPcpd 276
Cdd:PRK05620 92 NPLNKQLMNDQIVHIIN----HAEDEVI----VADPRLAE--QLGEILKECPCV----RAVVFIGPSDADSAAAHMP--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 277 vqiswnEGVDLWWHELMQKaGDECEPEWCDAE--DPLFILYTSGSTGKPKGV-------------LHTVGGYMLYVATTF 341
Cdd:PRK05620 155 ------EGIKVYSYEALLD-GRSTVYDWPELDetTAAAICYSTGTTGAPKGVvyshrslylqslsLRTTDSLAVTHGESF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 342 KY-VFDFHAedVFWCTADIGWITGhsyvtygplangaTSVLFEGiptyPDVS--RLWNIVEKYKVTKFYTAPTA-IRLLM 417
Cdd:PRK05620 228 LCcVPIYHV--LSWGVPLAAFMSG-------------TPLVFPG----PDLSapTLAKIIATAMPRVAHGVPTLwIQLMV 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 418 KFGDEPvtkHSRASLQVLGTVGEPINPEAW-LWYHRVvGAQrcpIVDTFWQTETG--GHMLTPLPGAipmkPGSATFPFF 494
Cdd:PRK05620 289 HYLKNP---PERMSLQEIYVGGSAVPPILIkAWEERY-GVD---VVHVWGMTETSpvGTVARPPSGV----SGEARWAYR 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 495 ---GVAPAILNESGEELEGEAEGY------LVFKQPW-------------PGIMRTVYGNHERFETTYFKKfPGYYVTGD 552
Cdd:PRK05620 358 vsqGRFPASLEYRIVNDGQVMESTdrnegeIQVRGNWvtasyyhspteegGGAASTFRGEDVEDANDRFTA-DGWLRTGD 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 553 GCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSPALTEELK 632
Cdd:PRK05620 437 VGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAERLR 516
|
570
....*....|....*
gi 1387203675 633 KQIREKIGPIATPDY 647
Cdd:PRK05620 517 DQLRDRLPNWMLPEY 531
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
550-663 |
1.00e-08 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 58.28 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 550 TGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSPaltE 629
Cdd:PRK08315 431 TGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTE---E 507
|
90 100 110
....*....|....*....|....*....|....*
gi 1387203675 630 ELKKQIREKIGPIATPDYIQNAPGLPKTRSGN-QK 663
Cdd:PRK08315 508 DVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKiQK 542
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
300-605 |
1.19e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 58.18 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 300 CEPEWCDAED-----PLF-------ILYTSGSTGKPKGVLHTVGGYMLYV-ATTFKYVFDFHAEDVF-----------WC 355
Cdd:PRK07008 156 CYETLVGAQDgdydwPRFdenqassLCYTSGTTGNPKGALYSHRSTVLHAyGAALPDAMGLSARDAVlpvvpmfhvnaWG 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 356 TADIGWITGHSYVTYGPLANGATsvlfegiptypdvsrLWNIVEKYKVTkfYTA--PTAIRLLMKFGDEPVTKHSRASLQ 433
Cdd:PRK07008 236 LPYSAPLTGAKLVLPGPDLDGKS---------------LYELIEAERVT--FSAgvPTVWLGLLNHMREAGLRFSTLRRT 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 434 VLGtvGEPINPEAWLWYHRVVGAQrcpIVDTFWQTE----------TGGHMLTPLPG--AIPMKPGSAtfpFFGVAPAIL 501
Cdd:PRK07008 299 VIG--GSACPPAMIRTFEDEYGVE---VIHAWGMTEmsplgtlcklKWKHSQLPLDEqrKLLEKQGRV---IYGVDMKIV 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 502 NESGEelegeaegylvfKQPWPGImrtVYGN-HER---FETTYFKK-----FPGYYVTGDGCRRDKDGYYWITGRIDDML 572
Cdd:PRK07008 371 GDDGR------------ELPWDGK---AFGDlQVRgpwVIDRYFRGdasplVDGWFPTGDVATIDADGFMQITDRSKDVI 435
|
330 340 350
....*....|....*....|....*....|...
gi 1387203675 573 NVSGHLLSTAEVESALVEHKAVAEAAVVGHPHP 605
Cdd:PRK07008 436 KSGGEWISSIDIENVAVAHPAVAEAACIACAHP 468
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
136-648 |
1.22e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 58.64 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 136 ITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLITTD 215
Cdd:PRK05691 2214 LSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDR 2293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 216 AFYRGeklvnLKELADEALEKCQEKGFPvkccivvkhlgraeLVTGDSPSQSPPIKRPcpdvqiswnegvdlwwhelmqk 295
Cdd:PRK05691 2294 ALFEA-----LGELPAGVARWCLEDDAA--------------ALAAYSDAPLPFLSLP---------------------- 2332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 296 agdecepewcdaEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKyVFDFHAEDvfwCTADIGWIT--GHSYVTYGPL 373
Cdd:PRK05691 2333 ------------QHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIE-RFGMRADD---CELHFYSINfdAASERLLVPL 2396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 374 ANGATSVL-FEGiptYPDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFgdePVTKHSRASLQVLGTVGEPINPEAWLWYHR 452
Cdd:PRK05691 2397 LCGARVVLrAQG---QWGAEEICQLIREQQVSILGFTPSYGSQLAQW---LAGQGEQLPVRMCITGGEALTGEHLQRIRQ 2470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 453 VVGAQRcpIVDTFWQTETgghMLTPLPGAIP--MKPGSATFPFFGVAPA----ILNESGEELEGEAEGYLvfkqpWPGIM 526
Cdd:PRK05691 2471 AFAPQL--FFNAYGPTET---VVMPLACLAPeqLEEGAASVPIGRVVGArvayILDADLALVPQGATGEL-----YVGGA 2540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 527 RTVYGNH-------ERFETTYFKKFPG-YYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAA 598
Cdd:PRK05691 2541 GLAQGYHdrpgltaERFVADPFAADGGrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAV 2620
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1387203675 599 VVGHPHPvKGECLYCFV---TLCDGHIFSPALTEELKKQIREKIgpiatPDYI 648
Cdd:PRK05691 2621 VLALDTP-SGKQLAGYLvsaVAGQDDEAQAALREALKAHLKQQL-----PDYM 2667
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
135-666 |
1.27e-08 |
|
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: 57.75 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 135 QITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSivfagfsseslcerildsncslLITT 214
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAA----------------------LINY 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 215 DAfyRGEKLVNLKELADealekcqekgfpVKCCIVvkhlgraelvtgdspsqsppikrpcpdvqiswnegvdlwwhelmq 294
Cdd:cd05940 61 NL--RGESLAHCLNVSS------------AKHLVV--------------------------------------------- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 295 kagdecepewcdaeDPLFILYTSGSTGKPKGVLHTVGGYmLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLA 374
Cdd:cd05940 82 --------------DAALYIYTSGTTGLPKAAIISHRRA-WRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLA 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 375 NGATSVLFEGIptypDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEPVTK-HsraslQVLGTVGEPINPEAWLWYHRV 453
Cdd:cd05940 147 SGATLVIRKKF----SASNFWDDIRKYQATIFQYIGELCRYLLNQPPKPTERkH-----KVRMIFGNGLRPDIWEEFKER 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 454 VGAQRcpiVDTFWQTETGGHMLTPLPGaipmKPGSAtfpffGVAPAILnesgeeleGEAEGYLVFK------QPW----- 522
Cdd:cd05940 218 FGVPR---IAEFYAATEGNSGFINFFG----KPGAI-----GRNPSLL--------RKVAPLALVKydlesgEPIrdaeg 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 523 ---------PGIMRTVYGNHERFE-------------TTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLS 580
Cdd:cd05940 278 rcikvprgePGLLISRINPLEPFDgytdpaatekkilRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVS 357
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 581 TAEVESALVEHKAVAEAAVVGHPHP-VKGECLYCFVTLCDGHIFSpalTEELKKQIREKIGPIATPDYIQNAPGLPKTRS 659
Cdd:cd05940 358 TTEVAAVLGAFPGVEEANVYGVQVPgTDGRAGMAAIVLQPNEEFD---LSALAAHLEKNLPGYARPLFLRLQPEMEITGT 434
|
....*..
gi 1387203675 660 GNQKRVD 666
Cdd:cd05940 435 FKQQKVD 441
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
115-660 |
2.28e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 57.08 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 115 KKLGDKVAFYWEGNepeettQITYRELLVQVCRFSNVLRKQ-GICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAG 193
Cdd:PRK05677 35 QRFADKPAFSNLGK------TLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 194 FSSESLCERILDSNCSLLITtdafyrgekLVNLKELADEALEKCQekgfpvkccivVKHLgraeLVTgDSPSQSPPIKRP 273
Cdd:PRK05677 109 YTAREMEHQFNDSGAKALVC---------LANMAHLAEKVLPKTG-----------VKHV----IVT-EVADMLPPLKRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 274 CPDVQISWNEGVDLWWH---------ELMQKAGDECEPEWCDAEDPLFILYTSGSTGKPKGVLHT---VGGYMLYVATTF 341
Cdd:PRK05677 164 LINAVVKHVKKMVPAYHlpqavkfndALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLThrnLVANMLQCRALM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 342 K-------------------YVFDFHaedvfwCTAdigwitghsyvtygPLANGATSVLfegIPTYPDVSRLWNIVEKYK 402
Cdd:PRK05677 244 GsnlnegceiliaplplyhiYAFTFH------CMA--------------MMLIGNHNIL---ISNPRDLPAMVKELGKWK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 403 VTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETgghmlTPLPGAI 482
Cdd:PRK05677 301 FSGFVGLNTLFVALCN--NEAFRKLDFSALKLTLSGGMALQLATAERWKEVTG---CAICEGYGMTET-----SPVVSVN 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 483 PMK---PGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHErfETTYFKKFPGYYVTGDGCRRDKD 559
Cdd:PRK05677 371 PSQaiqVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGP--QVMKGYWQRPE--ATDEILDSDGWLKTGDIALIQED 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 560 GYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGhifsPALTEE-LKKQIREK 638
Cdd:PRK05677 447 GYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPG----ETLTKEqVMEHMRAN 522
|
570 580
....*....|....*....|..
gi 1387203675 639 IGPIATPDYIQNAPGLPKTRSG 660
Cdd:PRK05677 523 LTGYKVPKAVEFRDELPTTNVG 544
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
115-660 |
1.11e-07 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 54.83 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 115 KKLGDKVAFYWEGnepeetTQITYRELLVQVCRFSNVLRKQ-GICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAG 193
Cdd:PRK12492 35 KKFADRPAFSNLG------VTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 194 FSSESLCERILDSNCSLLITTDAFyrgEKLVNlKELADEALEKCQE----------KGFPVKccIVVKHLGRaeLVTGDS 263
Cdd:PRK12492 109 YTAREMRHQFKDSGARALVYLNMF---GKLVQ-EVLPDTGIEYLIEakmgdllpaaKGWLVN--TVVDKVKK--MVPAYH 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 264 PSQSPPIKRPcpdvqiswnegvdlwwheLMQKAGDECEPEWCDAEDPLFILYTSGSTGKPKGVLHTVGGYmlyVAttfky 343
Cdd:PRK12492 181 LPQAVPFKQA------------------LRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNL---VA----- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 344 vfdfHAEDVFWCTADIGwITGHS---------------YVTYGPLAN-------GATSVLFegipTYP-DVSRLWNIVEK 400
Cdd:PRK12492 235 ----NMLQVRACLSQLG-PDGQPlmkegqevmiaplplYHIYAFTANcmcmmvsGNHNVLI----TNPrDIPGFIKELGK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 401 YKVTKFYTAPTAIRLLMkfgDEPVTKHSRAS-LQVLGTVGEPI---NPEAWlwyHRVVGaqrCPIVDTFWQTETgghmlT 476
Cdd:PRK12492 306 WRFSALLGLNTLFVALM---DHPGFKDLDFSaLKLTNSGGTALvkaTAERW---EQLTG---CTIVEGYGLTET-----S 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 477 PLPGAIPM----KPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHErfETTYFKKFPGYYVTGD 552
Cdd:PRK12492 372 PVASTNPYgelaRLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGP--QVMKGYWQQPE--ATAEALDAEGWFKTGD 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 553 GCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDghifsPALT-EEL 631
Cdd:PRK12492 448 IAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARD-----PGLSvEEL 522
|
570 580
....*....|....*....|....*....
gi 1387203675 632 KKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:PRK12492 523 KAYCKENFTGYKVPKHIVLRDSLPMTPVG 551
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
545-670 |
1.40e-07 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 54.23 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 545 PGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFs 624
Cdd:PRK07445 323 QGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSIS- 401
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1387203675 625 palTEELKKQIREKIGPIATPDYIQNAPGLPKTrsgnqkrvdPQGK 670
Cdd:PRK07445 402 ---LEELKTAIKDQLSPFKQPKHWIPVPQLPRN---------PQGK 435
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
548-664 |
2.40e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.40 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 548 YVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAvVGHPHPVKGECLYCFVTLCDGHIFSPAL 627
Cdd:PRK05691 4104 YRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAA-VAVQEGVNGKHLVGYLVPHQTVLAQGAL 4182
|
90 100 110
....*....|....*....|....*....|....*..
gi 1387203675 628 TEELKKQIREKIGPIATPDYIQNAPGLPKTRSGNQKR 664
Cdd:PRK05691 4183 LERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDR 4219
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
546-660 |
3.65e-07 |
|
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: 52.69 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 546 GYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGHIFSP 625
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTE 296
|
90 100 110
....*....|....*....|....*....|....*
gi 1387203675 626 AlteELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:cd17636 297 A---ELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
546-664 |
3.65e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 53.08 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 546 GYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTLCDGhifSP 625
Cdd:PRK13383 396 GMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPG---SG 472
|
90 100 110
....*....|....*....|....*....|....*....
gi 1387203675 626 ALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGNQKR 664
Cdd:PRK13383 473 VDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLR 511
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
545-664 |
8.49e-07 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 51.58 E-value: 8.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 545 PGYYVTGDGCRRDkDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVtLCDGHifs 624
Cdd:PRK07824 233 PGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAV-VGDGG--- 307
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1387203675 625 PALT-EELKKQIREKIGPIATPDYIQNAPGLPKTRSGNQKR 664
Cdd:PRK07824 308 PAPTlEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDR 348
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
306-660 |
8.84e-07 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 52.23 E-value: 8.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 306 DAEDPLFILYTSGSTGKPKGVL---HTVGGYMLYVATtfkyVFDFHAEDVfwctadigwITG-----HSY----VTYGPL 373
Cdd:PRK08633 780 KPDDTATIIFSSGSEGEPKGVMlshHNILSNIEQISD----VFNLRNDDV---------ILSslpffHSFgltvTLWLPL 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 374 ANGATSVlFEGIPTypDVSRLWNIVEKYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLgtvgepinpeawlwyhrV 453
Cdd:PRK08633 847 LEGIKVV-YHPDPT--DALGIAKLVAKHRATILLGTPTFLRLYLR--NKKLHPLMFASLRLV-----------------V 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 454 VGAQRCP--IVDTFWQ------------TETgghmlTP-----LPGA--------IPMKPGSATFPFFGVAPAILNESGE 506
Cdd:PRK08633 905 AGAEKLKpeVADAFEEkfgirilegygaTET-----SPvasvnLPDVlaadfkrqTGSKEGSVGMPLPGVAVRIVDPETF 979
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 507 ELEGEAEGYLVFKQPwPGIMRTVYGNHERF-ETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVE 585
Cdd:PRK08633 980 EELPPGEDGLILIGG-PQVMKGYLGDPEKTaEVIKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVE 1058
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 586 SALveHKAVAEA----AVVGHPHPVKGECLYCFVTLcdghifSPALTEELKKQIRE-KIGPIATPDYIQNAPGLPKTRSG 660
Cdd:PRK08633 1059 EEL--AKALGGEevvfAVTAVPDEKKGEKLVVLHTC------GAEDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSG 1130
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
110-375 |
1.19e-06 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 51.77 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 110 RIVHEKKLGDKVafyWegnepeettqITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACA-------- 181
Cdd:PLN02861 65 RQVTDSKVGPYV---W----------LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNsqgityvp 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 182 ---RLGAL-------HSIVFAGFSSESLCERILD--SNCSLLITTdafyrgekLVNLKELADEALEKCQEKGfpVKCciv 249
Cdd:PLN02861 132 lydTLGANavefiinHAEVSIAFVQESKISSILSclPKCSSNLKT--------IVSFGDVSSEQKEEAEELG--VSC--- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 250 vkhlgraelvtgdspsqsppikrpcpdvqISWNEgvdlwwheLMQKAGDECEPEWCDAEDPLFILYTSGSTGKPKGVLHT 329
Cdd:PLN02861 199 -----------------------------FSWEE--------FSLMGSLDCELPPKQKTDICTIMYTSGTTGEPKGVILT 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1387203675 330 VGGYMLYVATTFKYVFdfhaedvfwcTADIGWITGHSYVTYGPLAN 375
Cdd:PLN02861 242 NRAIIAEVLSTDHLLK----------VTDRVATEEDSYFSYLPLAH 277
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
550-665 |
1.56e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 50.81 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 550 TGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGE--CLycfvTLCDGHIFSPAl 627
Cdd:PRK08308 295 TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGErvKA----KVISHEEIDPV- 369
|
90 100 110
....*....|....*....|....*....|....*...
gi 1387203675 628 teELKKQIREKIGPIATPDYIQNAPGLPKTRSGNQKRV 665
Cdd:PRK08308 370 --QLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRK 405
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
106-326 |
1.68e-06 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 51.05 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 106 NVLDRIVH-EKKLGDKVAFYWEGnepeetTQITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLG 184
Cdd:PRK04813 3 DIIETIEEfAQTQPDFPAYDYLG------EKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 185 alHSIVFAGFSSESlcERILD----SNCSLLITTDAFyrGEKLVNLKELADEALEkcqekgfpvkccivvkhlgrAELVT 260
Cdd:PRK04813 77 --HAYIPVDVSSPA--ERIEMiievAKPSLIIATEEL--PLEILGIPVITLDELK--------------------DIFAT 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387203675 261 GDSPSQSPPIKrpcpdvqiswnegvdlwwhelmqkaGDecepewcdaeDPLFILYTSGSTGKPKGV 326
Cdd:PRK04813 131 GNPYDFDHAVK-------------------------GD----------DNYYIIFTSGTTGKPKGV 161
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
137-337 |
3.25e-06 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 50.20 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 137 TYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARL-------------GALHSIV------FAgFSSE 197
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHslicvplydtlgpGAVDYIVdhaeidFV-FVQD 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 198 SLCERILDSNCSllittdAFYRGEKLVNLKELADEALEKCQEKGFPVKCCIVVKHLGRaelvtgDSPSQ-SPPikrpcpd 276
Cdd:PLN02430 157 KKIKELLEPDCK------SAKRLKAIVSFTSVTEEESDKASQIGVKTYSWIDFLHMGK------ENPSEtNPP------- 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387203675 277 vqiswnegvdlwwhelmqKAGDECEpewcdaedplfILYTSGSTGKPKGVLHTVGGYMLYV 337
Cdd:PLN02430 218 ------------------KPLDICT-----------IMYTSGTSGDPKGVVLTHEAVATFV 249
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
307-632 |
3.26e-06 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 50.15 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 307 AEDPLFILYTSGSTGKPKGVLHTVGGYMLYVAtTFKYVFDFHAEDVFWCTADIgwitghsYVTYGPlANGATSVLFEGIP 386
Cdd:cd05910 84 ADEPAAILFTSGSTGTPKGVVYRHGTFAAQID-ALRQLYGIRPGEVDLATFPL-------FALFGP-ALGLTSVIPDMDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 387 TYP---DVSRLWNIVEKYKVTKFYTAPTAIRLLMKFGDEpvTKHSRASLQVLGTVGEPINPEAWLWYHRVV--------- 454
Cdd:cd05910 155 TRParaDPQKLVGAIRQYGVSIVFGSPALLERVARYCAQ--HGITLPSLRRVLSAGAPVPIALAARLRKMLsdeaeiltp 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 455 -GAQRC-PIvdtfwqTETGGHMLTPLPGAIPmKPGSAT---FPFFGVAPAILNESGEELEGEAEGYLVfkQPW------- 522
Cdd:cd05910 233 yGATEAlPV------SSIGSRELLATTTAAT-SGGAGTcvgRPIPGVRVRIIEIDDEPIAEWDDTLEL--PRGeigeitv 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 523 --PGIMRTVYGnheRFETTYFKKFPG-----YYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVA 595
Cdd:cd05910 304 tgPTVTPTYVN---RPVATALAKIDDnsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVR 380
|
330 340 350
....*....|....*....|....*....|....*..
gi 1387203675 596 EAAVVGHPHPVKGECLYCFVTLCDGHIFSPALTEELK 632
Cdd:cd05910 381 RSALVGVGKPGCQLPVLCVEPLPGTITPRARLEQELR 417
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
136-406 |
3.36e-06 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 49.98 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 136 ITYRELLVQVCRFSNVLRKQ-GICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLITT 214
Cdd:cd05938 6 YTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 215 DAfyrgeklvnLKELADEALEKCQEKGfpVKCCIV--------VKHLGRAelvTGDSPSQSPPikrPCPDVQISWNegvd 286
Cdd:cd05938 86 PE---------LQEAVEEVLPALRADG--VSVWYLshtsntegVISLLDK---VDAASDEPVP---ASLRAHVTIK---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 287 lwwhelmqkagdecepewcdaeDPLFILYTSGSTGKPKGVLhtVGGYMLYVATTFKYVFDFHAEDVFWCTA----DIGWI 362
Cdd:cd05938 145 ----------------------SPALYIYTSGTTGLPKAAR--ISHLRVLQCSGFLSLCGVTADDVIYITLplyhSSGFL 200
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1387203675 363 TGHSyvtyGPLANGATSVLFEGIPTypdvSRLWNIVEKYKVTKF 406
Cdd:cd05938 201 LGIG----GCIELGATCVLKPKFSA----SQFWDDCRKHNVTVI 236
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
136-420 |
3.82e-06 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 49.91 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 136 ITYRELLVQVCRFSNVLRKQGIC--KGDRVAIYMPMIPELVVAMLACARLGalhsivfagfsseslcerildsncsllIT 213
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYS---------------------------LV 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 214 TDAFYrgeklvnlKELADEALEkcqekgfpvkccIVVKHlGRAELVTGDspsqsppikrpcpdvqiswnEGVDLW-WHEL 292
Cdd:cd05927 59 TVPLY--------DTLGPEAIE------------YILNH-AEISIVFCD--------------------AGVKVYsLEEF 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 293 MQK-AGDECEPEWCDAEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKYVFDFHAEDVFwctaDIgwitghsYVTYG 371
Cdd:cd05927 98 EKLgKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPT----DV-------YISYL 166
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387203675 372 PLAN---------------------GATSVLFEGI----PTY-PDVSRLWNIVEKYKVTKFYTAPTAIRLLMKFG 420
Cdd:cd05927 167 PLAHifervvealflyhgakigfysGDIRLLLDDIkalkPTVfPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFA 241
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
135-447 |
3.98e-06 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 49.90 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 135 QITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERILDSNCSLLITt 214
Cdd:PRK09274 41 ELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIG- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 215 dafyrgeklvnlkeladealekcqekgfpvkccIVVKHLGRaeLVTGdspsqsppikRPCPDVQISWNEGVDLWW----- 289
Cdd:PRK09274 120 ---------------------------------IPKAHLAR--RLFG----------WGKPSVRRLVTVGGRLLWggttl 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 290 HELMQK-AGDECEPEWCDAEDPLFILYTSGSTGKPKGVLHTVGgymlyvattfkyvfDFHA------EDVFWCTADIGWI 362
Cdd:PRK09274 155 ATLLRDgAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHG--------------MFEAqiealrEDYGIEPGEIDLP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 363 TGHSYVTYGPlANGATSVLFEGIPTYP---DVSRLWNIVEKYKVTKFYTAPTAIrllmkfgdEPVTKHSRASLQVLGTV- 438
Cdd:PRK09274 221 TFPLFALFGP-ALGMTSVIPDMDPTRPatvDPAKLFAAIERYGVTNLFGSPALL--------ERLGRYGEANGIKLPSLr 291
|
330
....*....|....
gi 1387203675 439 -----GEPINPEAW 447
Cdd:PRK09274 292 rvisaGAPVPIAVI 305
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
136-329 |
7.12e-06 |
|
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: 49.20 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 136 ITYRELLVQVCRFSNVLRKQGICKGDRVAIYMPMIPELVVAMLACARLGALHSIVFAGFSSESLCERIldsncsllittd 215
Cdd:cd05906 40 QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPNARL------------ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 216 afyrgEKLVNLKELADEalekcqekgfpvkcCIVvkhLGRAELVTGDSPSQSPpikRPCPDVQISWNEgvdlwwhELMQK 295
Cdd:cd05906 108 -----RKLRHIWQLLGS--------------PVV---LTDAELVAEFAGLETL---SGLPGIRVLSIE-------ELLDT 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 1387203675 296 AGDecePEW--CDAEDPLFILYTSGSTGKPKGVLHT 329
Cdd:cd05906 156 AAD---HDLpqSRPDDLALLMLTSGSTGFPKAVPLT 188
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
299-382 |
1.53e-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: 47.98 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 299 ECEPEWCD--AEDPLFILYTSGSTGKPKGVLHTVGGYMLYVATTFKYVFDFHAEDvfwctadigwitgHSYVTYGPLAN- 375
Cdd:cd17639 77 ECSAIFTDgkPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGPD-------------DRYLAYLPLAHi 143
|
90
....*....|
gi 1387203675 376 ---GATSVLF 382
Cdd:cd17639 144 felAAENVCL 153
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
306-602 |
4.50e-05 |
|
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: 46.58 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 306 DAEDPLFILYTSGSTGKPKGVLHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIgWitgHSY---VTYGPLANGAtSVLF 382
Cdd:cd17640 86 DSDDLATIIYTSGTTGNPKGVMLTHAN-LLHQIRSLSDIVPPQPGDRFLSILPI-W---HSYersAEYFIFACGC-SQAY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 383 EGIPTYPD------------VSRLWNIVEKYKVTKFYTAPTAIRLLMKFgdepvtkhsrasLQVLGTVGEPINpeawlwy 450
Cdd:cd17640 160 TSIRTLKDdlkrvkphyivsVPRLWESLYSGIQKQVSKSSPIKQFLFLF------------FLSGGIFKFGIS------- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 451 hrvvGAQRCPI-VDTFWQ------------TETGGHMLTPLPGAIpmKPGSATFPFFGVAPAILNESGEELEGEAEGYLV 517
Cdd:cd17640 221 ----GGGALPPhVDTFFEaigievlngyglTETSPVVSARRLKCN--VRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 518 FKQPwPGIMRTVYGNHErfETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVS-GHLLSTAEVESALVEHKAVAE 596
Cdd:cd17640 295 WVRG-PQVMKGYYKNPE--ATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQ 371
|
....*.
gi 1387203675 597 AAVVGH 602
Cdd:cd17640 372 IMVVGQ 377
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
306-664 |
5.84e-05 |
|
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: 46.01 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 306 DAEDPLFILYTSGSTGKPKGVL---HTvggyMLYVATTFKYVFDFHAEDVFWCTADIGWiTGHSYVTYGPLANGAT-SVL 381
Cdd:cd17645 102 NPDDLAYVIYTSGSTGLPKGVMiehHN----LVNLCEWHRPYFGVTPADKSLVYASFSF-DASAWEIFPHLTAGAAlHVV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 382 FEGIPTypDVSRLWNIVEKYKVTKFYTaPTAIRllmkfgdEPVTKHSRASLQVLGTVGEPINPEAWLWYHRV--VGAQRC 459
Cdd:cd17645 177 PSERRL--DLDALNDYFNQEGITISFL-PTGAA-------EQFMQLDNQSLRVLLTGGDKLKKIERKGYKLVnnYGPTEN 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 460 PIVDTFWQTEtgghmltPLPGAIPMKPgsatfPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRtvyGNHERFETT 539
Cdd:cd17645 247 TVVATSFEID-------KPYANIPIGK-----PIDNTRVYILDEALQLQPIGVAGELCIAGE--GLAR---GYLNRPELT 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 540 YfKKF------PG--YYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECL 611
Cdd:cd17645 310 A-EKFivhpfvPGerMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYL 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1387203675 612 YCFVTlcdghIFSPALTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGNQKR 664
Cdd:cd17645 389 VAYVT-----APEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDR 436
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
301-445 |
4.39e-04 |
|
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: 43.25 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 301 EPEWCDAEDPL-FILYTSGSTGKPKGVL---HTVGGYMLYVATTfkyvFDFHAEDVF--W--CTADIGWITGHsyvtYGP 372
Cdd:cd05908 98 EEVLCELADELaFIQFSSGSTGDPKGVMlthENLVHNMFAILNS----TEWKTKDRIlsWmpLTHDMGLIAFH----LAP 169
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387203675 373 LANGATSVLfegIPTYPDVSR--LW-NIVEKYKVTKFYTAPTAIRLLMK-FGDEPVTKHSRASLQVLGTVGEPINPE 445
Cdd:cd05908 170 LIAGMNQYL---MPTRLFIRRpiLWlKKASEHKATIVSSPNFGYKYFLKtLKPEKANDWDLSSIRMILNGAEPIDYE 243
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
545-660 |
6.55e-04 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 42.78 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 545 PGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAAVVGHPHPVKGECLYCFVTlcdghifS 624
Cdd:PRK08043 590 RGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEALVLFTT-------D 662
|
90 100 110
....*....|....*....|....*....|....*...
gi 1387203675 625 PALT-EELKKQIREKIGP-IATPDYIQNAPGLPKTRSG 660
Cdd:PRK08043 663 SELTrEKLQQYAREHGVPeLAVPRDIRYLKQLPLLGSG 700
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
306-388 |
1.17e-03 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 42.26 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 306 DAEDPLFILYTSGSTGKPKGVL--HTvggYMLYVATTFKYVFDFHAEDVFWCTADIgwitGHSyvtYGpLANGATSVLFE 383
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGVVlsHR---NLLANRAQVAARIDFSPEDKVFNALPV----FHS---FG-LTGGLVLPLLS 859
|
....*
gi 1387203675 384 GIPTY 388
Cdd:PRK06814 860 GVKVF 864
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
521-659 |
1.99e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 41.63 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 521 PWPGIMRTVYGNHERFETTyfkkfpGYYVtgdgcRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHKAVAEAavV 600
Cdd:PRK07868 822 PTASVKRGVFAPADTWIST------EYLF-----RRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLA--V 888
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387203675 601 GHPHPVKGECL-YCFVTLCDGHIFSPA-LTEELkkqirEKIGPIATPDYIQNAPGLPKTRS 659
Cdd:PRK07868 889 TYGVEVGGRQLaVAAVTLRPGAAITAAdLTEAL-----ASLPVGLGPDIVHVVPEIPLSAT 944
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
287-353 |
3.27e-03 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 40.85 E-value: 3.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387203675 287 LW--WHELM-QKAGDECEPEwcdaeDPLFILYTSGSTGKPKGVLHTVGGYMLYVaTTFKYVFDFHAEDVF 353
Cdd:PRK08043 346 LWifAHLLMpRLAQVKQQPE-----DAALILFTSGSEGHPKGVVHSHKSLLANV-EQIKTIADFTPNDRF 409
|
|
| |
