|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
29-693 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 1440.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 29 VLGESLASEENDLVFPSKEFSGQALVSSPQQYMEMHKRSMDDPAAFWSDIASEFYWKQKW-GDQVFSENLDVRKGPISIE 107
Cdd:PLN02654 1 VLGESLASEENDLVFPSKDFSAQALVSSPQQYMEMYKRSVDDPAGFWSDIASQFYWKQKWeGDEVCSENLDVRKGPISIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 108 WFKGGITNICYNCLDKNVEAGLGDKTAIHWEGNELGVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPI 187
Cdd:PLN02654 81 WFKGGKTNICYNCLDRNVEAGNGDKIAIYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 188 AMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVILTCNAVKRGPKTINLKAIVDAALDQSSKDGVSVGICLTYDNSLA 267
Cdd:PLN02654 161 AMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITCNAVKRGPKTINLKDIVDAALDESAKNGVSVGICLTYENQLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 268 TTRENTKWQNGRDVWWQDVISQYPTSCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMIYTATTFKYAFDYKSTDVY 347
Cdd:PLN02654 241 MKREDTKWQEGRDVWWQDVVPNYPTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 348 WCTADCGWITGHSYVTYGPMLNGATVVVFEGAPNYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSLR 427
Cdd:PLN02654 321 WCTADCGWITGHSYVTYGPMLNGATVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 428 VLGSVGEPINPSAWRWFFNVVGDSRCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGNEIEGECS 507
Cdd:PLN02654 401 VLGSVGEPINPSAWRWFFNVVGDSRCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGKEIEGECS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 508 GYLCVKGSWPGAFRTLFGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQ 587
Cdd:PLN02654 481 GYLCVKKSWPGAFRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 588 CAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKIASR 667
Cdd:PLN02654 561 CAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASR 640
|
650 660
....*....|....*....|....*.
gi 332006737 668 QLEELGDTSTLADPSVVDQLIALADV 693
Cdd:PLN02654 641 QLDELGDTSTLADPGVVDQLIALADS 666
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
58-680 |
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: 1168.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 58 QQYMEMHKRSMDDPAAFWSDIASEFYWKQKWgDQVfsenLDVRKGPISIEWFKGGITNICYNCLDKNVEAgLGDKTAIHW 137
Cdd:cd05966 1 EQYKELYKQSIEDPEEFWGEIAKELDWFKPW-DKV----LDWSKGPPFIKWFEGGKLNISYNCLDRHLKE-RGDKVAIIW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 138 EGNELGVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVD 217
Cdd:cd05966 75 EGDEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRIND 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 218 CKPNVILTCNAVKRGPKTINLKAIVDAALDQsskdGVSVGICLTYDNslatTRENTKWQNGRDVWWQDVISQYPTSCEVE 297
Cdd:cd05966 155 AQCKLVITADGGYRGGKVIPLKEIVDEALEK----CPSVEKVLVVKR----TGGEVPMTEGRDLWWHDLMAKQSPECEPE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 298 WVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMIYTATTFKYAFDYKSTDVYWCTADCGWITGHSYVTYGPMLNGATVVVFE 377
Cdd:cd05966 227 WMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMFE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 378 GAPNYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDSRCPISD 457
Cdd:cd05966 307 GTPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGKERCPIVD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 458 TWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGSWPGAFRTLFGDHERYETTYFKP 537
Cdd:cd05966 387 TWWQTETGGIMITPLPGATPLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPWPGMARTIYGDHERYEDTYFSK 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 538 FAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPY 617
Cdd:cd05966 467 FPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEP 546
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332006737 618 SEELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKIASRQlEELGDTSTLAD 680
Cdd:cd05966 547 SDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGE-EELGDTSTLAD 608
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
44-689 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 1134.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 44 PSKEFSGQALVSsPQQYMEMHKRSMDDPAAFWSDIASEFYWKQKWgDQVFSENldvrkgPISIEWFKGGITNICYNCLDK 123
Cdd:PRK00174 4 PPAEFAANALID-MEQYKALYQESVEDPEGFWAEQAKRLDWFKPF-DTVLDWN------APFIKWFEDGELNVSYNCLDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 124 NVEAGlGDKTAIHWEGNELGVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVF 203
Cdd:PRK00174 76 HLKTR-GDKVAIIWEGDDPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 204 AGFSADSLAQRIVDCKPNVILTCNAVKRGPKTINLKAIVDAALDqsskdgvsvgICLTYDNSLATTR--ENTKWQNGRDV 281
Cdd:PRK00174 155 GGFSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALA----------NCPSVEKVIVVRRtgGDVDWVEGRDL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 282 WWQDVISQYPTSCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMIYTATTFKYAFDYKSTDVYWCTADCGWITGHSY 361
Cdd:PRK00174 225 WWHELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSY 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 362 VTYGPMLNGATVVVFEGAPNYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSLRVLGSVGEPINPSAW 441
Cdd:PRK00174 305 IVYGPLANGATTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSSLRLLGSVGEPINPEAW 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 442 RWFFNVVGDSRCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGSWPGAFR 521
Cdd:PRK00174 385 EWYYKVVGGERCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDPWPGMMR 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 522 TLFGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVK 601
Cdd:PRK00174 465 TIYGDHERFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIK 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 602 GQGIYAFVTLLEGVPYSEELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKIASRQlEELGDTSTLADP 681
Cdd:PRK00174 545 GQGIYAFVTLKGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEGE-EILGDTSTLADP 623
|
....*...
gi 332006737 682 SVVDQLIA 689
Cdd:PRK00174 624 SVVEKLIE 631
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
54-689 |
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: 1058.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 54 VSSPQQYMEMHKRSMDDPAAFWSDIASE-FYWKQKWgDQVFSENLdvrkgPISIEWFKGGITNICYNCLDKNVEAgLGDK 132
Cdd:TIGR02188 1 IANLEQYKELYEESIEDPDKFWAKLARElLDWFKPF-TKVLDWSF-----PPFYKWFVGGELNVSYNCVDRHLEA-RPDK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 133 TAIHWEGNELGVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLA 212
Cdd:TIGR02188 74 VAIIWEGDEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 213 QRIVDCKPNVILTCNAVKRGPKTINLKAIVDAALDQSskdGVSVGICLTYDNslaTTRENTKWQNGRDVWWQDVISQYPT 292
Cdd:TIGR02188 154 DRINDAGAKLVITADEGLRGGKVIPLKAIVDEALEKC---PVSVEHVLVVRR---TGNPVVPWVEGRDVWWHDLMAKASA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 293 SCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMIYTATTFKYAFDYKSTDVYWCTADCGWITGHSYVTYGPMLNGAT 372
Cdd:TIGR02188 228 YCEPEPMDSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGAT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 373 VVVFEGAPNYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDSR 452
Cdd:TIGR02188 308 TVMFEGVPTYPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKER 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 453 CPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGNEIEG-ECSGYLCVKGSWPGAFRTLFGDHERYE 531
Cdd:TIGR02188 388 CPIVDTWWQTETGGIMITPLPGATPTKPGSATLPFFGIEPAVVDEEGNPVEGpGEGGYLVIKQPWPGMLRTIYGDHERFV 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 532 TTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTL 611
Cdd:TIGR02188 468 DTYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTL 547
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332006737 612 LEGVPYSEELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKIASRQLEELGDTSTLADPSVVDQLIA 689
Cdd:TIGR02188 548 KDGYEPDDELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEAEILGDTSTLEDPSVVEELIE 625
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
107-689 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 887.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 107 EWFKGGITNICYNCLDKNVEaGLGDKTAIHWEGnELGVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELP 186
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAE-GRGDKVALIWEG-EDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 187 IAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVILTCNAVKRGPKTINLKAIVDAALDQSSkdgvSVGICLTYDnsl 266
Cdd:COG0365 79 IAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELP----SLEHVIVVG--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 267 attRENTKWQNGRDVWWQDVISQYPTSCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMIYTATTFKYAFDYKSTDV 346
Cdd:COG0365 152 ---RTGADVPMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 347 YWCTADCGWITGHSYVTYGPMLNGATVVVFEGAPNYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSL 426
Cdd:COG0365 229 FWCTADIGWATGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 427 RVLGSVGEPINPSAWRWFFNVVGdsrCPISDTWWQTETGGFMITPLPGaWPQKPGSATFPFFGVQPVIVDEKGNEIEGEC 506
Cdd:COG0365 309 RLLGSAGEPLNPEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLPG-LPVKPGSMGKPVPGYDVAVVDEDGNPVPPGE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 507 SGYLCVKGSWPGAFRTLFGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHP 586
Cdd:COG0365 385 EGELVIKGPWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 587 QCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKIAS 666
Cdd:COG0365 465 AVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAE 544
|
570 580
....*....|....*....|...
gi 332006737 667 RqlEELGDTSTLADPSVVDQLIA 689
Cdd:COG0365 545 G--RPLGDTSTLEDPEALDEIKE 565
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
60-657 |
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: 721.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 60 YMEMHKRSMDDPAAFWSDIASEFYWKqkWGDQVfSENLDVRKGPISIEWFKGGITNICYNCLDKNVEAGlGDKTAIHWEG 139
Cdd:cd17634 1 YETKYRQSINDPDTFWGEAGKILDWI--TPYQK-VKNTSFAPGAPSIKWFEDATLNLAANALDRHLREN-GDRTAIIYEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 140 NELGVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCK 219
Cdd:cd17634 77 DDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 220 PNVILTCNAVKRGPKTINLKAIVDAALDQSskdGVSVGICLTYDNslatTRENTKWQNGRDVWWQDVISQYPTSCEVEWV 299
Cdd:cd17634 157 SRLLITADGGVRAGRSVPLKKNVDDALNPN---VTSVEHVIVLKR----TGSDIDWQEGRDLWWRDLIAKASPEHQPEAM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 300 DAEDPLFLLYTSGSTGKPKGVLHTTGGYMIYTATTFKYAFDYKSTDVYWCTADCGWITGHSYVTYGPMLNGATVVVFEGA 379
Cdd:cd17634 230 NAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 380 PNYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDSRCPISDTW 459
Cdd:cd17634 310 PNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPVVDTW 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 460 WQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGSWPGAFRTLFGDHERYETTYFKPFA 539
Cdd:cd17634 390 WQTETGGFMITPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWPGQTRTLFGDHERFEQTYFSTFK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 540 GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSE 619
Cdd:cd17634 470 GMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSP 549
|
570 580 590
....*....|....*....|....*....|....*...
gi 332006737 620 ELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIM 657
Cdd:cd17634 550 ELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
60-687 |
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: 643.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 60 YMEMHKRSMDDPAAFWSDIASEFYWKQKWgDQVFSenldvRKGPISIEWFKGGITNICYNCLDKNVEAGLGDKTAIHWEG 139
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARLIDWFKPP-EKILD-----NSNPPFTRWFVGGRLNTCYNALDRHVEAGRGDQIALIYDS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 140 NELGVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCK 219
Cdd:cd05967 75 PVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 220 PNVILTCNAVKRGPKTINLKAIVDAALDQSSKDGVSVgicLTYDNSLATTRENTKwqnGRDVWWQDVISQYpTSCEVEWV 299
Cdd:cd05967 155 PKLIVTASCGIEPGKVVPYKPLLDKALELSGHKPHHV---LVLNRPQVPADLTKP---GRDLDWSELLAKA-EPVDCVPV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 300 DAEDPLFLLYTSGSTGKPKGVLHTTGGYMIYTATTFKYAFDYKSTDVYWCTADCGWITGHSYVTYGPMLNGATVVVFEGA 379
Cdd:cd05967 228 AATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEGK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 380 P-NYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDD--KFVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGdsrCPIS 456
Cdd:cd05967 308 PvGTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPdgKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLG---VPVI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 457 DTWWQTETGGFMITPLPG--AWPQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGSW-PGAFRTLFGDHERYETT 533
Cdd:cd05967 385 DHWWQTETGWPITANPVGlePLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPLpPGCLLTLWKNDERFKKL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 534 YFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLE 613
Cdd:cd05967 465 YLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKE 544
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332006737 614 GVPYS-EELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKIAsrQLEELGDTSTLADPSVVDQL 687
Cdd:cd05967 545 GVKITaEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIA--DGEDYTIPSTIEDPSVLDEI 617
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
58-687 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 580.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 58 QQYMEMHKRSMDDPAAFWSDIASEFYWKQKWgDQVfsenLDVRKGPISiEWFKGGITNICYNCLDKNVEAGlGDKTAIHW 137
Cdd:PRK10524 2 MSYSEFYQRSIDDPEAFWAEQARRIDWQTPF-TQV----LDYSNPPFA-RWFVGGRTNLCHNAVDRHLAKR-PEQLALIA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 138 EGNELGVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVD 217
Cdd:PRK10524 75 VSTETDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 218 CKPNVILTCNAVKRGPKTINLKAIVDAALDQSSKDGVSVgicLTYDNSLATTRentkWQNGRDVWWQDVISQY-PTSCEV 296
Cdd:PRK10524 155 AKPVLIVSADAGSRGGKVVPYKPLLDEAIALAQHKPRHV---LLVDRGLAPMA----RVAGRDVDYATLRAQHlGARVPV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 297 EWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMIYTATTFKYAFDYKSTDVYWCTADCGWITGHSYVTYGPMLNGATVVVF 376
Cdd:PRK10524 228 EWLESNEPSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 377 EGAPNYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGdsrCPIS 456
Cdd:PRK10524 308 EGLPTRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLDEPTASWISEALG---VPVI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 457 DTWWQTETGGFMITPLPG--AWPQKPGSATFPFFGVQPVIVDEK-GNEIEGECSGYLCVKGSW-PGAFRTLFGDHERYET 532
Cdd:PRK10524 385 DNYWQTETGWPILAIARGveDRPTRLGSPGVPMYGYNVKLLNEVtGEPCGPNEKGVLVIEGPLpPGCMQTVWGDDDRFVK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 533 TYFKPFAG-YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTL 611
Cdd:PRK10524 465 TYWSLFGRqVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVP 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 612 LEGVPY-SEELRKSL--VLM--VRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKIASRQleELGDTSTLADPSVVDQ 686
Cdd:PRK10524 545 KDSDSLaDREARLALekEIMalVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAEGR--DPGDLTTIEDPAALQQ 622
|
.
gi 332006737 687 L 687
Cdd:PRK10524 623 I 623
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
58-681 |
7.62e-175 |
|
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: 512.81 E-value: 7.62e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 58 QQYMEMHKRSMDDPAAFWSDIASEF-YWKQKWGDQVfsenLDVRKGPISIEWFKGGITNICYNCLDKNVeAGLGDKTAIH 136
Cdd:cd05968 7 PDLEAFLERSAEDNAWFWGEFVKDVgIEWYEPPYQT----LDLSGGKPWAAWFVGGRMNIVEQLLDKWL-ADTRTRPALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 137 WEGnELGVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIV 216
Cdd:cd05968 82 WEG-EDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 217 DCKPNVILTCNAVKRGPKTINLKAIVDAALDQsskdgvsvgiCLTYDNSLATTR--ENTKWQNGRDVWWQDVISQYPTsc 294
Cdd:cd05968 161 DAEAKALITADGFTRRGREVNLKEEADKACAQ----------CPTVEKVVVVRHlgNDFTPAKGRDLSYDEEKETAGD-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 295 EVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMIYTATTFKYAFDYKSTD-VYWCTaDCGWITGhSYVTYGPMLNGATV 373
Cdd:cd05968 229 GAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDlLTWFT-DLGWMMG-PWLIFGGLILGATM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 374 VVFEGAPNYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDSRC 453
Cdd:cd05968 307 VLYDGAPDHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 454 PISDTWWQTET-----GGFMITPLpgawpqKPGSATFPFFGVQPVIVDEKGNEIEGEcSGYLCVKGSWPGAFRTLFGDHE 528
Cdd:cd05968 387 PIINYSGGTEIsggilGNVLIKPI------KPSSFNGPVPGMKADVLDESGKPARPE-VGELVLLAPWPGMTRGFWRDED 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 529 RYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAF 608
Cdd:cd05968 460 RYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCF 539
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332006737 609 VTLLEGVPYSEELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRkiASRQLEELGDTSTLADP 681
Cdd:cd05968 540 VVLKPGVTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR--AAYLGKELGDLSSLENP 610
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
98-680 |
4.34e-174 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 509.05 E-value: 4.34e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 98 DVRKgpiSIEWFKGGITNICYNCLDKNVEAGLGDKTAIHWEGNELGVDasLTYSELLQRVCQLANYLKDNGVKKGDAVVI 177
Cdd:PRK04319 29 EVEK---EFSWLETGKVNIAYEAIDRHADGGRKDKVALRYLDASRKEK--YTYKELKELSNKFANVLKELGVEKGDRVFI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 178 YLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVILTCNAV---KRGPKTINLKAIVDAALDQSSKDGv 254
Cdd:PRK04319 104 FMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALlerKPADDLPSLKHVLLVGEDVEEGPG- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 255 svgiCLTYDNSLAttrentkwqngrdvwwqdvisQYPTSCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGyMIYTATT 334
Cdd:PRK04319 183 ----TLDFNALME---------------------QASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNA-MLQHYQT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 335 FKYAFDYKSTDVYWCTADCGWITGHSYVTYGPMLNGATVVVFEGAPnypDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDD 414
Cdd:PRK04319 237 GKYVLDLHEDDVYWCTADPGWVTGTSYGIFAPWLNGATNVIDGGRF---SPERWYRILEDYKVTVWYTAPTAIRMLMGAG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 415 DKFVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGdsrCPISDTWWQTETGGFMITPLPgAWPQKPGSATFPFFGVQPVI 494
Cdd:PRK04319 314 DDLVKKYDLSSLRHILSVGEPLNPEVVRWGMKVFG---LPIHDNWWMTETGGIMIANYP-AMDIKPGSMGKPLPGIEAAI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 495 VDEKGNEIEGECSGYLCVKGSWPGAFRTLFGDHERYETtYFKPfaGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIG 574
Cdd:PRK04319 390 VDDQGNELPPNRMGNLAIKKGWPSMMRGIWNNPEKYES-YFAG--DWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVG 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 575 TAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSG 654
Cdd:PRK04319 467 PFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSG 546
|
570 580
....*....|....*....|....*..
gi 332006737 655 KIMRRILRkiaSRQLE-ELGDTSTLAD 680
Cdd:PRK04319 547 KIMRRVLK---AWELGlPEGDLSTMED 570
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
148-666 |
6.02e-143 |
|
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: 424.61 E-value: 6.02e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 148 LTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVILTCN 227
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 228 AVKRgpKTinlkaivdaaldqsskdgvsvgicltydnslattrentkwqngrdvwwqdvisqyptscevewvDAEDPLFL 307
Cdd:cd05969 81 ELYE--RT----------------------------------------------------------------DPEDPTLL 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 308 LYTSGSTGKPKGVLHTTGGyMIYTATTFKYAFDYKSTDVYWCTADCGWITGHSYVTYGPMLNGATVVVFEGAPnypDPGR 387
Cdd:cd05969 95 HYTSGTTGTPKGVLHVHDA-MIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRF---DAES 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 388 CWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGdsrCPISDTWWQTETGGF 467
Cdd:cd05969 171 WYGIIERVKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFG---VPIHDTWWQTETGSI 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 468 MITPLPGAwPQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGSWPGAFRTLFGDHERYETtYFKpfAGYYFSGDG 547
Cdd:cd05969 248 MIANYPCM-PIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPGWPSMFRGIWNDEERYKN-SFI--DGWYLTGDL 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 548 CSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEELRKSLVL 627
Cdd:cd05969 324 AYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIIN 403
|
490 500 510
....*....|....*....|....*....|....*....
gi 332006737 628 MVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKIAS 666
Cdd:cd05969 404 FVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKEL 442
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
148-663 |
1.06e-117 |
|
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: 359.34 E-value: 1.06e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 148 LTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIvdckpnviltcn 227
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRL------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 228 avkrgpKTINLKAIVdaaldqsskdgvsvgicltydnslattrentkwqngrdvwwqdvisqyptscevewVDAEDPLFL 307
Cdd:cd05972 69 ------EAAGAKAIV--------------------------------------------------------TDAEDPALI 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 308 LYTSGSTGKPKGVLHTTGgYMIYTATTFKYAFDYKSTDVYWCTADCGWITGHSYVTYGPMLNGATVVVFEGAPNypDPGR 387
Cdd:cd05972 87 YFTSGTTGLPKGVLHTHS-YPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRF--DAER 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 388 CWDIVDKYKVSIFYTAPTLVRSLMRDDdkfVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGdsrCPISDTWWQTETGgF 467
Cdd:cd05972 164 ILELLERYGVTSFCGPPTAYRMLIKQD---LSSYKFSHLRLVVSAGEPLNPEVIEWWRAATG---LPIRDGYGQTETG-L 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 468 MITPLPGAwPQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGSWPGAFRTLFGDHERYETTYFkpfAGYYFSGDG 547
Cdd:cd05972 237 TVGNFPDM-PVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPPPGLFLGYVGDPEKTEASIR---GDYYLTGDR 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 548 CSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEELRKSLVL 627
Cdd:cd05972 313 AYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQG 392
|
490 500 510
....*....|....*....|....*....|....*.
gi 332006737 628 MVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRK 663
Cdd:cd05972 393 HVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
127-569 |
6.24e-113 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 346.61 E-value: 6.24e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 127 AGLGDKTAIhwegnELGVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGF 206
Cdd:pfam00501 6 ARTPDKTAL-----EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 207 SADSLAQRIVDCKPNVILTCNAVKrgpktinlkaIVDAALDQSSKDGVSVGICLTYDNSLATtrentkwqngrDVWWQDV 286
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALK----------LEELLEALGKLEVVKLVLVLDRDPVLKE-----------EPLPEEA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 287 ISQYPTSCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTgGYMIYTATTFK----YAFDYKSTDVYWCTADCGWITGHSYV 362
Cdd:pfam00501 140 KPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTH-RNLVANVLSIKrvrpRGFGLGPDDRVLSTLPLFHDFGLSLG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 363 TYGPMLNGATVVVFEGAPNyPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSrkSLRVLGSVGEPINPSAWR 442
Cdd:pfam00501 219 LLGPLLAGATVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLS--SLRLVLSGGAPLPPELAR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 443 WFFNVVGdsrCPISDTWWQTETGGFMITPLPGAWPQ-KPGSATFPFFGVQPVIVDEK-GNEIEGECSGYLCVKGswPGAF 520
Cdd:pfam00501 296 RFRELFG---GALVNGYGLTETTGVVTTPLPLDEDLrSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRG--PGVM 370
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 332006737 521 RTLFGDHERYETTYFKPfaGYYFSGDGCSRDKDGYYWLTGRVDDVINVS 569
Cdd:pfam00501 371 KGYLNDPELTAEAFDED--GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
130-671 |
4.93e-97 |
|
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: 306.35 E-value: 4.93e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 130 GDKTAIHWEGnelgvdASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAD 209
Cdd:COG0318 13 PDRPALVFGG------RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 210 SLAQRIVDCKPNVILTCnavkrgpktinlkaivdaaldqsskdgvsvgicltydnslattrentkwqngrdvwwqdvisq 289
Cdd:COG0318 87 ELAYILEDSGARALVTA--------------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 290 yptscevewvdaedplFLLYTSGSTGKPKGVLHTTGGyMIYTATTFKYAFDYKSTDVYWCTADCGWITGHSYVTYGPMLN 369
Cdd:COG0318 104 ----------------LILYTSGTTGRPKGVMLTHRN-LLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLA 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 370 GATVVVFEGapnyPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKfvTRHSRKSLRVLGSVGEPINPSAWRWFFNVVG 449
Cdd:COG0318 167 GATLVLLPR----FDPERVLELIERERVTVLFGVPTMLARLLRHPEF--ARYDLSSLRLVVSGGAPLPPELLERFEERFG 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 450 dsrCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGNEI----EGEcsgyLCVKGswPGAFRTLFG 525
Cdd:COG0318 241 ---VRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELppgeVGE----IVVRG--PNVMKGYWN 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 526 DHEryETTyfKPFA-GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQG 604
Cdd:COG0318 312 DPE--ATA--EAFRdGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGER 387
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332006737 605 IYAFVTLLEGVPYS-EELRKSLvlmvRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKIASRQLEE 671
Cdd:COG0318 388 VVAFVVLRPGAELDaEELRAFL----RERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGALE 451
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
303-657 |
5.86e-89 |
|
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: 281.48 E-value: 5.86e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 303 DPLFLLYTSGSTGKPKGVLHTTGGYMIYTATTFKYaFDYKSTDVYWCTADCGWItGHSYVTYGPMLNGATVVVFEGapny 382
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS-GGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 383 PDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKfvTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGdsrCPISDTWWQT 462
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKAPES--AGYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 463 ETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGSWPGAFRTLfgdheRYETTYFKPFAGYY 542
Cdd:cd04433 150 ETGGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWN-----NPEATAAVDEDGWY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 543 FSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGV-PYSEEL 621
Cdd:cd04433 225 RTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGAdLDAEEL 304
|
330 340 350
....*....|....*....|....*....|....*.
gi 332006737 622 RKSlvlmVRNQIGAFAAPDRIHWAPGLPKTRSGKIM 657
Cdd:cd04433 305 RAH----VRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
60-685 |
2.21e-87 |
|
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: 286.47 E-value: 2.21e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 60 YMEMHKRSMDDPAAFWSDIasefyWKqkWGDQVFS---ENLDVRKGPI-SIEWFKGGITNICYNCLDKnveAGLGDKTAI 135
Cdd:cd05943 19 YAALHRWSVDDPGAFWAAV-----WD--FSGVRGSkpyDVVVVSGRIMpGARWFPGARLNYAENLLRH---ADADDPAAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 136 HweGNELGVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRI 215
Cdd:cd05943 89 Y--AAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 216 VDCKPNVILTCNAVKRGPKTINLKAIVDAALDQSSKDGVSVGICLTYDNSLATTRENTKWqngrdVWWQDVISQYPT-SC 294
Cdd:cd05943 167 GQIEPKVLFAVDAYTYNGKRHDVREKVAELVKGLPSLLAVVVVPYTVAAGQPDLSKIAKA-----LTLEDFLATGAAgEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 295 EVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMIYTATTFKYAFDYKSTDVYWCTADCGWITGHSYVTYgpMLNGATVV 374
Cdd:cd05943 242 EFEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRLFYYTTCGWMMWNWLVSG--LAVGATIV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 375 VFEGAPNYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGdsrcp 454
Cdd:cd05943 320 LYDGSPFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIK----- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 455 iSDTWWQTETGG------FMIT-PLpgaWPQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKG--SWPGAFrtlFG 525
Cdd:cd05943 395 -PDVLLASISGGtdiiscFVGGnPL---LPVYRGEIQCRGLGMAVEAFDEEGKPVWGEKGELVCTKPfpSMPVGF---WN 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 526 DHE--RYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQ 603
Cdd:cd05943 468 DPDgsRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDE 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 604 GIYAFVTLLEGVPYSEELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKIASRqlEELGDTSTLADPSV 683
Cdd:cd05943 548 RVILFVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKIIAG--RPVKNAGALANPES 625
|
..
gi 332006737 684 VD 685
Cdd:cd05943 626 LD 627
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
55-663 |
8.04e-81 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 269.69 E-value: 8.04e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 55 SSPQQYMEMHKRSMDDPAAFWSDIASEF-YWkQKWGDQVFSENldvrkgPISIEWFKGGITNICYNCLDKNVEAGLG-DK 132
Cdd:PTZ00237 5 SDPFDYENDSNYANSNPESFWDEVAKKYvHW-DKMYDKVYSGD------EIYPDWFKGGELNTCYNVLDIHVKNPLKrDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 133 TAIHWEGNELGVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLA 212
Cdd:PTZ00237 78 DALIYECPYLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 213 QRIVDCKPNVILTCNAVKRGPKTI----NLKA-------------------IVDAALDQSSKDGVSVGICLTYDNSLATT 269
Cdd:PTZ00237 158 DRIETITPKLIITTNYGILNDEIItftpNLKEaielstfkpsnvitlfrndITSESDLKKIETIPTIPNTLSWYDEIKKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 270 RENTkwqngrdvwwQDVISQYPTscevewVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMIYTATTFKYAFDYKSTDVYWC 349
Cdd:PTZ00237 238 KENN----------QSPFYEYVP------VESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 350 TADCGWITGHSYVtYGPMLNGATVVVFEGA----PNYPDpgRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSR-- 423
Cdd:PTZ00237 302 HSSIGWVSFHGFL-YGSLSLGNTFVMFEGGiiknKHIED--DLWNTIEKHKVTHTLTLPKTIRYLIKTDPEATIIRSKyd 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 424 -KSLRVLGSVGEPINPSAWRWFFNVVgdsRCPISDTWWQTETGgfmITPLPG-AWPQKPGSAT-FPFFGVQPVIVDEKGN 500
Cdd:PTZ00237 379 lSNLKEIWCGGEVIEESIPEYIENKL---KIKSSRGYGQTEIG---ITYLYCyGHINIPYNATgVPSIFIKPSILSEDGK 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 501 EIEGECSGYLCVKGSWPGAFRTLFGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVES 580
Cdd:PTZ00237 453 ELNVNEIGEVAFKLPMPPSFATTFYKNDEKFKQLFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIET 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 581 ALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSE----ELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKI 656
Cdd:PTZ00237 533 SILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQSidlnKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKI 612
|
....*..
gi 332006737 657 MRRILRK 663
Cdd:PTZ00237 613 PRQIISK 619
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
60-691 |
2.68e-79 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 265.89 E-value: 2.68e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 60 YMEMHKRSMDDPAAFWSDIASEFYWKQKWGDQVFsenLDVRKGPISiEWFKGGITNICYNCLdknvEAGLGDKTAIHWEG 139
Cdd:PRK03584 36 YAALWRWSVEDLEAFWQSVWDFFGVIGSTPYTVV---LAGRRMPGA-RWFPGARLNYAENLL----RHRRDDRPAIIFRG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 140 nELGVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCK 219
Cdd:PRK03584 108 -EDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQGVLDRFGQIE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 220 PNVILTCNAVKRGPKTINLKAIVDAALDQ--SSKDGVSVgiclTYDNSLATTRENTKWQNgrdvwWQDVISQYPTS-CEV 296
Cdd:PRK03584 187 PKVLIAVDGYRYGGKAFDRRAKVAELRAAlpSLEHVVVV----PYLGPAAAAAALPGALL-----WEDFLAPAEAAeLEF 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 297 EWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMIYTATTFKYAFDYKSTDVY-WCTAdCGWITGHSYVtyGPMLNGATVVV 375
Cdd:PRK03584 258 EPVPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDRFfWYTT-CGWMMWNWLV--SGLLVGATLVL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 376 FEGAPNYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGdsrcpi 455
Cdd:PRK03584 335 YDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPLPPEGFDWVYEHVK------ 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 456 SDTWWQTETGGfmiTPLPGAW-------PQKPGSATFPFFGVQPVIVDEKGNEIEGEcSGYLCVKGSWPgAFRTLF---G 525
Cdd:PRK03584 409 ADVWLASISGG---TDICSCFvggnpllPVYRGEIQCRGLGMAVEAWDEDGRPVVGE-VGELVCTKPFP-SMPLGFwndP 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 526 DHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGI 605
Cdd:PRK03584 484 DGSRYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRM 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 606 YAFVTLLEGVPYSEELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIM----RRILRKiasRQLEELGDTSTLADP 681
Cdd:PRK03584 564 PLFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVelpvKKLLHG---RPVKKAVNRDALANP 640
|
650
....*....|
gi 332006737 682 SVVDQLIALA 691
Cdd:PRK03584 641 EALDWFADLA 650
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
148-663 |
2.99e-79 |
|
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: 259.37 E-value: 2.99e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 148 LTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVILtCN 227
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVV-TD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 228 AVKRgpktinlkaivdAALDqsskdgvsvgicltydnslattrentkwqngrdvwwqdvisqyptscevewvdaEDPLFL 307
Cdd:cd05973 80 AANR------------HKLD------------------------------------------------------SDPFVM 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 308 LYTSGSTGKPKGVLHTT------GGYMiytattfKYAFDYKSTDVYWCTADCGWITGHSYVTYGPMLNGATVVVFEGAPN 381
Cdd:cd05973 94 MFTSGTTGLPKGVPVPLralaafGAYL-------RDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGFS 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 382 YPDpgrCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRhSRKSLRVLGSVGEPINPSAWRWFFNVVGdsrCPISDTWWQ 461
Cdd:cd05973 167 VES---TWRVIERLGVTNLAGSPTAYRLLMAAGAEVPAR-PKGRLRRVSSAGEPLTPEVIRWFDAALG---VPIHDHYGQ 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 462 TETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGS-----WpgafrtlFGDHERYETTyfK 536
Cdd:cd05973 240 TELGMVLANHHALEHPVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIDIAnsplmW-------FRGYQLPDTP--A 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 537 PFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVP 616
Cdd:cd05973 311 IDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHE 390
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 332006737 617 YSEELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRK 663
Cdd:cd05973 391 GTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
149-662 |
4.98e-75 |
|
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: 248.50 E-value: 4.98e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 149 TYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVILTcna 228
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 229 vkrgpktinlkaivdaaldqsskDGvsvgicltydnslattrentkwqngrdvwwqdvisqyptscevewvdAEDPLFLL 308
Cdd:cd05971 85 -----------------------DG-----------------------------------------------SDDPALII 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 309 YTSGSTGKPKGVLHTTGgYMIYTATTFKYAFDY--KSTDVYWCTADCGWITGHSYVTYGPMLNGATVVVFEGAPNypDPG 386
Cdd:cd05971 95 YTSGTTGPPKGALHAHR-VLLGHLPGVQFPFNLfpRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKF--DPK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 387 RCWDIVDKYKVSIFYTAPTLVRsLMRDDDKfVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDsrcPISDTWWQTEtGG 466
Cdd:cd05971 172 AALDLMSRYGVTTAFLPPTALK-MMRQQGE-QLKHAQVKLRAIATGGESLGEELLGWAREQFGV---EVNEFYGQTE-CN 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 467 FMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGSWPGAFRTLFGDHERYEttyfKPFAGYYF-SG 545
Cdd:cd05971 246 LVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDPVAFLGYWNNPSATE----KKMAGDWLlTG 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 546 DGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEELRKSL 625
Cdd:cd05971 322 DLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALAREI 401
|
490 500 510
....*....|....*....|....*....|....*..
gi 332006737 626 VLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILR 662
Cdd:cd05971 402 QELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
121-662 |
1.00e-67 |
|
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: 230.72 E-value: 1.00e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 121 LDKNVEAGLGDKTAIhwegneLGVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHS 200
Cdd:cd05959 9 VDLNLNEGRGDKTAF------IDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 201 VVFAGFSADSLAQRIVDCKPNVILTCNAvkrgpktinLKAIVDAALDQSSKDGVSVGICltydnslattreNTKWQNGRD 280
Cdd:cd05959 83 PVNTLLTPDDYAYYLEDSRARVVVVSGE---------LAPVLAAALTKSEHTLVVLIVS------------GGAGPEAGA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 281 VWWQDVISQYPTSCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGyMIYTATTF-KYAFDYKSTDVYWCTADCGWITGH 359
Cdd:cd05959 142 LLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHAD-IYWTAELYaRNVLGIREDDVCFSAAKLFFAYGL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 360 SYVTYGPMLNGATVVVFegaPNYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDkfVTRHSRKSLRVLGSVGEPINPS 439
Cdd:cd05959 221 GNSLTFPLSVGATTVLM---PERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPN--LPSRDLSSLRLCVSAGEALPAE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 440 AWRWFFNVVGdsrCPISDTWWQTETGGFMITPLPGAwpQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGSwpga 519
Cdd:cd05959 296 VGERWKARFG---LDILDGIGSTEMLHIFLSNRPGR--VRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGP---- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 520 fRTLFGDHERYETTYfKPFAGYYF-SGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEH 598
Cdd:cd05959 367 -SSATMYWNNRDKTR-DTFQGEWTrTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVED 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332006737 599 EVKGQGIYAFVTLLEGVPYSEELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILR 662
Cdd:cd05959 445 EDGLTKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
131-662 |
9.13e-66 |
|
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: 226.22 E-value: 9.13e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 131 DKTAIHWeGNELGVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADS 210
Cdd:cd05970 32 DKLALVW-CDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 211 LAQRIVDCKPNVILtCNAVKRGPKTINlKAIVDAALDQ---SSKDGVSVGIClTYDNSLATTREntkwqngrdvwwqdvI 287
Cdd:cd05970 111 IVYRIESADIKMIV-AIAEDNIPEEIE-KAAPECPSKPklvWVGDPVPEGWI-DFRKLIKNASP---------------D 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 288 SQYPTSCEveWVDAEDPLFLLYTSGSTGKPKGVLHTTGgYMIYTATTFKYAFDYKSTDVYWCTADCGWITGHSYVTYGPM 367
Cdd:cd05970 173 FERPTANS--YPCGEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWGKIYGQW 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 368 LNGATVVVFEGapNYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDdkfVTRHSRKSLRVLGSVGEPINPSAWRWFFNV 447
Cdd:cd05970 250 IAGAAVFVYDY--DKFDPKALLEKLSKYGVTTFCAPPTIYRFLIRED---LSRYDLSSLRYCTTAGEALNPEVFNTFKEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 448 VGDSrcpISDTWWQTETGgFMITPLPGAWPqKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCV---KGSWPGAFRTLF 524
Cdd:cd05970 325 TGIK---LMEGFGQTETT-LTIATFPWMEP-KPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtsKGKPVGLFGGYY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 525 GDHERYETTYFKpfaGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQG 604
Cdd:cd05970 400 KDAEKTAEVWHD---GYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQV 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 332006737 605 IYAFVTLLEGVPYSEELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILR 662
Cdd:cd05970 477 VKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
121-662 |
4.17e-63 |
|
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: 217.43 E-value: 4.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 121 LDKNVeAGLGDKTAIHWEGnelgvdASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVhs 200
Cdd:cd05936 5 LEEAA-RRFPDKTALIFMG------RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAV-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 201 VVfagfsadslaqrivdckP-NVILTcnavkrgpkTINLKAIVDaaldqssKDGVSVGICltydnslattrentkwqngr 279
Cdd:cd05936 76 VV-----------------PlNPLYT---------PRELEHILN-------DSGAKALIV-------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 280 DVWWQDVISQYPTSCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGG-YMIYTATTFKYAFDYKSTDVYWCTADCgwitg 358
Cdd:cd05936 103 AVSFTDLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNlVANALQIKAWLEDLLEGDDVVLAALPL----- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 359 hsYVTYG-------PMLNGATVVVFegaPNyPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDkfVTRHSRKSLRVLGS 431
Cdd:cd05936 178 --FHVFGltvalllPLALGATIVLI---PR-FRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPE--FKKRDFSSLRLCIS 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 432 VGEPINPSAWRWFFNVVGdsrCPISDTWWQTETGgfmitPL----PGAWPQKPGSATFPFFGVQPVIVDEKGNEIE-GEc 506
Cdd:cd05936 250 GGAPLPVEVAERFEELTG---VPIVEGYGLTETS-----PVvavnPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPpGE- 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 507 SGYLCVKGswPGAFRTLFGDHERYETTyFKpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHP 586
Cdd:cd05936 321 VGELWVRG--PQVMKGYWNRPEETAEA-FV--DGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHP 395
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332006737 587 QCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEElrkSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILR 662
Cdd:cd05936 396 AVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEE---EIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
118-662 |
1.00e-62 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 217.75 E-value: 1.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 118 YNCLDKNVEAgLGDKTAIHWEGNELgvdaslTYSELLQRVCQLANYLKDNGVKKGDAVVIYL---PMLMElpiAMLACAR 194
Cdd:PRK06187 9 GRILRHGARK-HPDKEAVYFDGRRT------TYAELDERVNRLANALRALGVKKGDRVAVFDwnsHEYLE---AYFAVPK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 195 IGAV-HSV-VFagFSADSLAQRIVDCKPNVILTcnavkrGPKTINLKAIVDAALDqsskdgvSVGICLTYDnslATTREN 272
Cdd:PRK06187 79 IGAVlHPInIR--LKPEEIAYILNDAEDRVVLV------DSEFVPLLAAILPQLP-------TVRTVIVEG---DGPAAP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 273 TKWQNGRdvwWQDVIS-QYPTSCEVEwVDAEDPLFLLYTSGSTGKPKGVLHT----TGGYMIYTAttfkyAFDYKSTDVY 347
Cdd:PRK06187 141 LAPEVGE---YEELLAaASDTFDFPD-IDENDAAAMLYTSGTTGHPKGVVLShrnlFLHSLAVCA-----WLKLSRDDVY 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 348 -----------WctadcGWitghsyvTYGPMLNGATVVvfegapnYP---DPGRCWDIVDKYKVSIFYTAPTLVRSLMRD 413
Cdd:PRK06187 212 lvivpmfhvhaW-----GL-------PYLALMAGAKQV-------IPrrfDPENLLDLIETERVTFFFAVPTIWQMLLKA 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 414 ddKFVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGdsrCPISDTWWQTETGGFM-ITPL----PGAWPqKPGSATFPFF 488
Cdd:PRK06187 273 --PRAYFVDFSSLRLVIYGGAALPPALLREFKEKFG---IDLVQGYGMTETSPVVsVLPPedqlPGQWT-KRRSAGRPLP 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 489 GVQPVIVDEKGNEIE--GECSGYLCVKGSWpgafRTL--FGDHERYETTYFKpfaGYYFSGDGCSRDKDGYYWLTGRVDD 564
Cdd:PRK06187 347 GVEARIVDDDGDELPpdGGEVGEIIVRGPW----LMQgyWNRPEATAETIDG---GWLHTGDVGYIDEDGYLYITDRIKD 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 565 VINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSE-ELRKSLvlmvRNQIGAFAAPDRIH 643
Cdd:PRK06187 420 VIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAkELRAFL----RGRLAKFKLPKRIA 495
|
570
....*....|....*....
gi 332006737 644 WAPGLPKTRSGKIMRRILR 662
Cdd:PRK06187 496 FVDELPRTSVGKILKRVLR 514
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
130-658 |
1.65e-62 |
|
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: 214.78 E-value: 1.65e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 130 GDKTAIHWEGNelgvdaSLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAD 209
Cdd:cd17631 9 PDRTALVFGGR------SLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 210 SLAQRIVDCKPNVILtcnavkrgpktinlkaivdaaldqsskdgvsvgicltydnslattrentkwqngrdvwwqdvisq 289
Cdd:cd17631 83 EVAYILADSGAKVLF----------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 290 yptscevewvdaEDPLFLLYTSGSTGKPKGVLHTTGGYMIYTATTFkYAFDYKSTDVYWCTADCGWITGHSYVTYGPMLN 369
Cdd:cd17631 98 ------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNAL-AALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLR 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 370 GATVVVFEGapnyPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSrkSLRVLGSVGEPINPSAWRWF--FNV 447
Cdd:cd17631 165 GGTVVILRK----FDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLS--SLRAVIYGGAPMPERLLRALqaRGV 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 448 VgdsrcpISDTWWQTETGGfMITPLPGAWPQ-KPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGswPGAFRTLFGD 526
Cdd:cd17631 239 K------FVQGYGMTETSP-GVTFLSPEDHRrKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRG--PHVMAGYWNR 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 527 HERYETTYFKpfaGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIY 606
Cdd:cd17631 310 PEATAAAFRD---GWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVV 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 332006737 607 AFVTLLEGVPYSEElrkSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMR 658
Cdd:cd17631 387 AVVVPRPGAELDED---ELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
145-662 |
1.04e-61 |
|
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: 212.71 E-value: 1.04e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 145 DASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVIL 224
Cdd:cd05919 8 DRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 225 TcnavkrgpktinlkaivdaaldqsskdgvsvgicltydnslattrentkwqngrdvwwqdvisqyptscevewvDAEDP 304
Cdd:cd05919 88 T--------------------------------------------------------------------------SADDI 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 305 LFLLYTSGSTGKPKGVLHTTGGYMIYTATTFKYAFDYKSTDVYWCTADC--GWITGHSyvTYGPMLNGATVVVFEGAPny 382
Cdd:cd05919 94 AYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNS--LWFPLAVGASAVLNPGWP-- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 383 pDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDkfVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGdsrCPISDTWWQT 462
Cdd:cd05919 170 -TAERVLATLARFRPTVLYGVPTFYANLLDSCA--GSPDALRSLRLCVSAGEALPRGLGERWMEHFG---GPILDGIGAT 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 463 ETGGFMITPLPGAWpqKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGswPGAFRTLFGDHERYETTYFkpfAGYY 542
Cdd:cd05919 244 EVGHIFLSNRPGAW--RLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRG--PSAAVGYWNNPEKSRATFN---GGWY 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 543 FSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEELR 622
Cdd:cd05919 317 RTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLA 396
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 332006737 623 KSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILR 662
Cdd:cd05919 397 RDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
131-663 |
7.23e-61 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 212.87 E-value: 7.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 131 DKTAIHWEgnelgvDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADS 210
Cdd:PRK08316 26 DKTALVFG------DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 211 LAQRIVDCKPNVILTCNAvkrgpktinLKAIVDAALDQSSKDGVsvgiclTYDNSLATTRENTKWQNGRDvwWQDviSQY 290
Cdd:PRK08316 100 LAYILDHSGARAFLVDPA---------LAPTAEAALALLPVDTL------ILSLVLGGREAPGGWLDFAD--WAE--AGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 291 PTSCEVEwVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMI-YTATTFkyAFDYKSTDV-------YWCTAdcgwitghSYV 362
Cdd:PRK08316 161 VAEPDVE-LADDDLAQILYTSGTESLPKGAMLTHRALIAeYVSCIV--AGDMSADDIplhalplYHCAQ--------LDV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 363 TYGPMLN-GATVVVFEGapnyPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDkFVTRHSRkSLR------------VL 429
Cdd:PRK08316 230 FLGPYLYvGATNVILDA----PDPELILRTIEAERITSFFAPPTVWISLLRHPD-FDTRDLS-SLRkgyygasimpveVL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 430 GSVGEPInPSAWrwFFNVVGdsrcpisdtwwQTEtggfmITPL-----PGAWPQKPGSATFPFFGVQPVIVDEKGNEI-E 503
Cdd:PRK08316 304 KELRERL-PGLR--FYNCYG-----------QTE-----IAPLatvlgPEEHLRRPGSAGRPVLNVETRVVDDDGNDVaP 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 504 GE-----------CSGYlcvkgswpgafrtlFGDHERYETTyfkpFAGYYF-SGDGCSRDKDGYYWLTGRVDDVINVSGH 571
Cdd:PRK08316 365 GEvgeivhrspqlMLGY--------------WDDPEKTAEA----FRGGWFhSGDLGVMDEEGYITVVDRKKDMIKTGGE 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 572 RIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEElrkSLVLMVRNQIGAFAAPDRIHWAPGLPKT 651
Cdd:PRK08316 427 NVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTED---ELIAHCRARLAGFKVPKRVIFVDELPRN 503
|
570
....*....|..
gi 332006737 652 RSGKIMRRILRK 663
Cdd:PRK08316 504 PSGKILKRELRE 515
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
137-663 |
1.24e-58 |
|
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: 206.93 E-value: 1.24e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 137 WEGNELGVDASLTYSELLQRVCQLANYLKDN-GVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRI 215
Cdd:cd05928 31 WWVNGKGDEVKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 216 VDCKPNVILTCNAvkrgpktinLKAIVDAALDQsskdgvsvgiCLTYDNSLATTrentkwQNGRDVW--WQDVISQYPTS 293
Cdd:cd05928 111 QASKAKCIVTSDE---------LAPEVDSVASE----------CPSLKTKLLVS------EKSRDGWlnFKELLNEASTE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 294 CEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMIYTATTFKYAFDYKSTDVYWCTADCGWITGHSYVTYGPMLNGATV 373
Cdd:cd05928 166 HHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGACV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 374 VVFEgAPNYpDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDdkfVTRHSRKSLRVLGSVGEPINPSA---WRwffNVVGd 450
Cdd:cd05928 246 FVHH-LPRF-DPLVILKTLSSYPITTFCGAPTVYRMLVQQD---LSSYKFPSLQHCVTGGEPLNPEVlekWK---AQTG- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 451 srCPISDTWWQTETGgfMITPLPGAWPQKPGS--ATFPFFGVQpvIVDEKGNEI----EGECSgyLCVKGSWP-GAFRTL 523
Cdd:cd05928 317 --LDIYEGYGQTETG--LICANFKGMKIKPGSmgKASPPYDVQ--IIDDNGNVLppgtEGDIG--IRVKPIRPfGLFSGY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 524 FGDHERYETTYFKPFagyYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQ 603
Cdd:cd05928 389 VDNPEKTAATIRGDF---YLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGE 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332006737 604 GIYAFVTLleGVPYS----EELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRK 663
Cdd:cd05928 466 VVKAFVVL--APQFLshdpEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
144-657 |
5.79e-54 |
|
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: 192.81 E-value: 5.79e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 144 VDA----SLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCK 219
Cdd:cd05911 3 IDAdtgkELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 220 PNVILTCNAVkrgpktinlkaiVDAALDQSSKDGVSVGICLTYDNSLATTRENTKWQ--NGRDVWWQDVISQyptsceve 297
Cdd:cd05911 83 PKVIFTDPDG------------LEKVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLSptLGEEDEDLPPPLK-------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 298 wVDAEDPLFLLYTSGSTGKPKGVL--HTTGGYMIYTATTFKYAfDYKSTDVYWCTADCGWITG-HSYVTYgpMLNGATVV 374
Cdd:cd05911 143 -DGKDDTAAILYSSGTTGLPKGVClsHRNLIANLSQVQTFLYG-NDGSNDVILGFLPLYHIYGlFTTLAS--LLNGATVI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 375 VFegapNYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDkfVTRHSRKSLRVLGSVGEPInpsaWRWFFNVVG--DSR 452
Cdd:cd05911 219 IM----PKFDSELFLDLIEKYKITFLYLVPPIAAALAKSPL--LDKYDLSSLRVILSGGAPL----SKELQELLAkrFPN 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 453 CPISDTWWQTETGGfMITPLPGaWPQKPGSATFPFFGVQPVIVDEKGNEIEGECS-GYLCVKGswPGAFRTLFGDHERYE 531
Cdd:cd05911 289 ATIKQGYGMTETGG-ILTVNPD-GDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEpGEICVRG--PQVMKGYYNNPEATK 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 532 TTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTL 611
Cdd:cd05911 365 ETFDE--DGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVR 442
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 332006737 612 LEGvpySEELRKSLVLMVRNQIGAFAA-PDRIHWAPGLPKTRSGKIM 657
Cdd:cd05911 443 KPG---EKLTEKEVKDYVAKKVASYKQlRGGVVFVDEIPKSASGKIL 486
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
121-663 |
2.44e-52 |
|
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: 188.89 E-value: 2.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 121 LDKNVEAGLGDKTAIhwegnelgVD--ASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAV 198
Cdd:TIGR02262 10 LDRNVVEGRGGKTAF--------IDdiSSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 199 HSVVFAGFSADSLAQRIVDCKPNVILTCN--------AVKRGPktiNLKAIVDAALDQSSKDGVSvgicltydNSLATTr 270
Cdd:TIGR02262 82 PVALNTLLTADDYAYMLEDSRARVVFVSGallpvikaALGKSP---HLEHRVVVGRPEAGEVQLA--------ELLATE- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 271 entkwqngrdvwwQDVISQYPTScevewvdAEDPLFLLYTSGSTGKPKGVLHTTGGyMIYTATTF-KYAFDYKSTDVYWC 349
Cdd:TIGR02262 150 -------------SEQFKPAATQ-------ADDPAFWLYSSGSTGMPKGVVHTHSN-PYWTAELYaRNTLGIREDDVCFS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 350 TADCGWITGHSYVTYGPMLNGATVVVFegaPNYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDkfVTRHSRKSLRVL 429
Cdd:TIGR02262 209 AAKLFFAYGLGNALTFPMSVGATTVLM---GERPTPDAVFDRLRRHQPTIFYGVPTLYAAMLADPN--LPSEDQVRLRLC 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 430 GSVGEPINPSA---WRWFFNVvgdsrcPISDTWWQTETGGFMITPLPGAwpQKPGSATFPFFGVQPVIVDEKGNEIEGEC 506
Cdd:TIGR02262 284 TSAGEALPAEVgqrWQARFGV------DIVDGIGSTEMLHIFLSNLPGD--VRYGTSGKPVPGYRLRLVGDGGQDVADGE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 507 SGYLCVKGswPGAFRTLFGDHERYETTYFKPFAGyyfSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHP 586
Cdd:TIGR02262 356 PGELLISG--PSSATMYWNNRAKSRDTFQGEWTR---SGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHP 430
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332006737 587 QCAEAAVVGIEHEVKGQGIYAFVTLLEGvpySEELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRK 663
Cdd:TIGR02262 431 AVLEAAVVGVADEDGLIKPKAFVVLRPG---QTALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
145-663 |
1.11e-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: 186.75 E-value: 1.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 145 DASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVIL 224
Cdd:cd05926 12 TPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 225 TCN-----AVKRGPKTinLKAIVDAALDqsskdgvsVGICLTYD--NSLATTRENTKWQNGRDVwwqdvisqyptsceve 297
Cdd:cd05926 92 TPKgelgpASRAASKL--GLAILELALD--------VGVLIRAPsaESLSNLLADKKNAKSEGV---------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 298 wVDAEDPLFLLYTSGSTGKPKGVLHTTGgyMIYTATTfKYAFDYKSTDvywctADCGWIT-----GHSYVT--YGPMLNG 370
Cdd:cd05926 146 -PLPDDLALILHTSGTTGRPKGVPLTHR--NLAASAT-NITNTYKLTP-----DDRTLVVmplfhVHGLVAslLSTLAAG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 371 ATVVVfegaPNYPDPGRCWDIVDKYKVSiFYTA-PTLVRSLMRDDDKfVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVG 449
Cdd:cd05926 217 GSVVL----PPRFSASTFWPDVRDYNAT-WYTAvPTIHQILLNRPEP-NPESPPPKLRFIRSCSASLPPAVLEALEATFG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 450 dsrCPISDTWWQTETGGFMIT-PLPGAwPQKPGSATFPFfGVQPVIVDEKGNEIEGECSGYLCVKGswPGAFRTLFGDHE 528
Cdd:cd05926 291 ---APVLEAYGMTEAAHQMTSnPLPPG-PRKPGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRG--PNVTRGYLNNPE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 529 RYETTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAF 608
Cdd:cd05926 364 ANAEAAFK--DGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAA 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 332006737 609 VTLLEGVPYS-EELRKSLvlmvRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRK 663
Cdd:cd05926 442 VVLREGASVTeEELRAFC----RKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
148-665 |
1.33e-51 |
|
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: 185.08 E-value: 1.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 148 LTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRivdckpnviltcn 227
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDR------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 228 aVKRGPKTInlkAIVDaaldqsskdgvsvgicltydnslattrENTKwqngrdvwwqdvisqyptscevewvdAEDPLFL 307
Cdd:cd05974 68 -VDRGGAVY---AAVD---------------------------ENTH--------------------------ADDPMLL 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 308 LYTSGSTGKPKGVLHTTGGYMIYTATTFkYAFDYKSTDVYWCTADCGWiTGHSYVT-YGPMLNGATVVVFegapNYP--D 384
Cdd:cd05974 91 YFTSGTTSKPKLVEHTHRSYPVGHLSTM-YWIGLKPGDVHWNISSPGW-AKHAWSCfFAPWNAGATVFLF----NYArfD 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 385 PGRCWDIVDKYKVSIFYTAPTLVRSLMRDDdkfVTRhSRKSLRVLGSVGEPINPSAWRWFFNVVGDSrcpISDTWWQTET 464
Cdd:cd05974 165 AKRVLAALVRYGVTTLCAPPTVWRMLIQQD---LAS-FDVKLREVVGAGEPLNPEVIEQVRRAWGLT---IRDGYGQTET 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 465 GGfMITPLPGAwPQKPGSATFPFFGVQPVIVDEKGNEI-EGECSgyLCVKGSWP-GAFRTLFGDHERyetTYFKPFAGYY 542
Cdd:cd05974 238 TA-LVGNSPGQ-PVKAGSMGRPLPGYRVALLDPDGAPAtEGEVA--LDLGDTRPvGLMKGYAGDPDK---TAHAMRGGYY 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 543 FSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEELR 622
Cdd:cd05974 311 RTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETA 390
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 332006737 623 KSLVLMVRNQIGAFAAPDRIHWAPgLPKTRSGKIMRRILRKIA 665
Cdd:cd05974 391 LEIFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRRRE 432
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
149-662 |
5.14e-51 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 182.88 E-value: 5.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 149 TYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVILTcna 228
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 229 vkrgpktinlkaivdaaldqsskdgvsvgicltydnslattrentkwqngrdvwwqdvisqyptscevewvdaeDPLFLL 308
Cdd:cd05934 82 --------------------------------------------------------------------------DPASIL 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 309 YTSGSTGKPKGVLhTTGGYMIYTATTFKYAFDYKSTDVYWCTADCGWITGHSYVTYGPMLNGATVVVfegAPNYpDPGRC 388
Cdd:cd05934 88 YTSGTTGPPKGVV-ITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVL---LPRF-SASRF 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 389 WDIVDKYKVSIFYTAPTLVRSLM----RDDDkfvtRHSRksLRVLGsvGEPINPSAWRWFFNVVGdsrCPISDTWWQTET 464
Cdd:cd05934 163 WSDVRRYGATVTNYLGAMLSYLLaqppSPDD----RAHR--LRAAY--GAPNPPELHEEFEERFG---VRLLEGYGMTET 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 465 GGFMITPLPGawPQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGSWP-GAFRTLFGDHERYEttyfKPFA-GYY 542
Cdd:cd05934 232 IVGVIGPRDE--PRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRGLRGwGFFKGYYNMPEATA----EAMRnGWF 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 543 FSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEElr 622
Cdd:cd05934 306 HTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPE-- 383
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 332006737 623 kSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILR 662
Cdd:cd05934 384 -ELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
145-662 |
3.22e-49 |
|
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: 178.44 E-value: 3.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 145 DASLTYSELLQRVCQLANYLKDNGV-KKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVI 223
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGiVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 224 LTCNAVkrgpktinlkaivdaaldqsskdgvsvgicltydnslaTTREntkwqngrdvwwqdvisqyptscevewvdaeD 303
Cdd:cd05958 88 LCAHAL--------------------------------------TASD-------------------------------D 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 304 PLFLLYTSGSTGKPKGVLHTTGGYMIYTATTFKYAFDYKSTDVYWCTADCGWITGHSYVTYGPMLNGATVVVFEGApnyp 383
Cdd:cd05958 99 ICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEA---- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 384 DPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKfvTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGdsrCPISDTWWQTE 463
Cdd:cd05958 175 TPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDA--AGPDLSSLRKCVSAGEALPAALHRAWKEATG---IPIIDGIGSTE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 464 TGGFMITPLPGAwpQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGswPGAFRTLFGDHERyetTYFKpfAGYYF 543
Cdd:cd05958 250 MFHIFISARPGD--ARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRG--PTGCRYLADKRQR---TYVQ--GGWNI 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 544 SGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEELRK 623
Cdd:cd05958 321 TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLAR 400
|
490 500 510
....*....|....*....|....*....|....*....
gi 332006737 624 SLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILR 662
Cdd:cd05958 401 ELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
131-659 |
1.28e-48 |
|
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: 176.95 E-value: 1.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 131 DKTAIHWEGNelgvdaSLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADS 210
Cdd:cd05930 2 DAVAVVDGDQ------SLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 211 LAQRIVDCKPNVILTcnavkrgpktinlkaivdaaldqsskdgvsvgicltydnslattrentkwqngrdvwwqdvisqy 290
Cdd:cd05930 76 LAYILEDSGAKLVLT----------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 291 ptscevewvDAEDPLFLLYTSGSTGKPKGVLHTTGGYMIYTATtFKYAFDYKSTDVYWCTADCGWItGHSYVTYGPMLNG 370
Cdd:cd05930 91 ---------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW-MQEAYPLTPGDRVLQFTSFSFD-VSVWEIFGALLAG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 371 ATVVVfegAPN--YPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVtrhsRKSLRVLGSVGEPINPSAWR-WF--- 444
Cdd:cd05930 160 ATLVV---LPEevRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAA----LPSLRLVLVGGEALPPDLVRrWRell 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 445 -----FNVVGDSRCPISDTWWQTETGGFMITPLP-GAwpqkpgsatfPFFGVQPVIVDEKGNE----IEGEcsgyLCVKG 514
Cdd:cd05930 233 pgarlVNLYGPTEATVDATYYRVPPDDEEDGRVPiGR----------PIPNTRVYVLDENLRPvppgVPGE----LYIGG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 515 swPGAFRtlfGDHERYETTYFK----PFAG---YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQ 587
Cdd:cd05930 299 --AGLAR---GYLNRPELTAERfvpnPFGPgerMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPG 373
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332006737 588 CAEAAVVGIEHEVKGQGIYAFVTLLEGVPYS-EELRKSLvlmvRNQIGAFAAPDRIHWAPGLPKTRSGKIMRR 659
Cdd:cd05930 374 VREAAVVAREDGDGEKRLVAYVVPDEGGELDeEELRAHL----AERLPDYMVPSAFVVLDALPLTPNGKVDRK 442
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
147-663 |
4.18e-47 |
|
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: 172.57 E-value: 4.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 147 SLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVILTc 226
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 227 navkrgpktinlkaivdaaldqsskdgvsvgicltydnslattrentkwqngRDVWWQDVISQYPtscevewvdaEDPLF 306
Cdd:cd05903 80 ----------------------------------------------------PERFRQFDPAAMP----------DAVAL 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 307 LLYTSGSTGKPKGVLHTTGGYMiytATTFKYAFDYKST--DVYWCTADCGWITGHSYVTYGPMLNGATVVVFEGApnypD 384
Cdd:cd05903 98 LLFTSGTTGEPKGVMHSHNTLS---ASIRQYAERLGLGpgDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIW----D 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 385 PGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRksLRVLGSVGEPINPSAWRWFFNVVGDSRCPIsdtWWQTET 464
Cdd:cd05903 171 PDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSR--LRTFVCGGATVPRSLARRAAELLGAKVCSA---YGSTEC 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 465 GGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGswPGAFrtlFGDHERYETTYFKPFAGYYFS 544
Cdd:cd05903 246 PGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRG--PSVF---LGYLDRPDLTADAAPEGWFRT 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 545 GDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEG-VPYSEELRK 623
Cdd:cd05903 321 GDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGaLLTFDELVA 400
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 332006737 624 SLvlmVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRK 663
Cdd:cd05903 401 YL---DRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
129-663 |
2.69e-43 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 163.54 E-value: 2.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 129 LGDKTAIHWEGNelgvdaSLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSA 208
Cdd:PRK07656 18 FGDKEAYVFGDQ------RLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 209 DSLAQRIVDCKPNVILTCNAVkrgpktinlkaivdAALDQSSKDGV----SVGICLTYDNSLATTRENTkwqngrdvwWQ 284
Cdd:PRK07656 92 DEAAYILARGDAKALFVLGLF--------------LGVDYSATTRLpaleHVVICETEEDDPHTEKMKT---------FT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 285 DVISQYPTSCEVEWVDAEDPLFLLYTSGSTGKPKGVLhTTGGYMIYTATTFKYAFDYKSTDVYWC----------TAdcG 354
Cdd:PRK07656 149 DFLAAGDPAERAPEVDPDDVADILFTSGTTGRPKGAM-LTHRQLLSNAADWAEYLGLTEGDRYLAanpffhvfgyKA--G 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 355 WITghsyvtygPMLNGATVV---VFegapnypDPGRCWDIVDKYKVSIFYTAPTLVRSL----MRDDDKFvtrhsrKSLR 427
Cdd:PRK07656 226 VNA--------PLMRGATILplpVF-------DPDEVFRLIETERITVLPGPPTMYNSLlqhpDRSAEDL------SSLR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 428 VLGSVGEPINPSAWRWF---FNVVgdsrcPISDTWWQTETGGFM-ITPLPGAWPQKPGSATFPFFGVQPVIVDEKGNEIE 503
Cdd:PRK07656 285 LAVTGAASMPVALLERFeseLGVD-----IVLTGYGLSEASGVTtFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVP 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 504 GECSGYLCVKGswPGAFRTLFGDHEryETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALV 583
Cdd:PRK07656 360 VGEVGELLVRG--PNVMKGYYDDPE--ATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLY 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 584 LHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEElrkSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRK 663
Cdd:PRK07656 436 EHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEE---ELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
130-665 |
7.36e-43 |
|
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: 162.62 E-value: 7.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 130 GDKTAIhwegneLGVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAV-------H--- 199
Cdd:COG1021 39 PDRIAV------VDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIpvfalpaHrra 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 200 ----------------SVVFAGFSADSLAQRIVDCKPnviltcnavkrGPKTInlkaIVDAaldqSSKDGVSvgicltyd 263
Cdd:COG1021 113 eishfaeqseavayiiPDRHRGFDYRALARELQAEVP-----------SLRHV----LVVG----DAGEFTS-------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 264 nslattrentkwqngrdvwWQDVISQyPTSCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYmIYTATTFKYAFDYKS 343
Cdd:COG1021 166 -------------------LDALLAA-PADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDY-LYSVRASAEICGLDA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 344 TDVYWCTADcgwiTGHSY-----VTYGPMLNGATVVVfegAPNyPDPGRCWDIVDKYKVSIfyTA--PTLVRSLMRDDDK 416
Cdd:COG1021 225 DTVYLAALP----AAHNFplsspGVLGVLYAGGTVVL---APD-PSPDTAFPLIERERVTV--TAlvPPLALLWLDAAER 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 417 fvTRHSRKSLRVLGSVGEPINPSAWR--------WFFNVVG------------DSR--------CPIS--DTWWqtetgg 466
Cdd:COG1021 295 --SRYDLSSLRVLQVGGAKLSPELARrvrpalgcTLQQVFGmaeglvnytrldDPEevilttqgRPISpdDEVR------ 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 467 fmitplpgawpqkpgsatfpffgvqpvIVDEKGNEI-EGECsGYLCVKGswPGAFRTLFGDHErYETTYFKPfAGYYFSG 545
Cdd:COG1021 367 ---------------------------IVDEDGNPVpPGEV-GELLTRG--PYTIRGYYRAPE-HNARAFTP-DGFYRTG 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 546 DGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEELRKSL 625
Cdd:COG1021 415 DLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRGEPLTLAELRRFL 494
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 332006737 626 vlmvRNQ-IGAFAAPDRIHWAPGLPKTRSGKIMRRILRKIA 665
Cdd:COG1021 495 ----RERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRAAL 531
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
149-593 |
4.27e-42 |
|
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: 157.81 E-value: 4.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 149 TYSELLQRVCQLANYLKDN-GVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVILTcn 227
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 228 avkrgpktinlkaivDAALDQSSKDGVSVGICLTYDNSLATTRENTKwqngrdvwwqdvisqyPTSCEVewVDAEDPLFL 307
Cdd:TIGR01733 79 ---------------DSALASRLAGLVLPVILLDPLELAALDDAPAP----------------PPPDAP--SGPDDLAYV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 308 LYTSGSTGKPKGVLHTTGGyMIYTATTFKYAFDYKSTDVywctadcgWITGHSYV-------TYGPMLNGATVVVFEGAP 380
Cdd:TIGR01733 126 IYTSGSTGRPKGVVVTHRS-LVNLLAWLARRYGLDPDDR--------VLQFASLSfdasveeIFGALLAGATLVVPPEDE 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 381 NYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKfvtrhSRKSLRVLGSVGEPINPSA---WRWffnVVGDSRcpisd 457
Cdd:TIGR01733 197 ERDDAALLAALIAEHPVTVLNLTPSLLALLAAALPP-----ALASLRLVILGGEALTPALvdrWRA---RGPGAR----- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 458 tWWQ----TE-TGGFMITPLPGAWPQKPGSATF--PFFGVQPVIVDEKGNEIEGECSGYLCVKGswPGAFRTLFGDHERY 530
Cdd:TIGR01733 264 -LINlygpTEtTVWSTATLVDPDDAPRESPVPIgrPLANTRLYVLDDDLRPVPVGVVGELYIGG--PGVARGYLNRPELT 340
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332006737 531 ETTYFK-PFAG-----YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAV 593
Cdd:TIGR01733 341 AERFVPdPFAGgdgarLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
130-661 |
8.25e-42 |
|
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: 158.61 E-value: 8.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 130 GDKTAIHWEgnelgvDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAD 209
Cdd:cd12116 1 PDATAVRDD------DRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPAD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 210 SLAQRIVDCKPNVILTcnavkrgpktinlkaivdaalDQSSKDGVSVGICLTYDNSLATTRentkwqngrdvwwqDVISQ 289
Cdd:cd12116 75 RLRYILEDAEPALVLT---------------------DDALPDRLPAGLPVLLLALAAAAA--------------APAAP 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 290 YPTscevewVDAEDPLFLLYTSGSTGKPKGV-----------------LHTTGGYMIYTATTfkYAFDYKSTDVYWctad 352
Cdd:cd12116 120 RTP------VSPDDLAYVIYTSGSTGRPKGVvvshrnlvnflhsmrerLGLGPGDRLLAVTT--YAFDISLLELLL---- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 353 cgwitghsyvtygPMLNGATVVVFEGAPNYpDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKfvtrhSRKSLRVL-Gs 431
Cdd:cd12116 188 -------------PLLAGARVVIAPRETQR-DPEALARLIEAHSITVMQATPATWRMLLDAGWQ-----GRAGLTALcG- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 432 vGEPINP-----------SAWrwffNVVGdsrcPISDTWWQTetggfmITPLPGAWPQKPgsATFPFFGVQPVIVDEKGN 500
Cdd:cd12116 248 -GEALPPdlaarllsrvgSLW----NLYG----PTETTIWST------AARVTAAAGPIP--IGRPLANTQVYVLDAALR 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 501 EI-EGECsGYLCVKGswPGAFRtlfGDHERYETTYFK----PFAG----YYFSGDGCSRDKDGYYWLTGRVDDVINVSGH 571
Cdd:cd12116 311 PVpPGVP-GELYIGG--DGVAQ---GYLGRPALTAERfvpdPFAGpgsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGH 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 572 RIGTAEVESALVLHPQCAEAAVVgIEHEVKGQGIYAFVTLLEGVPYS-EELRKSLvlmvRNQIGAFAAPDRIHWAPGLPK 650
Cdd:cd12116 385 RIELGEIEAALAAHPGVAQAAVV-VREDGGDRRLVAYVVLKAGAAPDaAALRAHL----RATLPAYMVPSAFVRLDALPL 459
|
570
....*....|.
gi 332006737 651 TRSGKIMRRIL 661
Cdd:cd12116 460 TANGKLDRKAL 470
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
46-678 |
1.70e-41 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 161.40 E-value: 1.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 46 KEFSGQALVSSPQQYMEMHKRSMDDPaafwsdiasEFYWKQKWGDQ--VFSENldvrkgPISI-----------EWFKGG 112
Cdd:PLN03052 108 KELLGSKYKDPISSFSEFQRFSVENP---------EVYWSIVLDELslVFSVP------PRCIldtsdesnpggQWLPGA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 113 ITNICYNCLDKNVEAGLgDKTAIHW--EGNE-LGVDaSLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAM 189
Cdd:PLN03052 173 VLNVAECCLTPKPSKTD-DSIAIIWrdEGSDdLPVN-RMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIY 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 190 LACARIGAVHSVVFAGFSADSLAQRIVDCKPNVILTCNAVKRGPKTINLKA-IVDAaldQSSK------DGVSVGICLty 262
Cdd:PLN03052 251 LAIILAGCVVVSIADSFAPSEIATRLKISKAKAIFTQDVIVRGGKSIPLYSrVVEA---KAPKaivlpaDGKSVRVKL-- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 263 dnslattRENtkwqngrDVWWQDVISQY-PTSCEVEWVDAEDPL----FLLYTSGSTGKPKGVLHTtggymiyTATTFKY 337
Cdd:PLN03052 326 -------REG-------DMSWDDFLARAnGLRRPDEYKAVEQPVeaftNILFSSGTTGEPKAIPWT-------QLTPLRA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 338 A------FDYKSTDVY-WCTaDCGWITGHsYVTYGPMLNGATVVVFEGAPNYPDPGRcwdIVDKYKVSIFYTAPTLVRS- 409
Cdd:PLN03052 385 AadawahLDIRKGDIVcWPT-NLGWMMGP-WLVYASLLNGATLALYNGSPLGRGFAK---FVQDAKVTMLGTVPSIVKTw 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 410 ----LMRDDDKFvtrhsrkSLRVLGSVGEPINPSAWRWFFnvvgdSRC---PISDTWWQTETGGFMITplpGAWPQKPGS 482
Cdd:PLN03052 460 kntnCMAGLDWS-------SIRCFGSTGEASSVDDYLWLM-----SRAgykPIIEYCGGTELGGGFVT---GSLLQPQAF 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 483 ATF--PFFGVQPVIVDEKGNEI--EGECSGYLCVKGSWPGAFRTLF-GDHERyetTYFK--P-FAGYYFS--GDGCSRDK 552
Cdd:PLN03052 525 AAFstPAMGCKLFILDDSGNPYpdDAPCTGELALFPLMFGASSTLLnADHYK---VYFKgmPvFNGKILRrhGDIFERTS 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 553 DGYYWLTGRVDDVINVSGHRIGTAEVESAL-VLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYS----EELRKSLVL 627
Cdd:PLN03052 602 GGYYRAHGRADDTMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPPGGGPEQLVIAAVLKDPPGSnpdlNELKKIFNS 681
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 332006737 628 MVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKiasrQLEELGDTSTL 678
Cdd:PLN03052 682 AIQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQ----QLAQELSRSKL 728
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
144-661 |
5.41e-41 |
|
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: 157.01 E-value: 5.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 144 VDAS----LTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCK 219
Cdd:cd05904 25 IDAAtgraLTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 220 PNVILTCNAvkrgpktiNLKAIVDAALdqsskdgvSVGICLTYDNSLATTRENTKWQNgrdvwwqdvisqyPTSCEVEWV 299
Cdd:cd05904 105 AKLAFTTAE--------LAEKLASLAL--------PVVLLDSAEFDSLSFSDLLFEAD-------------EAEPPVVVI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 300 DAEDPLFLLYTSGSTGKPKGVLHTTGGYMIYTA-TTFKYAFDYKSTDVYWCTADCGWITGHSYVTYGPMLNGATVVVFEG 378
Cdd:cd05904 156 KQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAqFVAGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 379 ApnypDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDkfVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDsrCPISDT 458
Cdd:cd05904 236 F----DLEELLAAIERYKVTHLPVVPPIVLALVKSPI--VDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPN--VDLGQG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 459 WWQTE-TGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGNEIEGEC-SGYLCVKGswPGAFRTLFGDHERYETTYFK 536
Cdd:cd05904 308 YGMTEsTGVVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDPETGESLPPNqTGELWIRG--PSIMKGYLNNPEATAATIDK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 537 pfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVP 616
Cdd:cd05904 386 --EGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSS 463
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 332006737 617 YSEELRKSLvlmVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRIL 661
Cdd:cd05904 464 LTEDEIMDF---VAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
147-685 |
1.28e-39 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 154.73 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 147 SLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLAcariGAVHSVVFA---GFSADSLAQRIVDCKPNVI 223
Cdd:PRK07529 58 TWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG----GEAAGIANPinpLLEPEQIAELLRAAGAKVL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 224 LT-------------CNAVKRGPktiNLKAIVDAALdqsskdgvsvGICLTYDNSLATTRENTKWQNgRDVWWQDVISQY 290
Cdd:PRK07529 134 VTlgpfpgtdiwqkvAEVLAALP---ELRTVVEVDL----------ARYLPGPKRLAVPLIRRKAHA-RILDFDAELARQ 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 291 PTSCEV--EWVDAEDPLFLLYTSGSTGKPKGVLHTTGGyMIYTATTFKYAFDYKSTDVYWCTADCGWITGhSYVT-YGPM 367
Cdd:PRK07529 200 PGDRLFsgRPIGPDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDTVFCGLPLFHVNA-LLVTgLAPL 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 368 LNGATVVvFEGAPNYPDPG---RCWDIVDKYKVSIFYTAPTLVRSLMrddDKFVTRHSRKSLRVLGSVGEPINPSAWRWF 444
Cdd:PRK07529 278 ARGAHVV-LATPQGYRGPGviaNFWKIVERYRINFLSGVPTVYAALL---QVPVDGHDISSLRYALCGAAPLPVEVFRRF 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 445 FNVVGdsrCPISDTWWQTE-TGGFMITPLPGawPQKPGSA--TFPFFGVQPVIVDEKGNEIEgECS----GYLCVKGswP 517
Cdd:PRK07529 354 EAATG---VRIVEGYGLTEaTCVSSVNPPDG--ERRIGSVglRLPYQRVRVVILDDAGRYLR-DCAvdevGVLCIAG--P 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 518 GAFRT-LFGDHER---YETTYFKpfagyyfSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAV 593
Cdd:PRK07529 426 NVFSGyLEAAHNKglwLEDGWLN-------TGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAA 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 594 VGIEHEVKGQGIYAFVTLLEGVPYSEElrkSLVLMVRNQIGAFAA-PDRIHWAPGLPKTRSGKIMRRILRKIASRQ---- 668
Cdd:PRK07529 499 VGRPDAHAGELPVAYVQLKPGASATEA---ELLAFARDHIAERAAvPKHVRILDALPKTAVGKIFKPALRRDAIRRvlra 575
|
570
....*....|....*...
gi 332006737 669 -LEELGdtstlADPSVVD 685
Cdd:PRK07529 576 aLRDAG-----VEAEVVD 588
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
131-662 |
1.68e-39 |
|
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: 152.11 E-value: 1.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 131 DKTAIHWEGnelgvdASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADS 210
Cdd:cd17651 10 DAPALVAEG------RRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 211 LAQRIVDCKPNVILTcnavkrgpktinlkaivdAALDQSSKDGVSVGICLTYDNSLATtrentkwqngrdvwwqdvisQY 290
Cdd:cd17651 84 LAFMLADAGPVLVLT------------------HPALAGELAVELVAVTLLDQPGAAA--------------------GA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 291 PTSCEVEwVDAEDPLFLLYTSGSTGKPKGVL------------HTTGGYMIYTATTFKYA---FDYKSTDVYwctadcgw 355
Cdd:cd17651 126 DAEPDPA-LDADDLAYVIYTSGSTGRPKGVVmphrslanlvawQARASSLGPGARTLQFAglgFDVSVQEIF-------- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 356 itghsyvtyGPMLNGATVVVfegAPNY--PDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSrkSLRVLGSVG 433
Cdd:cd17651 197 ---------STLCAGATLVL---PPEEvrTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLA--ALRYLLTGG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 434 EP-INPSAWRWFFNVVGDSRcpISDTWWQTET---GGFMITPLPGAWPQKPGSATfPFFGVQPVIVDEKGNEIEGECSGY 509
Cdd:cd17651 263 EQlVLTEDLREFCAGLPGLR--LHNHYGPTEThvvTALSLPGDPAAWPAPPPIGR-PIDNTRVYVLDAALRPVPPGVPGE 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 510 LCVKGswPGAFRTLFGD----HERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLH 585
Cdd:cd17651 340 LYIGG--AGLARGYLNRpeltAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARH 417
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332006737 586 PQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYS-EELRKSLvlmvRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILR 662
Cdd:cd17651 418 PGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDaAELRAAL----ATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
145-661 |
1.81e-39 |
|
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: 152.10 E-value: 1.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 145 DASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVhsVVFAGFSadslaQRIVDckpnviL 224
Cdd:cd05920 38 DRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--PVLALPS-----HRRSE------L 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 225 TCNAVKRGPKTInlkaIVDAALDQsskdgvsvgicltyDNSLATTREntkwqngrdvwwqdVISQYPtscevewvdaeDP 304
Cdd:cd05920 105 SAFCAHAEAVAY----IVPDRHAG--------------FDHRALARE--------------LAESIP-----------EV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 305 LFLLYTSGSTGKPKGVLHTTGGYmIYTATTfkyafdykSTDVYWCTAD----CGWITGHSYVTYGP-----MLNGATVVV 375
Cdd:cd05920 142 ALFLLSGGTTGTPKLIPRTHNDY-AYNVRA--------SAEVCGLDQDtvylAVLPAAHNFPLACPgvlgtLLAGGRVVL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 376 fegAPNyPDPGRCWDIVDKYKVsifyTAPTLVRSL-MRDDDKFVTRHSR-KSLRVLGSVGEPINPSAWRWFFNVVGdsrC 453
Cdd:cd05920 213 ---APD-PSPDAAFPLIEREGV----TVTALVPALvSLWLDAAASRRADlSSLRLLQVGGARLSPALARRVPPVLG---C 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 454 PISDTWWQTE-----------------TGGFMITPLPGAWpqkpgsatfpffgvqpvIVDEKGNEI-EGEcSGYLCVKGs 515
Cdd:cd05920 282 TLQQVFGMAEgllnytrlddpdeviihTQGRPMSPDDEIR-----------------VVDEEGNPVpPGE-EGELLTRG- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 516 wPGAFRTLFgDHERYETTYFKPfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVG 595
Cdd:cd05920 343 -PYTIRGYY-RAPEHNARAFTP-DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVA 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332006737 596 IEHEVKGQGIYAFVTLLEGVPYSEELRKSLVLMvrnQIGAFAAPDRIHWAPGLPKTRSGKIMRRIL 661
Cdd:cd05920 420 MPDELLGERSCAFVVLRDPPPSAAQLRRFLRER---GLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
130-661 |
6.99e-39 |
|
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: 150.43 E-value: 6.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 130 GDKTAIHWEgnelgvDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAD 209
Cdd:cd12117 11 PDAVAVVYG------DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 210 SLAQRIVDCKPNVILTCNAVKRGPKTINLKAIVDAALDQSSKDGVSVGicltydnslattrentkwqngrdvwwqdvisq 289
Cdd:cd12117 85 RLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVP-------------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 290 yptscevewVDAEDPLFLLYTSGSTGKPKGV---------LHTTGGYMIYTA-TTF----KYAFDYKSTDVYwctadcgw 355
Cdd:cd12117 133 ---------VSPDDLAYVMYTSGSTGRPKGVavthrgvvrLVKNTNYVTLGPdDRVlqtsPLAFDASTFEIW-------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 356 itghsyvtyGPMLNGATVVVFEGAPnYPDPGRCWDIVDKYKVS-IFYTAPtLVRSLMRDD-DKFvtrhsrKSLRVLGSVG 433
Cdd:cd12117 196 ---------GALLNGARLVLAPKGT-LLDPDALGALIAEEGVTvLWLTAA-LFNQLADEDpECF------AGLRELLTGG 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 434 EPINPSAWRWFFNVVGDSRcpISDTWWQTETGGF----MITPLPGAWPQKP-GSatfPFFGVQPVIVDEKGNEIEGECSG 508
Cdd:cd12117 259 EVVSPPHVRRVLAACPGLR--LVNGYGPTENTTFttshVVTELDEVAGSIPiGR---PIANTRVYVLDEDGRPVPPGVPG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 509 YLCVKGSwpGAFRTLFGD----HERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVL 584
Cdd:cd12117 334 ELYVGGD--GLALGYLNRpaltAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRA 411
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332006737 585 HPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPySEELRKSLvlmvRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRIL 661
Cdd:cd12117 412 HPGVREAVVVVREDAGGDKRLVAYVVAEGALD-AAELRAFL----RERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
131-661 |
2.79e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 146.64 E-value: 2.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 131 DKTAIHWEGNELgvdaslTYSELLQRVCQLANYLKD-NGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAD 209
Cdd:PRK08314 25 DKTAIVFYGRAI------SYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 210 SLAQRIVDCKPNVILT----CNAVKRGPKTINLKAIVDA----ALDQSSKDGVSVGicltydnsLATTRENTKWQNGRDV 281
Cdd:PRK08314 99 ELAHYVTDSGARVAIVgselAPKVAPAVGNLRLRHVIVAqysdYLPAEPEIAVPAW--------LRAEPPLQALAPGGVV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 282 WWQDVISQYPTSCEVEwVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMiYTATTFKYAFDYKSTDVYWCTADCGWITGHSY 361
Cdd:PRK08314 171 AWKEALAAGLAPPPHT-AGPDDLAVLPYTSGTTGVPKGCMHTHRTVM-ANAVGSVLWSNSTPESVVLAVLPLFHVTGMVH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 362 VTYGPMLNGATVVVF-----EGAPnypdpgrcwDIVDKYKVSIFYTAPTLVRSLMRDDDkfVTRHSRKSLRVLGSVGEPI 436
Cdd:PRK08314 249 SMNAPIYAGATVVLMprwdrEAAA---------RLIERYRVTHWTNIPTMVVDFLASPG--LAERDLSSLRYIGGGGAAM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 437 NPSAWRWFFNVVGdsrCPISDTWWQTETGGFMITPLPGAwpQKPGSATFPFFGVQPVIVD-EKGNEI-EGEcSGYLCVKG 514
Cdd:PRK08314 318 PEAVAERLKELTG---LDYVEGYGLTETMAQTHSNPPDR--PKLQCLGIPTFGVDARVIDpETLEELpPGE-VGEIVVHG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 515 swPGAFRTLFGDHERYETTyFKPFAGYYF--SGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAA 592
Cdd:PRK08314 392 --PQVFKGYWNRPEATAEA-FIEIDGKRFfrTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEAC 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332006737 593 VVGIEHEVKGQGIYAFVTL---LEGVPYSEELRKslvlMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRIL 661
Cdd:PRK08314 469 VIATPDPRRGETVKAVVVLrpeARGKTTEEEIIA----WAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
149-663 |
3.36e-37 |
|
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: 146.24 E-value: 3.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 149 TYSELLQRVCQLANYLKDNGVKKGDAVVIylpML------MELpiaMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNV 222
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVAT---LAwnthrhLEL---YYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 223 ILTcnavkrgpkTINLKAIVDAALDQssKDGVSVGICLTYDNSLATTRENTKWQngrdvwWQDVISQYPTSCEVEWVDAE 302
Cdd:cd12119 101 VFV---------DRDFLPLLEAIAPR--LPTVEHVVVMTDDAAMPEPAGVGVLA------YEELLAAESPEYDWPDFDEN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 303 DPLFLLYTSGSTGKPKGV--------LHTTGGYMiytattfKYAFDYKSTDVY-----------WCTADCGWITGHSYVT 363
Cdd:cd12119 164 TAAAICYTSGTTGNPKGVvyshrslvLHAMAALL-------TDGLGLSESDVVlpvvpmfhvnaWGLPYAAAMVGAKLVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 364 YGPMLNGATVVvfegapnypdpgrcwDIVDKYKVSIFYTAPTLVRSLMRDDDKfvTRHSRKSLRVLGSVGEPINPSAWRW 443
Cdd:cd12119 237 PGPYLDPASLA---------------ELIEREGVTFAAGVPTVWQGLLDHLEA--NGRDLSSLRRVVIGGSAVPRSLIEA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 444 FfnvvGDSRCPISDTWWQTETG--GFMITPLPG----------AWPQKPGsatFPFFGVQPVIVDEKGNEIE--GECSGY 509
Cdd:cd12119 300 F----EERGVRVIHAWGMTETSplGTVARPPSEhsnlsedeqlALRAKQG---RPVPGVELRIVDDDGRELPwdGKAVGE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 510 LCVKGSW-PGAFrtlFGDHERYEttyfKPFAGYYF-SGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQ 587
Cdd:cd12119 373 LQVRGPWvTKSY---YKNDEESE----ALTEDGWLrTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPA 445
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332006737 588 CAEAAVVGIEHEVKGQGIYAFVTLLEGV-PYSEELRKSLvlmvRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRK 663
Cdd:cd12119 446 VAEAAVIGVPHPKWGERPLAVVVLKEGAtVTAEELLEFL----ADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
143-662 |
8.18e-37 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 144.83 E-value: 8.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 143 GVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNV 222
Cdd:PRK13391 20 STGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 223 ILTCNAvKRGpktinlkaIVDAALDQSSKdgvsVGICLTYDNSLATTRentkWQNgrdvwWQDVISQYPtscevEWVDAE 302
Cdd:PRK13391 100 LITSAA-KLD--------VARALLKQCPG----VRHRLVLDGDGELEG----FVG-----YAEAVAGLP-----ATPIAD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 303 DPL--FLLYTSGSTGKPKGVLHTTGGYMIYTATT----FKYAFDYKSTDVYWCTADCGWITGHSYVTYGPMLnGATVVVF 376
Cdd:PRK13391 153 ESLgtDMLYSSGTTGRPKGIKRPLPEQPPDTPLPltafLQRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRL-GGTVIVM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 377 EgapnYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGdsrcPIS 456
Cdd:PRK13391 232 E----HFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWG----PII 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 457 DTWW-QTETGGFMITPlPGAWPQKPGSATFPFFGVqPVIVDEKGNEIEGECSGYLCVKGSWPgaFRTLFGDHERYETTYf 535
Cdd:PRK13391 304 HEYYaATEGLGFTACD-SEEWLAHPGTVGRAMFGD-LHILDDDGAELPPGEPGTIWFEGGRP--FEYLNDPAKTAEARH- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 536 kPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGV 615
Cdd:PRK13391 379 -PDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGV 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 332006737 616 PYSEELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILR 662
Cdd:PRK13391 458 DPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
303-663 |
8.66e-37 |
|
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: 143.58 E-value: 8.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 303 DPLFLLYTSGSTGKPKGVLHTTGGyMIYTATTFKYAFDYKSTDVYW-CTAdcgWITGHSYVT--YGPMLNGATVVVFega 379
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHAN-LAANVRALVDAWRWTEDDVLLhVLP---LHHVHGLVNalLCPLFAGASVEFL--- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 380 PNYpDPGRCWDIVDKYKVSIFYTAPTLVRSLMRD------DDKFVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDsrc 453
Cdd:cd05941 163 PKF-DPKEVAISRLMPSITVFMGVPTIYTRLLQYyeahftDPQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGH--- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 454 PISDTWWQTETGGFMITPLPGawPQKPGSATFPFFGVQPVIVDEKGNE-IEGECSGYLCVKGswPGAFRTLFGDHERYEt 532
Cdd:cd05941 239 TLLERYGMTEIGMALSNPLDG--ERRPGTVGMPLPGVQARIVDEETGEpLPRGEVGEIQVRG--PSVFKEYWNKPEATK- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 533 tyfKPFA--GYYFSGDGCSRDKDGYYWLTGRV-DDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFV 609
Cdd:cd05941 314 ---EEFTddGWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVV 390
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 332006737 610 TLLEGVP--YSEELRKslvlMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRK 663
Cdd:cd05941 391 VLRAGAAalSLEELKE----WAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
131-669 |
1.66e-36 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 144.51 E-value: 1.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 131 DKTAIHwegNELGvdASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADS 210
Cdd:PRK06087 38 DKIAVV---DNHG--ASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 211 LAQRIVDCKPNVILTCNAVKrgpKTINLKAIVDAALDQSSKDGVsVGIcltyDNSLATTRENTKWQngrdvwwqdVISQY 290
Cdd:PRK06087 113 LVWVLNKCQAKMFFAPTLFK---QTRPVDLILPLQNQLPQLQQI-VGV----DKLAPATSSLSLSQ---------IIADY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 291 PTSCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGyMIYTATTFKYAFDYKSTDVYWCTADCGWITGHSYVTYGPMLNG 370
Cdd:PRK06087 176 EPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNN-ILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 371 ATVVVFEgapnYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSrkSLRVLGSVGEPInPS-----AWRWff 445
Cdd:PRK06087 255 ARSVLLD----IFTPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLS--ALRFFLCGGTTI-PKkvareCQQR-- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 446 nvvGDSRCPIsdtWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGswPGAFRTLFG 525
Cdd:PRK06087 326 ---GIKLLSV---YGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRG--PNVFMGYLD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 526 DHERyeTTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGI 605
Cdd:PRK06087 398 EPEL--TARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERS 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332006737 606 YAFVTLLEGVpYSEELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKIASRQL 669
Cdd:PRK06087 476 CAYVVLKAPH-HSLTLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDIMRRL 538
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
121-655 |
2.12e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 143.87 E-value: 2.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 121 LDKNVEAgLGDKTAIHWEgnelgvDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVH- 199
Cdd:PRK07798 9 FEAVADA-VPDRVALVCG------DRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 200 -----------------SVVFAGFSADSLAQRIVDCKPnviltcnavkRGPKtinLKAIVDAAlDQSSKDGVSVGIclTY 262
Cdd:PRK07798 82 nvnyryvedelryllddSDAVALVYEREFAPRVAEVLP----------RLPK---LRTLVVVE-DGSGNDLLPGAV--DY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 263 DNSLATTRENtkwqngrdvwwQDVIsqyPTScevewvdaEDPLFLLYTSGSTGKPKGVLHTT--------GGYMIYTATT 334
Cdd:PRK07798 146 EDALAAGSPE-----------RDFG---ERS--------PDDLYLLYTGGTTGMPKGVMWRQedifrvllGGRDFATGEP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 335 fkyafdykSTDVYWCTADCGWITG----------H---SYVTYGPMLNGATVVVfegapnYP----DPGRCWDIVDKYKV 397
Cdd:PRK07798 204 --------IEDEEELAKRAAAGPGmrrfpapplmHgagQWAAFAALFSGQTVVL------LPdvrfDADEVWRTIEREKV 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 398 -SIFYT----APTLVRSLMRDDDKFVTrhsrkSLRVLGSVGEPINPS---AW-RWFFNVVgdsrcpISDTWWQTETGgFM 468
Cdd:PRK07798 270 nVITIVgdamARPLLDALEARGPYDLS-----SLFAIASGGALFSPSvkeALlELLPNVV------LTDSIGSSETG-FG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 469 ITPLPGAWPQKPGSATFPFfGVQPVIVDEKGNEIE--GECSGYLCVKGSWPGAFrtlFGDHERYETTyFKPFAG--YYFS 544
Cdd:PRK07798 338 GSGTVAKGAVHTGGPRFTI-GPRTVVLDEDGNPVEpgSGEIGWIARRGHIPLGY---YKDPEKTAET-FPTIDGvrYAIP 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 545 GDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEElrkS 624
Cdd:PRK07798 413 GDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLA---E 489
|
570 580 590
....*....|....*....|....*....|.
gi 332006737 625 LVLMVRNQIGAFAAPDRIHWAPGLPKTRSGK 655
Cdd:PRK07798 490 LRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
131-661 |
3.94e-36 |
|
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: 141.68 E-value: 3.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 131 DKTAIHWEgnelgvDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADS 210
Cdd:cd17643 2 EAVAVVDE------DRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 211 LAQRIVDCKPNVILTcnavkrgpktinlkaivdaaldqsskdgvsvgicltydnslattrentkwqngrdvwwqdvisqy 290
Cdd:cd17643 76 IAFILADSGPSLLLT----------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 291 ptscevewvDAEDPLFLLYTSGSTGKPKGVLHTTGGYM-IYTATTfkYAFDYKSTDVywctadcgWITGHSYV------- 362
Cdd:cd17643 91 ---------DPDDLAYVIYTSGSTGRPKGVVVSHANVLaLFAATQ--RWFGFNEDDV--------WTLFHSYAfdfsvwe 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 363 TYGPMLNGATVVVfegAPNYP--DPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSLRVLGsvGEPINPSA 440
Cdd:cd17643 152 IWGALLHGGRLVV---VPYEVarSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFG--GEALEAAM 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 441 WRWFFNVVGDSRCPISDTWWQTETGGFM----ITP--LPGAWPQKPGsATFPFFGVQpvIVDEKGNEIEGECSGYLCVKG 514
Cdd:cd17643 227 LRPWAGRFGLDRPQLVNMYGITETTVHVtfrpLDAadLPAAAASPIG-RPLPGLRVY--VLDADGRPVPPGVVGELYVSG 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 515 swPGAFRtlfGDHERYETTYFK----PFAG----YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHP 586
Cdd:cd17643 304 --AGVAR---GYLGRPELTAERfvanPFGGpgsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHP 378
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332006737 587 QCAEAAVVGIEHEVKGQGIYAFVTLLEGV-PYSEELRKSLvlmvRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRIL 661
Cdd:cd17643 379 SVRDAAVIVREDEPGDTRLVAYVVADDGAaADIAELRALL----KELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
131-661 |
1.63e-35 |
|
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: 139.76 E-value: 1.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 131 DKTAIHWEgnelgvDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADS 210
Cdd:cd12115 14 DAIALVCG------DESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPER 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 211 LAQRIVDCKPNVILTcnavkrgpktinlkaivdaaldqsskdgvsvgicltydnslattrentkwqngrdvwwqdvisqy 290
Cdd:cd12115 88 LRFILEDAQARLVLT----------------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 291 ptscevewvDAEDPLFLLYTSGSTGKPKGVLHTTGGymiytATTFkyafdykstdVYWCTADCG--WITGHSYVT----- 363
Cdd:cd12115 103 ---------DPDDLAYVIYTSGSTGRPKGVAIEHRN-----AAAF----------LQWAAAAFSaeELAGVLASTsicfd 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 364 ------YGPMLNGATVVVFEGAPNYPD-PGRCwdivdkyKVSIFYTAPTLVRSLMRDDdKFVTrhsrkSLRVLGSVGEPI 436
Cdd:cd12115 159 lsvfelFGPLATGGKVVLADNVLALPDlPAAA-------EVTLINTVPSAAAELLRHD-ALPA-----SVRVVNLAGEPL 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 437 N----------PSAWRwFFNVVGdsrcPISDTWWQTetgGFMITPLPGAWPqkpgSATFPFFGVQPVIVDEKGNEIEGEC 506
Cdd:cd12115 226 PrdlvqrlyarLQVER-VVNLYG----PSEDTTYST---VAPVPPGASGEV----SIGRPLANTQAYVLDRALQPVPLGV 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 507 SGYLCVKGswPGAFRTLFGD----HERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESAL 582
Cdd:cd12115 294 PGELYIGG--AGVARGYLGRpgltAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAAL 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 583 VLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGV-PYSEELRKSLvlmvRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRIL 661
Cdd:cd12115 372 RSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAaGLVEDLRRHL----GTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
179-662 |
7.08e-35 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 138.80 E-value: 7.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 179 LPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVILTCNAVKRGPKTINLKAIVdaaldqsskdgVSVGI 258
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKV-----------VEAAP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 259 CLTYDNSLATTRENTKWQNGrDVWWQDVI-SQYPTSC------EVEWVDAEDPLFLLYTSGSTGKPKGV--LHTTGgymI 329
Cdd:PLN03051 70 AKAIVLPAAGEPVAVPLREQ-DLSWCDFLgVAAAQGSvggneySPVYAPVESVTNILFSSGTTGEPKAIpwTHLSP---L 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 330 YTATTFKYAFDYKSTDVYWCTADCGWITGhSYVTYGPMLNGATVVVFEGAPNYPDPGrcwDIVDKYKVSIFYTAPTLVRS 409
Cdd:PLN03051 146 RCASDGWAHMDIQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGAPLGRGFG---KFVQDAGVTVLGLVPSIVKA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 410 LMRDDDKFVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDSRcPISDTWWQTETGGFMI--TPLPgawPQKPGSATFPF 487
Cdd:PLN03051 222 WRHTGAFAMEGLDWSKLRVFASTGEASAVDDVLWLSSVRGYYK-PVIEYCGGTELASGYIssTLLQ---PQAPGAFSTAS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 488 FGVQPVIVDEKGNEI--EGECSGYLCVKGSWPGAF-RTLFGDHERyetTYFKPFAGYYFS-------GDGCSRDKDGYYW 557
Cdd:PLN03051 298 LGTRFVLLNDNGVPYpdDQPCVGEVALAPPMLGASdRLLNADHDK---VYYKGMPMYGSKgmplrrhGDIMKRTPGGYFC 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 558 LTGRVDDVINVSGHRIGTAEVESALVLHPQC-AEAAVVGIEHEVKGQG---IYAFVTLLEGVPYS---EELRKSLVLMVR 630
Cdd:PLN03051 375 VQGRADDTMNLGGIKTSSVEIERACDRAVAGiAETAAVGVAPPDGGPEllvIFLVLGEEKKGFDQarpEALQKKFQEAIQ 454
|
490 500 510
....*....|....*....|....*....|..
gi 332006737 631 NQIGAFAAPDRIHWAPGLPKTRSGKIMRRILR 662
Cdd:PLN03051 455 TNLNPLFKVSRVKIVPELPRNASNKLLRRVLR 486
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
131-665 |
2.43e-34 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 138.26 E-value: 2.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 131 DKTAIHWEGNELGVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAV----------HS 200
Cdd:PRK13295 39 DKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVlnplmpifreRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 201 V----------------VFAGFSADSLAQRIVDCKPNviltcnavkrgpktinLKAIVdaALDQSSKDGvsvgicltYDN 264
Cdd:PRK13295 119 LsfmlkhaeskvlvvpkTFRGFDHAAMARRLRPELPA----------------LRHVV--VVGGDGADS--------FEA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 265 SLATTRentkWQNGRDVwwqDVISQYPTScevewvDAEDPLFLLYTSGSTGKPKGVLHTTGGYMiytATTFKYA--FDYK 342
Cdd:PRK13295 173 LLITPA----WEQEPDA---PAILARLRP------GPDDVTQLIYTSGTTGEPKGVMHTANTLM---ANIVPYAerLGLG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 343 STDVYWCTADCGWITGHSYVTYGPMLNGATVVVFEgapnYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRdddkfVTRHS 422
Cdd:PRK13295 237 ADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQD----IWDPARAAELIRTEGVTFTMASTPFLTDLTR-----AVKES 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 423 RK---SLRVLGSVGEPINPS----AWRwffnVVGDSRCPisdTWWQTETGGFMITpLPGAWPQKpGSAT--FPFFGVQPV 493
Cdd:PRK13295 308 GRpvsSLRTFLCAGAPIPGAlverARA----ALGAKIVS---AWGMTENGAVTLT-KLDDPDER-ASTTdgCPLPGVEVR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 494 IVDEKGNEIEGECSGYLCVKGswPGAFRTLFGDHERYETTyfkpFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRI 573
Cdd:PRK13295 379 VVDADGAPLPAGQIGRLQVRG--CSNFGGYLKRPQLNGTD----ADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENI 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 574 GTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEElrkSLVLMVRNQIGAFA-APDRIHWAPGLPKTR 652
Cdd:PRK13295 453 PVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFE---EMVEFLKAQKVAKQyIPERLVVRDALPRTP 529
|
570
....*....|...
gi 332006737 653 SGKIMRRILRKIA 665
Cdd:PRK13295 530 SGKIQKFRLREML 542
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
147-661 |
3.22e-34 |
|
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: 135.68 E-value: 3.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 147 SLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCkpnviltc 226
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDS-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 227 navkrGPKTinlkAIVDAALDqsskdgvsvgicltydnslattrentkwqngrdvwwqdvisqyptscevewvdaeDPLF 306
Cdd:cd05935 73 -----GAKV----AVVGSELD-------------------------------------------------------DLAL 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 307 LLYTSGSTGKPKGVLHTTGGyMIYTATTFKYAFDYKSTDVYWCTADCGWITGHSYVTYGPMLNGATVVVF-----EGAPn 381
Cdd:cd05935 89 IPYTSGTTGLPKGCMHTHFS-AAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMarwdrETAL- 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 382 ypdpgrcwDIVDKYKVSIFYTAPTLVRSLMrDDDKFVTRhSRKSLRVLGSVGEPINPSAWRWFFNVVGdsrCPISDTWWQ 461
Cdd:cd05935 167 --------ELIEKYKVTFWTNIPTMLVDLL-ATPEFKTR-DLSSLKVLTGGGAPMPPAVAEKLLKLTG---LRFVEGYGL 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 462 TETggfmITPLPGAWPQKPGSATF--PFFGVQPVIVD-EKGNEIEGECSGYLCVKGswPGAFRTLFGDHERYETTYFKPF 538
Cdd:cd05935 234 TET----MSQTHTNPPLRPKLQCLgiP*FGVDARVIDiETGRELPPNEVGEIVVRG--PQIFKGYWNRPEETEESFIEIK 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 539 AGYYF-SGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGV-- 615
Cdd:cd05935 308 GRRFFrTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYrg 387
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 332006737 616 PYSEElrkSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRIL 661
Cdd:cd05935 388 KVTEE---DIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
131-661 |
9.34e-34 |
|
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: 134.68 E-value: 9.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 131 DKTAIHWEGnelgvdASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADS 210
Cdd:cd05945 6 DRPAVVEGG------RTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 211 LAQRIVDCKPNVILtcnavkrgpktinlkaivdaaldqsskdgvsvgicltydnslattrentkwqngrdvwwqdvisqy 290
Cdd:cd05945 80 IREILDAAKPALLI------------------------------------------------------------------ 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 291 ptscevewVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMIYT---------------ATTFKYAFDYKSTDVYwctadCGW 355
Cdd:cd05945 94 --------ADGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTnwmlsdfplgpgdvfLNQAPFSFDLSVMDLY-----PAL 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 356 ITGhsyvtygpmlnGATVVVFEGApnYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDkfVTRHSRKSLRVLGSVGEP 435
Cdd:cd05945 161 ASG-----------ATLVPVPRDA--TADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPT--FTPESLPSLRHFLFCGEV 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 436 I-NPSAWRWFfnvvgdSR---CPISDTWWQTETggfMITPLPGAWPQKPGSAT------FPFFGVQPVIVDEKGNEIEGE 505
Cdd:cd05945 226 LpHKTARALQ------QRfpdARIYNTYGPTEA---TVAVTYIEVTPEVLDGYdrlpigYAKPGAKLVILDEDGRPVPPG 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 506 CSGYLCVKGswPGAFRTLFGDHERYETTYFkPFAGY--YFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALV 583
Cdd:cd05945 297 EKGELVISG--PSVSKGYLNNPEKTAAAFF-PDEGQraYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALR 373
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 584 LHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPY--SEELRKSLvlmvRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRIL 661
Cdd:cd05945 374 QVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAglTKAIKAEL----AERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
130-662 |
2.50e-33 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 134.81 E-value: 2.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 130 GDKTAIHWEGNElGVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAD 209
Cdd:PRK08008 21 GHKTALIFESSG-GVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 210 SLAQRIVDCKPNVILTcnavkrGPKTINLKAIVDAALDQSSKdgvsvGICLTydnslattRENTKWQNGRDVWWQDVISQ 289
Cdd:PRK08008 100 ESAWILQNSQASLLVT------SAQFYPMYRQIQQEDATPLR-----HICLT--------RVALPADDGVSSFTQLKAQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 290 YPTSCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTT-----GGYmiYTAttFKYAFDYKstDVYW-----------CTADC 353
Cdd:PRK08008 161 PATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHynlrfAGY--YSA--WQCALRDD--DVYLtvmpafhidcqCTAAM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 354 gwitghsyvtygPMLN-GATVVVFEgapNYpDPGRCWDIVDKYKVSIFYTAPTLVRSLM----RDDDKfvTRHSRKSLRV 428
Cdd:PRK08008 235 ------------AAFSaGATFVLLE---KY-SARAFWGQVCKYRATITECIPMMIRTLMvqppSANDR--QHCLREVMFY 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 429 LG-SVGEPinpSAWRWFFNVvgdsrcPISDTWWQTETGGFMITPLPGA---WPqkpgSATFPFFGVQPVIVDEKGNEIEG 504
Cdd:PRK08008 297 LNlSDQEK---DAFEERFGV------RLLTSYGMTETIVGIIGDRPGDkrrWP----SIGRPGFCYEAEIRDDHNRPLPA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 505 ECSGYLCVKGSwPGafRTLF-GDHERYETT--YFKPfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESA 581
Cdd:PRK08008 364 GEIGEICIKGV-PG--KTIFkEYYLDPKATakVLEA-DGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENI 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 582 LVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEElrkSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRIL 661
Cdd:PRK08008 440 IATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEE---EFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
.
gi 332006737 662 R 662
Cdd:PRK08008 517 K 517
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
131-662 |
6.24e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 133.57 E-value: 6.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 131 DKTAIHWEgnelgvDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLP----MLMELPIAMLACARIGAVHSVVfagf 206
Cdd:PRK06188 27 DRPALVLG------DTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLnrpeVLMAIGAAQLAGLRRTALHPLG---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 207 SADSLAQRIVDCKPNViLTCNAVKRGPKTINLKAIVDaaldqSSKDGVSVGICltydnslattrentkwQNGRDVWwqDV 286
Cdd:PRK06188 97 SLDDHAYVLEDAGIST-LIVDPAPFVERALALLARVP-----SLKHVLTLGPV----------------PDGVDLL--AA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 287 ISQYPTSCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMIYTAttfkyafdykstdvyWCTADCGWITGHSYVTYGP 366
Cdd:PRK06188 153 AAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQ---------------IQLAEWEWPADPRFLMCTP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 367 ------------MLNGATVVVFEGApnypDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDkfVTRHSRKSLRVLGSVGE 434
Cdd:PRK06188 218 lshaggafflptLLRGGTVIVLAKF----DPAEVLRAIEEQRITATFLVPTMIYALLDHPD--LRTRDLSSLETVYYGAS 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 435 PINPSAWRWFFNVVGdsrcPI-SDTWWQTETGGFmITPLP-----GAWPQKPGSATFPFFGVQPVIVDEKGNEIE-GEcS 507
Cdd:PRK06188 292 PMSPVRLAEAIERFG----PIfAQYYGQTEAPMV-ITYLRkrdhdPDDPKRLTSCGRPTPGLRVALLDEDGREVAqGE-V 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 508 GYLCVKGswPGAFRtlfGDHERYETTYfKPFA-GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHP 586
Cdd:PRK06188 366 GEICVRG--PLVMD---GYWNRPEETA-EAFRdGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHP 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332006737 587 QCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEElrkSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILR 662
Cdd:PRK06188 440 AVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAA---ELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
309-668 |
1.14e-32 |
|
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: 129.52 E-value: 1.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 309 YTSGSTGKPKGVLHTTGGyMIYTATTFKYAFDYKSTDVYWCTADCGWITGhSYVTYGPMLNGATVVVFEGAPNYPDPG-- 386
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNG-SVVTLLTPLASGAHVVLAGPAGYRNPGlf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 387 -RCWDIVDKYKVSIFYTAPTLVRSLM-RDDDKFVTrhsrkSLRVLGSVGEPINPSAWRWFFNVVGdsrCPISDTWWQTET 464
Cdd:cd05944 87 dNFWKLVERYRITSLSTVPTVYAALLqVPVNADIS-----SLRFAMSGAAPLPVELRARFEDATG---LPVVEGYGLTEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 465 GGFMITPLPGAwPQKPGSA--TFPFFGVQPVIVDEKGN---EIEGECSGYLCVKGswPGAFR-TLFGDHERyettyfKPF 538
Cdd:cd05944 159 TCLVAVNPPDG-PKRPGSVglRLPYARVRIKVLDGVGRllrDCAPDEVGEICVAG--PGVFGgYLYTEGNK------NAF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 539 A--GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVP 616
Cdd:cd05944 230 VadGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAV 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 332006737 617 YSEElrkSLVLMVRNQIGAFAA-PDRIHWAPGLPKTRSGKIMRRILRKIASRQ 668
Cdd:cd05944 310 VEEE---ELLAWARDHVPERAAvPKHIEVLEELPVTAVGKVFKPALRADAIHR 359
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
131-662 |
1.30e-32 |
|
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: 131.34 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 131 DKTAIHWEgnelgvDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVhsvvFAGFSADS 210
Cdd:cd17649 2 DAVALVFG------DQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGA----YVPLDPEY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 211 LAQRIvdckpnviltcnavkrgpktinLKAIVDAaldqsskdGVSVgicltydnslattrentkwqngrdvwwqdVISQY 290
Cdd:cd17649 72 PAERL----------------------RYMLEDS--------GAGL-----------------------------LLTHH 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 291 PtscevewvdaEDPLFLLYTSGSTGKPKGVLHTTGGYMIYTATTFKYaFDYKSTDVYWCTADCGWITGHSYVtYGPMLNG 370
Cdd:cd17649 93 P----------RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGDRELQFASFNFDGAHEQL-LPPLICG 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 371 ATVVVfEGAPNYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKfVTRHSRKSLRVLGSVGEPINPSAWR-------W 443
Cdd:cd17649 161 ACVVL-RPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADR-TGDGRPPSLRLYIFGGEALSPELLRrwlkapvR 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 444 FFNVVGDSRCPISDTWWQTETGgfmitpLPGAWPQKP-GSatfPFFGVQPVIVDEKGNEIEGECSGYLCVKGswPGAFRt 522
Cdd:cd17649 239 LFNAYGPTEATVTPLVWKCEAG------AARAGASMPiGR---PLGGRSAYILDADLNPVPVGVTGELYIGG--EGLAR- 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 523 lfGDHERYETT--------YFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVV 594
Cdd:cd17649 307 --GYLGRPELTaerfvpdpFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVV 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332006737 595 GiEHEVKGQGIYAFVtLLEGVPYSEELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILR 662
Cdd:cd17649 385 A-LDGAGGKQLVAYV-VLRAAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
130-661 |
1.47e-32 |
|
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: 132.01 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 130 GDKTAIHWEGnelgvdASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAD 209
Cdd:cd17646 12 PDAPAVVDEG------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 210 SLAQRIVDCKPNVILTcnavkrgpktinlkaiVDAALDQSSKDGVSVGICLTYDNSLATTREntkwqngrdvwwqdvisq 289
Cdd:cd17646 86 RLAYMLADAGPAVVLT----------------TADLAARLPAGGDVALLGDEALAAPPATPP------------------ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 290 yptscEVEwVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMIYTATtFKYAFDYKSTDVYWCTADCG-----WitghsyVTY 364
Cdd:cd17646 132 -----LVP-PRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLW-MQDEYPLGPGDRVLQKTPLSfdvsvW------ELF 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 365 GPMLNGATVVVFEgAPNYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDkfvtRHSRKSLRVLGSVGEPINPSAWRWF 444
Cdd:cd17646 199 WPLVAGARLVVAR-PGGHRDPAYLAALIREHGVTTCHFVPSMLRVFLAEPA----AGSCASLRRVFCSGEALPPELAARF 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 445 F--------NVVGDSRCPISDTWWQTEtggfmitplpGAWPQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGsw 516
Cdd:cd17646 274 LalpgaelhNLYGPTEAAIDVTHWPVR----------GPAETPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGG-- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 517 PGAFRTLFG----DHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAA 592
Cdd:cd17646 342 VQLARGYLGrpalTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAV 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332006737 593 VVGIEHEVKGQGIYAFVTLLEG--VPYSEELRKSLvlmvRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRIL 661
Cdd:cd17646 422 VVARAAPAGAARLVGYVVPAAGaaGPDTAALRAHL----AERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
131-693 |
2.24e-32 |
|
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: 134.60 E-value: 2.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 131 DKTAIHWEgnelgvDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADS 210
Cdd:COG1020 491 DAVAVVFG------DQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAER 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 211 LAQRIVDCKPNVILTcnavkrgpktinlkaivDAALDQS-SKDGVSVgICLtyDnslattrentkwqngrdvwwQDVISQ 289
Cdd:COG1020 565 LAYMLEDAGARLVLT-----------------QSALAARlPELGVPV-LAL--D--------------------ALALAA 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 290 YPTSCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGyMIYTATTFKYAFDYKSTDVywctadCGWITGHS-----YVTY 364
Cdd:COG1020 605 EPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRA-LVNLLAWMQRRYGLGPGDR------VLQFASLSfdasvWEIF 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 365 GPMLNGATVVVF--EGApnyPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDdkfvtRHSRKSLRVLGSVGEPINPSAWR 442
Cdd:COG1020 678 GALLSGATLVLAppEAR---RDPAALAELLARHRVTVLNLTPSLLRALLDAA-----PEALPSLRLVLVGGEALPPELVR 749
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 443 WFFNVVGDSRC-----PisdtwwqTETG----GFMITPLPGAWPQKP-GSatfPFFGVQPVIVDEKGNE----IEGEcsg 508
Cdd:COG1020 750 RWRARLPGARLvnlygP-------TETTvdstYYEVTPPDADGGSVPiGR---PIANTRVYVLDAHLQPvpvgVPGE--- 816
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 509 yLCVKGswPGafrtL----FGDH----ERYETTYFkPFAG--YYFSGDGCSRDKDG---YywlTGRVDDVINVSGHRIGT 575
Cdd:COG1020 817 -LYIGG--AG----LargyLNRPeltaERFVADPF-GFPGarLYRTGDLARWLPDGnleF---LGRADDQVKIRGFRIEL 885
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 576 AEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEELRKSLVLMVRNQIgafAAPDRIHWAPGLPKTRSGK 655
Cdd:COG1020 886 GEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPY---MVPAAVVLLLPLPLTGNGK 962
|
570 580 590
....*....|....*....|....*....|....*...
gi 332006737 656 IMRRILRKIASRQLEELGDTSTLADPSVVDQLIALADV 693
Cdd:COG1020 963 LDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLV 1000
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
145-662 |
2.32e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 131.56 E-value: 2.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 145 DASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVIL 224
Cdd:PRK08276 9 GEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 225 TCNAvkrgpktinLKAIVDAALDQSSKDgvsVGICLTYDNSLATTRENTKWQNGrdvwwqdvisQYPTSCEVEWVDAEdp 304
Cdd:PRK08276 89 VSAA---------LADTAAELAAELPAG---VPLLLVVAGPVPGFRSYEEALAA----------QPDTPIADETAGAD-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 305 lfLLYTSGSTGKPKGVL--------HTTGGYMiytATTFKYAFDYKSTDVYWCTADcgwiTGHSYVT-YGPMLN--GATV 373
Cdd:PRK08276 145 --MLYSSGTTGRPKGIKrplpgldpDEAPGMM---LALLGFGMYGGPDSVYLSPAP----LYHTAPLrFGMSALalGGTV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 374 VVFEGApnypDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSLRVLGSVGEPinpsawrwffnvvgdsrC 453
Cdd:PRK08276 216 VVMEKF----DAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYDVSSLRVAIHAAAP-----------------C 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 454 PIS------DtWW---------QTETGGF-MITPlpGAWPQKPGSATFPFFGVqpV-IVDEKGNEI----EG----ECSG 508
Cdd:PRK08276 275 PVEvkramiD-WWgpiiheyyaSSEGGGVtVITS--EDWLAHPGSVGKAVLGE--VrILDEDGNELppgeIGtvyfEMDG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 509 YlcvkgswpgAFrTLFGDHERYETTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQC 588
Cdd:PRK08276 350 Y---------PF-EYHNDPEKTAAARNP--HGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKV 417
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332006737 589 AEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILR 662
Cdd:PRK08276 418 ADVAVFGVPDEEMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
129-674 |
2.59e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 131.70 E-value: 2.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 129 LGDKTAIHWEgnelgvDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHsvvfagfsa 208
Cdd:PRK07470 20 FPDRIALVWG------DRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVW--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 209 dslaqrivdCKPNVILTCNAVkrgpktinlkaivdAALDQSSkdGVSVGICLT----YDNSLATTRENTKWQ-------N 277
Cdd:PRK07470 85 ---------VPTNFRQTPDEV--------------AYLAEAS--GARAMICHAdfpeHAAAVRAASPDLTHVvaiggarA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 278 GRDVwwQDVISQYP-TSCEVEWVDAEDPLFLLYTSGSTGKPK-GVLhtTGGYMIYTATTfkyafdyKSTDVYWCT--ADC 353
Cdd:PRK07470 140 GLDY--EALVARHLgARVANAAVDHDDPCWFFFTSGTTGRPKaAVL--THGQMAFVITN-------HLADLMPGTteQDA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 354 gwitghSYVTyGPMLNGATV-----------VVFEGAPNYpDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDkfVTRHS 422
Cdd:PRK07470 209 ------SLVV-APLSHGAGIhqlcqvargaaTVLLPSERF-DPAEVWALVERHRVTNLFTVPTILKMLVEHPA--VDRYD 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 423 RKSLRVLGSVGEPI----NPSAWRWFFNVV----GDSRCpisdtwwqteTGGfmITPLPGAW------PQ-KPGSATFPF 487
Cdd:PRK07470 279 HSSLRYVIYAGAPMyradQKRALAKLGKVLvqyfGLGEV----------TGN--ITVLPPALhdaedgPDaRIGTCGFER 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 488 FGVQPVIVDEKGNEIEGECSGYLCVKGswPGAFRTLFGDHERYEttyfKPFAGYYF-SGDGCSRDKDGYYWLTGRVDDVI 566
Cdd:PRK07470 347 TGMEVQIQDDEGRELPPGETGEICVIG--PAVFAGYYNNPEANA----KAFRDGWFrTGDLGHLDARGFLYITGRASDMY 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 567 NVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEElrkSLVLMVRNQIGAFAAPDRIHWAP 646
Cdd:PRK07470 421 ISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEA---ELLAWLDGKVARYKLPKRFFFWD 497
|
570 580
....*....|....*....|....*...
gi 332006737 647 GLPKTRSGKIMRRILRKiasrQLEELGD 674
Cdd:PRK07470 498 ALPKSGYGKITKKMVRE----ELEERGL 521
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
131-656 |
4.37e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 128.62 E-value: 4.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 131 DKTAIHWEGNELgvdaslTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADS 210
Cdd:PRK06178 48 QRPAIIFYGHVI------TYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 211 LAQRIVDCKPNVILTCNAvkrgpktinLKAIVDAALDQSSKDGV---SVGICLTYDNSL---ATTRENTKWQNGrdvwWQ 284
Cdd:PRK06178 122 LSYELNDAGAEVLLALDQ---------LAPVVEQVRAETSLRHVivtSLADVLPAEPTLplpDSLRAPRLAAAG----AI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 285 DVISQY---PTSCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGgYMIYTATTF-KYAFDYKSTDVYWCTADCGWITGHS 360
Cdd:PRK06178 189 DLLPALracTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQR-DMVYTAAAAyAVAVVGGEDSVFLSFLPEFWIAGEN 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 361 YVTYGPMLNGATVVVFegapNYPDPGRCWDIVDKYKVSIfytAPTLVRS---LMrdDDKFVTRHSRKSLRVLGSVG--EP 435
Cdd:PRK06178 268 FGLLFPLFSGATLVLL----ARWDAVAFMAAVERYRVTR---TVMLVDNaveLM--DHPRFAEYDLSSLRQVRVVSfvKK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 436 INPsawrwffnvvgDSRcpisdTWWQTETGGFMITplpGAW--PQKPGSATF--------------PFFGVQPV------ 493
Cdd:PRK06178 339 LNP-----------DYR-----QRWRALTGSVLAE---AAWgmTETHTCDTFtagfqdddfdllsqPVFVGLPVpgtefk 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 494 IVDEKGNEI-----EGEcsgyLCV------KGSW--PGAFRTLFGDheryettyfkpfaGYYFSGDGCSRDKDGYYWLTG 560
Cdd:PRK06178 400 ICDFETGELlplgaEGE----IVVrtpsllKGYWnkPEATAEALRD-------------GWLHTGDIGKIDEQGFLHYLG 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 561 RVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEElrkSLVLMVRNQIGAFAAPD 640
Cdd:PRK06178 463 RRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAA---ALQAWCRENMAVYKVPE 539
|
570
....*....|....*.
gi 332006737 641 rIHWAPGLPKTRSGKI 656
Cdd:PRK06178 540 -IRIVDALPMTATGKV 554
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
148-661 |
7.77e-31 |
|
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: 126.85 E-value: 7.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 148 LTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIvdckpnviltcn 227
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELI------------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 228 avKRGPKTINLKAiVDAALDQSSKDGvsvGICLTYDNSLATTRENTKWQngrdvwwqDVISqyPTSCEVEwvdaeDPLFL 307
Cdd:cd05923 97 --ERGEMTAAVIA-VDAQVMDAIFQS---GVRVLALSDLVGLGEPESAG--------PLIE--DPPREPE-----QPAFV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 308 LYTSGSTGKPKGVL---HTTGGYMIYTATTFKYAFDykSTDVYWCTADCGWITGHSYVTYGPMLNGATVVVfegaPNYPD 384
Cdd:cd05923 156 FYTSGTTGLPKGAVipqRAAESRVLFMSTQAGLRHG--RHNVVLGLMPLYHVIGFFAVLVAALALDGTYVV----VEEFD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 385 PGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSrkSLRVLGSVGEPINPSAWRWFFNVVGDsrcPISDTWWQTET 464
Cdd:cd05923 230 PADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLS--SLRHVTFAGATMPDAVLERVNQHLPG---EKVNIYGTTEA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 465 GGFMITPLPgawpqKPGSATFPFFG--VQPVIVDEKGNEI-----EGEcsgyLCVKGSWPGAFRtlfGDHERYETTYFKP 537
Cdd:cd05923 305 MNSLYMRDA-----RTGTEMRPGFFseVRIVRIGGSPDEAlangeEGE----LIVAAAADAAFT---GYLNQPEATAKKL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 538 FAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPY 617
Cdd:cd05923 373 QDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLS 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 332006737 618 SEELRKslvLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRIL 661
Cdd:cd05923 453 ADELDQ---FCRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
148-664 |
1.71e-30 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 126.41 E-value: 1.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 148 LTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVIltcn 227
Cdd:PRK06155 47 WTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLL---- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 228 avkrgpktinlkaIVDAALdQSSKDGVSVGicltyDNSLATTrentkWQNGRDVWWQ-----DVISQYPTSCEVEWVDAE 302
Cdd:PRK06155 123 -------------VVEAAL-LAALEAADPG-----DLPLPAV-----WLLDAPASVSvpagwSTAPLPPLDAPAPAAAVQ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 303 --DPLFLLYTSGSTGKPKGVLHTTGGYMIYTATTfkyafdykstdvywcTADCGWITGHSYVTYGP-------------M 367
Cdd:PRK06155 179 pgDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNS---------------AEDLEIGADDVLYTTLPlfhtnalnaffqaL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 368 LNGATVVV---FEGApnypdpgRCWDIVDKYKVSIFY----TAPTLVRSLMRDDDKfvtRHSrksLRV-LGSVGEPINPS 439
Cdd:PRK06155 244 LAGATYVLeprFSAS-------GFWPAVRRHGATVTYllgaMVSILLSQPARESDR---AHR---VRVaLGPGVPAALHA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 440 AWRWFFNVvgdsrcPISDTWWQTETGGFMITPLPGawpQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGSWPGA 519
Cdd:PRK06155 311 AFRERFGV------DLLDGYGSTETNFVIAVTHGS---QRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADEPFA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 520 FRT-LFGDHEryETTyfKPFAGYYF-SGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIE 597
Cdd:PRK06155 382 FATgYFGMPE--KTV--EAWRNLWFhTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVP 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332006737 598 HEVKGQGIYAFVTLLEGVPYSEElrkSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKI 664
Cdd:PRK06155 458 SELGEDEVMAAVVLRDGTALEPV---ALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
156-662 |
3.22e-30 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 124.47 E-value: 3.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 156 RVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQ--RIV--DCKPNViltcnavkr 231
Cdd:cd05922 2 GVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPTLKESvlRYLvaDAGGRI--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 232 gpktinlkAIVDAALDQSSKDGVSVgiclTYDNSLATtrentkwqnGRDVWWQDvisqyPTSCEVEWVDAEDPLFLLYTS 311
Cdd:cd05922 73 --------VLADAGAADRLRDALPA----SPDPGTVL---------DADGIRAA-----RASAPAHEVSHEDLALLLYTS 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 312 GSTGKPKGVL--HTTggyMIYTATTFKYAFDYKSTDVYWCTADCGWITGHSYVTYGpMLNGATVVVfegAPNYPDPGRCW 389
Cdd:cd05922 127 GSTGSPKLVRlsHQN---LLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTH-LLRGATLVL---TNDGVLDDAFW 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 390 DIVDKYKVSIFYTAPT---LVRSLMRDDDKFvtrhsrKSLRVLGSVGEPINPSAWRWFFNVVGDSRcpISDTWWQTETGG 466
Cdd:cd05922 200 EDLREHGATGLAGVPStyaMLTRLGFDPAKL------PSLRYLTQAGGRLPQETIARLRELLPGAQ--VYVMYGQTEATR 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 467 FMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGswPGAFRTLFGD--HERYETTyfkpFAGYYFS 544
Cdd:cd05922 272 RMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRG--PNVMKGYWNDppYRRKEGR----GGGVLHT 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 545 GDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVkGQGIYAFVTLLEGVPYSEELRKs 624
Cdd:cd05922 346 GDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKIDPKDVLRS- 423
|
490 500 510
....*....|....*....|....*....|....*...
gi 332006737 625 lvlmVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILR 662
Cdd:cd05922 424 ----LAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
131-664 |
4.12e-30 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 124.59 E-value: 4.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 131 DKTAIhwegneLGVDASLTYSELLQRVCQLANYLKDN-GVKKGDAVVIYLPMLMELPIAMLACARIGAVhSVVFagfsad 209
Cdd:PRK06839 17 DRIAI------ITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECI-AVPL------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 210 slaqrivdckpNVILTcnavkrgpktinlkaivDAALDQSSKD-GVSVGIC-LTYDNSLATTRENTKWQngRDVWWQDV- 286
Cdd:PRK06839 84 -----------NIRLT-----------------ENELIFQLKDsGTTVLFVeKTFQNMALSMQKVSYVQ--RVISITSLk 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 287 -ISQYPTSCEVEwVDAEDPLFLLYTSGSTGKPKGVLHTTGGyMIYTATTFKYAFDYKSTDVYWCTADCGWITGHSYVTYG 365
Cdd:PRK06839 134 eIEDRKIDNFVE-KNESASFIICYTSGTTGKPKGAVLTQEN-MFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 366 PMLNGATVVVfegaPNYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTrhsrkslrvlgsvgepiNPSAWRWFF 445
Cdd:PRK06839 212 TLFAGGVIIV----PRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETT-----------------NLQSVRWFY 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 446 NvvGDSRCPI-------------SDTWWQTETGG--FMITPLPGAwpQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYL 510
Cdd:PRK06839 271 N--GGAPCPEelmrefidrgflfGQGFGMTETSPtvFMLSEEDAR--RKVGSIGKPVLFCDYELIDENKNKVEVGEVGEL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 511 CVKGswPGAFRTLFGDHERYETTYFKpfaGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAE 590
Cdd:PRK06839 347 LIRG--PNVMKEYWNRPDATEETIQD---GWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYE 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332006737 591 AAVVGIEHEVKGQGIYAFVTLLEGVPYSEElrkSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKI 664
Cdd:PRK06839 422 VAVVGRQHVKWGEIPIAFIVKKSSSVLIEK---DVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
149-662 |
5.35e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 124.15 E-value: 5.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 149 TYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVILTcna 228
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLG--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 229 vkrgpktinlkaivDAALDQSSKDGVSVgicltydnslattrentkwqngrDVWWQDVISQYPTscEVEWVDAEDPLFLL 308
Cdd:PRK09088 101 --------------DDAVAAGRTDVEDL-----------------------AAFIASADALEPA--DTPSIPPERVSLIL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 309 YTSGSTGKPKGVLHTTGGyMIYTATTFKYAFDYKSTDVYWCTADCGWITGHSYVTYGPMLNGATVVVFEGApnypDPGRC 388
Cdd:PRK09088 142 FTSGTSGQPKGVMLSERN-LQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGF----EPKRT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 389 --WDIVDKYKVSIFYTAPTLVRSLmRDDDKFVTRHSRkSLRVLGSVGEPINPSAWRWFFnvvgDSRCPISDTWWQTETGG 466
Cdd:PRK09088 217 lgRLGDPALGITHYFCVPQMAQAF-RAQPGFDAAALR-HLTALFTGGAPHAAEDILGWL----DDGIPMVDGFGMSEAGT 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 467 FMITPL-PGAWPQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGswPGAFRTLFGDHEryETTYFKPFAGYYFSG 545
Cdd:PRK09088 291 VFGMSVdCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRG--PNLSPGYWRRPQ--ATARAFTGDGWFRTG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 546 DGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYS-EELRKS 624
Cdd:PRK09088 367 DIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDlERIRSH 446
|
490 500 510
....*....|....*....|....*....|....*...
gi 332006737 625 LVlmvrNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILR 662
Cdd:PRK09088 447 LS----TRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
140-662 |
1.82e-29 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 123.33 E-value: 1.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 140 NELGvdaSLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAvHSVVF-AGFSADSLAQRIVDC 218
Cdd:PRK13382 64 DELG---TLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGA-DILLLnTSFAGPALAEVVTRE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 219 KPNVILTCNavkrgpktiNLKAIVDAALDQSSKdgvsvgicltydnslaTTReNTKWQNGRDVWWQDVISQYPTSCEVEW 298
Cdd:PRK13382 140 GVDTVIYDE---------EFSATVDRALADCPQ----------------ATR-IVAWTDEDHDLTVEVLIAAHAGQRPEP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 299 VDAEDPLFLLyTSGSTGKPKGVLHT-TGGYMIYTATTFKYAfdykstdvywctadcgWITGHSYVTYGPMLN--GATVVV 375
Cdd:PRK13382 194 TGRKGRVILL-TSGTTGTPKGARRSgPGGIGTLKAILDRTP----------------WRAEEPTVIVAPMFHawGFSQLV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 376 FEGAPNYP-------DPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSLRVLGSVGEPINPSAWRWFFNVV 448
Cdd:PRK13382 257 LAASLACTivtrrrfDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQF 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 449 GDSrcpISDTWWQTETGgfMI-TPLPGAWPQKPGSATFPFFGVQPVIVDEKGNEI-EGECsGYLCVKGSwpgafrTLFgd 526
Cdd:PRK13382 337 GDV---IYNNYNATEAG--MIaTATPADLRAAPDTAGRPAEGTEIRILDQDFREVpTGEV-GTIFVRND------TQF-- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 527 hERYETTYFKPF-AGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGI 605
Cdd:PRK13382 403 -DGYTSGSTKDFhDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRL 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 332006737 606 YAFVTLLEGVPYSEELRKSlvlMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILR 662
Cdd:PRK13382 482 AAFVVLKPGASATPETLKQ---HVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
131-671 |
2.62e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 123.22 E-value: 2.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 131 DKTAIHWEGNELgvdaslTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADS 210
Cdd:PRK06710 39 EKKALHFLGKDI------TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 211 LAQRIVDCKPNVILTCNAVKrgPKTINLKAI--VDAALDQSSKDGVSVGICLTYDnSLATTREN--TKWQNGRDV-WWQD 285
Cdd:PRK06710 113 LEYQLHDSGAKVILCLDLVF--PRVTNVQSAtkIEHVIVTRIADFLPFPKNLLYP-FVQKKQSNlvVKVSESETIhLWNS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 286 VISQYPTSCEVEwVDAEDPLFLL-YTSGSTGKPKGVLHTTGGYMIYTATTFKYAFDYKS-TDVYWCTADCGWITGHSYVT 363
Cdd:PRK06710 190 VEKEVNTGVEVP-CDPENDLALLqYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEgEEVVLGVLPFFHVYGMTAVM 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 364 YGPMLNGATVVVFegaPNYpDPGRCWDIVDKYKVSIFYTAPTLVRSLMrdDDKFVTRHSRKSLRVLGSVGEPINPSAWRW 443
Cdd:PRK06710 269 NLSIMQGYKMVLI---PKF-DMKMVFEAIKKHKVTLFPGAPTIYIALL--NSPLLKEYDISSIRACISGSAPLPVEVQEK 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 444 FFNVVGDSrcpISDTWWQTETGGfmITPLPGAWPQK-PGSATFPFFGVQPVIVD-EKGNEIEGECSGYLCVKGSwpgafR 521
Cdd:PRK06710 343 FETVTGGK---LVEGYGLTESSP--VTHSNFLWEKRvPGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGP-----Q 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 522 TLFGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVK 601
Cdd:PRK06710 413 IMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYR 492
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 602 GQGIYAFVTLLEGVPYSEElrkSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKIASRQLEE 671
Cdd:PRK06710 493 GETVKAFVVLKEGTECSEE---ELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEKRKNED 559
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
130-663 |
9.30e-29 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 120.48 E-value: 9.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 130 GDKTAIHWegnelgVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYL---PMLMELPIAMLACariGAVHSVVFAGF 206
Cdd:cd12118 18 PDRTSIVY------GDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLApntPAMYELHFGVPMA---GAVLNALNTRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 207 SADSLAQRIVDCKPNVILTcnavkrgpktinlkaivdaalDQSskdgvsvgicLTYDNSLATTRENTKWQngrdvWWQDv 286
Cdd:cd12118 89 DAEEIAFILRHSEAKVLFV---------------------DRE----------FEYEDLLAEGDPDFEWI-----PPAD- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 287 isqyptscevEWvdaeDPLFLLYTSGSTGKPKGVLHT-TGGYMIYTATTfkYAFDYKSTDVYWCTAD----CGWItghsy 361
Cdd:cd12118 132 ----------EW----DPIALNYTSGTTGRPKGVVYHhRGAYLNALANI--LEWEMKQHPVYLWTLPmfhcNGWC----- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 362 VTYGPMLNGATVVVFEGApnypDPGRCWDIVDKYKVSIFYTAPTlVRSLMRDDDKFVTRHSRKSLRVLgSVGEPINPS-- 439
Cdd:cd12118 191 FPWTVAAVGGTNVCLRKV----DAKAIYDLIEKHKVTHFCGAPT-VLNMLANAPPSDARPLPHRVHVM-TAGAPPPAAvl 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 440 --AWRWFFNVVgdsrcpisDTWWQTETGGFMITplpGAWpqKPGSATFP--------------FFGVQPVIVDEK----- 498
Cdd:cd12118 265 akMEELGFDVT--------HVYGLTETYGPATV---CAW--KPEWDELPteerarlkarqgvrYVGLEEVDVLDPetmkp 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 499 ----GNEIeGEC--SGYLCVKGSW--PGAFRTLFGDheryettyfkpfaGYYFSGDGCSRDKDGYYWLTGRVDDVINVSG 570
Cdd:cd12118 332 vprdGKTI-GEIvfRGNIVMKGYLknPEATAEAFRG-------------GWFHSGDLAVIHPDGYIEIKDRSKDIIISGG 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 571 HRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEElrkSLVLMVRNQIGAFAAPDRIHWAPgLPK 650
Cdd:cd12118 398 ENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEE---EIIAFCREHLAGFMVPKTVVFGE-LPK 473
|
570
....*....|...
gi 332006737 651 TRSGKIMRRILRK 663
Cdd:cd12118 474 TSTGKIQKFVLRD 486
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
145-664 |
1.44e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 120.80 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 145 DASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAqrivdckpnvil 224
Cdd:PRK07788 72 RGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLA------------ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 225 tcnavkrgpktinlkaivdaalDQSSKDGVSVgicLTYDNSLATTRENTKWQNGR-DVWWQDVISQYPTSCEVEWVD--- 300
Cdd:PRK07788 140 ----------------------EVAAREGVKA---LVYDDEFTDLLSALPPDLGRlRAWGGNPDDDEPSGSTDETLDdli 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 301 ---AEDPL--------FLLYTSGSTGKPKGVLH------TTGGyMIYTATTFKyafdykSTDVYWCTADCGWITGHSYVT 363
Cdd:PRK07788 195 agsSTAPLpkppkpggIVILTSGTTGTPKGAPRpepsplAPLA-GLLSRVPFR------AGETTLLPAPMFHATGWAHLT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 364 YGPMLnGATVVV---FegapnypDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSLRVLGSVGEPINPSA 440
Cdd:PRK07788 268 LAMAL-GSTVVLrrrF-------DPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSPEL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 441 WRWFFNVVGDSRCpisDTWWQTETGgFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGSWPgaf 520
Cdd:PRK07788 340 ATRALEAFGPVLY---NLYGSTEVA-FATIATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFP--- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 521 rtlFgdhERYETTYFKPFA-GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHE 599
Cdd:PRK07788 413 ---F---EGYTDGRDKQIIdGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDE 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332006737 600 VKGQGIYAFVTLLEGVPYSEELRKSlvlMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKI 664
Cdd:PRK07788 487 EFGQRLRAFVVKAPGAALDEDAIKD---YVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
131-661 |
5.94e-28 |
|
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: 117.76 E-value: 5.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 131 DKTAIHwegnelGVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADS 210
Cdd:cd12114 2 DATAVI------CGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 211 LAQRIVDCKPNVILTCNAVKRGPKTINLKAIVDAALDQSSKDGVSVGicltydnslattrentkwqngrdvwwqdvisqy 290
Cdd:cd12114 76 REAILADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVD--------------------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 291 ptscevewVDAEDPLFLLYTSGSTGKPKGVLHTTGGYM-IYTATTFKYA--------------FDYKSTDVYwctadcgw 355
Cdd:cd12114 123 --------VAPDDLAYVIFTSGSTGTPKGVMISHRAALnTILDINRRFAvgpddrvlalsslsFDLSVYDIF-------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 356 itghsyvtyGPMLNGATVVVFEGAPNyPDPGRCWDIVDKYKVSIFYTAPTLVRSLMrDDDKFVTRHSRkSLR-VLGSvGE 434
Cdd:cd12114 187 ---------GALSAGATLVLPDEARR-RDPAHWAELIERHGVTLWNSVPALLEMLL-DVLEAAQALLP-SLRlVLLS-GD 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 435 PIN---PSAWRWFF---NVV---GDSRCPISDTWWQtetggfmITPLPGAWPQKP-GsatFPFFGVQPVIVDEKGNEIEG 504
Cdd:cd12114 254 WIPldlPARLRALApdaRLIslgGATEASIWSIYHP-------IDEVPPDWRSIPyG---RPLANQRYRVLDPRGRDCPD 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 505 ECSGYLCVKGswPGAFRTLFGDHERYETTYFKPFAG--YYFSGD-GCSRDkDGYYWLTGRVDDVINVSGHRIGTAEVESA 581
Cdd:cd12114 324 WVPGELWIGG--RGVALGYLGDPELTAARFVTHPDGerLYRTGDlGRYRP-DGTLEFLGRRDGQVKVRGYRIELGEIEAA 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 582 LVLHPQCAEAAVVGIEhEVKGQGIYAFVTLLEGVP--YSEELRKSLVLMVRnqigAFAAPDRIHWAPGLPKTRSGKIMRR 659
Cdd:cd12114 401 LQAHPGVARAVVVVLG-DPGGKRLAAFVVPDNDGTpiAPDALRAFLAQTLP----AYMIPSRVIALEALPLTANGKVDRA 475
|
..
gi 332006737 660 IL 661
Cdd:cd12114 476 AL 477
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
131-662 |
6.27e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 118.06 E-value: 6.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 131 DKTAIHWEGNELGvdasltYSELLQRVCQLANYLKDNGVKKGDAVVIYL---PMLMELpiaMLACARIGAVHSVVFAGFS 207
Cdd:PRK06145 17 DRAALVYRDQEIS------YAEFHQRILQAAGMLHARGIGQGDVVALLMknsAAFLEL---AFAASYLGAVFLPINYRLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 208 ADSLAQRIVDCKPNVILTCNAVKRGPKTINLKAIVDAALDQSSKdgvsvgicltydnslattrentkwqngrdvwwqdVI 287
Cdd:PRK06145 88 ADEVAYILGDAGAKLLLVDEEFDAIVALETPKIVIDAAAQADSR----------------------------------RL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 288 SQYPTSCEVEWVDAEDPLF-LLYTSGSTGKPKGVLHTTGGymiytattfkyaFDYKSTDVywcTADCGWITGHSYVTYGP 366
Cdd:PRK06145 134 AQGGLEIPPQAAVAPTDLVrLMYTSGTTDRPKGVMHSYGN------------LHWKSIDH---VIALGLTASERLLVVGP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 367 M-------LNGATVVVFEGA----PNYpDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFvtRHSRKSLRVLGSVGEP 435
Cdd:PRK06145 199 LyhvgafdLPGIAVLWVGGTlrihREF-DPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRD--RFDLDSLAWCIGGGEK 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 436 INPSAWRWFFNVVGDSRcpISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGs 515
Cdd:PRK06145 276 TPESRIRDFTRVFTRAR--YIDAYGLTETCSGDTLMEAGREIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRG- 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 516 wPGAFRTLFGDHERYETTYFkpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVG 595
Cdd:PRK06145 353 -PKVTKGYWKDPEKTAEAFY---GDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIG 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332006737 596 IEHEVKGQGIYAFVTLLEGVPYS-EELRKSlvlmVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILR 662
Cdd:PRK06145 429 VHDDRWGERITAVVVLNPGATLTlEALDRH----CRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
301-662 |
8.46e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 117.80 E-value: 8.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 301 AEDPL--FLLYTSGSTGKPKGV--------LHTTGGYMIYTATTFkyaFDYKSTDVYWCTADcgwITGHSYVTYGPMLN- 369
Cdd:PRK13390 145 TEQPCgaVMLYSSGTTGFPKGIqpdlpgrdVDAPGDPIVAIARAF---YDISESDIYYSSAP---IYHAAPLRWCSMVHa 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 370 -GATVVVfegAPNYpDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSLRVLGSVGEPINPSAWRWFFNVV 448
Cdd:PRK13390 219 lGGTVVL---AKRF-DAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWL 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 449 GdsrcPISDTWWQ-TETGGFMITPLPgAWPQKPGSATFPFFGVQPvIVDEKGNEI-EGECSGYLCVKGSWPgaFRTLFGD 526
Cdd:PRK13390 295 G----PIVYEYYSsTEAHGMTFIDSP-DWLAHPGSVGRSVLGDLH-ICDDDGNELpAGRIGTVYFERDRLP--FRYLNDP 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 527 HERYETTY-FKPFagYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGI 605
Cdd:PRK13390 367 EKTAAAQHpAHPF--WTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQV 444
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 332006737 606 YAFVTLLEGVPYSEELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILR 662
Cdd:PRK13390 445 KAVIQLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
577-655 |
5.75e-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: 104.16 E-value: 5.75e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332006737 577 EVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVpysEELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGK 655
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGV---ELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
131-663 |
8.41e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 115.26 E-value: 8.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 131 DKTAIHWEGNelgvdaSLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADS 210
Cdd:PRK07786 32 DAPALRFLGN------TTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 211 LAQRIVDCKPNVILT-------CNAVKRGPKTINLKAIVDAAldqsSKDGVsvgicLTYDNSLAttrentkwQNGRDVWW 283
Cdd:PRK07786 106 IAFLVSDCGAHVVVTeaalapvATAVRDIVPLLSTVVVAGGS----SDDSV-----LGYEDLLA--------EAGPAHAP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 284 QDVisqyptscevewvdAED-PLFLLYTSGSTGKPKG-VL-HTTggyMIYTATTFKYAFDY-KSTDVYWCTADCGWITGH 359
Cdd:PRK07786 169 VDI--------------PNDsPALIMYTSGTTGRPKGaVLtHAN---LTGQAMTCLRTNGAdINSDVGFVGVPLFHIAGI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 360 SYVTYGPMLNGATVVVFEGAPnypDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDkfvTRHSRKSLRVLGSVGEPINPS 439
Cdd:PRK07786 232 GSMLPGLLLGAPTVIYPLGAF---DPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQ---ARPRDLALRVLSWGAAPASDT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 440 AWRWFFNVVGDSRcpISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGSwpga 519
Cdd:PRK07786 306 LLRQMAATFPEAQ--ILAAFGQTEMSPVTCMLLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAP---- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 520 frTLFGDHERYETTYFKPFAGYYF-SGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEH 598
Cdd:PRK07786 380 --TLMSGYWNNPEATAEAFAGGWFhSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRAD 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332006737 599 EVKGQGIYAFVTLLEGvpySEELR-KSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRK 663
Cdd:PRK07786 458 EKWGEVPVAVAAVRND---DAALTlEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRE 520
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
147-664 |
8.53e-27 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 115.32 E-value: 8.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 147 SLTYSELLQRVCQLANYLKDN-GVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPnvilt 225
Cdd:PLN02574 66 SISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSV----- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 226 cnavkrgpktinlkAIVDAALDQSSKDGvSVGIcltydnSLATTRENTKWQNGRDVW--WQDVISQYPTSCEVEWVDAED 303
Cdd:PLN02574 141 --------------GLAFTSPENVEKLS-PLGV------PVIGVPENYDFDSKRIEFpkFYELIKEDFDFVPKPVIKQDD 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 304 PLFLLYTSGSTGKPKGVLHTTGGY--MIYTATTFKYA-FDYKSTD-VYWCTADCGWITGHSYVTYGPMLNGATVVVFEGA 379
Cdd:PLN02574 200 VAAIMYSSGTTGASKGVVLTHRNLiaMVELFVRFEASqYEYPGSDnVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRF 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 380 pnypDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDdKFVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVgdSRCPISDTW 459
Cdd:PLN02574 280 ----DASDMVKVIDRFKVTHFPVVPPILMALTKKA-KGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTL--PHVDFIQGY 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 460 WQTE-----TGGFMITPLpgawpQKPGSATFPFFGVQPVIVD-EKGNEIEGECSGYLCVKGswPGAFRTLFGDHERYETT 533
Cdd:PLN02574 353 GMTEstavgTRGFNTEKL-----SKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQG--PGVMKGYLNNPKATQST 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 534 YFKPfaGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLE 613
Cdd:PLN02574 426 IDKD--GWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQ 503
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 332006737 614 GVPYSEElrkSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKI 664
Cdd:PLN02574 504 GSTLSQE---AVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRS 551
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
145-662 |
1.09e-26 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 114.41 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 145 DASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVI- 223
Cdd:PRK12406 9 DRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 224 ----LTCNAVKRGPKTINLKAIVDAALDQSSkdgvsVGIcltyDNSLATTRENTkwqngrdVWWQDVISQYPTScevEWV 299
Cdd:PRK12406 89 ahadLLHGLASALPAGVTVLSVPTPPEIAAA-----YRI----SPALLTPPAGA-------IDWEGWLAQQEPY---DGP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 300 DAEDPLFLLYTSGSTGKPKGVLHTTGgymiyTATTFKYAFDYKSTdVYwctadcGWITGHSYVTYGPMLNGA-------- 371
Cdd:PRK12406 150 PVPQPQSMIYTSGTTGHPKGVRRAAP-----TPEQAAAAEQMRAL-IY------GLKPGIRALLTGPLYHSApnayglra 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 372 ----TVVVFEgaPNYpDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSLRVLGSVGEPINPSAWR----W 443
Cdd:PRK12406 218 grlgGVLVLQ--PRF-DPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAPCPADVKRamieW 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 444 FFNVvgdsrcpISDTWWQTETGGfMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGswPGAfrTL 523
Cdd:PRK12406 295 WGPV-------IYEYYGSTESGA-VTFATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRI--AGN--PD 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 524 FGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQ 603
Cdd:PRK12406 363 FTYHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGE 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 604 GIYAFVTLLEGVPYSEE-LRKSLvlmvRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILR 662
Cdd:PRK12406 443 ALMAVVEPQPGATLDEAdIRAQL----KARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
307-662 |
1.21e-26 |
|
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: 114.01 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 307 LLYTSGSTGKPKGVLHTTGGYMIYTATTFKYAFDykstdvywctadCGWITGHSYVTYGPM-------------LNGATV 373
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAALG------------FGPGADSVYLSPAPLyhaapfrwsmtalFMGGTL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 374 VVFEgapNYpDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSLRVLGSVGEPinpsawrwffnvvgdsrC 453
Cdd:cd05929 198 VLME---KF-DPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAP-----------------C 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 454 PIS-----DTWW---------QTETGGFmiTPLPGA-WPQKPGSATFPFFGVQPvIVDEKGNEIEGECSGYLCVKGSWPg 518
Cdd:cd05929 257 PPWvkeqwIDWGgpiiweyygGTEGQGL--TIINGEeWLTHPGSVGRAVLGKVH-ILDEDGNEVPPGEIGEVYFANGPG- 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 519 afrtlFGDHERYETTYFKPFAGYYFS-GDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIE 597
Cdd:cd05929 333 -----FEYTNDPEKTAAARNEGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVP 407
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332006737 598 HEVKGQGIYAFVTLLEGVPYSEELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILR 662
Cdd:cd05929 408 DEELGQRVHAVVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
131-668 |
7.83e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 111.59 E-value: 7.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 131 DKTAIHWEgnelgvDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVhsVVFAG--FSA 208
Cdd:PRK03640 17 DRTAIEFE------EKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAV--AVLLNtrLSR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 209 DSLAQRIVDCKPNVILTcnavkrgpktinlkaivdaalDQSSKDGVSVGICLTYDNSLATTRENTKWQngrdvwwqdvis 288
Cdd:PRK03640 89 EELLWQLDDAEVKCLIT---------------------DDDFEAKLIPGISVKFAELMNGPKEEAEIQ------------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 289 qyptscevEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMiYTATTFKYAFDYKSTDVYWCTADCGWITGHSYVTYGPML 368
Cdd:PRK03640 136 --------EEFDLDEVATIMYTSGTTGKPKGVIQTYGNHW-WSAVGSALNLGLTEDDCWLAAVPIFHISGLSILMRSVIY 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 369 nGATVVVFEGApnypDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKfvtRHSRKSLR--VLGsvGEPINPSawrwFFN 446
Cdd:PRK03640 207 -GMRVVLVEKF----DAEKINKLLQTGGVTIISVVSTMLQRLLERLGE---GTYPSSFRcmLLG--GGPAPKP----LLE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 447 VVGDSRCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEkGNEIEGECSGYLCVKGS--WPGAFRtlf 524
Cdd:PRK03640 273 QCKEKGIPVYQSYGMTETASQIVTLSPEDALTKLGSAGKPLFPCELKIEKD-GVVVPPFEEGEIVVKGPnvTKGYLN--- 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 525 gdheRYETTYfKPFA-GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQ 603
Cdd:PRK03640 349 ----REDATR-ETFQdGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQ 423
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332006737 604 GIYAFVTLLEGVPySEELRkslvLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKIASRQ 668
Cdd:PRK03640 424 VPVAFVVKSGEVT-EEELR----HFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVEEM 483
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
131-661 |
1.05e-25 |
|
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: 111.27 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 131 DKTAIHWEgnelgvDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADS 210
Cdd:cd17655 12 DHTAVVFE------DQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 211 LAQRIVDCKPNVILTCNAVKrgPKTINLKAIVDAALDQSSKDGVSvgicltydnSLAttrentkwqngrdvwwqdVISQy 290
Cdd:cd17655 86 IQYILEDSGADILLTQSHLQ--PPIAFIGLIDLLDEDTIYHEESE---------NLE------------------PVSK- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 291 ptscevewvdAEDPLFLLYTSGSTGKPKGVLHTTGG-----------YMIYTATTF----KYAFDYKSTDVYwctadcgw 355
Cdd:cd17655 136 ----------SDDLAYVIYTSGSTGKPKGVMIEHRGvvnlvewankvIYQGEHLRValfaSISFDASVTEIF-------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 356 itghsyvtyGPMLNGATVVVFEGAPNYPDPGRCwDIVDKYKVSIFYTAPTLVRSLMRDDDKfvtrhSRKSLRVLGSVGEP 435
Cdd:cd17655 198 ---------ASLLSGNTLYIVRKETVLDGQALT-QYIRQNRITIIDLTPAHLKLLDAADDS-----EGLSLKHLIVGGEA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 436 INPSAWRWFFNVVGDSrCPISDTWWQTETG-GFMITPLPGAWPQKP----GSatfPFFGVQPVIVDEKGNEIEGECSGYL 510
Cdd:cd17655 263 LSTELAKKIIELFGTN-PTITNAYGPTETTvDASIYQYEPETDQQVsvpiGK---PLGNTRIYILDQYGRPQPVGVAGEL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 511 CVKGSwpGAFRtlfGDHERYETTYFK----PFAG---YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALV 583
Cdd:cd17655 339 YIGGE--GVAR---GYLNRPELTAEKfvddPFVPgerMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLL 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 584 LHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPySEELRKSLvlmvRNQIGAFAAP------DRIhwapglPKTRSGKIM 657
Cdd:cd17655 414 QHPDIKEAVVIARKDEQGQNYLCAYIVSEKELP-VAQLREFL----ARELPDYMIPsyfiklDEI------PLTPNGKVD 482
|
....
gi 332006737 658 RRIL 661
Cdd:cd17655 483 RKAL 486
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
131-670 |
2.50e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 110.25 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 131 DKTAIHWEgnelgvDASLTYSELLQRVCQLANYLKDNGvKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADS 210
Cdd:PRK07638 16 NKIAIKEN------DRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 211 LAQRIVDCKPNVILTcNAVKRGPKTINLKAIVDaaLDQsskdgvsvgicltydnslattrentkwqngrdvwWQDVISQY 290
Cdd:PRK07638 89 LKERLAISNADMIVT-ERYKLNDLPDEEGRVIE--IDE----------------------------------WKRMIEKY 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 291 -PTSCEVEwvDAE-DPLFLLYTSGSTGKPKGVLHTTGGYMiytattfkYAFDYKSTDVYWCTADCGWITG---HSYVTYG 365
Cdd:PRK07638 132 lPTYAPIE--NVQnAPFYMGFTSGSTGKPKAFLRAQQSWL--------HSFDCNVHDFHMKREDSVLIAGtlvHSLFLYG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 366 P---MLNGATVVVFegaPNYpDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDD------DKFVT------RHSRKSLRVlg 430
Cdd:PRK07638 202 AistLYVGQTVHLM---RKF-IPNQVLDKLETENISVMYTVPTMLESLYKENrvienkMKIISsgakweAEAKEKIKN-- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 431 svgepINPSAWRWFFnvvgdsrcpisdtwWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYL 510
Cdd:PRK07638 276 -----IFPYAKLYEF--------------YGASELSFVTALVDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTV 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 511 CVKGswPGAFRTLFGDHERYETTyfkPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAE 590
Cdd:PRK07638 337 YVKS--PQFFMGYIIGGVLAREL---NADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDE 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 591 AAVVGIEHEVKGQGIYAFVtllEGVPYSEELRKslvlMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKIASRQLE 670
Cdd:PRK07638 412 IVVIGVPDSYWGEKPVAII---KGSATKQQLKS----FCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQEK 484
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
303-665 |
4.81e-25 |
|
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: 106.65 E-value: 4.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 303 DPLFLLYTSGSTGKPKGVLHTTGGyMIYTATTFKYAFDYKSTDVYWCTADCGWITGHsYVTYGPMLNGATVVVFEGAP-- 380
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAAN-LLASAAGLHSRLGFGGGDSWLLSLPLYHVGGL-AILVRSLLAGAELVLLERNQal 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 381 --NYPDPGRCWdivdkykVSIfytAPTLVRSLMRDDdkfVTRHSRKSLRVLGSVGEPINPSAWRWFfnvvGDSRCPISDT 458
Cdd:cd17630 79 aeDLAPPGVTH-------VSL---VPTQLQRLLDSG---QGPAALKSLRAVLLGGAPIPPELLERA----ADRGIPLYTT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 459 WWQTETGGfMITPLPGAWPQKPGSATfPFFGVQPVIVDEkgneiegecsGYLCVKGswpgafRTLFGDHERYETTYFKPF 538
Cdd:cd17630 142 YGMTETAS-QVATKRPDGFGRGGVGV-LLPGRELRIVED----------GEIWVGG------ASLAMGYLRGQLVPEFNE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 539 AGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPyS 618
Cdd:cd17630 204 DGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPAD-P 282
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 332006737 619 EELRKSLvlmvRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKIA 665
Cdd:cd17630 283 AELRAWL----KDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
299-663 |
5.29e-25 |
|
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: 108.20 E-value: 5.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 299 VDAEDPLFLLYTSGSTGKPKGVLHTTGGYMiYTATTFKYAFDYKSTDVYWCTADCGWITGHSYVTYGpMLNGATVVVFEG 378
Cdd:cd05912 74 VKLDDIATIMYTSGTTGKPKGVQQTFGNHW-WSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRS-VIYGMTVYLVDK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 379 ApnypDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSLrvLGsvGEPINPSawrwFFNVVGDSRCPISDT 458
Cdd:cd05912 152 F----DAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRCIL--LG--GGPAPKP----LLEQCKEKGIPVYQS 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 459 WWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGNEIE-GEcsgyLCVKGS--WPGAFRTLFGDHERYETTYF 535
Cdd:cd05912 220 YGMTETCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPPYEvGE----ILLKGPnvTKGYLNRPDATEESFENGWF 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 536 KpfagyyfSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEgv 615
Cdd:cd05912 296 K-------TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSER-- 366
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 332006737 616 PYSEElrkSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRK 663
Cdd:cd05912 367 PISEE---ELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
148-661 |
5.48e-25 |
|
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: 108.71 E-value: 5.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 148 LTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVILTcn 227
Cdd:cd17650 13 LTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLT-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 228 avkrgpktinlkaivdaaldqsskdgvsvgicltydnslattrentkwqngrdvwwqdvisqyptscevewvDAEDPLFL 307
Cdd:cd17650 91 ------------------------------------------------------------------------QPEDLAYV 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 308 LYTSGSTGKPKGVLHTTGGYM-IYTATTFKYAFDYK----------STDVYwctadcgwiTGHSYVTygpMLNGATVVVf 376
Cdd:cd17650 99 IYTSGTTGKPKGVMVEHRNVAhAAHAWRREYELDSFpvrllqmasfSFDVF---------AGDFARS---LLNGGTLVI- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 377 egAPN--YPDPGRCWDIVDKYKVSIFYTAPTLVRSLMrdddKFVTRHSRK--SLRVL--GSVGEPINPSAWRW------- 443
Cdd:cd17650 166 --CPDevKLDPAALYDLILKSRITLMESTPALIRPVM----AYVYRNGLDlsAMRLLivGSDGCKAQDFKTLAarfgqgm 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 444 -FFNVVGDSRCPISDTWWQTETGgfmitPLPGAWPQKPGSatfPFFGVQPVIVDEKGNEIEGECSGYLCVKGSwpGAFRT 522
Cdd:cd17650 240 rIINSYGVTEATIDSTYYEEGRD-----PLGDSANVPIGR---PLPNTAMYVLDERLQPQPVGVAGELYIGGA--GVARG 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 523 LFGD----HERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVgIEH 598
Cdd:cd17650 310 YLNRpeltAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVA-VRE 388
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332006737 599 EVKGQ-GIYAFVTLLEgVPYSEELRKSLVlmvrNQIGAFAAPDRIHWAPGLPKTRSGKIMRRIL 661
Cdd:cd17650 389 DKGGEaRLCAYVVAAA-TLNTAELRAFLA----KELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
142-671 |
5.53e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 109.45 E-value: 5.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 142 LGVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPN 221
Cdd:PRK06164 30 IDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRAR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 222 VIltcnAVKRGPKTINLKAIVDAALDQSSKD--GVSVgICLTYDNSLATTRentkwqnGRDVWWQDVISQYPTSCEVEWV 299
Cdd:PRK06164 110 WL----VVWPGFKGIDFAAILAAVPPDALPPlrAIAV-VDDAADATPAPAP-------GARVQLFALPDPAPPAAAGERA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 300 DAEDPLFLLY-TSGSTGKPKGVLHTTGGyMIYTATTFKYAFDYKSTDVYWCTAD-CGwITGHSYVTyGPMLNGATVV--- 374
Cdd:PRK06164 178 ADPDAGALLFtTSGTTSGPKLVLHRQAT-LLRHARAIARAYGYDPGAVLLAALPfCG-VFGFSTLL-GALAGGAPLVcep 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 375 VFEGApnypdpgRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKfvtRHSRKSLRVLGSVGepiNPSAWRWFFNVVGDSRCP 454
Cdd:PRK06164 255 VFDAA-------RTARALRRHRVTHTFGNDEMLRRILDTAGE---RADFPSARLFGFAS---FAPALGELAALARARGVP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 455 ISDTWWQTE-----TGGFMITP-----LPGAWPQKPgsatfpffGVQPVIVDEKGNEI--EGEcSGYLCVKGswPGAFRT 522
Cdd:PRK06164 322 LTGLYGSSEvqalvALQPATDPvsvriEGGGRPASP--------EARVRARDPQDGALlpDGE-SGEIEIRA--PSLMRG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 523 LFGDHERYETTyFKPfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEvkG 602
Cdd:PRK06164 391 YLDNPDATARA-LTD-DGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRD--G 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332006737 603 QGI-YAFVTLLEGVPYSEElrkSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSG---KIMRRILRKIASRQLEE 671
Cdd:PRK06164 467 KTVpVAFVIPTDGASPDEA---GLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMAQARLAA 536
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
303-658 |
1.03e-24 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 105.57 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 303 DPLFLLYTSGSTGKPKGVLHTTGGYMiytattfkYAFDYKSTDVYWCTADCGWITG---HSYVTYGPM---LNGATVVVF 376
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWI--------ESFVCNEDLFNISGEDAILAPGplsHSLFLYGAIsalYLGGTFIGQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 377 EGApnypDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDdkfVTRHSRKSLRvlgSVGEPINPSAWRWFFNVVGDSRcpIS 456
Cdd:cd17633 73 RKF----NPKSWIRKINQYNATVIYLVPTMLQALARTL---EPESKIKSIF---SSGQKLFESTKKKLKNIFPKAN--LI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 457 DTWWQTETGgfMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGNEIegecsGYLCVKGswPGAFrtlfgdhERYETTYFK 536
Cdd:cd17633 141 EFYGTSELS--FITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEI-----GKIFVKS--EMVF-------SGYVRGGFS 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 537 PFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQgIYAFVTLLEGVP 616
Cdd:cd17633 205 NPDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGE-IAVALYSGDKLT 283
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 332006737 617 YSEELRKSLVLMVRNQIgafaaPDRIHWAPGLPKTRSGKIMR 658
Cdd:cd17633 284 YKQLKRFLKQKLSRYEI-----PKKIIFVDSLPYTSSGKIAR 320
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
145-661 |
1.03e-24 |
|
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: 107.72 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 145 DASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVIL 224
Cdd:cd17652 10 DETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 225 TcnavkrgpktinlkaivdaaldqsskdgvsvgicltydnslattrentkwqngrdvwwqdvisqyptscevewvDAEDP 304
Cdd:cd17652 90 T--------------------------------------------------------------------------TPDNL 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 305 LFLLYTSGSTGKPKGVLHTTGGyMIYTATTFKYAFDYK-----------STDVY---WCTAdcgwitghsyvtygpMLNG 370
Cdd:cd17652 96 AYVIYTSGSTGRPKGVVVTHRG-LANLAAAQIAAFDVGpgsrvlqfaspSFDASvweLLMA---------------LLAG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 371 ATVVVFEGAPNYPDPGRCwDIVDKYKVSIFYTAPTLVRSLMRDDDKfvtrhsrkSLRVLGSVGEPINPS-AWRW-----F 444
Cdd:cd17652 160 ATLVLAPAEELLPGEPLA-DLLREHRITHVTLPPAALAALPPDDLP--------DLRTLVVAGEACPAElVDRWapgrrM 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 445 FNVVGDSRCPISDTWWQTETGGFMItPLPGAWPqkpgsatfpffGVQPVIVDEKGNEIEGECSGYLCVKGswPGAFRtlf 524
Cdd:cd17652 231 INAYGPTETTVCATMAGPLPGGGVP-PIGRPVP-----------GTRVYVLDARLRPVPPGVPGELYIAG--AGLAR--- 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 525 GDHERYETTYFK----PFAG----YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGI 596
Cdd:cd17652 294 GYLNRPGLTAERfvadPFGApgsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVR 373
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332006737 597 EHEVKGQGIYAFVTLLEGV-PYSEELRKSLvlmvRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRIL 661
Cdd:cd17652 374 DDRPGDKRLVAYVVPAPGAaPTAAELRAHL----AERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
145-673 |
2.35e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 109.66 E-value: 2.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 145 DASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVIL 224
Cdd:PRK12316 2026 DQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLL 2105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 225 TCNAV-KRGPKTINLKaivdaaldqsskdgvsvgiCLTYDnslattrentkwqngRDVWWQDvisqYPTSCEVEWVDAED 303
Cdd:PRK12316 2106 TQRHLlERLPLPAGVA-------------------RLPLD---------------RDAEWAD----YPDTAPAVQLAGEN 2147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 304 PLFLLYTSGSTGKPKGVLHTTGGYMIYTATTFKYafdYKSTDvywctADC--------------GWITghsyvtygPMLN 369
Cdd:PRK12316 2148 LAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGER---YELSP-----ADCelqfmsfsfdgaheQWFH--------PLLN 2211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 370 GATVVVFEGApnYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDkfVTRHsRKSLRVLGSVGEPINPSAWRWFFNVVG 449
Cdd:PRK12316 2212 GARVLIRDDE--LWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAE--RDGR-PPAVRVYCFGGEAVPAASLRLAWEALR 2286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 450 DSRcpISDTWWQTETggfMITPLpgAW---PQKPGSATFPFFGvQPV------IVDEKGNEIEGECSGYLCVKGSwpGAF 520
Cdd:PRK12316 2287 PVY--LFNGYGPTEA---VVTPL--LWkcrPQDPCGAAYVPIG-RALgnrrayILDADLNLLAPGMAGELYLGGE--GLA 2356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 521 RtlfGDHERYETTYFK----PFAG----YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAA 592
Cdd:PRK12316 2357 R---GYLNRPGLTAERfvpdPFSAsgerLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAV 2433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 593 VVGIEhEVKGQGIYAFVTlleGVPYSEELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKIASRQLEEL 672
Cdd:PRK12316 2434 VVAQD-GASGKQLVAYVV---PDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQA 2509
|
.
gi 332006737 673 G 673
Cdd:PRK12316 2510 Y 2510
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
149-674 |
3.92e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 106.96 E-value: 3.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 149 TYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVILT--- 225
Cdd:PRK08162 45 TWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVdte 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 226 -CNAVKRGPKTI-NLKAIVDAALDQSSKDGVSVGiCLTYDNSLATTRENTKWQNGRDVWwqDVISqyptscevewvdaed 303
Cdd:PRK08162 125 fAEVAREALALLpGPKPLVIDVDDPEYPGGRFIG-ALDYEAFLASGDPDFAWTLPADEW--DAIA--------------- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 304 plfLLYTSGSTGKPKGVL-HTTGGYMIYTATTFkyAFDYKSTDVY-----------WCTAdcgW-ITghsyvtygpmLNG 370
Cdd:PRK08162 187 ---LNYTSGTTGNPKGVVyHHRGAYLNALSNIL--AWGMPKHPVYlwtlpmfhcngWCFP---WtVA----------ARA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 371 ATVVVFEGApnypDPGRCWDIVDKYKVSIFYTAPtLVRSLM---RDDDKFVTRHsrkslRVLGSVGEPINPSAwrwffnV 447
Cdd:PRK08162 249 GTNVCLRKV----DPKLIFDLIREHGVTHYCGAP-IVLSALinaPAEWRAGIDH-----PVHAMVAGAAPPAA------V 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 448 VGdsrcpisdtwwQTETGGFMITPLPG-----------AWpqKPGSATFPFF---------GV----------------Q 491
Cdd:PRK08162 313 IA-----------KMEEIGFDLTHVYGltetygpatvcAW--QPEWDALPLDeraqlkarqGVryplqegvtvldpdtmQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 492 PVIVDekgNEIEGEC--SGYLCVKGswpgafrtlfgdheryettYFK-------PFAGYYF-SGDGCSRDKDGYYWLTGR 561
Cdd:PRK08162 380 PVPAD---GETIGEImfRGNIVMKG-------------------YLKnpkateeAFAGGWFhTGDLAVLHPDGYIKIKDR 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 562 VDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEElrkSLVLMVRNQIGAFAAPDR 641
Cdd:PRK08162 438 SKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEE---EIIAHCREHLAGFKVPKA 514
|
570 580 590
....*....|....*....|....*....|...
gi 332006737 642 IHWAPgLPKTRSGKIMRRILRKIAsRQLEELGD 674
Cdd:PRK08162 515 VVFGE-LPKTSTGKIQKFVLREQA-KSLKAIDL 545
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
147-670 |
5.54e-24 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 106.61 E-value: 5.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 147 SLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVhsVVFAGFSADSL-----AQRIvdcKPN 221
Cdd:PRK10946 48 QFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNALFSHQRSelnayASQI---EPA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 222 VILtcnaVKRGPKTINLKAIVDAALDQSSKDGVSVGICLTYDNSLATTREntkwQNGRDVWWQdvisqyPTScevewvdA 301
Cdd:PRK10946 123 LLI----ADRQHALFSDDDFLNTLVAEHSSLRVVLLLNDDGEHSLDDAIN----HPAEDFTAT------PSP-------A 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 302 EDPLFLLYTSGSTGKPKGVLHTTGGYmiytattfkyafDY---KSTDVYWCTAD----CGWITGHSYVTYGP-----MLN 369
Cdd:PRK10946 182 DEVAFFQLSGGSTGTPKLIPRTHNDY------------YYsvrRSVEICGFTPQtrylCALPAAHNYPMSSPgalgvFLA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 370 GATVVVfegAPNyPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVG 449
Cdd:PRK10946 250 GGTVVL---APD-PSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKLLQVGGARLSETLARRIPAELG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 450 dsrCPIS----------------DTWWQT-ETGGFMITPLPGAWpqkpgsatfpffgvqpvIVDEKGNEI-EGEcSGYLC 511
Cdd:PRK10946 326 ---CQLQqvfgmaeglvnytrldDSDERIfTTQGRPMSPDDEVW-----------------VADADGNPLpQGE-VGRLM 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 512 VKGswPGAFRTLFGDHErYETTYFKPfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEA 591
Cdd:PRK10946 385 TRG--PYTFRGYYKSPQ-HNASAFDA-NGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHA 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 592 AVVGIEHEVKGQGIYAFVTLLEGVPySEELRKSLvlmvRNQ-IGAFAAPDRIHWAPGLPKTRSGKIMRRILRKIASRQLE 670
Cdd:PRK10946 461 ALVSMEDELMGEKSCAFLVVKEPLK-AVQLRRFL----REQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLASRAS 535
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
130-595 |
5.55e-24 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 106.72 E-value: 5.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 130 GDKTAIHWEgnELGVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAD 209
Cdd:COG1022 25 PDRVALREK--EDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 210 SLAQRIVDCKPNVILTCNA------VKRGPKTINLKAIVdaALDQssKDGVSVGICLTYDNSLATtrentkwqnGRDVWW 283
Cdd:COG1022 103 EVAYILNDSGAKVLFVEDQeqldklLEVRDELPSLRHIV--VLDP--RGLRDDPRLLSLDELLAL---------GREVAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 284 QDVISQYPTScevewVDAEDPLFLLYTSGSTGKPKGVLHTTGGyMIYTATTFKYAFDYKSTDVY-----WCtadcgWITG 358
Cdd:COG1022 170 PAELEARRAA-----VKPDDLATIIYTSGTTGRPKGVMLTHRN-LLSNARALLERLPLGPGDRTlsflpLA-----HVFE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 359 HSyVTYGPMLNGATVVVFEGAPNYPD-------------PgRCW-----DIVDK------YKVSIFYTA----------- 403
Cdd:COG1022 239 RT-VSYYALAAGATVAFAESPDTLAEdlrevkptfmlavP-RVWekvyaGIQAKaeeaggLKRKLFRWAlavgrryarar 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 404 ------PTLVRSLMRDDDKFVTRHSRKSL----RVLGSVGEPINPSAWRwFFNVVGdsrCPISDTWWQTETGGFMITPLP 473
Cdd:COG1022 317 lagkspSLLLRLKHALADKLVFSKLREALggrlRFAVSGGAALGPELAR-FFRALG---IPVLEGYGLTETSPVITVNRP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 474 GAwpQKPGSATFPFFGVQpVIVDEKGnEIegecsgylCVKGswPGAFRTLFGDHEryETTyfKPFA--GYYFSGD-GcSR 550
Cdd:COG1022 393 GD--NRIGTVGPPLPGVE-VKIAEDG-EI--------LVRG--PNVMKGYYKNPE--ATA--EAFDadGWLHTGDiG-EL 453
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 332006737 551 DKDGYYWLTGRVDDVINVS-GHRIGTAEVESALVLHPQCAEAAVVG 595
Cdd:COG1022 454 DEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
145-693 |
6.13e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 108.32 E-value: 6.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 145 DASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVIL 224
Cdd:PRK12467 3118 DQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLL 3197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 225 TCNAV-KRGPKTINLKAIVdaaLDqsskdgvsvgicltydnslattrentkwqngRDVWWQdvisqYPTSCEVEWVDAED 303
Cdd:PRK12467 3198 TQAHLlEQLPAPAGDTALT---LD-------------------------------RLDLNG-----YSENNPSTRVMGEN 3238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 304 PLFLLYTSGSTGKPKGV--------LHTTGGYMIY--TATT-----FKYAFDYKSTDVYWctadcgwitghsyvtygPML 368
Cdd:PRK12467 3239 LAYVIYTSGSTGKPKGVgvrhgalaNHLCWIAEAYelDANDrvllfMSFSFDGAQERFLW-----------------TLI 3301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 369 NGATVVVfegAPNYP-DPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDkfvtRHSRKSLRVLGSVGEPINPSAW------ 441
Cdd:PRK12467 3302 CGGCLVV---RDNDLwDPEELWQAIHAHRISIACFPPAYLQQFAEDAG----GADCASLDIYVFGGEAVPPAAFeqvkrk 3374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 442 ---RWFFNVVGDSRCPISDTWWQTETGGfmiTPLPGAWPqkpgsATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGSwpG 518
Cdd:PRK12467 3375 lkpRGLTNGYGPTEAVVTVTLWKCGGDA---VCEAPYAP-----IGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGV--G 3444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 519 AFRtlfGDHERYETTYFK----PFAG----YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAE 590
Cdd:PRK12467 3445 LAR---GYHQRPSLTAERfvadPFSGsggrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVRE 3521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 591 AAVVGIEHEvKGQGIYAFVTL-LEGVPYSEELRKSLvlmvRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKIASRQL 669
Cdd:PRK12467 3522 AVVLARDGA-GGKQLVAYVVPaDPQGDWRETLRDHL----AASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGS 3596
|
570 580
....*....|....*....|....*.
gi 332006737 670 EELgdtstLADPSVVDQLIAL--ADV 693
Cdd:PRK12467 3597 REY-----VAPRSEVEQQLAAiwADV 3617
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
145-663 |
8.17e-24 |
|
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: 105.59 E-value: 8.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 145 DASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVIL 224
Cdd:cd05915 22 VHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 225 tcnavkrgpktinlkaiVDAALDQSSKDGVSVgicltydnsLATTRENTKWQNGRDVWWQDVISQYPTSCEVEWVDAEDP 304
Cdd:cd05915 102 -----------------FDPNLLPLVEAIRGE---------LKTVQHFVVMDEKAPEGYLAYEEALGEEADPVRVPERAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 305 LFLLYTSGSTGKPKGVLHT-TGGYMIYTATTFKYAFDYKSTDVYWCTADCGWITGHSYVTYGPMLNGATVVVFEgapnYP 383
Cdd:cd05915 156 CGMAYTTGTTGLPKGVVYShRALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGP----RL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 384 DPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKfVTRHSRKSLRVLGSVGEPinPSAWRWF-----FNVVGDSRCP---- 454
Cdd:cd05915 232 DPASLVELFDGEGVTFTAGVPTVWLALADYLES-TGHRLKTLRRLVVGGSAA--PRSLIARfermgVEVRQGYGLTetsp 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 455 --ISDTW---WQT--ETGGFMITPLPG-------AWPQKPGSATFPFFGVQPVIVDEKGNEIegeCSGYlcvkgswpgaf 520
Cdd:cd05915 309 vvVQNFVkshLESlsEEEKLTLKAKTGlpiplvrLRVADEEGRPVPKDGKALGEVQLKGPWI---TGGY----------- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 521 rtlFGDHERYETTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEV 600
Cdd:cd05915 375 ---YGNEEATRSALTP--DGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPK 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332006737 601 KGQGIYAFVTLLEGVPYSEElrksLVLMVRNQIGAFAA-PDRIHWAPGLPKTRSGKIMRRILRK 663
Cdd:cd05915 450 WQERPLAVVVPRGEKPTPEE----LNEHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
121-671 |
1.64e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 105.08 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 121 LDKNVeAGLGDKTAIHWEGnelgvdASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAV-- 198
Cdd:PRK05605 38 YDNAV-ARFGDRPALDFFG------ATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVvv 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 199 -HS------------------VVFAGFSADSLAQRIV-DCKPNVILTCNAVKRGP--KTINLKAIVDAALDQSSKDGVSV 256
Cdd:PRK05605 111 eHNplytahelehpfedhgarVAIVWDKVAPTVERLRrTTPLETIVSVNMIAAMPllQRLALRLPIPALRKARAALTGPA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 257 GICLTYDNSLATTRentkwqnGRDvwwqDVISQYPTscevewVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMiytattfk 336
Cdd:PRK05605 191 PGTVPWETLVDAAI-------GGD----GSDVSHPR------PTPDDVALILYTSGTTGKPKGAQLTHRNLF-------- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 337 yafdykstdvywCTADCG--WITG---------------HSY-----VTYGPMLnGATVVVFegaPNyPDPGRCWDIVDK 394
Cdd:PRK05605 246 ------------ANAAQGkaWVPGlgdgpervlaalpmfHAYgltlcLTLAVSI-GGELVLL---PA-PDIDLILDAMKK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 395 YKVSIFYTAPTLVRSLMRdddkfVTRHSRKSLrvlgsvgepinpSAWRWFFNvvGDSRCPISDT-WWQTETGGFMI---- 469
Cdd:PRK05605 309 HPPTWLPGVPPLYEKIAE-----AAEERGVDL------------SGVRNAFS--GAMALPVSTVeLWEKLTGGLLVegyg 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 470 ----TPLPGAWP----QKPGSATFPFFGVQPVIVD-EKGNEI--EGEcSGYLCVKGswPGAFRtlfGDHERYETTYFKPF 538
Cdd:PRK05605 370 ltetSPIIVGNPmsddRRPGYVGVPFPDTEVRIVDpEDPDETmpDGE-EGELLVRG--PQVFK---GYWNRPEETAKSFL 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 539 AGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYS 618
Cdd:PRK05605 444 DGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALD 523
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 332006737 619 EE-LRKSLvlmvRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKIASRQLEE 671
Cdd:PRK05605 524 PEgLRAYC----REHLTRYKVPRRFYHVDELPRDQLGKVRRREVREELLEKLGA 573
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
148-671 |
2.45e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 106.58 E-value: 2.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 148 LTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVILT-C 226
Cdd:PRK12316 4577 LTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTqS 4656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 227 NAVKRGPktinlkaivdaaldqsSKDGVSvgiCLTYDnslattrentkwqngRDVWWQDvisqYPTSCEVEWVDAEDPLF 306
Cdd:PRK12316 4657 HLLQRLP----------------IPDGLA---SLALD---------------RDEDWEG----FPAHDPAVRLHPDNLAY 4698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 307 LLYTSGSTGKPKGVLHTTGGYMIYTATTFKYafdykstdvYWCTADCGWITGHSYV-------TYGPMLNGATVVVfeGA 379
Cdd:PRK12316 4699 VIYTSGSTGRPKGVAVSHGSLVNHLHATGER---------YELTPDDRVLQFMSFSfdgshegLYHPLINGASVVI--RD 4767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 380 PNYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKfvtRHSRKSLRVLGSVGEPINPS----AWR-----WFFNVVGD 450
Cdd:PRK12316 4768 DSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAER---DGEPPSLRVYCFGGEAVAQAsydlAWRalkpvYLFNGYGP 4844
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 451 SRCPISDTWWQTETGgfmitplpgawpQKPGSATFPFFGVQP----VIVDEKGNEIEGECSG--YLCVKGSWPGAFRTLF 524
Cdd:PRK12316 4845 TETTVTVLLWKARDG------------DACGAAYMPIGTPLGnrsgYVLDGQLNPLPVGVAGelYLGGEGVARGYLERPA 4912
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 525 GDHERYETTYF-KPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVkGQ 603
Cdd:PRK12316 4913 LTAERFVPDPFgAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAV-GK 4991
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332006737 604 GIYAFVT-----LLEGVPYSEELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKIASRQLEE 671
Cdd:PRK12316 4992 QLVGYVVpqdpaLADADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQ 5064
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
147-665 |
7.36e-23 |
|
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: 102.41 E-value: 7.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 147 SLTYSELLQRVCQLANYLKDNgVKKGDAVVIYLPMLMELPIAMLACARIGAVhsVVFAGFSADSLAQR--IVDCKPNVIL 224
Cdd:cd05909 7 SLTYRKLLTGAIALARKLAKM-TKEGENVGVMLPPSAGGALANFALALSGKV--PVMLNYTAGLRELRacIKLAGIKTVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 225 TCnavKRGPKTINLKAIVDAALDQ------------SSKDGVSVGICLTYdnslattrentkwqngRDVWWqdvISQYPT 292
Cdd:cd05909 84 TS---KQFIEKLKLHHLFDVEYDArivyledlrakiSKADKCKAFLAGKF----------------PPKWL---LRIFGV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 293 SCevewVDAEDPLFLLYTSGSTGKPKGVLHTTGGYM--IYTATTFkyaFDYKSTDVYwctadCGWITG-HSY----VTYG 365
Cdd:cd05909 142 AP----VQPDDPAVILFTSGSEGLPKGVVLSHKNLLanVEQITAI---FDPNPEDVV-----FGALPFfHSFgltgCLWL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 366 PMLNGATVVVfegAPNYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRdddkFVTRHSRKSLRVLGSVGEPINPSAWRWFF 445
Cdd:cd05909 210 PLLSGIKVVF---HPNPLDYKKIPELIYDKKATILLGTPTFLRGYAR----AAHPEDFSSLRLVVAGAEKLKDTLRQEFQ 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 446 NVVGdsrCPISDTWWQTETGGFMITPLPGAwPQKPGSATFPFFGVQPVIVDEKGNE--IEGEcSGYLCVKGswPGAFRTL 523
Cdd:cd05909 283 EKFG---IRILEGYGTTECSPVISVNTPQS-PNKEGTVGRPLPGMEVKIVSVETHEevPIGE-GGLLLVRG--PNVMLGY 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 524 FGDHERyetTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESAL-VLHPQCAEAAVVGIEHEVKG 602
Cdd:cd05909 356 LNEPEL---TSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILsEILPEDNEVAVVSVPDGRKG 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332006737 603 QGIYAFVTLLEGVPyseelrKSLVLMVRN-QIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKIA 665
Cdd:cd05909 433 EKIVLLTTTTDTDP------SSLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
302-655 |
8.24e-23 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 100.53 E-value: 8.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 302 EDPLFLLYTSGSTGKPKGVLHTTG--GYMIYTATTFKYAFDYKSTDVYWCTAD---------CGWITGHSYVTYGPMLNG 370
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGVMWRQEdiFRMLMGGADFGTGEFTPSEDAHKAAAAaagtvmfpaPPLMHGTGSWTAFGGLLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 371 ATVVVFEGaPNYpDPGRCWDIVDKYKV-SIFYTAPTLVRSLMrddDKFVTRHSR--KSLRVLGSVGEPINPSAWRWFFNV 447
Cdd:cd05924 83 GQTVVLPD-DRF-DPEEVWRTIEKHKVtSMTIVGDAMARPLI---DALRDAGPYdlSSLFAISSGGALLSPEVKQGLLEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 448 VGDSRcpISDTWWQTETGgFMITPLPGawPQKPGSATFPFFGVQPVIVDEKGNEIE--GECSGYLCVKGSWPGAFrtlFG 525
Cdd:cd05924 158 VPNIT--LVDAFGSSETG-FTGSGHSA--GSGPETGPFTRANPDTVVLDDDGRVVPpgSGGVGWIARRGHIPLGY---YG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 526 DHERYETTyFKPFAG--YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQ 603
Cdd:cd05924 230 DEAKTAET-FPEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQ 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 332006737 604 GIYAFVTLLEGVPYSEElrkSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGK 655
Cdd:cd05924 309 EVVAVVQLREGAGVDLE---ELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
303-658 |
1.00e-22 |
|
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: 100.04 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 303 DPLFLLYTSGSTGKPKGVLHTTGGyMIYTATTFKYAFDYKSTDVYWCTADCGWITGHSYVTYGPMLNGATVVV--Fegap 380
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGN-LIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMekF---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 381 nypDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKfvTRHSRKSLRVLGSVGEPINPSAWRwffnvvgdSRCPisDTWW 460
Cdd:cd17637 76 ---DPAEALELIEEEKVTLMGSFPPILSNLLDAAEK--SGVDLSSLRHVLGLDAPETIQRFE--------ETTG--ATFW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 461 ----QTETGGFmITPLPGAwpQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGswPGAFRTLFGDHERYETTYFK 536
Cdd:cd17637 141 slygQTETSGL-VTLSPYR--ERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRG--PLVFQGYWNLPELTAYTFRN 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 537 pfaGYYFSGDGCSRDKDGYYWLTGRV--DDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEG 614
Cdd:cd17637 216 ---GWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPG 292
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 332006737 615 VPYSEElrkSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMR 658
Cdd:cd17637 293 ATLTAD---ELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
148-661 |
1.49e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 103.88 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 148 LTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVILTCN 227
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQS 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 228 AVKRgpktinlKAIVDAALDQsskdgvsvgicLTYDNSlattrenTKWQNGrdvwwqdvisqYPTSCEVEWVDAEDPLFL 307
Cdd:PRK12316 617 HLGR-------KLPLAAGVQV-----------LDLDRP-------AAWLEG-----------YSEENPGTELNPENLAYV 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 308 LYTSGSTGKPKGVLHTTGG---YMIYTATTFK------------YAFDYKSTDVYWctadcgwitghsyvtygPMLNGAT 372
Cdd:PRK12316 661 IYTSGSTGKPKGAGNRHRAlsnRLCWMQQAYGlgvgdtvlqktpFSFDVSVWEFFW-----------------PLMSGAR 723
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 373 VVVfEGAPNYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKfvtrHSRKSLRVLGSVGEPINPSAW------RW--- 443
Cdd:PRK12316 724 LVV-AAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDV----ASCTSLRRIVCSGEALPADAQeqvfakLPqag 798
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 444 FFNVVGDSRCPISDTWWQTETGGFMITPLpGAwpqkpgsatfPFFGVQPVIVDEKGNEIEGECSGYLCVKGSwpGAFRTL 523
Cdd:PRK12316 799 LYNLYGPTEAAIDVTHWTCVEEGGDSVPI-GR----------PIANLACYILDANLEPVPVGVLGELYLAGR--GLARGY 865
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 524 FG----DHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEhe 599
Cdd:PRK12316 866 HGrpglTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD-- 943
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332006737 600 vkGQGIYAFVtllegVPYSE--ELRKSLVLMVRNQIGAFAAPDriHWAP--GLPKTRSGKIMRRIL 661
Cdd:PRK12316 944 --GKQLVGYV-----VLESEggDWREALKAHLAASLPEYMVPA--QWLAleRLPLTPNGKLDRKAL 1000
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
149-663 |
1.51e-22 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 102.14 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 149 TYSELLQRVCQLANYLKDNGVKKGDAVviylpmlmelpiAMLA--CAR----------IGAVHSVVFAGFSADSLAQRIV 216
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRV------------ATIAwnTWRhleawygimgIGAICHTVNPRLFPEQIAWIIN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 217 DCKPNVILTcnavkrgpkTINLKAIVDAALDQSSKdgVSVGICLTYDNSL-ATTRENTkwqngrdVWWQDVISQYPTSCE 295
Cdd:PRK06018 109 HAEDRVVIT---------DLTFVPILEKIADKLPS--VERYVVLTDAAHMpQTTLKNA-------VAYEEWIAEADGDFA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 296 VEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMIYT-ATTFKYAFDYKSTDVY-----------WCTADCGWITGHSYVT 363
Cdd:PRK06018 171 WKTFDENTAAGMCYTSGTTGDPKGVLYSHRSNVLHAlMANNGDALGTSAADTMlpvvplfhansWGIAFSAPSMGTKLVM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 364 YGPMLNGATVvvfegapnypdpgrcWDIVDKYKVSIFYTAPTLVRSLMRDDDKfvtrhSRKSLRVLGSVgepinpsawrw 443
Cdd:PRK06018 251 PGAKLDGASV---------------YELLDTEKVTFTAGVPTVWLMLLQYMEK-----EGLKLPHLKMV----------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 444 ffnVVGDSRCPIS-------------DTWWQTETGGF-MITPLPGAWPQKPGSAT--------FPFFGVQPVIVDEKGNE 501
Cdd:PRK06018 300 ---VCGGSAMPRSmikafedmgvevrHAWGMTEMSPLgTLAALKPPFSKLPGDARldvlqkqgYPPFGVEMKITDDAGKE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 502 I--EGECSGYLCVKGswPGAFRTLFgdheRYETTYFKPfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVE 579
Cdd:PRK06018 377 LpwDGKTFGRLKVRG--PAVAAAYY----RVDGEILDD-DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 580 SALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGV-PYSEELRKSLvlmvRNQIGAFAAPDRIHWAPGLPKTRSGKIMR 658
Cdd:PRK06018 450 NLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGEtATREEILKYM----DGKIAKWWMPDDVAFVDAIPHTATGKILK 525
|
....*
gi 332006737 659 RILRK 663
Cdd:PRK06018 526 TALRE 530
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
477-662 |
1.77e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 101.22 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 477 PQKPGSATFPFFGVQPVIVDEKGNEI--EGECSGYLCVKGSwpgafrTLF-GDHERYETT--YFKPfAGYYFSGDGCSRD 551
Cdd:PRK07787 289 ERRPGWVGLPLAGVETRLVDEDGGPVphDGETVGELQVRGP------TLFdGYLNRPDATaaAFTA-DGWFRTGDVAVVD 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 552 KDGYYWLTGRVD-DVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEelrksLVLMVR 630
Cdd:PRK07787 362 PDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAADE-----LIDFVA 436
|
170 180 190
....*....|....*....|....*....|..
gi 332006737 631 NQIGAFAAPDRIHWAPGLPKTRSGKIMRRILR 662
Cdd:PRK07787 437 QQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
147-595 |
4.43e-22 |
|
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: 99.59 E-value: 4.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 147 SLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVIltc 226
Cdd:cd05907 5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 227 navkrgpktinlkaIVDaaldqsskdgvsvgicltydnslattrentkwqngrdvwwqdvisqyptscevewvDAEDPLF 306
Cdd:cd05907 82 --------------FVE--------------------------------------------------------DPDDLAT 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 307 LLYTSGSTGKPKGVLHTTGGYMiYTATTFKYAFDYKSTDVYWCTADCGWITGHSYVTYGPMLNGATVVVFEGAPNYPDpg 386
Cdd:cd05907 92 IIYTSGTTGRPKGVMLSHRNIL-SNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLLD-- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 387 rcwDIVdKYKVSIFYTAPTL---VRSLMRDDD------KFVTRHSRKSLRVLGSVGEPINPSAWRwFFNVVGdsrCPISD 457
Cdd:cd05907 169 ---DLS-EVRPTVFLAVPRVwekVYAAIKVKAvpglkrKLFDLAVGGRLRFAASGGAPLPAELLH-FFRALG---IPVYE 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 458 TWWQTETGGFMITPLPGAWpqKPGSATFPFFGVQPVIVDekgneiEGEcsgyLCVKGswPGAFRTLFGDHEryETTYFKP 537
Cdd:cd05907 241 GYGLTETSAVVTLNPPGDN--RIGTVGKPLPGVEVRIAD------DGE----ILVRG--PNVMLGYYKNPE--ATAEALD 304
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 332006737 538 FAGYYFSGDGCSRDKDGYYWLTGRVDDVI-NVSGHRIGTAEVESALVLHPQCAEAAVVG 595
Cdd:cd05907 305 ADGWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
127-663 |
6.68e-22 |
|
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: 100.01 E-value: 6.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 127 AGLGDKTAIHWEGNELGVDASLTYSELLQRVCQLANYLKDNGvKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFA-- 204
Cdd:cd05931 4 AARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPpt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 205 -GFSADSLAQRIVDCKPNVILTCNAVKRGpktinlkaiVDAALDQSSKDGVSVGICLTydnSLATTRENTkwqngrdvwW 283
Cdd:cd05931 83 pGRHAERLAAILADAGPRVVLTTAAALAA---------VRAFAASRPAAGTPRLLVVD---LLPDTSAAD---------W 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 284 QDVIsqyptscevewVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMIYTATTFK-YAFDYKSTDVYW--CTADCGWITGhs 360
Cdd:cd05931 142 PPPS-----------PDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRaYGLDPGDVVVSWlpLYHDMGLIGG-- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 361 yvTYGPMLNGATVVVFegAPNY--PDPGRcW-DIVDKYKVSIFYtAPT----LVRSLMRDDDKFVTRHSrkSLRVLGSVG 433
Cdd:cd05931 209 --LLTPLYSGGPSVLM--SPAAflRRPLR-WlRLISRYRATISA-APNfaydLCVRRVRDEDLEGLDLS--SWRVALNGA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 434 EPINPSAWRWFFN--------------------------VVGDSRCPISDTWWQTETGGfmitPLPGAWPQKPGSATF-- 485
Cdd:cd05931 281 EPVRPATLRRFAEafapfgfrpeafrpsyglaeatlfvsGGPPGTGPVVLRVDRDALAG----RAVAVAADDPAARELvs 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 486 ---PFFGVQPVIVDEKGNE-----IEGE--------CSGYLCVKGSWPGAFRTLFGDHERyettyfkpfaGYYFSGD-GC 548
Cdd:cd05931 357 cgrPLPDQEVRIVDPETGRelpdgEVGEiwvrgpsvASGYWGRPEATAETFGALAATDEG----------GWLRTGDlGF 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 549 SRDkdGYYWLTGRVDDVINVSGHRIGTAEVESAL-----VLHPQCAEAAVVGIEHEVKGqGIYAFVTLLEGVPYSEELRK 623
Cdd:cd05931 427 LHD--GELYITGRLKDLIIVRGRNHYPQDIEATAeeahpALRPGCVAAFSVPDDGEERL-VVVAEVERGADPADLAAIAA 503
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 332006737 624 SLVLMVRNQIGafAAPDRIHWAP--GLPKTRSGKIMRRILRK 663
Cdd:cd05931 504 AIRAAVAREHG--VAPADVVLVRpgSIPRTSSGKIQRRACRA 543
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
145-693 |
6.70e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 101.96 E-value: 6.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 145 DASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVIL 224
Cdd:PRK12316 3080 EQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLL 3159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 225 TcnavkrgpktinlkaivDAALDQSSKDGVSVgICLTYDNSlattrentkwqngrdvwwqdvisQYPTSCEVEWVDAEDP 304
Cdd:PRK12316 3160 S-----------------QSHLRLPLAQGVQV-LDLDRGDE-----------------------NYAEANPAIRTMPENL 3198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 305 LFLLYTSGSTGKPKGVLHTTGGYMIYT-ATTFKYAFDYKSTDVYWCTADcgwITGHSYVTYGPMLNGATVVVfEGAPNYP 383
Cdd:PRK12316 3199 AYVIYTSGSTGKPKGVGIRHSALSNHLcWMQQAYGLGVGDRVLQFTTFS---FDVFVEELFWPLMSGARVVL-AGPEDWR 3274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 384 DPGRCWDIVDKYKVSIfytaPTLVRSLMRDDDKFVTRHSRKSLRVLGSVGEPINPS-AWRWF-----FNVVGDSRCPISD 457
Cdd:PRK12316 3275 DPALLVELINSEGVDV----LHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADlQQQVFaglplYNLYGPTEATITV 3350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 458 TWWQTETGGFMITPLPGAWPQKpgSATFPFFGVQPVIVDEKGNEiegecsgYLCVKGSWPGAFRTLFGDHERYETTYFKP 537
Cdd:PRK12316 3351 THWQCVEEGKDAVPIGRPIANR--ACYILDGSLEPVPVGALGEL-------YLGGEGLARGYHNRPGLTAERFVPDPFVP 3421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 538 FAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVgiehEVKGQGIYAFVTLLEGVPy 617
Cdd:PRK12316 3422 GERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYVVPEDEAG- 3496
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332006737 618 seELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKIASRQLEelgdTSTLADPSVVDQLIA--LADV 693
Cdd:PRK12316 3497 --DLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQ----QDYVAPVNELERRLAaiWADV 3568
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
127-673 |
7.31e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 99.85 E-value: 7.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 127 AGLGDKTAIHWEGNELGV----DASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAV---- 198
Cdd:PRK12583 21 GDAFDATVARFPDREALVvrhqALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAIlvni 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 199 ------------------HSVVFA-GFSADSLAQRIVDCKPNVILTCNAVKRGPKTINLKAIVdaALDQSSKDGVsvgic 259
Cdd:PRK12583 101 npayraseleyalgqsgvRWVICAdAFKTSDYHAMLQELLPGLAEGQPGALACERLPELRGVV--SLAPAPPPGF----- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 260 LTYDNSLATtrentkwqnGRDVWWQDVISQYPTscevewVDAEDPLFLLYTSGSTGKPKGVLHT-----TGGYMIYTATT 334
Cdd:PRK12583 174 LAWHELQAR---------GETVSREALAERQAS------LDRDDPINIQYTSGTTGFPKGATLShhnilNNGYFVAESLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 335 FKyafdykSTDV-------YWCTadcgwitGHSYVTYGPMLNGATVVVfegaPN-YPDPGRCWDIVDKYKVSIFYTAPTL 406
Cdd:PRK12583 239 LT------EHDRlcvpvplYHCF-------GMVLANLGCMTVGACLVY----PNeAFDPLATLQAVEEERCTALYGVPTM 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 407 VRSLMRDDDKfvTRHSRKSLRVLGSVGEPINPSAWRwffNVVGDSRCP-ISDTWWQTETGGfmITPLPGAWPQKPGSATf 485
Cdd:PRK12583 302 FIAELDHPQR--GNFDLSSLRTGIMAGAPCPIEVMR---RVMDEMHMAeVQIAYGMTETSP--VSLQTTAADDLERRVE- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 486 PFFGVQP----VIVDEKGNEI----EGE-CS-GYLCVKGSWPGAFRTLFGDHERyettyfkpfaGYYFSGDGCSRDKDGY 555
Cdd:PRK12583 374 TVGRTQPhlevKVVDPDGATVprgeIGElCTrGYSVMKGYWNNPEATAESIDED----------GWMHTGDLATMDEQGY 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 556 YWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYS-EELRKslvlMVRNQIG 634
Cdd:PRK12583 444 VRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASeEELRE----FCKARIA 519
|
570 580 590
....*....|....*....|....*....|....*....
gi 332006737 635 AFAAPDRIHWAPGLPKTRSGKIMRRILRKIAsrqLEELG 673
Cdd:PRK12583 520 HFKVPRYFRFVDEFPMTVTGKVQKFRMREIS---IEELA 555
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
148-689 |
1.19e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 101.01 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 148 LTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVILTCN 227
Cdd:PRK12467 1600 LTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQS 1679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 228 AV-KRGPKTINLKAIVdaaLDQSskdgvsvgicltydnslattrentkwqngrdvwwQDVISQYPTSCEVEWVDAEDPLF 306
Cdd:PRK12467 1680 HLqARLPLPDGLRSLV---LDQE----------------------------------DDWLEGYSDSNPAVNLAPQNLAY 1722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 307 LLYTSGSTGKPKGVLHTTGGYM-IYTATTFKYAFdykstdvywCTADCgWITGHSYV-------TYGPMLNGATVVVfeG 378
Cdd:PRK12467 1723 VIYTSGSTGRPKGAGNRHGALVnRLCATQEAYQL---------SAADV-VLQFTSFAfdvsvweLFWPLINGARLVI--A 1790
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 379 APN-YPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVtrHSRkSLRVLGSVGEPINPSAWR-WF--------FNVV 448
Cdd:PRK12467 1791 PPGaHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVE--HPL-SLRRVVCGGEALEVEALRpWLerlpdtglFNLY 1867
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 449 GDSRCPISDTWWQTETGgfmitPLPGAWPQKPGSatfPFFGVQPVIVDEKGNEIEGECSGYLCVKGSwpGAFRtlfGDHE 528
Cdd:PRK12467 1868 GPTETAVDVTHWTCRRK-----DLEGRDSVPIGQ---PIANLSTYILDASLNPVPIGVAGELYLGGV--GLAR---GYLN 1934
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 529 RYETTYFK----PFAGY----YFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEV 600
Cdd:PRK12467 1935 RPALTAERfvadPFGTVgsrlYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGAN 2014
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 601 KGQGIYAFVTLLEGVPYSEELRKSLVLMVRNQIGAfAAPDRI---HWA--PGLPKTRSGKIMRRILRKIASRQLEelgdT 675
Cdd:PRK12467 2015 GKQLVAYVVPTDPGLVDDDEAQVALRAILKNHLKA-SLPEYMvpaHLVflARMPLTPNGKLDRKALPAPDASELQ----Q 2089
|
570
....*....|....
gi 332006737 676 STLADPSVVDQLIA 689
Cdd:PRK12467 2090 AYVAPQSELEQRLA 2103
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
146-663 |
1.77e-21 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 98.51 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 146 ASLTYSE--LLQRvcQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVI 223
Cdd:PLN02246 49 RVYTYADveLLSR--RVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 224 LTcnavkrgpktinLKAIVDAALDQSSKDGVSVgICL--TYDNSLATTrentkwqngrdvwwqDVISQYPTSCEVEWVDA 301
Cdd:PLN02246 127 IT------------QSCYVDKLKGLAEDDGVTV-VTIddPPEGCLHFS---------------ELTQADENELPEVEISP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 302 EDPLFLLYTSGSTGKPKGVLHTTGGYMiytaTTFKYAFDYKSTDVYWCTAD---CGWITGHSYVTYGPMLN----GATVV 374
Cdd:PLN02246 179 DDVVALPYSSGTTGLPKGVMLTHKGLV----TSVAQQVDGENPNLYFHSDDvilCVLPMFHIYSLNSVLLCglrvGAAIL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 375 VFegaPNYpDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDkfVTRHSRKSLRVLGSVGEPINPS---AWRwffnvvgdS 451
Cdd:PLN02246 255 IM---PKF-EIGALLELIQRHKVTIAPFVPPIVLAIAKSPV--VEKYDLSSIRMVLSGAAPLGKEledAFR--------A 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 452 RCP---ISDTWWQTETG-------GFMITPLPgawpQKPGSATFPFFGVQPVIVD-EKGNEIEGECSGYLCVKGswPGAF 520
Cdd:PLN02246 321 KLPnavLGQGYGMTEAGpvlamclAFAKEPFP----VKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICIRG--PQIM 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 521 RTLFGDHERYETTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEV 600
Cdd:PLN02246 395 KGYLNDPEATANTIDK--DGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEV 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332006737 601 KGQGIYAFVTLLEGVPYSEELRKSLvlmVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRK 663
Cdd:PLN02246 473 AGEVPVAFVVRSNGSEITEDEIKQF---VAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRA 532
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
131-662 |
3.48e-21 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 97.64 E-value: 3.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 131 DKTAIhwegnELGVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADS 210
Cdd:PRK07514 17 DAPFI-----ETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 211 LAQRIVDCKPNVILtCNAVKRGPktinLKAIVDAAldqsskdgvSVGICLTYD----NSLAttrentkwqngrdvwwqDV 286
Cdd:PRK07514 92 LDYFIGDAEPALVV-CDPANFAW----LSKIAAAA---------GAPHVETLDadgtGSLL-----------------EA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 287 ISQYPTSCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGyMIYTATTFKYAFDYKSTDVYWctadcgwitgHS------ 360
Cdd:PRK07514 141 AAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGN-LLSNALTLVDYWRFTPDDVLI----------HAlpifht 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 361 ---YV-TYGPMLNGATVVVFegaPNYpDPGRcwdIVDKY-KVSIFYTAPTLVRSLMRDD--DKFVTRHSRksLRVLGSVg 433
Cdd:PRK07514 210 hglFVaTNVALLAGASMIFL---PKF-DPDA---VLALMpRATVMMGVPTFYTRLLQEPrlTREAAAHMR--LFISGSA- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 434 ePINPSAWRWFFNVVGDsrcPISDTWWQTETGgfMIT--PLPGAwpQKPGSATFPFFGVQPVIVD-EKGNEIEGECSGYL 510
Cdd:PRK07514 280 -PLLAETHREFQERTGH---AILERYGMTETN--MNTsnPYDGE--RRAGTVGFPLPGVSLRVTDpETGAELPPGEIGMI 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 511 CVKGswPGAFRtlfGDHERYETTY--FKPfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQC 588
Cdd:PRK07514 352 EVKG--PNVFK---GYWRMPEKTAeeFRA-DGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGV 425
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332006737 589 AEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEElrkSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILR 662
Cdd:PRK07514 426 VESAVIGVPHPDFGEGVTAVVVPKPGAALDEA---AILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
143-663 |
4.64e-21 |
|
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: 96.61 E-value: 4.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 143 GVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVfagfSADSLAQRIvdckpnv 222
Cdd:cd17653 18 SLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPL----DAKLPSARI------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 223 iltcnavkrgpktinlkaivDAALDQSSKDgvsvgICLTYDNslattrentkwqngrdvwwqdvisqyptscevewvdAE 302
Cdd:cd17653 87 --------------------QAILRTSGAT-----LLLTTDS------------------------------------PD 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 303 DPLFLLYTSGSTGKPKGV-----------------LHTTGGYMIytATTFKYAFDYkstdvywCTAdcgwitghsyVTYG 365
Cdd:cd17653 106 DLAYIIFTSGSTGIPKGVmvphrgvlnyvsqpparLDVGPGSRV--AQVLSIAFDA-------CIG----------EIFS 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 366 PMLNGATVVVFEGAPNYPDPGRcwdivdkyKVSIFYTAPTLVRSLMRDDdkfvtrhsRKSLRVLGSVGEPINPS---AW- 441
Cdd:cd17653 167 TLCNGGTLVLADPSDPFAHVAR--------TVDALMSTPSILSTLSPQD--------FPNLKTIFLGGEAVPPSlldRWs 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 442 --RWFFNVVGDSRCPISDTWWQTETGGFMI--TPLPGAwpqkpgsatfpffGVqpVIVDEKGNEIEGECSGYLCVKGswP 517
Cdd:cd17653 231 pgRRLYNAYGPTECTISSTMTELLPGQPVTigKPIPNS-------------TC--YILDADLQPVPEGVVGEICISG--V 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 518 GAFRTLFGDHERyETTYFKPFAGY-----YFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAA 592
Cdd:cd17653 294 QVARGYLGNPAL-TASKFVPDPFWpgsrmYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQA 372
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332006737 593 VVgIEHEvkgQGIYAFVTllegvPYS---EELRKSLvlmvRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRK 663
Cdd:cd17653 373 AA-IVVN---GRLVAFVT-----PETvdvDGLRSEL----AKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
302-662 |
9.93e-21 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 94.27 E-value: 9.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 302 EDPLFLLYTSGSTGKPKGVLHT-----TGGYMIytattfKYAFDYKSTDV-------YWCTadcGWITGH-SYVTYGpml 368
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLThhnivNNGYFI------GERLGLTEQDRlcipvplFHCF---GSVLGVlACLTHG--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 369 ngATVVVfeGAPNYpDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKfvTRHSRKSLR--VLGsvGEPINPSAWRWFFN 446
Cdd:cd05917 70 --ATMVF--PSPSF-DPLAVLEAIEKEKCTALHGVPTMFIAELEHPDF--DKFDLSSLRtgIMA--GAPCPPELMKRVIE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 447 VVGDSRCPISdtWWQTET--GGFMITPLPGAwPQKPGSATFPFFGVQPVIVDEKGNE-----IEGE--CSGYLCVKGSWp 517
Cdd:cd05917 141 VMNMKDVTIA--YGMTETspVSTQTRTDDSI-EKRVNTVGRIMPHTEAKIVDPEGGIvppvgVPGElcIRGYSVMKGYW- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 518 gafrtlfGDHERYETTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIE 597
Cdd:cd05917 217 -------NDPEKTAEAIDG--DGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVP 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332006737 598 HEVKGQGIYAFVTLLEGVPYSEE-LRKslvlMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILR 662
Cdd:cd05917 288 DERYGEEVCAWIRLKEGAELTEEdIKA----YCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
146-662 |
5.48e-20 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 94.35 E-value: 5.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 146 ASLTYSELLQRVCQLANYLKDN-GVKKGDAVVIYLPMLMELPIAMLACARIGAV--------------HSVVFAGFSA-- 208
Cdd:PRK08974 47 EVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNLLQYPIALFGILRAGMIvvnvnplytpreleHQLNDSGAKAiv 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 209 -----DSLAQRIVDCKP--NVILT--CNAVKRGPKTInlkaiVDAALDQSSKdgvsvgICLTYDNSLATTRENTkWQNGR 279
Cdd:PRK08974 127 ivsnfAHTLEKVVFKTPvkHVILTrmGDQLSTAKGTL-----VNFVVKYIKR------LVPKYHLPDAISFRSA-LHKGR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 280 DVwwqdvisQY--PTscevewVDAEDPLFLLYTSGSTGKPKGVLHTTGGyMIytattfkyafdyksTDVYWCTAdcgwit 357
Cdd:PRK08974 195 RM-------QYvkPE------LVPEDLAFLQYTGGTTGVAKGAMLTHRN-ML--------------ANLEQAKA------ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 358 ghsyvTYGPMLNGATVVVFEGAPNY---PDPGRCWDIVDKYKVSIFYTAPtlvrslmRDDDKFVTRHSRKSLRVLGSVGE 434
Cdd:PRK08974 241 -----AYGPLLHPGKELVVTALPLYhifALTVNCLLFIELGGQNLLITNP-------RDIPGFVKELKKYPFTAITGVNT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 435 PINPSAWRWFFNVVGDSRCPIS-----------DTWWQTETG-----GFMIT---PLPGAWP----QKPGSATFPFFGVQ 491
Cdd:PRK08974 309 LFNALLNNEEFQELDFSSLKLSvgggmavqqavAERWVKLTGqylleGYGLTecsPLVSVNPydldYYSGSIGLPVPSTE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 492 PVIVDEKGNEIEGECSGYLCVKGSwpgafRTLFGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGH 571
Cdd:PRK08974 389 IKLVDDDGNEVPPGEPGELWVKGP-----QVMLGYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGF 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 572 RIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEELRKSlvlmVRNQIGAFAAPDRIHWAPGLPKT 651
Cdd:PRK08974 464 NVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLTEEELITH----CRRHLTGYKVPKLVEFRDELPKS 539
|
570
....*....|.
gi 332006737 652 RSGKIMRRILR 662
Cdd:PRK08974 540 NVGKILRRELR 550
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
148-678 |
5.49e-20 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 94.10 E-value: 5.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 148 LTYSELLQRVCQLANYLKDNGVKKGDAVVI-------YLPMlmelpiaMLACARIGAVHSVVFAGFSADSLAQRIVDCKP 220
Cdd:PLN02860 33 RTGHEFVDGVLSLAAGLLRLGLRNGDVVAIaalnsdlYLEW-------LLAVACAGGIVAPLNYRWSFEEAKSAMLLVRP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 221 NVILTCNAVKRGPKTINLKAI----VDAALDQSSKDGVSVgicltyDNSLATTRENTKWQNGrdvwwqdvisqyPTSCEV 296
Cdd:PLN02860 106 VMLVTDETCSSWYEELQNDRLpslmWQVFLESPSSSVFIF------LNSFLTTEMLKQRALG------------TTELDY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 297 EWVdAEDPLFLLYTSGSTGKPKGVL--HTTggymIYTATTFKYAF-DYKSTDVYWCTADCGWITGHSYVTYGPMLNGATV 373
Cdd:PLN02860 168 AWA-PDDAVLICFTSGTTGRPKGVTisHSA----LIVQSLAKIAIvGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 374 VVfegaPNYpDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSLRVL----GSVGEPINPSAWRWFfnvvg 449
Cdd:PLN02860 243 LL----PKF-DAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRKIlnggGSLSSRLLPDAKKLF----- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 450 dSRCPISDTWWQTETGG---FMitPLPGAWPQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGSWPGAFRT--LF 524
Cdd:PLN02860 313 -PNAKLFSAYGMTEACSsltFM--TLHDPTLESPKQTLQTVNQTKSSSVHQPQGVCVGKPAPHVELKIGLDESSRVgrIL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 525 --GDH--ERY-----ETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVG 595
Cdd:PLN02860 390 trGPHvmLGYwgqnsETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 596 IEHEVKGQGIYAFVTLLEGVPYS----EELRKSLVL-------MVRNQ-IGAFAAPDRI-HWAPGLPKTRSGKIMRRILR 662
Cdd:PLN02860 470 VPDSRLTEMVVACVRLRDGWIWSdnekENAKKNLTLssetlrhHCREKnLSRFKIPKLFvQWRKPFPLTTTGKIRRDEVR 549
|
570
....*....|....*.
gi 332006737 663 KIASRQLEELgdTSTL 678
Cdd:PLN02860 550 REVLSHLQSL--PSNL 563
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
131-661 |
5.59e-20 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 95.62 E-value: 5.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 131 DKTAIHWEGnelgvdASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADS 210
Cdd:PRK05691 1146 ERIALVWDG------GSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAER 1219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 211 LAQRIVDCKPNVILTCNAV-KRGPKTINLKAIvdaALDQsskdgvsvgicLTYDNslattrentkwqngrdvwwqdvisq 289
Cdd:PRK05691 1220 LAYMLADSGVELLLTQSHLlERLPQAEGVSAI---ALDS-----------LHLDS------------------------- 1260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 290 YPTSCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGG------YMIYTattfkYAFDykSTDVYWCTA---------DCG 354
Cdd:PRK05691 1261 WPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAAlaerlqWMQAT-----YALD--DSDVLMQKApisfdvsvwECF 1333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 355 WitghsyvtygPMLNGATVVVfEGAPNYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRhsrkSLRVLGSVGE 434
Cdd:PRK05691 1334 W----------PLITGCRLVL-AGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACT----SLRRLFSGGE 1398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 435 PInPSAWR----------WFFNVVGDSRCPISDTWWQTETGGFMITPLpgawpqkpGSatfPFFGVQPVIVDEKGNEIEG 504
Cdd:PRK05691 1399 AL-PAELRnrvlqrlpqvQLHNRYGPTETAINVTHWQCQAEDGERSPI--------GR---PLGNVLCRVLDAELNLLPP 1466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 505 ECSGYLCVKGSwpGAFRTLFG----DHERY-ETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVE 579
Cdd:PRK05691 1467 GVAGELCIGGA--GLARGYLGrpalTAERFvPDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQ 1544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 580 SALVLHPQCAEAAVVgIEHEVKGQGIYAFVTLLEGV-PYSEELRKSLVL-----MVRNQIGAFAApdrihwapgLPKTRS 653
Cdd:PRK05691 1545 ARLLAQPGVAQAAVL-VREGAAGAQLVGYYTGEAGQeAEAERLKAALAAelpeyMVPAQLIRLDQ---------MPLGPS 1614
|
....*...
gi 332006737 654 GKIMRRIL 661
Cdd:PRK05691 1615 GKLDRRAL 1622
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
60-120 |
1.43e-19 |
|
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: 82.52 E-value: 1.43e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332006737 60 YMEMHKRSMDDPAAFWSDIASEFYWKQKWgDQVfsenLDVRKGPiSIEWFKGGITNICYNC 120
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKELDWFKPF-DKV----LDGSNGP-FAKWFVGGKLNVCYNC 55
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
302-658 |
1.99e-19 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 90.01 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 302 EDPLFLLYTSGSTGKPKGVLHTTGGYMIYTATTFKYAFDYKSTDVYWCTADCGWITGhsyvtygpMLNGATVVVFEGA-- 379
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGG--------LWWILTCLIHGGLcv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 380 --PNYPDPGRCWDIVDKYKVSIFYTAPTL---VRSLMRDDDKFVtrhsrKSLRVLGSVGE-PINpsAWRWFFNVVGDSRc 453
Cdd:cd17635 73 tgGENTTYKSLFKILTTNAVTTTCLVPTLlskLVSELKSANATV-----PSLRLIGYGGSrAIA--ADVRFIEATGLTN- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 454 pISDTWWQTETGGFMITPLpGAWPQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGSWpgafrTLFGDHERYETT 533
Cdd:cd17635 145 -TAQVYGLSETGTALCLPT-DDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPA-----NMLGYWNNPERT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 534 YFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLle 613
Cdd:cd17635 218 AEVLIDGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVA-- 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 332006737 614 gvpySEELRKS----LVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMR 658
Cdd:cd17635 296 ----SAELDENairaLKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
149-664 |
2.51e-19 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 91.82 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 149 TYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVILtcnA 228
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVF---C 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 229 VKRG-PKTINLkaivdaaldQSSKDGVSVGICLTYDNSLATTRENTKWQNGRDVWWQDVISQYPTSCEVEwvdaEDPLFL 307
Cdd:cd17642 123 SKKGlQKVLNV---------QKKLKIIKTIIILDSKEDYKGYQCLYTFITQNLPPGFNEYDFKPPSFDRD----EQVALI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 308 LYTSGSTGKPKGVLHT--------------------TGGYMIYTATTFKYAFDYKSTDVYWCtadCGWitghsYVTYGPM 367
Cdd:cd17642 190 MNSSGSTGLPKGVQLThknivarfshardpifgnqiIPDTAILTVIPFHHGFGMFTTLGYLI---CGF-----RVVLMYK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 368 LNGATVVvfegapnypdpgrcwDIVDKYKVSIFYTAPTLVRSLMRDddKFVTRHSRKSLRVLGSVGEPINPS---AWRWF 444
Cdd:cd17642 262 FEEELFL---------------RSLQDYKVQSALLVPTLFAFFAKS--TLVDKYDLSNLHEIASGGAPLSKEvgeAVAKR 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 445 FNVVGdsrcpISDTWWQTE-TGGFMITPlpgAWPQKPGSA--TFPFFGVQpVIVDEKGNEIEGECSGYLCVKGswPGAFR 521
Cdd:cd17642 325 FKLPG-----IRQGYGLTEtTSAILITP---EGDDKPGAVgkVVPFFYAK-VVDLDTGKTLGPNERGELCVKG--PMIMK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 522 TLFGDHERYETTYFKPfaGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVK 601
Cdd:cd17642 394 GYVNNPEATKALIDKD--GWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDA 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332006737 602 GQGIYAFVTLLEGVPYSEelrKSLVLMVRNQIGAfAAPDR--IHWAPGLPKTRSGKIMRRILRKI 664
Cdd:cd17642 472 GELPAAVVVLEAGKTMTE---KEVMDYVASQVST-AKRLRggVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
133-661 |
5.07e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 90.83 E-value: 5.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 133 TAIHWEGNELGVD--ASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADS 210
Cdd:PRK13383 44 TAARWPGRTAIIDddGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 211 LAQRIVDCKPNVILtCNavkrgpktinlkaivDAALDQSSKDGVSVgicLTYDNSLATTREntkwqngrdvwwqdvisqy 290
Cdd:PRK13383 124 LAAALRAHHISTVV-AD---------------NEFAERIAGADDAV---AVIDPATAGAEE------------------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 291 ptsCEVEWVDAEDPLFLLYTSGSTGKPKGVlhttggymiytattfKYAFDYKSTDVYWCT--ADCGWITGHSYVTYGPML 368
Cdd:PRK13383 166 ---SGGRPAVAAPGRIVLLTSGTTGKPKGV---------------PRAPQLRSAVGVWVTilDRTRLRTGSRISVAMPMF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 369 NG-------------ATVVVFEgapnYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSLRVLGSVGEP 435
Cdd:PRK13383 228 HGlglgmlmltialgGTVLTHR----HFDAEAALAQASLHRADAFTAVPVVLARILELPPRVRARNPLPQLRVVMSSGDR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 436 INPSAWRWFFNVVGDSrcpISDTWWQTETG-GFMITPLP-GAWPQKPGSatfPFFGVQPVIVDEKGNEIEGECSGYLCVK 513
Cdd:PRK13383 304 LDPTLGQRFMDTYGDI---LYNGYGSTEVGiGALATPADlRDAPETVGK---PVAGCPVRILDRNNRPVGPRVTGRIFVG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 514 GSWPGafrtlfgdhERYETTYFKPFA-GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAA 592
Cdd:PRK13383 378 GELAG---------TRYTDGGGKAVVdGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNA 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 593 VVGIEHEVKGQGIYAFVTLLEGVPY-SEELRKSLvlmvRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRIL 661
Cdd:PRK13383 449 VIGVPDERFGHRLAAFVVLHPGSGVdAAQLRDYL----KDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
145-661 |
7.88e-19 |
|
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: 90.23 E-value: 7.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 145 DASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVIL 224
Cdd:cd17656 11 NQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 225 TCNAVKRGPKtinlkaivdaaldqsskdgvsvgicltyDNSLATTRENtkwqngrdvwwqDVISQYPTSCEVEWVDAEDP 304
Cdd:cd17656 91 TQRHLKSKLS----------------------------FNKSTILLED------------PSISQEDTSNIDYINNSDDL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 305 LFLLYTSGSTGKPKGVL--HTTggymiyTATTFKYAFDYKSTDVYwctADCGWITGHSY-VTY----GPMLNGATVVVFE 377
Cdd:cd17656 131 LYIIYTSGTTGKPKGVQleHKN------MVNLLHFEREKTNINFS---DKVLQFATCSFdVCYqeifSTLLSGGTLYIIR 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 378 GAPNYpDPGRCWDIVDKYKVSIFYTaPTLVRSLMRDDDKFVTRHSrKSLRVLGSVGEPI---NPsawrwFFNVVGDSRCP 454
Cdd:cd17656 202 EETKR-DVEQLFDLVKRHNIEVVFL-PVAFLKFIFSEREFINRFP-TCVKHIITAGEQLvitNE-----FKEMLHEHNVH 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 455 ISDTWWQTET---GGFMITPLPgAWPQKPGSATfPFFGVQPVIVDEKGNEIEGECSGYLCVKGSwpGAFRTLFGD----H 527
Cdd:cd17656 274 LHNHYGPSEThvvTTYTINPEA-EIPELPPIGK-PISNTWIYILDQEQQLQPQGIVGELYISGA--SVARGYLNRqeltA 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 528 ERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYA 607
Cdd:cd17656 350 EKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCA 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 332006737 608 FVTLLEGVPySEELRKSLvlmvRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRIL 661
Cdd:cd17656 430 YFVMEQELN-ISQLREYL----AKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
130-663 |
3.54e-18 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 88.78 E-value: 3.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 130 GDKTAIHWEgnelgvDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAD 209
Cdd:PRK08279 51 PDRPALLFE------DQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 210 SLAQRIVDCKPNVIltcnavkrgpktinlkaIVDAALD---QSSKDGVSVGICLTYDNSLATTRENTkwqngrdvwWQDV 286
Cdd:PRK08279 125 VLAHSLNLVDAKHL-----------------IVGEELVeafEEARADLARPPRLWVAGGDTLDDPEG---------YEDL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 287 ---ISQYPTSCEVEW--VDAEDPLFLLYTSGSTGKPKGVLHTTGGYMIYTAtTFKYAFDYKSTDVYWCT--------ADC 353
Cdd:PRK08279 179 aaaAAGAPTTNPASRsgVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMG-GFGGLLRLTPDDVLYCClplyhntgGTV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 354 GWitghsyvtyGPMLN-GATVVVFE--GAPNYpdpgrcWDIVDKYKVSIFYTAPTLVRSLM----RDDDKfvtRHsrkSL 426
Cdd:PRK08279 258 AW---------SSVLAaGATLALRRkfSASRF------WDDVRRYRATAFQYIGELCRYLLnqppKPTDR---DH---RL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 427 RVLgsVGEPINPSAWRWFFNVVGDSRcpISDTWWQTEtGGFMITPLPGawpqKPGSATF-PFFGVQPV-IVD---EKGNE 501
Cdd:PRK08279 317 RLM--IGNGLRPDIWDEFQQRFGIPR--ILEFYAASE-GNVGFINVFN----FDGTVGRvPLWLAHPYaIVKydvDTGEP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 502 IEGEcSGyLCVKGSwPGAFRTLFGdheryETTYFKPFAGY--------------------YF-SGDGCSRDKDGYYWLTG 560
Cdd:PRK08279 388 VRDA-DG-RCIKVK-PGEVGLLIG-----RITDRGPFDGYtdpeasekkilrdvfkkgdaWFnTGDLMRDDGFGHAQFVD 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 561 RVDDVI-----NVSghrigTAEVESALVLHPQCAEAAVVGIE-HEVKGQGIYAFVTLLEGVPYSeelRKSLVLMVRNQIG 634
Cdd:PRK08279 460 RLGDTFrwkgeNVA-----TTEVENALSGFPGVEEAVVYGVEvPGTDGRAGMAAIVLADGAEFD---LAALAAHLYERLP 531
|
570 580
....*....|....*....|....*....
gi 332006737 635 AFAAPDRIHWAPGLPKTRSGKIMRRILRK 663
Cdd:PRK08279 532 AYAVPLFVRLVPELETTGTFKYRKVDLRK 560
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
131-667 |
8.41e-18 |
|
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: 86.83 E-value: 8.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 131 DKTAIH-WEGnelgvdaSLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAvhsvVFAGFSAD 209
Cdd:cd05918 14 DAPAVCaWDG-------SLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGG----AFVPLDPS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 210 SLAQRIV----DCKPNVILTCnavkrgpktinlkaivdaaldqsskdgvsvgicltydnslattrentkwqngrdvwwqd 285
Cdd:cd05918 83 HPLQRLQeilqDTGAKVVLTS----------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 286 visqyptscevewvDAEDPLFLLYTSGSTGKPKGVL--HTT--------GGYMIYTATT----F-KYAFDykstdvywct 350
Cdd:cd05918 104 --------------SPSDAAYVIFTSGSTGKPKGVVieHRAlstsalahGRALGLTSESrvlqFaSYTFD---------- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 351 adcgwitGHSYVTYGPMLNGATVVVfegaPnyPDPGRCWDIVD---KYKVS-IFYTaPTLVRSLMRDDDkfvtrhsrKSL 426
Cdd:cd05918 160 -------VSILEIFTTLAAGGCLCI----P--SEEDRLNDLAGfinRLRVTwAFLT-PSVARLLDPEDV--------PSL 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 427 RVLGSVGEPINPSawrwffnVVgdsrcpisDTWWQ----------TETGGFMITPLPGAwPQKPGSATFPfFGVQPVIVD 496
Cdd:cd05918 218 RTLVLGGEALTQS-------DV--------DTWADrvrlinaygpAECTIAATVSPVVP-STDPRNIGRP-LGATCWVVD 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 497 EKGNE------------IEGE--CSGYL----CVKGSwpgafrtlFGDHERYETTYFKPFAGY-YFSGDGCSRDKDG--Y 555
Cdd:cd05918 281 PDNHDrlvpigavgellIEGPilARGYLndpeKTAAA--------FIEDPAWLKQEGSGRGRRlYRTGDLVRYNPDGslE 352
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 556 YwlTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEELRKSLVLMVRNQIGA 635
Cdd:cd05918 353 Y--VGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDEF 430
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 332006737 636 FAAPDRI---------------HWAP--GLPKTRSGKIMRRILRKIASR 667
Cdd:cd05918 431 RALVAELrsklrqrlpsymvpsVFLPlsHLPLTASGKIDRRALRELAES 479
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
147-663 |
1.17e-17 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 86.96 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 147 SLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVhsvvFAGFSADSLAQRIvdckpnviltc 226
Cdd:PLN02330 55 AVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGV----FSGANPTALESEI----------- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 227 navKRGPKTINLKAIVDAALDQSSKDGVSVGICLTYDNSLATTrentkwqngrdVWWQDVIS---QYPTSCEVEWVDAED 303
Cdd:PLN02330 120 ---KKQAEAAGAKLIVTNDTNYGKVKGLGLPVIVLGEEKIEGA-----------VNWKELLEaadRAGDTSDNEEILQTD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 304 PLFLLYTSGSTGKPKGVLHT--------------TGGYMIYTATTFKYAFDYKstdVYWCTADCgwitghsyvtYGPMLN 369
Cdd:PLN02330 186 LCALPFSSGTTGISKGVMLThrnlvanlcsslfsVGPEMIGQVVTLGLIPFFH---IYGITGIC----------CATLRN 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 370 GATVVVfegapnypdpgrcwdiVDKYKVSIFYTA------------PTLVRSLMRDD--DKFVTrhSRKSLRVLGSVGEP 435
Cdd:PLN02330 253 KGKVVV----------------MSRFELRTFLNAlitqevsfapivPPIILNLVKNPivEEFDL--SKLKLQAIMTAAAP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 436 INPSAWRWFfnvvgDSRCP---ISDTWWQTETGGFMIT---PLPGAWPQKPGSATFPFFGVQPVIVD-EKGNEIEGECSG 508
Cdd:PLN02330 315 LAPELLTAF-----EAKFPgvqVQEAYGLTEHSCITLThgdPEKGHGIAKKNSVGFILPNLEVKFIDpDTGRSLPKNTPG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 509 YLCVKGSWpgAFRTLFGDHERYETTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQC 588
Cdd:PLN02330 390 ELCVRSQC--VMQGYYNNKEETDRTIDE--DGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSV 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332006737 589 AEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEElrkSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRK 663
Cdd:PLN02330 466 EDAAVVPLPDEEAGEIPAACVVINPKAKESEE---DILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
283-663 |
1.20e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 86.66 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 283 WQDVISQYP-TSCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTG-----GYMIytATTFKYAFDykstDVYWCTAD---- 352
Cdd:PRK07867 132 WADELAAHRdAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRkvasaGVML--AQRFGLGPD----DVCYVSMPlfhs 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 353 ----CGWITGhsyvtygpMLNGATVVV---FEGAPNYPDpgrcwdiVDKYKVSIF-YTAPTLVRSLM---RDDDkfvtRH 421
Cdd:PRK07867 206 navmAGWAVA--------LAAGASIALrrkFSASGFLPD-------VRRYGATYAnYVGKPLSYVLAtpeRPDD----AD 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 422 SrkSLRVL-GSVGEPINPSAWRWFFNvvgdsrCPISDTWWQTEtGGFMITPLPGAwpqKPGSATFPFFGVQ--------- 491
Cdd:PRK07867 267 N--PLRIVyGNEGAPGDIARFARRFG------CVVVDGFGSTE-GGVAITRTPDT---PPGALGPLPPGVAivdpdtgte 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 492 --PVIVDEKGNEIEGECSGYLcVKGSWPGAFRTLFGDHEryeTTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVS 569
Cdd:PRK07867 335 cpPAEDADGRLLNADEAIGEL-VNTAGPGGFEGYYNDPE---ADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVD 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 570 GHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEElRKSLVLMVRNQIGAFAAPDRIHWAPGLP 649
Cdd:PRK07867 411 GENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPD-AFAEFLAAQPDLGPKQWPSYVRVCAELP 489
|
410
....*....|....
gi 332006737 650 KTRSGKIMRRILRK 663
Cdd:PRK07867 490 RTATFKVLKRQLSA 503
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
126-680 |
1.26e-17 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 87.01 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 126 EAGLGDKTAIHwegnelgVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAG 205
Cdd:PRK06060 16 EAGWYDRPAFY-------AADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 206 FSADSLAQRIVDCKPNVILTCNAVKRGPKTINlkaIVDAA--LDQSSKDGVSvgicltydnslattrentkwqngrdvww 283
Cdd:PRK06060 89 LHRDDHALAARNTEPALVVTSDALRDRFQPSR---VAEAAelMSEAARVAPG---------------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 284 qdvisqyptscEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMIYTATTFKYAFDYKSTDVYWCTADCGWITGHSYVT 363
Cdd:PRK06060 138 -----------GYEPMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 364 YGPMLNGATVVVfEGAPNYPDPGRCwdIVDKYKVSIFYTAPTLVRSLMrdddKFVTRHSRKSLRVLGSVGEPINPS-AWR 442
Cdd:PRK06060 207 WFPLATGGSAVI-NSAPVTPEAAAI--LSARFGPSVLYGVPNFFARVI----DSCSPDSFRSLRCVVSAGEALELGlAER 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 443 W--FFNVVgdsrcPISDTWWQTETGGFMITPLPGAWpqKPGS--ATFPFFGVQPVIVD--EKGNEIEGEcsgyLCVKG-- 514
Cdd:PRK06060 280 LmeFFGGI-----PILDGIGSTEVGQTFVSNRVDEW--RLGTlgRVLPPYEIRVVAPDgtTAGPGVEGD----LWVRGpa 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 515 ------SWPgafRTLFGDheryettyfkpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQC 588
Cdd:PRK06060 349 iakgywNRP---DSPVAN------------EGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAV 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 589 AEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILR-KIASR 667
Cdd:PRK06060 414 AEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRkQSPTK 493
|
570
....*....|...
gi 332006737 668 QLEELGDTSTLAD 680
Cdd:PRK06060 494 PIWELSLTEPGSG 506
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
307-658 |
3.76e-17 |
|
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: 83.32 E-value: 3.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 307 LLYTSGSTGKPKGVLhttggyMIYTATTFKYAfdykstdvYWCtaDCGWIT-GHSYVTYGP--------------MLNGA 371
Cdd:cd17638 5 IMFTSGTTGRSKGVM------CAHRQTLRAAA--------AWA--DCADLTeDDRYLIINPffhtfgykagivacLLTGA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 372 TVV---VFegapnypDPGRCWDIVDKYKVSIFYTAPTLVRSLMR--DDDKFvtrhSRKSLRvlgsvgepinpsawrwfFN 446
Cdd:cd17638 69 TVVpvaVF-------DVDAILEAIERERITVLPGPPTLFQSLLDhpGRKKF----DLSSLR-----------------AA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 447 VVGDSRCPISDTWWQTETGGFMITpLPGAWPQKPGSATFPFFGVQPVIVDEK------GNEIEGECSGYLCVKGswPGAF 520
Cdd:cd17638 121 VTGAATVPVELVRRMRSELGFETV-LTAYGLTEAGVATMCRPGDDAETVATTcgracpGFEVRIADDGEVLVRG--YNVM 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 521 RTLFGDHERYETTYFKPfaGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEV 600
Cdd:cd17638 198 QGYLDDPEATAEAIDAD--GWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDER 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 332006737 601 KGQGIYAFVTLLEGVPYSEElrkSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMR 658
Cdd:cd17638 276 MGEVGKAFVVARPGVTLTEE---DVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
148-663 |
9.96e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 85.21 E-value: 9.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 148 LTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVILTCN 227
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQS 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 228 AV-KRGPKTINLKAIVDAALDqsskdgvsvgicltydnslattrentkwqngrdvwwqDVISQYPTSCEVEWVDAEDPLF 306
Cdd:PRK12467 618 HLlAQLPVPAGLRSLCLDEPA-------------------------------------DLLCGYSGHNPEVALDPDNLAY 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 307 LLYTSGSTGKPKGVLHTTGGYMIYTATTFKYafdykstdvYWCTADCGWITGHSY-------VTYGPMLNGATVVVFeGA 379
Cdd:PRK12467 661 VIYTSGSTGQPKGVAISHGALANYVCVIAER---------LQLAADDSMLMVSTFafdlgvtELFGALASGATLHLL-PP 730
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 380 PNYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRhSRKSLRVLGSVGEPINPSAWRWF------FNVVGDSRC 453
Cdd:PRK12467 731 DCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPR-PQRALVCGGEALQVDLLARVRALgpgarlINHYGPTET 809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 454 PISDTWWQTETGGFMITPLPGAWPQkPGSATFpffgvqpvIVDEKGNEIEGECSGYLCVKGSwpGAFRtlfGDHERYETT 533
Cdd:PRK12467 810 TVGVSTYELSDEERDFGNVPIGQPL-ANLGLY--------ILDHYLNPVPVGVVGELYIGGA--GLAR---GYHRRPALT 875
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 534 --YF--KPFAG----YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGI 605
Cdd:PRK12467 876 aeRFvpDPFGAdggrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLV 955
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332006737 606 YAFVTLL-----EGVPYSEELRKSLvlmvRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRK 663
Cdd:PRK12467 956 AYLVPAAvadgaEHQATRDELKAQL----RQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPK 1014
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
540-673 |
1.14e-16 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 83.74 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 540 GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSE 619
Cdd:PLN02479 430 GWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSD 509
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 332006737 620 E--LRKSLVLMVRNQIGAFAAPDRIHWAPgLPKTRSGKIMRRILRKIAsrqlEELG 673
Cdd:PLN02479 510 EaaLAEDIMKFCRERLPAYWVPKSVVFGP-LPKTATGKIQKHVLRAKA----KEMG 560
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
148-659 |
1.89e-16 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 83.01 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 148 LTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVIL--T 225
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLidA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 226 CNAVKRGPKTINLKAIvdaALDQSSKDGVSVGICL-TYDNSLATTRENTKWQNGRDvwwqdvisqyptscevewvdaeDP 304
Cdd:PRK05852 124 DGPHDRAEPTTRWWPL---TVNVGGDSGPSGGTLSvHLDAATEPTPATSTPEGLRP----------------------DD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 305 LFLLYTSGSTGKPKGVLHTTGGYmiytattfkyafdykSTDVYWCTADCGWITGHSYVTYGPMLNGATVV-------VFE 377
Cdd:PRK05852 179 AMIMFTGGTTGLPKMVPWTHANI---------------ASSVRAIITGYRLSPRDATVAVMPLYHGHGLIaallatlASG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 378 GAPNYPDPGRC-----WDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGdsr 452
Cdd:PRK05852 244 GAVLLPARGRFsahtfWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFA--- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 453 CPISDTWWQTET---------GGFMITPLPGAWPQKPGSATfpffGVQPVIVDEKGNEIEGECSGYLCVKGswPGAFRTL 523
Cdd:PRK05852 321 APVVCAFGMTEAthqvtttqiEGIGQTENPVVSTGLVGRST----GAQIRIVGSDGLPLPAGAVGEVWLRG--TTVVRGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 524 FGDHERYETTYFKpfaGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQ 603
Cdd:PRK05852 395 LGDPTITAANFTD---GWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGE 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 332006737 604 GIYAFVTLLEGVPYSeelRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRR 659
Cdd:PRK05852 472 AVAAVIVPRESAPPT---AEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
143-595 |
2.50e-16 |
|
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: 82.52 E-value: 2.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 143 GVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQrivdckpnv 222
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRY--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 223 ILTCNAVKrgpktinlkAIVDAALD--QSSKDGVSVGI--CLTYDNSLATTRENtkwqngrdvwWQDVISQYPTSCEVEW 298
Cdd:cd05932 73 VLEHSESK---------ALFVGKLDdwKAMAPGVPEGLisISLPPPSAANCQYQ----------WDDLIAQHPPLEERPT 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 299 VDAEDPLFLLYTSGSTGKPKGVLHTTGGYMiYTATTFKYAFDYKSTDVYWCTADCGWITGHSYVTYGPMLNGATVVVFEG 378
Cdd:cd05932 134 RFPEQLATLIYTSGTTGQPKGVMLTFGSFA-WAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAES 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 379 APNYPDPgrcwdiVDKYKVSIFYTAPTL-VRSLMRDDDK-----------------FVTRHSRKSL-----RVLGSVGEP 435
Cdd:cd05932 213 LDTFVED------VQRARPTLFFSVPRLwTKFQQGVQDKipqqklnlllkipvvnsLVKRKVLKGLgldqcRLAGCGSAP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 436 INPSAWRWFFNVvgdsRCPISDTWWQTETGGFMITPLPGAwpQKPGSATFPFFGVQPVIVDEkgneiegecsGYLCVKGs 515
Cdd:cd05932 287 VPPALLEWYRSL----GLNILEAYGMTENFAYSHLNYPGR--DKIGTVGNAGPGVEVRISED----------GEILVRS- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 516 wPGAFRTLFGDHERYETTYFKPfaGYYFSGDGCSRDKDGYYWLTGRVDDVINVS-GHRIGTAEVESALVLHPQCAEAAVV 594
Cdd:cd05932 350 -PALMMGYYKDPEATAEAFTAD--GFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVI 426
|
.
gi 332006737 595 G 595
Cdd:cd05932 427 G 427
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
145-662 |
3.25e-16 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 82.38 E-value: 3.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 145 DASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDC--KPNV 222
Cdd:PRK07059 46 GKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSgaEAIV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 223 IL-----TCNAVKrgPKTiNLKAIVDAAL-DQSSKDGVSVGICLtydnslattRENTK----WQNGRDVWWQDVISQ--- 289
Cdd:PRK07059 126 VLenfatTVQQVL--AKT-AVKHVVVASMgDLLGFKGHIVNFVV---------RRVKKmvpaWSLPGHVRFNDALAEgar 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 290 ---YPTScevewVDAEDPLFLLYTSGSTGKPKG--VLHTT-GGYMIYTATTFKYAFDYKSTD-------------VYWCT 350
Cdd:PRK07059 194 qtfKPVK-----LGPDDVAFLQYTGGTTGVSKGatLLHRNiVANVLQMEAWLQPAFEKKPRPdqlnfvcalplyhIFALT 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 351 AdCGWITghsyvtygpMLNGATVVVFegaPNYPD-PGRCWDIvDKYKVSIFYTAPTLVRSLMRDDDkFVTRHSRKSLRVL 429
Cdd:PRK07059 269 V-CGLLG---------MRTGGRNILI---PNPRDiPGFIKEL-KKYQVHIFPAVNTLYNALLNNPD-FDKLDFSKLIVAN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 430 G---SVGEPInpsAWRWFfNVVGdsrCPISDTWWQTETGGfMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGNEIE-GE 505
Cdd:PRK07059 334 GggmAVQRPV---AERWL-EMTG---CPITEGYGLSETSP-VATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPlGE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 506 cSGYLCVKGSwpgafRTLFGDHERYETTYFKPFA-GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVL 584
Cdd:PRK07059 406 -PGEICIRGP-----QVMAGYWNRPDETAKVMTAdGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVAS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 585 HPQCAEAAVVGIEHEVKGQGIYAFVtllegvpyseeLRKSLVLmVRNQIGAFAA--------PDRIHWAPGLPKTRSGKI 656
Cdd:PRK07059 480 HPGVLEVAAVGVPDEHSGEAVKLFV-----------VKKDPAL-TEEDVKAFCKerltnykrPKFVEFRTELPKTNVGKI 547
|
....*.
gi 332006737 657 MRRILR 662
Cdd:PRK07059 548 LRRELR 553
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
131-661 |
3.68e-16 |
|
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: 81.71 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 131 DKTAIHWEGNELgvdaslTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHsvvfagfsads 210
Cdd:cd17644 15 DAVAVVFEDQQL------TYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAY----------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 211 laqriVDCKPNViltcnavkrgPKTiNLKAIVDAAldqsskdGVSVgicltydnsLATTRENTkwqngrdvwwqdvisqy 290
Cdd:cd17644 78 -----VPLDPNY----------PQE-RLTYILEDA-------QISV---------LLTQPENL----------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 291 ptscevewvdaedpLFLLYTSGSTGKPKGVL--------HTTGGYMIYTATT-------FKYAFDYKSTDVywctadcgw 355
Cdd:cd17644 109 --------------AYVIYTSGSTGKPKGVMiehqslvnLSHGLIKEYGITSsdrvlqfASIAFDVAAEEI--------- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 356 itghsYVTygpMLNGATVVVfegAPN--YPDPGRCWDIVDKYKVSIFYTAPTLVRSLMrDDDKFVTRHSRKSLRVLGSVG 433
Cdd:cd17644 166 -----YVT---LLSGATLVL---RPEemRSSLEDFVQYIQQWQLTVLSLPPAYWHLLV-LELLLSTIDLPSSLRLVIVGG 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 434 EPINPSAWR-W---------FFNVVGDSRCPISDTWwqtetggFMITPLPGAWPQKPGSATfPFFGVQPVIVDEKGNEIE 503
Cdd:cd17644 234 EAVQPELVRqWqknvgnfiqLINVYGPTEATIAATV-------CRLTQLTERNITSVPIGR-PIANTQVYILDENLQPVP 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 504 GECSG--YLCVKGSWPGAFRTLFGDHERYETTYF--KPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVE 579
Cdd:cd17644 306 VGVPGelHIGGVGLARGYLNRPELTAEKFISHPFnsSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIE 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 580 SALVLHPQCAEAAVVGIEHEVKGQGIYAF-VTLLEGVPYSEELRKSLvlmvRNQIGAFAAPDRIHWAPGLPKTRSGKIMR 658
Cdd:cd17644 386 AVLSQHNDVKTAVVIVREDQPGNKRLVAYiVPHYEESPSTVELRQFL----KAKLPDYMIPSAFVVLEELPLTPNGKIDR 461
|
...
gi 332006737 659 RIL 661
Cdd:cd17644 462 RAL 464
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
283-662 |
4.15e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 82.00 E-value: 4.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 283 WQDVISQYPTSCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGY-MIYTATTFKYafDYKSTDVYWCTADcgwiTGHS- 360
Cdd:PRK13388 131 YAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLaFAGRALTERF--GLTRDDVCYVSMP----LFHSn 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 361 --YVTYGPML-NGATVVV---FEGAPNYPDpgrcwdiVDKYKVSIF-YTAPTLVRSLM---RDDDkfvtrhSRKSLRV-L 429
Cdd:PRK13388 205 avMAGWAPAVaSGAAVALpakFSASGFLDD-------VRRYGATYFnYVGKPLAYILAtpeRPDD------ADNPLRVaF 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 430 GSVGEPINPSAWRWFFnvvgdsRCPISDTWWQTETGGfMITPLPGAwPqkPGSATFPFFGVqpVIVDEKGNEiegECSgy 509
Cdd:PRK13388 272 GNEASPRDIAEFSRRF------GCQVEDGYGSSEGAV-IVVREPGT-P--PGSIGRGAPGV--AIYNPETLT---ECA-- 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 510 lcvkgswpgafRTLFGDH-----------ERYETTYFKPFAGYY---------------FSGDGCSRDKDGYYWLTGRVD 563
Cdd:PRK13388 335 -----------VARFDAHgallnadeaigELVNTAGAGFFEGYYnnpeataermrhgmyWSGDLAYRDADGWIYFAGRTA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 564 DVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEElrkSLVLMVRNQ--IGAFAAPDR 641
Cdd:PRK13388 404 DWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPD---AFAAFLAAQpdLGTKAWPRY 480
|
410 420
....*....|....*....|.
gi 332006737 642 IHWAPGLPKTRSGKIMRRILR 662
Cdd:PRK13388 481 VRIAADLPSTATNKVLKRELI 501
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
142-665 |
5.52e-16 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 81.41 E-value: 5.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 142 LGVdaSLTYSELLQRVCQLANYL-KDNGVKKGDAVVIYLPMLMELPIAMLACARIGAV--------------HSVVFAGF 206
Cdd:PRK12492 46 LGV--TLSYAELERHSAAFAAYLqQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIvvntnplytaremrHQFKDSGA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 207 SA----DSLAQRIVDCKPN-VILTCNAVKRGPKTINLKA-IVDAALDQSSK--DGVSVGICLTYDNSLattrentkwQNG 278
Cdd:PRK12492 124 RAlvylNMFGKLVQEVLPDtGIEYLIEAKMGDLLPAAKGwLVNTVVDKVKKmvPAYHLPQAVPFKQAL---------RQG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 279 RDvwwqdvISQYPTScevewVDAEDPLFLLYTSGSTGKPKGVLHTTGGyMIYTATTFKYAFDYKSTD------------- 345
Cdd:PRK12492 195 RG------LSLKPVP-----VGLDDIAVLQYTGGTTGLAKGAMLTHGN-LVANMLQVRACLSQLGPDgqplmkegqevmi 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 346 -------VYWCTADCGWItghsyvtygpMLNGATVVVFEgapNYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFV 418
Cdd:PRK12492 263 aplplyhIYAFTANCMCM----------MVSGNHNVLIT---NPRDIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 419 TRHSRksLRVLGSVGEP-INPSAWRWFfNVVGdsrCPISDTWWQTETggfmiTPLPGAWP----QKPGSATFPFFGVQPV 493
Cdd:PRK12492 330 LDFSA--LKLTNSGGTAlVKATAERWE-QLTG---CTIVEGYGLTET-----SPVASTNPygelARLGTVGIPVPGTALK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 494 IVDEKGNEIE-GEcSGYLCVKGSwpgafRTLFGDHERYETTYFKPFA-GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGH 571
Cdd:PRK12492 399 VIDDDGNELPlGE-RGELCIKGP-----QVMKGYWQQPEATAEALDAeGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGF 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 572 RIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEELRKslvlMVRNQIGAFAAPDRIHWAPGLPKT 651
Cdd:PRK12492 473 NVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVEELKA----YCKENFTGYKVPKHIVLRDSLPMT 548
|
570
....*....|....
gi 332006737 652 RSGKIMRRILRKIA 665
Cdd:PRK12492 549 PVGKILRRELRDIA 562
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
148-665 |
7.37e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 81.22 E-value: 7.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 148 LTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVILtcn 227
Cdd:PLN03102 40 FTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILF--- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 228 aVKRgpktiNLKAIVDAALDQSSKDGVSVGICLTYDNSLattrENTKWQNGRDVWWQDVISQ-YPTSCEVEWV----DAE 302
Cdd:PLN03102 117 -VDR-----SFEPLAREVLHLLSSEDSNLNLPVIFIHEI----DFPKRPSSEELDYECLIQRgEPTPSLVARMfriqDEH 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 303 DPLFLLYTSGSTGKPKGVLHT-TGGYMiyTATTFKYAFDYKSTDVYWCTA---DC-GWItghsyVTYGPMLNGATVVVFE 377
Cdd:PLN03102 187 DPISLNYTSGTTADPKGVVIShRGAYL--STLSAIIGWEMGTCPVYLWTLpmfHCnGWT-----FTWGTAARGGTSVCMR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 378 --GAPnypdpgRCWDIVDKYKVSIFYTAPTLVRSLMRDDDkfvTRHSRKSLRVLGSVGEPINPSAW-----RWFFNVVgd 450
Cdd:PLN03102 260 hvTAP------EIYKNIEMHNVTHMCCVPTVFNILLKGNS---LDLSPRSGPVHVLTGGSPPPAALvkkvqRLGFQVM-- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 451 srcpisDTWWQTE-TGGFMITPLPGAWPQKPGSATFPFFGVQPVI------VDEKGNEI------EGECSGYLCVKGSwp 517
Cdd:PLN03102 329 ------HAYGLTEaTGPVLFCEWQDEWNRLPENQQMELKARQGVSilgladVDVKNKETqesvprDGKTMGEIVIKGS-- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 518 gafrTLFGDHERYETTYFKPFA-GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGI 596
Cdd:PLN03102 401 ----SIMKGYLKNPKATSEAFKhGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAM 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332006737 597 EHEVKGQGIYAFVTLLEGVPYSEELRKSLVLMVRNQIG-------AFAAPDRIHWAPGLPKTRSGKIMRRILRKIA 665
Cdd:PLN03102 477 PHPTWGETPCAFVVLEKGETTKEDRVDKLVTRERDLIEycrenlpHFMCPRKVVFLQELPKNGNGKILKPKLRDIA 552
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
145-670 |
1.73e-15 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 80.86 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 145 DASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVIL 224
Cdd:PRK10252 481 RYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLI 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 225 TcnavkrgpktinlkaivdAALDQSSKDGVSVGICLTYDNSLATtrentkwqngrdvwwQDVISQYPTSCevewvdaEDP 304
Cdd:PRK10252 561 T------------------TADQLPRFADVPDLTSLCYNAPLAP---------------QGAAPLQLSQP-------HHT 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 305 LFLLYTSGSTGKPKGVL--HT---------------TGGYMIYTATtfKYAFDYKSTDVYWctadcgwitghsyvtygPM 367
Cdd:PRK10252 601 AYIIFTSGSTGRPKGVMvgQTaivnrllwmqnhyplTADDVVLQKT--PCSFDVSVWEFFW-----------------PF 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 368 LNGATVVVfegAP--NYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSLRVLGSVGEPINPSAWRWF- 444
Cdd:PRK10252 662 IAGAKLVM---AEpeAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVFCSGEALPADLCREWq 738
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 445 -------FNVVGDSRCPISDTWWqtetggfmitPLPGAWPQKPGSAT----FPFFGVQPVIVDEKGNEIEGECSGYLCVK 513
Cdd:PRK10252 739 qltgaplHNLYGPTEAAVDVSWY----------PAFGEELAAVRGSSvpigYPVWNTGLRILDARMRPVPPGVAGDLYLT 808
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 514 GswpgafRTLF-GDHERYETTY-------FKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLH 585
Cdd:PRK10252 809 G------IQLAqGYLGRPDLTAsrfiadpFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQAL 882
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 586 PQCAEA---AVVGIEHEVKGQG---IYAFVTLLEGVPY-SEELRKSLvlmvRNQIGAFAAPDRIHWAPGLPKTRSGKIMR 658
Cdd:PRK10252 883 PDVEQAvthACVINQAAATGGDarqLVGYLVSQSGLPLdTSALQAQL----RERLPPHMVPVVLLQLDQLPLSANGKLDR 958
|
570
....*....|....*...
gi 332006737 659 RIL------RKIASRQLE 670
Cdd:PRK10252 959 KALplpelkAQVPGRAPK 976
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
141-656 |
1.92e-15 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 79.44 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 141 ELGVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVhsvvFAGFSADSLAQRIVDCKP 220
Cdd:cd17654 10 QTTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAA----YAPIDPASPEQRSLTVMK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 221 NVILTCNAVKRgpKTINLKAIVDAALDQSSKdgvSVGICLTYdnslattrentkwqngrdvwwqdvisqyptscevewvd 300
Cdd:cd17654 86 KCHVSYLLQNK--ELDNAPLSFTPEHRHFNI---RTDECLAY-------------------------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 301 aedplfLLYTSGSTGKPKGVlHTTGGYMIYTATTFKYAFDYKSTDVYWCTadcgwitghSYVTYGP--------MLNGAT 372
Cdd:cd17654 123 ------VIHTSGTTGTPKIV-AVPHKCILPNIQHFRSLFNITSEDILFLT---------SPLTFDPsvveiflsLSSGAT 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 373 VVVFEGAPNyPDPGRCWDIVDK-YKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSLRVLGSVGEPInPS-----AWRWFFN 446
Cdd:cd17654 187 LLIVPTSVK-VLPSKLADILFKrHRITVLQATPTLFRRFGSQSIKSTVLSATSSLRVLALGGEPF-PSlvilsSWRGKGN 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 447 vvgdsRCPISDTWWQTETGGFMIT--------PLPGAwpqkpgsatFPFFGVQPVIVDEKGNEIEGEcsgyLCVKGSWPG 518
Cdd:cd17654 265 -----RTRIFNIYGITEVSCWALAykvpeedsPVQLG---------SPLLGTVIEVRDQNGSEGTGQ----VFLGGLNRV 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 519 AFRtlfgdhERYETTyfkPFAGYYFSGDGCSRdKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQcAEAAVVGIEh 598
Cdd:cd17654 327 CIL------DDEVTV---PKGTMRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLG-VESCAVTLS- 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 332006737 599 evKGQGIYAFVTlleGVPYSEELRKSLVLmvrNQIGAFAAPDRIHWAPGLPKTRSGKI 656
Cdd:cd17654 395 --DQQRLIAFIV---GESSSSRIHKELQL---TLLSSHAIPDTFVQIDKLPLTSHGKV 444
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
131-661 |
2.05e-15 |
|
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: 79.14 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 131 DKTAIHWEGNelgvdaSLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADS 210
Cdd:cd17645 13 DHVAVVDRGQ------SLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGER 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 211 LAQRIVDCKPNVILTcnavkrgpktinlkaivdaaldqsskdgvsvgicltydnslattrentkwqngrdvwwqdvisqy 290
Cdd:cd17645 87 IAYMLADSSAKILLT----------------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 291 ptscevewvDAEDPLFLLYTSGSTGKPKGVL--HTTggyMIYTATTFKYAFDYKSTDVYWCTADCGWiTGHSYVTYGPML 368
Cdd:cd17645 102 ---------NPDDLAYVIYTSGSTGLPKGVMieHHN---LVNLCEWHRPYFGVTPADKSLVYASFSF-DASAWEIFPHLT 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 369 NGATVVVFEGAPNYpDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKfvtrhsrkSLRVLGSVGEPINPSAWRWF--FN 446
Cdd:cd17645 169 AGAALHVVPSERRL-DLDALNDYFNQEGITISFLPTGAAEQFMQLDNQ--------SLRVLLTGGDKLKKIERKGYklVN 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 447 VVGDSRCPIsdtwwqtetggfMITPLPGAWPQKPGSATFPFFGVQPVIVDEkGNEIEGE-CSGYLCVKGSwpGAFRTLFG 525
Cdd:cd17645 240 NYGPTENTV------------VATSFEIDKPYANIPIGKPIDNTRVYILDE-ALQLQPIgVAGELCIAGE--GLARGYLN 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 526 ----DHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVK 601
Cdd:cd17645 305 rpelTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADG 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 602 GQGIYAFVTLLEGVPYsEELRKSLvlmvRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRIL 661
Cdd:cd17645 385 RKYLVAYVTAPEEIPH-EELREWL----KNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
288-662 |
2.16e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 79.75 E-value: 2.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 288 SQYPTSCEVEWVDAED-----PLF-------LLYTSGSTGKPKGVLHTTGGYMIYT-ATTFKYAFDYKSTDVY------- 347
Cdd:PRK07008 150 GSTPLLCYETLVGAQDgdydwPRFdenqassLCYTSGTTGNPKGALYSHRSTVLHAyGAALPDAMGLSARDAVlpvvpmf 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 348 ----WCTADCGWITGHSYVTYGPMLNGATVvvfegapnypdpgrcWDIVDKYKVSIFYTAPT----LVRSLMRDDDKFVT 419
Cdd:PRK07008 230 hvnaWGLPYSAPLTGAKLVLPGPDLDGKSL---------------YELIEAERVTFSAGVPTvwlgLLNHMREAGLRFST 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 420 rhsrksLR--VLGSVGEPinPSAWRWFFNVVGdsrCPISDTWWQTETGGF-MITPLPGAWPQKPGSATF--------PFF 488
Cdd:PRK07008 295 ------LRrtVIGGSACP--PAMIRTFEDEYG---VEVIHAWGMTEMSPLgTLCKLKWKHSQLPLDEQRkllekqgrVIY 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 489 GVQPVIVDEKGNEI--EGECSGYLCVKGSWpgafrtlfgdherYETTYFK----PF-AGYYFSGDGCSRDKDGYYWLTGR 561
Cdd:PRK07008 364 GVDMKIVGDDGRELpwDGKAFGDLQVRGPW-------------VIDRYFRgdasPLvDGWFPTGDVATIDADGFMQITDR 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 562 VDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVpysEELRKSLVLMVRNQIGAFAAPDR 641
Cdd:PRK07008 431 SKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGA---EVTREELLAFYEGKVAKWWIPDD 507
|
410 420
....*....|....*....|.
gi 332006737 642 IHWAPGLPKTRSGKIMRRILR 662
Cdd:PRK07008 508 VVFVDAIPHTATGKLQKLKLR 528
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
145-663 |
3.29e-15 |
|
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: 78.62 E-value: 3.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 145 DASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIvdckpnvil 224
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCI--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 225 tcnavkrgpKTINLKAIVDAALDqsskdgvsvgicltydnSLATTrentkwqngrdvwwqdvISQYPTSCEVewVDAEDP 304
Cdd:cd05939 72 ---------TVSKAKALIFNLLD-----------------PLLTQ-----------------SSTEPPSQDD--VNFRDK 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 305 LFLLYTSGSTGKPKGVLHTTGGYMIYTATTFkYAFDYKSTDV-YWC-----TAdcGWITGHSYVtygpMLNGATVVVFE- 377
Cdd:cd05939 107 LFYIYTSGTTGLPKAAVIVHSRYYRIAAGAY-YAFGMRPEDVvYDClplyhSA--GGIMGVGQA----LLHGSTVVIRKk 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 378 -GAPNYpdpgrcWDIVDKYKVSIFYTAPTLVRSLM----RDDDKfvtRHsrkslRVLGSVGEPINPSAWRWF---FNV-- 447
Cdd:cd05939 180 fSASNF------WDDCVKYNCTIVQYIGEICRYLLaqppSEEEQ---KH-----NVRLAVGNGLRPQIWEQFvrrFGIpq 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 448 ----VGDSRCPISDTWWQTETG--GFMITPLPGAWPqkpgsatfpffgVQPVIVDEKGNEIEGECSGY--LCVKGSwPGA 519
Cdd:cd05939 246 igefYGATEGNSSLVNIDNHVGacGFNSRILPSVYP------------IRLIKVDEDTGELIRDSDGLciPCQPGE-PGL 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 520 F----------RTLFG------DHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALV 583
Cdd:cd05939 313 LvgkiiqndplRRFDGyvnegaTNKKIARDVFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILS 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 584 LHPQCAEAAVVGIE-HEVKGQ-GIYAFVTLLEGVP---YSEELRKSLVlmvrnqigAFAAPDRIHWAPGLPKTRSGKIMR 658
Cdd:cd05939 393 NVLGLEDVVVYGVEvPGVEGRaGMAAIVDPERKVDldrFSAVLAKSLP--------PYARPQFIRLLPEVDKTGTFKLQK 464
|
....*
gi 332006737 659 RILRK 663
Cdd:cd05939 465 TDLQK 469
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
147-665 |
3.94e-15 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 78.77 E-value: 3.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 147 SLTYSELLQRVCQLANYL-KDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVILT 225
Cdd:PRK08751 50 TITYREADQLVEQFAAYLlGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 226 ----CNAVKRGPKTINLKAIVDAALDQ--SSKDGVSVGICLTYDNSLATtrentKWQNGRDVWWQDVISQ-YPTSCEVEW 298
Cdd:PRK08751 130 idnfGTTVQQVIADTPVKQVITTGLGDmlGFPKAALVNFVVKYVKKLVP-----EYRINGAIRFREALALgRKHSMPTLQ 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 299 VDAEDPLFLLYTSGSTGKPKGVLHTTGGYMIYTATTFKyafdykstdvyWCTADCGWITGHSYV-TYGPML-------NG 370
Cdd:PRK08751 205 IEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQ-----------WLAGTGKLEEGCEVViTALPLYhifaltaNG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 371 ATVVVFEGA----PNYPD-PGRCWDIvDKYKVSIFYTAPTLVRSLMR----DDDKFvtrhsrKSLRVLGSVGEPINPS-A 440
Cdd:PRK08751 274 LVFMKIGGCnhliSNPRDmPGFVKEL-KKTRFTAFTGVNTLFNGLLNtpgfDQIDF------SSLKMTLGGGMAVQRSvA 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 441 WRWFfNVVGdsrCPISDTWWQTETG-GFMITPLpgAWPQKPGSATFPFFGVQPVIVDEKGNEIE-GECsGYLCVKGSwpg 518
Cdd:PRK08751 347 ERWK-QVTG---LTLVEAYGLTETSpAACINPL--TLKEYNGSIGLPIPSTDACIKDDAGTVLAiGEI-GELCIKGP--- 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 519 afRTLFGDHER-YETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIE 597
Cdd:PRK08751 417 --QVMKGYWKRpEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVP 494
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332006737 598 HEVKGQGIYAFVTLLEGVPYSEELRKSlvlmVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKIA 665
Cdd:PRK08751 495 DEKSGEIVKVVIVKKDPALTAEDVKAH----ARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAA 558
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
144-669 |
5.20e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 78.27 E-value: 5.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 144 VDASLTYSELLQRVCQLANYLKDN-GVKKGDAVVIYLPMLMELPIAMLACARIGAVhsVVFAG--FSA--------DSLA 212
Cdd:PRK05677 46 LGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLI--VVNTNplYTAremehqfnDSGA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 213 QRIVdCKPNviLTCNAVKRGPKTINLKAIVDAALDQSSK-DGVSVGICLTYDNSLATTrentkWQNGRDVWWQDVISQ-- 289
Cdd:PRK05677 124 KALV-CLAN--MAHLAEKVLPKTGVKHVIVTEVADMLPPlKRLLINAVVKHVKKMVPA-----YHLPQAVKFNDALAKga 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 290 YPTSCEVEwVDAEDPLFLLYTSGSTGKPKGVLHT-------------------TGGYMIYTATTFKYafdykstDVYWCT 350
Cdd:PRK05677 196 GQPVTEAN-PQADDVAVLQYTGGTTGVAKGAMLThrnlvanmlqcralmgsnlNEGCEILIAPLPLY-------HIYAFT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 351 ADCGWItghsyvtygpMLNGATVVVFegaPNYPD-PGRCWDIvDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRksLRVL 429
Cdd:PRK05677 268 FHCMAM----------MLIGNHNILI---SNPRDlPAMVKEL-GKWKFSGFVGLNTLFVALCNNEAFRKLDFSA--LKLT 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 430 GSVGEPINPSAWRWFFNVVGdsrCPISDTWWQTETggfmiTPLPGAWPQK---PGSATFPFFGVQPVIVDEKGNEIEGEC 506
Cdd:PRK05677 332 LSGGMALQLATAERWKEVTG---CAICEGYGMTET-----SPVVSVNPSQaiqVGTIGIPVPSTLCKVIDDDGNELPLGE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 507 SGYLCVKGswPGAFRtlfGDHERYETTYFKPFA-GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLH 585
Cdd:PRK05677 404 VGELCVKG--PQVMK---GYWQRPEATDEILDSdGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAAL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 586 PQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEElrkSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKIA 665
Cdd:PRK05677 479 PGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKE---QVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEE 555
|
....
gi 332006737 666 SRQL 669
Cdd:PRK05677 556 LKKA 559
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
130-663 |
5.93e-15 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 78.29 E-value: 5.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 130 GDKTAIHWEGNELgvdASLTYSELLQRVCQLANYLKDN-GVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSA 208
Cdd:PRK05620 24 GDTTVTTWGGAEQ---EQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 209 DSL-------AQRIVDCKP-------NVILTCNAVKR----GPKTINLKAIVDAaldqsskDGVSvgiCLTYDNSLattr 270
Cdd:PRK05620 101 DQIvhiinhaEDEVIVADPrlaeqlgEILKECPCVRAvvfiGPSDADSAAAHMP-------EGIK---VYSYEALL---- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 271 entkwqNGRdvwwqdvisqyptSCEVEW--VDAEDPLFLLYTSGSTGKPKGV-------------LHTTGGYMIYTATTF 335
Cdd:PRK05620 167 ------DGR-------------STVYDWpeLDETTAAAICYSTGTTGAPKGVvyshrslylqslsLRTTDSLAVTHGESF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 336 kyafdYKSTDVY----WCTADCGWITGHSYVTYGPMLNGATVVvfegapnypdpgrcwDIVDKYKVSIFYTAPTLVRSLM 411
Cdd:PRK05620 228 -----LCCVPIYhvlsWGVPLAAFMSGTPLVFPGPDLSAPTLA---------------KIIATAMPRVAHGVPTLWIQLM 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 412 RDDDKfvTRHSRKSLRVLGSVGEPINP---SAWRWFFNVvgdsrcPISDTWWQTETG--GFMITPLPGA-----WPQKPG 481
Cdd:PRK05620 288 VHYLK--NPPERMSLQEIYVGGSAVPPiliKAWEERYGV------DVVHVWGMTETSpvGTVARPPSGVsgearWAYRVS 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 482 SATFPFfGVQPVIVDEkGNEIEG--ECSGYLCVKGSW-------------PGAFRTLFGDHERYETTYFKPfAGYYFSGD 546
Cdd:PRK05620 360 QGRFPA-SLEYRIVND-GQVMEStdRNEGEIQVRGNWvtasyyhspteegGGAASTFRGEDVEDANDRFTA-DGWLRTGD 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 547 GCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEELRKSLV 626
Cdd:PRK05620 437 VGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAERLR 516
|
570 580 590
....*....|....*....|....*....|....*..
gi 332006737 627 LMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRK 663
Cdd:PRK05620 517 DQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
303-654 |
3.26e-14 |
|
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: 74.26 E-value: 3.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 303 DPLFLLYTSGSTGKPKGVLHTTGGYMIYTattfkyafdykstdvyWCTADCGWITGHS-YVTYGPM-----LNGATVVVF 376
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQA----------------LVLAVLQAIDEGTvFLNSGPLfhigtLMFTLATFH 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 377 EGAPNY----PDPGRCWDIVDKYKVS-IFYTAPTL--VRSLMRDDdkfvtRHSRKSLRVLgsvgepinPSAWRWFFNVvg 449
Cdd:cd17636 65 AGGTNVfvrrVDAEEVLELIEAERCThAFLLPPTIdqIVELNADG-----LYDLSSLRSS--------PAAPEWNDMA-- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 450 dsrcPISDTWW--------QTETGGFMITplpgAWPQKPGSATF----PFfgVQPVIVDEKGNEI-EGEcSGYLCVKGsw 516
Cdd:cd17636 130 ----TVDTSPWgrkpggygQTEVMGLATF----AALGGGAIGGAgrpsPL--VQVRILDEDGREVpDGE-VGEIVARG-- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 517 PGAFRTLFGdheRYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGI 596
Cdd:cd17636 197 PTVMAGYWN---RPEVNARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGV 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 332006737 597 EHEVKGQGIYAFVTLLEGVPYSEElrkSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSG 654
Cdd:cd17636 274 PDPRWAQSVKAIVVLKPGASVTEA---ELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
127-664 |
6.03e-14 |
|
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: 75.01 E-value: 6.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 127 AGLGDKTAIHWEGNELGVDAsLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACarigavhsvVFAGF 206
Cdd:cd05906 20 AERGPTKGITYIDADGSEEF-QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWAC---------VLAGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 207 SAdslaqrivdckpnVILTCNAVKRGPKTINLKAI-VDAALDQsskdgvsvGICLTYDNSLATTRENTKWQnGRDVWWQD 285
Cdd:cd05906 90 VP-------------APLTVPPTYDEPNARLRKLRhIWQLLGS--------PVVLTDAELVAEFAGLETLS-GLPGIRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 286 VISQYP-TSCEVEWV--DAEDPLFLLYTSGSTGKPKGVLHTTGGYMIYTATTFKyAFDYKSTDVY--WCTADcgWITGHS 360
Cdd:cd05906 148 SIEELLdTAADHDLPqsRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQ-HNGLTPQDVFlnWVPLD--HVGGLV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 361 YVTYGPMLNG------ATVVVFEgapnypDPGRCWDIVDKYKVSIFYtAPTLVRSLMRDD-DKFVTRH-SRKSLRVLGSV 432
Cdd:cd05906 225 ELHLRAVYLGcqqvhvPTEEILA------DPLRWLDLIDRYRVTITW-APNFAFALLNDLlEEIEDGTwDLSSLRYLVNA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 433 GEPINPSAWRWFFNVVGDSRCP---ISDTWWQTETGGFMITPLPGAWPQKPGSATF-----PFFGVQPVIVDEKGNEIEG 504
Cdd:cd05906 298 GEAVVAKTIRRLLRLLEPYGLPpdaIRPAFGMTETCSGVIYSRSFPTYDHSQALEFvslgrPIPGVSMRIVDDEGQLLPE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 505 ECSGYLCVKGswPGAFRTLFGDHERYETTYFKpfAGYYFSGD-GCSRDkdGYYWLTGRVDDVINVSGHRIGTAEVESAL- 582
Cdd:cd05906 378 GEVGRLQVRG--PVVTKGYYNNPEANAEAFTE--DGWFRTGDlGFLDN--GNLTITGRTKDTIIVNGVNYYSHEIEAAVe 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 583 ---VLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEELRKSLVLMVRNQIGafAAPDR-IHWAPG-LPKTRSGKIM 657
Cdd:cd05906 452 evpGVEPSFTAAFAVRDPGAETEELAIFFVPEYDLQDALSETLRAIRSVVSREVG--VSPAYlIPLPKEeIPKTSLGKIQ 529
|
....*..
gi 332006737 658 RRILRKI 664
Cdd:cd05906 530 RSKLKAA 536
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
149-663 |
8.82e-14 |
|
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: 74.01 E-value: 8.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 149 TYSELLQRVCQLANYLKDN-GVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLaqriVDCkpnvILTCN 227
Cdd:cd05937 7 TYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPL----IHC----LKLSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 228 AvkrgpktinlKAIVdaaldqsskdgvsvgicltydnslattrentkwqngrdvwwqdvisqyptscevewVDAEDPLFL 307
Cdd:cd05937 79 S----------RFVI--------------------------------------------------------VDPDDPAIL 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 308 LYTSGSTGKPKGVLHTTGgyMIY-TATTFKYAFDYKSTD-VYWC----------TADCGWITGHSYVTYGP--------- 366
Cdd:cd05937 93 IYTSGTTGLPKAAAISWR--RTLvTSNLLSHDLNLKNGDrTYTCmplyhgtaafLGACNCLMSGGTLALSRkfsasqfwk 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 367 --MLNGATVVVFEG--------APNYPDP-----------GRCWDIVDKYK----VSI---FYTAPTLVRSLmrdddkfv 418
Cdd:cd05937 171 dvRDSGATIIQYVGelcryllsTPPSPYDrdhkvrvawgnGLRPDIWERFRerfnVPEigeFYAATEGVFAL-------- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 419 TRHSRKSLrVLGSVGEpiNPSAWRWFFN-----VVGDsrcPISDTWWQTETGGFMI-TPLpgawpQKPGSATFPFFGVQp 492
Cdd:cd05937 243 TNHNVGDF-GAGAIGH--HGLIRRWKFEnqvvlVKMD---PETDDPIRDPKTGFCVrAPV-----GEPGEMLGRVPFKN- 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 493 vivdekgneiegecsgylcvKGSWPGAFRTLFGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHR 572
Cdd:cd05937 311 --------------------REAFQGYLHNEDATESKLVRDVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSEN 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 573 IGTAEVESALVLHPQCAEAAVVGIE---HEvkGQGIYAFVTLLEGVPYSEELRKS-LVLMVRNQIGAFAAPDRIHWAPGL 648
Cdd:cd05937 371 VSTTEVADVLGAHPDIAEANVYGVKvpgHD--GRAGCAAITLEESSAVPTEFTKSlLASLARKNLPSYAVPLFLRLTEEV 448
|
570
....*....|....*
gi 332006737 649 PKTRSGKIMRRILRK 663
Cdd:cd05937 449 ATTDNHKQQKGVLRD 463
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
146-661 |
1.31e-13 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 73.89 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 146 ASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVILT 225
Cdd:PRK05857 40 SALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 226 CNAVKRGPKTI--NLKAIVDAALDQSSKDGVSVgicltydNSLATTRENTKWQNGrdvwwqdvisqyptscevewvdAED 303
Cdd:PRK05857 120 APGSKMASSAVpeALHSIPVIAVDIAAVTRESE-------HSLDAASLAGNADQG----------------------SED 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 304 PLFLLYTSGSTGKPKGVLhttggymIYTATTFKYAFDYKSTDVYWCTadcgWITGHSyvTYGPM---------------L 368
Cdd:PRK05857 171 PLAMIFTSGTTGEPKAVL-------LANRTFFAVPDILQKEGLNWVT----WVVGET--TYSPLpathigglwwiltclM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 369 NGATVVVfeGAPNypdPGRCWDIVDKYKVSIFYTAPTLVRSLMrDDDKFvTRHSRKSLRVLGSVGEPINPSAWRwFFNVV 448
Cdd:PRK05857 238 HGGLCVT--GGEN---TTSLLEILTTNAVATTCLVPTLLSKLV-SELKS-ANATVPSLRLVGYGGSRAIAADVR-FIEAT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 449 GdsrCPISDTWWQTETGGFMITpLP---GAWPQ-KPGSATFPFFGVQPVIVDEKG---NEIEGECS---GYLCVKGswPG 518
Cdd:PRK05857 310 G---VRTAQVYGLSETGCTALC-LPtddGSIVKiEAGAVGRPYPGVDVYLAATDGigpTAPGAGPSasfGTLWIKS--PA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 519 AFRTLFGDHERYETTYFKpfaGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEH 598
Cdd:PRK05857 384 NMLGYWNNPERTAEVLID---GWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPD 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 599 EVKGqgiyAFVTLLEgVPYSE-------ELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRIL 661
Cdd:PRK05857 461 EEFG----ALVGLAV-VASAEldesaarALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
535-663 |
9.98e-13 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 70.07 E-value: 9.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 535 FKPFA--GYYFSGDGCSRDkDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVtll 612
Cdd:PRK07824 227 PDPFAepGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAV--- 302
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 332006737 613 EGVPYSEELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRK 663
Cdd:PRK07824 303 VGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
145-597 |
1.20e-12 |
|
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: 70.46 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 145 DASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVIl 224
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 225 tcnavkrgpktinlkaIVDAAldqsskdgvsvgicltydnslattrentkwqngrdvwwqdvisqyptscevewvdaedp 304
Cdd:cd05940 80 ----------------VVDAA----------------------------------------------------------- 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 305 lFLLYTSGSTGKPKGVLHTTGGYmIYTATTFKYAFDYKSTDVYWCTADCGWITGHSYVTYGPMLNGATVVVFE--GAPNY 382
Cdd:cd05940 85 -LYIYTSGTTGLPKAAIISHRRA-WRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKkfSASNF 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 383 pdpgrcWDIVDKYKVSIFYTAPTLVRSLM----RDDDKfvtRHsrkSLRVLgsVGEPINPSAWRWFFNVVGDSRcpISDT 458
Cdd:cd05940 163 ------WDDIRKYQATIFQYIGELCRYLLnqppKPTER---KH---KVRMI--FGNGLRPDIWEEFKERFGVPR--IAEF 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 459 WWQTE--TGGFMITPLPGAWPQKPgSATFPFFGVQPVIVD-EKGNEIEGEcSGYL--CVKGSwPGAFRTLFGDHERYEtT 533
Cdd:cd05940 227 YAATEgnSGFINFFGKPGAIGRNP-SLLRKVAPLALVKYDlESGEPIRDA-EGRCikVPRGE-PGLLISRINPLEPFD-G 302
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332006737 534 YFKPFA--------------GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIE 597
Cdd:cd05940 303 YTDPAAtekkilrdvfkkgdAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQ 380
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
306-693 |
2.24e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 70.97 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 306 FLLYTSGSTGKPKGVLHTTGGYMIYTATTFKYaFDYKSTDVYWCTADCGWITGHSYVTYGPMLNGATVVVfegaPN--YP 383
Cdd:PRK05691 3873 YVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPY-LALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIV----PNaiAH 3947
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 384 DPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDdkfvtRHSRKSLRVLGSVGEPINPS-AWRWF--------FNVVGDSRCP 454
Cdd:PRK05691 3948 DPQGLLAHVQAQGITVLESVPSLIQGMLAED-----RQALDGLRWMLPTGEAMPPElARQWLqrypqiglVNAYGPAECS 4022
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 455 ISDTWWQTETGGFMITPLPGAWPQKPGsatfpffgvQPVIVDEKGNEIEGECSGYLCVKGSwpGAFRTLFGDHERYETTY 534
Cdd:PRK05691 4023 DDVAFFRVDLASTRGSYLPIGSPTDNN---------RLYLLDEALELVPLGAVGELCVAGT--GVGRGYVGDPLRTALAF 4091
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 535 F-KPFAG----YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAvVGIEHEVKGQGIYAFV 609
Cdd:PRK05691 4092 VpHPFGApgerLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAA-VAVQEGVNGKHLVGYL 4170
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 610 TLLEGVPYSEELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKIASRQLEElgdTSTLADPSVVDQLIA 689
Cdd:PRK05691 4171 VPHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQS---QAYLAPRNELEQTLA 4247
|
....*.
gi 332006737 690 --LADV 693
Cdd:PRK05691 4248 tiWADV 4253
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
494-675 |
8.49e-12 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 68.30 E-value: 8.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 494 IVDEKGNEI-----EGE--CSGYLCVKGSWPGAFRTlfgdHERYETtyfkpfAGYYFSGDGCSRDKDGYYWLTGRVDDVI 566
Cdd:PRK08315 384 IVDPETGETvprgeQGElcTRGYSVMKGYWNDPEKT----AEAIDA------DGWMHTGDLAVMDEEGYVNIVGRIKDMI 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 567 NVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYS-EELRKSLvlmvRNQIGAFAAPDRIHWA 645
Cdd:PRK08315 454 IRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTeEDVRDFC----RGKIAHYKIPRYIRFV 529
|
170 180 190
....*....|....*....|....*....|
gi 332006737 646 PGLPKTRSGKIMRRILRKIAsrqLEELGDT 675
Cdd:PRK08315 530 DEFPMTVTGKIQKFKMREMM---IEELGLQ 556
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
148-658 |
1.41e-11 |
|
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: 67.08 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 148 LTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVILTcn 227
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 228 avkrgpktinlkaivdaaldqSSKDGVSVgicltydnslattrentkwqngrdvwwqdvisqyptscevewvdaedplfL 307
Cdd:cd05914 86 ---------------------SDEDDVAL--------------------------------------------------I 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 308 LYTSGSTGKPKGVLHTtgGYMIYTATTFKYAFD-YKSTDVYWCTADCGWITGHSYVTYGPMLNGATVVV----------- 375
Cdd:cd05914 95 NYTSGTTGNSKGVMLT--YRNIVSNVDGVKEVVlLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFldkipsakiia 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 376 ---FEGAPNYPDPgRCWDIVDKYKVSIFytaPTLVRSLMR-------DDDKFVTRHSRKSLRVLG-------SVGEPINP 438
Cdd:cd05914 173 lafAQVTPTLGVP-VPLVIEKIFKMDII---PKLTLKKFKfklakkiNNRKIRKLAFKKVHEAFGgnikefvIGGAKINP 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 439 SAWRwFFNVVGdsrCPISDTWWQTETGGFMITPLPGAwpQKPGSATFPFFGVQPVIVDEKGNEIEGE--CSGYLCVKGSW 516
Cdd:cd05914 249 DVEE-FLRTIG---FPYTIGYGMTETAPIISYSPPNR--IRLGSAGKVIDGVEVRIDSPDPATGEGEiiVRGPNVMKGYY 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 517 --PGAFRTLFgDHEryettyfkpfaGYYFSGDGCSRDKDGYYWLTGRVDDVI-NVSGHRIGTAEVESALVLHPQCAEAAV 593
Cdd:cd05914 323 knPEATAEAF-DKD-----------GWFHTGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMPFVLESLV 390
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332006737 594 VgiEHEVKGQGI------YAFVTLLEGVPYSEELRKSLVLMVRNQIGAFA--APDRIHWAPgLPKTRSGKIMR 658
Cdd:cd05914 391 V--VQEKKLVALayidpdFLDVKALKQRNIIDAIKWEVRDKVNQKVPNYKkiSKVKIVKEE-FEKTPKGKIKR 460
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
147-661 |
1.94e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 67.89 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 147 SLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVILTc 226
Cdd:PRK05691 2213 TLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLS- 2291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 227 navkrgpktinlkaivDAALDQSS---KDGVSVGiCLTYDnslattrentkwqngrdvwwQDVISQYPTSCEVEWVDAED 303
Cdd:PRK05691 2292 ----------------DRALFEALgelPAGVARW-CLEDD--------------------AAALAAYSDAPLPFLSLPQH 2334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 304 PLFLLYTSGSTGKPKGVLHTTGGYMIYTATTFKyAFDYKSTDV----YWCTADCGwitghSYVTYGPMLNGATVVV-FEG 378
Cdd:PRK05691 2335 QAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIE-RFGMRADDCelhfYSINFDAA-----SERLLVPLLCGARVVLrAQG 2408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 379 ApnypdpgrcWD------IVDKYKVSIFYTAPTLVRSLMRdddKFVTRHSRKSLRVLGSVGEPINPSAWR---------W 443
Cdd:PRK05691 2409 Q---------WGaeeicqLIREQQVSILGFTPSYGSQLAQ---WLAGQGEQLPVRMCITGGEALTGEHLQrirqafapqL 2476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 444 FFNVVGdsrcpisdtwwQTETggfMITPLPGAWPQ--KPGSATFPFFGV----QPVIVDEKGNEIEGECSGYLCVKGSwp 517
Cdd:PRK05691 2477 FFNAYG-----------PTET---VVMPLACLAPEqlEEGAASVPIGRVvgarVAYILDADLALVPQGATGELYVGGA-- 2540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 518 GAFRtlfGDHERYETTYFK----PFAG----YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCA 589
Cdd:PRK05691 2541 GLAQ---GYHDRPGLTAERfvadPFAAdggrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVR 2617
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332006737 590 EAAVVGIEHEVKGQGIYAFVTLLEGVPYSE--ELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRIL 661
Cdd:PRK05691 2618 EAVVLALDTPSGKQLAGYLVSAVAGQDDEAqaALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
148-367 |
5.95e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 62.69 E-value: 5.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 148 LTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSL--AQRIVDCKpnVILt 225
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALayALRETECK--AIV- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 226 CNAvKRGPKTINLkaivdaaldqsSKDGVSVGICLTYDNSLAttrENTKWQNGRDVWWQDVI-------SQYP-TSCEve 297
Cdd:PTZ00216 199 CNG-KNVPNLLRL-----------MKSGGMPNTTIIYLDSLP---ASVDTEGCRLVAWTDVVakghsagSHHPlNIPE-- 261
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 298 wvDAEDPLFLLYTSGSTGKPKGVLHTTGgymiyTATTFKYAFDYKSTDVYWCTADcgwitGHSYVTYGPM 367
Cdd:PTZ00216 262 --NNDDLALIMYTSGTTGDPKGVMHTHG-----SLTAGILALEDRLNDLIGPPEE-----DETYCSYLPL 319
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
300-661 |
2.11e-09 |
|
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: 60.11 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 300 DAEDPLFLLYTSGSTGKPKGVLHTTGGYM-IYTATTFKYAFDYKSTDVYWCTAdcgwitghSYV-------TYGPMLNGA 371
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSVVnLRTSLSERYFGRDNGDEAVLFFS--------NYVfdffveqMTLALLNGQ 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 372 TVVVFEGAPNYpDPGRCWDIVDKYKVSIFYTAPTLVRslMRDDDkfvtrhSRKSLRVLGSVGEPINPSAwrwFFNVVGDS 451
Cdd:cd17648 164 KLVVPPDEMRF-DPDRFYAYINREKVTYLSGTPSVLQ--QYDLA------RLPHLKRVDAAGEEFTAPV---FEKLRSRF 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 452 RCPISDTWWQTETGGF-MITPLPGAwPQKPGSATFPFFGV---------QPVIVDEKGN-EIEGEC--SGY-----LCVK 513
Cdd:cd17648 232 AGLIINAYGPTETTVTnHKRFFPGD-QRFDKSLGRPVRNTkcyvlndamKRVPVGAVGElYLGGDGvaRGYlnrpeLTAE 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 514 GSWPGAFRTlfgDHERYETTYfkpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAV 593
Cdd:cd17648 311 RFLPNPFQT---EQERARGRN----ARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAV 383
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332006737 594 VGIEHEVKGQG-----IYAFVTLLEGVPYSEELRKSLvlmvRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRIL 661
Cdd:cd17648 384 VAKEDASQAQSriqkyLVGYYLPEPGHVPESDLLSFL----RAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
535-670 |
3.36e-09 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 59.62 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 535 FKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEG 614
Cdd:PRK07445 319 ILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDP 398
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 332006737 615 VPYSEELRKSLvlmvRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKIASRQLE 670
Cdd:PRK07445 399 SISLEELKTAI----KDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQRLG 450
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
148-688 |
3.72e-09 |
|
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: 59.68 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 148 LTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVILtcn 227
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 228 avkrgpktinlkaivdaaLDQSSKDgvsvgicltydnsLATtrentkwqngrdvwwqdvisqyptscevewvdaedplfL 307
Cdd:cd17640 83 ------------------VENDSDD-------------LAT--------------------------------------I 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 308 LYTSGSTGKPKGVLHTTGGyMIYTATTFKYAFDYKSTDVYWCTADCgWitgHSY---VTYGPMLNGATVVvFEGAPNYPD 384
Cdd:cd17640 94 IYTSGTTGNPKGVMLTHAN-LLHQIRSLSDIVPPQPGDRFLSILPI-W---HSYersAEYFIFACGCSQA-YTSIRTLKD 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 385 pgrcwDIvDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSLRVLG---SVGE---PIN-----PSAWRWFFNVVGdsrC 453
Cdd:cd17640 168 -----DL-KRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLfflSGGIfkfGISgggalPPHVDTFFEAIG---I 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 454 PISDTWWQTETGGFMITPLPgaWPQKPGSATFPFFGVQPVIVDEKGNEI-EGECSGYLCVKGswPGAFRTLFGDHEryET 532
Cdd:cd17640 239 EVLNGYGLTETSPVVSARRL--KCNVRGSVGRPLPGTEIKIVDPEGNVVlPPGEKGIVWVRG--PQVMKGYYKNPE--AT 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 533 TYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVS-GHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIyafvtl 611
Cdd:cd17640 313 SKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLGALI------ 386
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332006737 612 legVPYSEELRKSLvlmvrNQIGAFAAPDRIHWAPGLPKTR--SGKIMRRILRKIASRQLEELGDTSTLADPSVVDQLI 688
Cdd:cd17640 387 ---VPNFEELEKWA-----KESGVKLANDRSQLLASKKVLKlyKNEIKDEISNRPGFKSFEQIAPFALLEEPFIENGEM 457
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
148-623 |
6.38e-09 |
|
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: 58.77 E-value: 6.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 148 LTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVILTcn 227
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIFT-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 228 avkrgpktinlkaivdaaldqsskdgvsvgicltyDNSlattrentkwqngrdvwwqdvisqyptscevewvdAEDPLFL 307
Cdd:cd17639 84 -----------------------------------DGK-----------------------------------PDDLACI 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 308 LYTSGSTGKPKGVLHTTGGyMIYTATTFkyafdykstdvywctadCGWITGH-----SYVTYGP-------------MLN 369
Cdd:cd17639 94 MYTSGSTGNPKGVMLTHGN-LVAGIAGL-----------------GDRVPELlgpddRYLAYLPlahifelaaenvcLYR 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 370 GATV-------------------------VVFEGAPnypdpgRCWDIVDK-----------YKVSIFYTAPTLVRSLMRD 413
Cdd:cd17639 156 GGTIgygsprtltdkskrgckgdltefkpTLMVGVP------AIWDTIRKgvlaklnpmggLKRTLFWTAYQSKLKALKE 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 414 D------DKFVTRHSRKS----LRVLGSVGEPINPSAWRwFFNVVGdsrCPISDTWWQTETGGFMITPLPGAWpqKPGSA 483
Cdd:cd17639 230 GpgtpllDELVFKKVRAAlggrLRYMLSGGAPLSADTQE-FLNIVL---CPVIQGYGLTETCAGGTVQDPGDL--ETGRV 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 484 TFPFFGVQPVIVD-EKGNEI--EGECSGYLCVKGswPGAFRTLFGDHERYETTYFKpfAGYYFSGDGCSRDKDGYYWLTG 560
Cdd:cd17639 304 GPPLPCCEIKLVDwEEGGYStdKPPPRGEILIRG--PNVFKGYYKNPEKTKEAFDG--DGWFHTGDIGEFHPDGTLKIID 379
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332006737 561 RVDD-VINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKgqgIYAFVtllegVPYSEELRK 623
Cdd:cd17639 380 RKKDlVKLQNGEYIALEKLESIYRSNPLVNNICVYADPDKSY---PVAIV-----VPNEKHLTK 435
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
131-596 |
4.33e-08 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 56.45 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 131 DKTAI----HWEGNELGVDASLTYSELLQRVCQLANYLKDNGVKKGD-AVVIYLPMLmELPIAMLACARIGAVHSVVFAG 205
Cdd:PRK09274 21 DQLAVavpgGRGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMrAVLMVTPSL-EFFALTFALFKAGAVPVLVDPG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 206 FSADSLAQRIVDCKPNVILTCnavkrgPKTINLKAIVDAALDqSSKDGVSVG-ICLTYDNSLATTRENTKwqngrdvwwq 284
Cdd:PRK09274 100 MGIKNLKQCLAEAQPDAFIGI------PKAHLARRLFGWGKP-SVRRLVTVGgRLLWGGTTLATLLRDGA---------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 285 dvisqyPTSCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGgymIYTA--TTFKYAFDYKSTDVYWCTADCgwitghsYV 362
Cdd:PRK09274 163 ------AAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHG---MFEAqiEALREDYGIEPGEIDLPTFPL-------FA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 363 TYGPMLnGATVVVFEGAPNYP---DPGRCWDIVDKYKVSIFYTAPTLVRSLmrdddkfvTRHSRKSLRVLGSV------G 433
Cdd:PRK09274 227 LFGPAL-GMTSVIPDMDPTRPatvDPAKLFAAIERYGVTNLFGSPALLERL--------GRYGEANGIKLPSLrrvisaG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 434 EPINPSAWRWF----------FNVVGDSRC-PIS---------DTWWQTETGGfmitplpGAWPQKPgsatfpffgVQPV 493
Cdd:PRK09274 298 APVPIAVIERFramlppdaeiLTPYGATEAlPISsiesreilfATRAATDNGA-------GICVGRP---------VDGV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 494 ------IVDEKGNEIEG--ECS----GYLCVKGswP----------------------GAFRTLFGDheryettyfkpfA 539
Cdd:PRK09274 362 evriiaISDAPIPEWDDalRLAtgeiGEIVVAG--PmvtrsyynrpeatrlakipdgqGDVWHRMGD------------L 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 332006737 540 GYyfsgdgcsRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGI 596
Cdd:PRK09274 428 GY--------LDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGV 476
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
133-320 |
7.20e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 55.72 E-value: 7.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 133 TAIHWEGNELGVDASLTYSELLQRVCQLANYLKDNGVkKGDAVVIYLPMLMELPIAMLA--CARIGAVH-SVVFAGFSAD 209
Cdd:PRK05850 21 TFIDYEQDPAGVAETLTWSQLYRRTLNVAEELRRHGS-TGDRAVILAPQGLEYIVAFLGalQAGLIAVPlSVPQGGAHDE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 210 SLAQRIVDCKPNVILTCNAVkrgpktinlkaIVDAALDQSSKDGVSVGICLTYDnSLattrentkwqngrdvwwqDVISq 289
Cdd:PRK05850 100 RVSAVLRDTSPSVVLTTSAV-----------VDDVTEYVAPQPGQSAPPVIEVD-LL------------------DLDS- 148
|
170 180 190
....*....|....*....|....*....|.
gi 332006737 290 yPTSCEVEWVDAEDPLFLLYTSGSTGKPKGV 320
Cdd:PRK05850 149 -PRGSDARPRDLPSTAYLQYTSGSTRTPAGV 178
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
301-596 |
2.29e-07 |
|
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: 54.00 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 301 AEDPLFLLYTSGSTGKPKGVLhttggymiYTATTFKYAFDYKSTDVYWCTADCGWITGHSYVTYGPMLnGATVVVFEGAP 380
Cdd:cd05910 84 ADEPAAILFTSGSTGTPKGVV--------YRHGTFAAQIDALRQLYGIRPGEVDLATFPLFALFGPAL-GLTSVIPDMDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 381 NYP---DPGRCWDIVDKYKVSIFYTAPTLVRSLMRdddkFVTRHSRK--SLRVLGSVGEPINP-SAWRW---------FF 445
Cdd:cd05910 155 TRParaDPQKLVGAIRQYGVSIVFGSPALLERVAR----YCAQHGITlpSLRRVLSAGAPVPIaLAARLrkmlsdeaeIL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 446 NVVGDSRC-PIS---DTWWQTETggfmiTPLPgawpqKPGSAT---FPFFGVQPVIV---DEKGNEIEGECS------GY 509
Cdd:cd05910 231 TPYGATEAlPVSsigSRELLATT-----TAAT-----SGGAGTcvgRPIPGVRVRIIeidDEPIAEWDDTLElprgeiGE 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 510 LCVKGswPGAFRTLfgdHERYETTYFK--PFAGYYF---SGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVL 584
Cdd:cd05910 301 ITVTG--PTVTPTY---VNRPVATALAkiDDNSEGFwhrMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNT 375
|
330
....*....|..
gi 332006737 585 HPQCAEAAVVGI 596
Cdd:cd05910 376 HPGVRRSALVGV 387
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
149-669 |
4.95e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 53.08 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 149 TYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMEL-PIAMLACARIGAV-------HSVVFAGFSADSLAqrivdckp 220
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIaPTAQGLWMRGASLtmlhqptPRTDLAVWAEDTLR-------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 221 nvilTCNAVkrGPKTINLKAIVDAALDQSSKDGVSVgicLTYDNSLAttrentkwqngrdvwwqdvisqyPTSCEVEWVD 300
Cdd:PRK07768 103 ----VIGMI--GAKAVVVGEPFLAAAPVLEEKGIRV---LTVADLLA-----------------------ADPIDPVETG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 301 AEDPLFLLYTSGSTGKPKGVLHTTG-----GYMIYTATTFKYAFDYKstdVYW--CTADCGWItghSYVTYgPMLNGATV 373
Cdd:PRK07768 151 EDDLALMQLTSGSTGSPKAVQITHGnlyanAEAMFVAAEFDVETDVM---VSWlpLFHDMGMV---GFLTV-PMYFGAEL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 374 VVFEGAPNYPDPGRCWDIVDKYKVSIfYTAPT-----LVRSLMRDDDKfvTRHSRKSLRVLGSVGEPINPSAWRWFFNVV 448
Cdd:PRK07768 224 VKVTPMDFLRDPLLWAELISKYRGTM-TAAPNfayalLARRLRRQAKP--GAFDLSSLRFALNGAEPIDPADVEDLLDAG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 449 G----DSRCPISDTWWQTETGGFMITPLPG-----------------AWPQKPGSAT------FPFFGVQPVIVDEKGN- 500
Cdd:PRK07768 301 ArfglRPEAILPAYGMAEATLAVSFSPCGAglvvdevdadllaalrrAVPATKGNTRrlatlgPPLPGLEVRVVDEDGQv 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 501 ---------EIEGEC--SGYLCVKGswpgaFRTLFGDHeryettyfkpfaGYYFSGDGCSRDKDGYYWLTGRVDDVINVS 569
Cdd:PRK07768 381 lpprgvgviELRGESvtPGYLTMDG-----FIPAQDAD------------GWLDTGDLGYLTEEGEVVVCGRVKDVIIMA 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 570 GHRIGTAEVESALV----LHPQCAEAavVGIEHEVKGQGiyaFVTLLEGVPYSEE-----LRKSLVLMVRNQIGafAAPD 640
Cdd:PRK07768 444 GRNIYPTDIERAAArvegVRPGNAVA--VRLDAGHSREG---FAVAVESNAFEDPaevrrIRHQVAHEVVAEVG--VRPR 516
|
570 580 590
....*....|....*....|....*....|.
gi 332006737 641 RIH-WAPG-LPKTRSGKimrriLRKIASRQL 669
Cdd:PRK07768 517 NVVvLGPGsIPKTPSGK-----LRRANAAEL 542
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
131-320 |
5.50e-07 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 52.59 E-value: 5.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 131 DKTAIHWEGnelgvdASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGavHSVVFAGFSadS 210
Cdd:PRK04813 17 DFPAYDYLG------EKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAG--HAYIPVDVS--S 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 211 LAQRIVD----CKPNVILtcnavkrgpktinlkAIVDAALDQsskDGVSVgicLTYDNSlattrentkwqngrdvwwQDV 286
Cdd:PRK04813 87 PAERIEMiievAKPSLII---------------ATEELPLEI---LGIPV---ITLDEL------------------KDI 127
|
170 180 190
....*....|....*....|....*....|....
gi 332006737 287 ISQYPTSCEVEWVDAEDPLFLLYTSGSTGKPKGV 320
Cdd:PRK04813 128 FATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGV 161
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
543-677 |
7.81e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 48.88 E-value: 7.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 543 FSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPySEELR 622
Cdd:PRK08308 294 FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEID-PVQLR 372
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 332006737 623 KslvlMVRNQIGAFAAPDRIHWAPGLPKTRSGKImrrilrkiaSRQLEELGDTST 677
Cdd:PRK08308 373 E----WCIQHLAPYQVPHEIESVTEIPKNANGKV---------SRKLLELGEVTA 414
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
581-692 |
4.12e-05 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 46.30 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 581 ALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVpYSEELRKSLVlmvrnQIGAFAAPDRIHWAPGLPKTRSGKIMRRI 660
Cdd:PRK09188 248 ALKSDPAVSDVAIALFSLPAKGVGLYAFVEAELPA-DEKSLRARLA-----GAKPPKPPEHIQPVAALPRDADGTVRDDI 321
|
90 100 110
....*....|....*....|....*....|..
gi 332006737 661 LRKIASRQLEELGDtsTLADPSVVDQLIALAD 692
Cdd:PRK09188 322 LRLIAMNQIDELDD--LLREPEIRGLVEAIAA 351
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
147-321 |
6.41e-05 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 46.60 E-value: 6.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 147 SLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGF-------------------- 206
Cdd:TIGR03443 270 SFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYpparqtiylsvakpralivi 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 207 -SADSLAQRIVDCKPN---VILTCNAVkrgpKTINLKAIVDAALDQSSKDgvsvgiCLTYDNSLATTRENtkwqngrdvw 282
Cdd:TIGR03443 350 eKAGTLDQLVRDYIDKeleLRTEIPAL----ALQDDGSLVGGSLEGGETD------VLAPYQALKDTPTG---------- 409
|
170 180 190
....*....|....*....|....*....|....*....
gi 332006737 283 wqdVIsqyptscevewVDAEDPLFLLYTSGSTGKPKGVL 321
Cdd:TIGR03443 410 ---VV-----------VGPDSNPTLSFTSGSEGIPKGVL 434
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
147-202 |
3.18e-04 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 44.05 E-value: 3.18e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 332006737 147 SLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVV 202
Cdd:cd17647 20 SFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVI 75
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
282-430 |
1.14e-03 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 42.11 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 282 WWQDVISQYPTSCEVEWV---------DAEDPLFLLYTSGSTGKPKGVLHTTGGYMIYTATTFKYaFDYKSTDVYWCTAD 352
Cdd:PRK06334 154 FWEKCRIGIYMSIPFEWLmrwfgvsdkDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKF-FSPKEDDVMMSFLP 232
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332006737 353 CGWITGHSYVTYGPMLNGATvVVFEGAPNYPDpgRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSLRVLG 430
Cdd:PRK06334 233 PFHAYGFNSCTLFPLLSGVP-VVFAYNPLYPK--KIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIG 307
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
309-347 |
5.87e-03 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 39.89 E-value: 5.87e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 332006737 309 YTSGSTGKPKGVLHTTGGYMIYTATTFKYAFDYKS---TDVY 347
Cdd:cd05927 121 YTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKinpTDVY 162
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
518-653 |
7.02e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 39.70 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332006737 518 GAFRTLFGDHERYETTyfkpfaGYYFSgdgcsRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIE 597
Cdd:PRK07868 825 SVKRGVFAPADTWIST------EYLFR-----RDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGVE 893
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 332006737 598 HEVKGQGIYAFVTLLEGVPYSEELRKSLVLMVRNQigafaAPDRIHWAPGLPKTRS 653
Cdd:PRK07868 894 VGGRQLAVAAVTLRPGAAITAADLTEALASLPVGL-----GPDIVHVVPEIPLSAT 944
|
|
| |
