|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
6-648 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 1347.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 6 KHPIPANIAERCLINPEQYKAQYQQSITDPDTFWGEQGKILDWIRPYtrvkNTSFAPGNISIKWYEDGTLNLAANCLDRH 85
Cdd:PRK00174 1 VFPPPAEFAANALIDMEQYKALYQESVEDPEGFWAEQAKRLDWFKPF----DTVLDWNAPFIKWFEDGELNVSYNCLDRH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 86 LAERGDQTAIIWEGDDASQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGG 165
Cdd:PRK00174 77 LKTRGDKVAIIWEGDDPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 166 FSPEAVAGRIIDSSSRLVITADEGLRAGRAIPLKKNVDDALKNPNvnSIEHVVVLKRTGGKIDWQEGRDLWWSDLMANAS 245
Cdd:PRK00174 157 FSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALANCP--SVEKVIVVRRTGGDVDWVEGRDLWWHELVAGAS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 246 AEHRPVEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGA 325
Cdd:PRK00174 235 DECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 326 TTLMFEGVPNWPTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNE 405
Cdd:PRK00174 315 TTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVGGE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 406 KCPVMDTWWQTETGGFMITPLPGAIELKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIADSWPGQARTLFGDHERFE 485
Cdd:PRK00174 395 RCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDPWPGMMRTIYGDHERFV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 486 QTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTL 565
Cdd:PRK00174 475 KTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 566 NHGEEPTPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDTsNLGDTSTLADPGVVEKLLEEK 645
Cdd:PRK00174 555 KGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEGEE-ILGDTSTLADPSVVEKLIEAR 633
|
...
gi 839746169 646 QAI 648
Cdd:PRK00174 634 QNR 636
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
18-644 |
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: 1203.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 18 LINPEQYKAQYQQSITDPDTFWGEQGK-ILDWIRPYTRVKNTSFAPgniSIKWYEDGTLNLAANCLDRHLAERGDQTAII 96
Cdd:TIGR02188 1 IANLEQYKELYEESIEDPDKFWAKLAReLLDWFKPFTKVLDWSFPP---FYKWFVGGELNVSYNCVDRHLEARPDKVAII 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 97 WEGDDASQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRII 176
Cdd:TIGR02188 78 WEGDEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRIN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 177 DSSSRLVITADEGLRAGRAIPLKKNVDDALKNPNVnSIEHVVVLKRTGGKID-WQEGRDLWWSDLMANASAEHRPVEMNA 255
Cdd:TIGR02188 158 DAGAKLVITADEGLRGGKVIPLKAIVDEALEKCPV-SVEHVLVVRRTGNPVVpWVEGRDVWWHDLMAKASAYCEPEPMDS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 256 EDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPN 335
Cdd:TIGR02188 237 EDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEGVPT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 336 WPTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEKCPVMDTWWQ 415
Cdd:TIGR02188 317 YPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKERCPIVDTWWQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 416 TETGGFMITPLPGAIELKAGSATRPFFGVQPVLVDNEGLPLDGATEGN-LAIADSWPGQARTLFGDHERFEQTYFSTFKN 494
Cdd:TIGR02188 397 TETGGIMITPLPGATPTKPGSATLPFFGIEPAVVDEEGNPVEGPGEGGyLVIKQPWPGMLRTIYGDHERFVDTYFSPFPG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 495 MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPE 574
Cdd:TIGR02188 477 YYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDE 556
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 575 LYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDTSNLGDTSTLADPGVVEKLLEE 644
Cdd:TIGR02188 557 LRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEAEILGDTSTLEDPSVVEELIEA 626
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
22-634 |
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: 1186.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 22 EQYKAQYQQSITDPDTFWGEQGKILDWIRPYTRVKNTSFapGNISIKWYEDGTLNLAANCLDRHLAERGDQTAIIWEGDD 101
Cdd:cd05966 1 EQYKELYKQSIEDPEEFWGEIAKELDWFKPWDKVLDWSK--GPPFIKWFEGGKLNISYNCLDRHLKERGDKVAIIWEGDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 102 ASQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSR 181
Cdd:cd05966 79 PDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 182 LVITADEGLRAGRAIPLKKNVDDALKNpnVNSIEHVVVLKRTGGKIDWQEGRDLWWSDLMANASAEHRPVEMNAEDPLFI 261
Cdd:cd05966 159 LVITADGGYRGGKVIPLKEIVDEALEK--CPSVEKVLVVKRTGGEVPMTEGRDLWWHDLMAKQSPECEPEWMDSEDPLFI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 262 LYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNWPTPAR 341
Cdd:cd05966 237 LYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMFEGTPTYPDPGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 342 MCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEKCPVMDTWWQTETGGF 421
Cdd:cd05966 317 YWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGKERCPIVDTWWQTETGGI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 422 MITPLPGAIELKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIADSWPGQARTLFGDHERFEQTYFSTFKNMYFSGDG 501
Cdd:cd05966 397 MITPLPGATPLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPWPGMARTIYGDHERYEDTYFSKFPGYYFTGDG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 502 ARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPELYAEVRN 581
Cdd:cd05966 477 ARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKELRK 556
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 839746169 582 WVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGdTSNLGDTSTLAD 634
Cdd:cd05966 557 HVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAG-EEELGDTSTLAD 608
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
24-611 |
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: 1047.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 24 YKAQYQQSITDPDTFWGEQGKILDWIRPYTRVKNTSFAPGNISIKWYEDGTLNLAANCLDRHLAERGDQTAIIWEGDDAS 103
Cdd:cd17634 1 YETKYRQSINDPDTFWGEAGKILDWITPYQKVKNTSFAPGAPSIKWFEDATLNLAANALDRHLRENGDRTAIIYEGDDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 104 QSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLV 183
Cdd:cd17634 81 QSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 184 ITADEGLRAGRAIPLKKNVDDALkNPNVNSIEHVVVLKRTGGKIDWQEGRDLWWSDLMANASAEHRPVEMNAEDPLFILY 263
Cdd:cd17634 161 ITADGGVRAGRSVPLKKNVDDAL-NPNVTSVEHVIVLKRTGSDIDWQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 264 TSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNWPTPARMC 343
Cdd:cd17634 240 TSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNWPTPARMW 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 344 QVVDKHKVSILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEKCPVMDTWWQTETGGFMI 423
Cdd:cd17634 320 QVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPVVDTWWQTETGGFMI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 424 TPLPGAIELKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIADSWPGQARTLFGDHERFEQTYFSTFKNMYFSGDGAR 503
Cdd:cd17634 400 TPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWPGQTRTLFGDHERFEQTYFSTFKGMYFSGDGAR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 504 RDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPELYAEVRNWV 583
Cdd:cd17634 480 RDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWV 559
|
570 580
....*....|....*....|....*...
gi 839746169 584 RKEIGPLATPDVLHWTDSLPKTRSGKIM 611
Cdd:cd17634 560 RKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
68-643 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 945.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 68 KWYEDGTLNLAANCLDRHLAERGDQTAIIWEGDDaSQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAV 147
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAEGRGDKVALIWEGED-GEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 148 AMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVITADEGLRAGRAIPLKKNVDDALKNpnVNSIEHVVVLKRTGGKI 227
Cdd:COG0365 80 AMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEE--LPSLEHVIVVGRTGADV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 228 DWQEgrDLWWSDLMANASAEHRPVEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADV 307
Cdd:COG0365 158 PMEG--DLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 308 GWVTGHSYLLYGPLACGATTLMFEGVPNWPTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVG 387
Cdd:COG0365 236 GWATGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 388 EPINPEAWEWYWKKIGnekCPVMDTWWQTETGGFMITPLPGaIELKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIA 467
Cdd:COG0365 316 EPLNPEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLPG-LPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 468 DSWPGQARTLFGDHERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAV 547
Cdd:COG0365 392 GPWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 548 VGIPHNIKGQAIYAYVTLNHGEEPTPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDtsNLG 627
Cdd:COG0365 472 VGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGR--PLG 549
|
570
....*....|....*.
gi 839746169 628 DTSTLADPGVVEKLLE 643
Cdd:COG0365 550 DTSTLEDPEALDEIKE 565
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
20-643 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 837.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 20 NPEQYKAQYQQSITDPDTFWGEQGKILDWIRPYTRVK----NTSFAPGNISIKWYEDGTLNLAANCLDRHL-AERGDQTA 94
Cdd:PLN02654 28 SPQQYMEMYKRSVDDPAGFWSDIASQFYWKQKWEGDEvcseNLDVRKGPISIEWFKGGKTNICYNCLDRNVeAGNGDKIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 95 IIWEGDDASQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGR 174
Cdd:PLN02654 108 IYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 175 IIDSSSRLVITADEGLRAGRAIPLKKNVDDALKNPNVNSI--------EHVVVLKRTGGKidWQEGRDLWWSDLMANASA 246
Cdd:PLN02654 188 IVDCKPKVVITCNAVKRGPKTINLKDIVDAALDESAKNGVsvgicltyENQLAMKREDTK--WQEGRDVWWQDVVPNYPT 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 247 EHrPVE-MNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGA 325
Cdd:PLN02654 266 KC-EVEwVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 326 TTLMFEGVPNWPTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNE 405
Cdd:PLN02654 345 TVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDS 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 406 KCPVMDTWWQTETGGFMITPLPGAIELKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIADSWPGQARTLFGDHERFE 485
Cdd:PLN02654 425 RCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVKKSWPGAFRTLYGDHERYE 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 486 QTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTL 565
Cdd:PLN02654 505 TTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTL 584
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 839746169 566 NHGEEPTPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDTSNLGDTSTLADPGVVEKLLE 643
Cdd:PLN02654 585 VEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQLDELGDTSTLADPGVVDQLIA 662
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
24-638 |
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: 668.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 24 YKAQYQQSITDPDTFWGEQGKILDWIRPYTRVKNTSFAPgniSIKWYEDGTLNLAANCLDRH-LAERGDQTAIIWEGDDA 102
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARLIDWFKPPEKILDNSNPP---FTRWFVGGRLNTCYNALDRHvEAGRGDQIALIYDSPVT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 103 SQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRL 182
Cdd:cd05967 78 GTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 183 VITADEGLRAGRAIPLKKNVDDALKNPNVNSiEHVVVLKRTGGKID-WQEGRDLWWSDLMANAsAEHRPVEMNAEDPLFI 261
Cdd:cd05967 158 IVTASCGIEPGKVVPYKPLLDKALELSGHKP-HHVLVLNRPQVPADlTKPGRDLDWSELLAKA-EPVDCVPVAATDPLYI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 262 LYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVP-NWPTPA 340
Cdd:cd05967 236 LYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPvGTPDPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 341 RMCQVVDKHKVSILYTAPTAIRALMAE--GDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGnekCPVMDTWWQTET 418
Cdd:cd05967 316 AFWRVIEKYQVNALFTAPTAIRAIRKEdpDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLG---VPVIDHWWQTET 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 419 GGFMITPLPG--AIELKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIADSW-PGQARTLFGDHERFEQTYFSTFKNM 495
Cdd:cd05967 393 GWPITANPVGlePLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPLpPGCLLTLWKNDERFKKLYLSKFPGY 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 496 YFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPE- 574
Cdd:cd05967 473 YDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEe 552
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 839746169 575 LYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDtsNLGDTSTLADPGVV 638
Cdd:cd05967 553 LEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGE--DYTIPSTIEDPSVL 614
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
22-648 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 636.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 22 EQYKAQYQQSITDPDTFWGEQGKILDWIRPYTRVKNTS---FApgnisiKWYEDGTLNLAANCLDRHLAERGDQTAIIWE 98
Cdd:PRK10524 2 MSYSEFYQRSIDDPEAFWAEQARRIDWQTPFTQVLDYSnppFA------RWFVGGRTNLCHNAVDRHLAKRPEQLALIAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 99 GDDASQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDS 178
Cdd:PRK10524 76 STETDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 179 SSRLVITADEGLRAGRAIPLKKNVDDALKNPNvNSIEHVVVLKRTGGKIDWQEGRDLWWSDLMANASAEHRPVE-MNAED 257
Cdd:PRK10524 156 KPVLIVSADAGSRGGKVVPYKPLLDEAIALAQ-HKPRHVLLVDRGLAPMARVAGRDVDYATLRAQHLGARVPVEwLESNE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 258 PLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNWP 337
Cdd:PRK10524 235 PSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPTRP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 338 TPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNekcPVMDTWWQTE 417
Cdd:PRK10524 315 DAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLDEPTASWISEALGV---PVIDNYWQTE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 418 TGGFMITPLPG--AIELKAGSATRPFFGVQPVLVDNE-GLPLDGATEGNLAIADSW-PGQARTLFGDHERFEQTYFSTF- 492
Cdd:PRK10524 392 TGWPILAIARGveDRPTRLGSPGVPMYGYNVKLLNEVtGEPCGPNEKGVLVIEGPLpPGCMQTVWGDDDRFVKTYWSLFg 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 493 KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHG---- 568
Cdd:PRK10524 472 RQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSdsla 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 569 -EEPTPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAG-DTsnlGDTSTLADPGVVEKLleeKQ 646
Cdd:PRK10524 552 dREARLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAEGrDP---GDLTTIEDPAALQQI---RQ 625
|
..
gi 839746169 647 AI 648
Cdd:PRK10524 626 AL 627
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
22-635 |
0e+00 |
|
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: 545.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 22 EQYKAQYQQSITDPDTFWGEQGKILD--WIRPYTRVKNTSfaPGNISIKWYEDGTLNLAANCLDRHLAERGDQTAIIWEG 99
Cdd:cd05968 7 PDLEAFLERSAEDNAWFWGEFVKDVGieWYEPPYQTLDLS--GGKPWAAWFVGGRMNIVEQLLDKWLADTRTRPALRWEG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 100 DDASqSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSS 179
Cdd:cd05968 85 EDGT-SRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 180 SRLVITADEGLRAGRAIPLKKNVDDALKNpnVNSIEHVVVLKRTGGKIDWQEGRDLWWSDLMANASAEHRpvEMNAEDPL 259
Cdd:cd05968 164 AKALITADGFTRRGREVNLKEEADKACAQ--CPTVEKVVVVRHLGNDFTPAKGRDLSYDEEKETAGDGAE--RTESEDPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 260 FILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGD-IYWCTaDVGWVTGhSYLLYGPLACGATTLMFEGVPNWPT 338
Cdd:cd05968 240 MIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDlLTWFT-DLGWMMG-PWLIFGGLILGATMVLYDGAPDHPK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 339 PARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEKCPVMDTWWQTET 418
Cdd:cd05968 318 ADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPIINYSGGTEI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 419 -----GGFMITPLpgaielKAGSATRPFFGVQPVLVDNEGLPLDGaTEGNLAIADSWPGQARTLFGDHERFEQTYFSTFK 493
Cdd:cd05968 398 sggilGNVLIKPI------KPSSFNGPVPGMKADVLDESGKPARP-EVGELVLLAPWPGMTRGFWRDEDRYLETYWSRFD 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 494 NMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTP 573
Cdd:cd05968 471 NVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTE 550
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 839746169 574 ELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDtsNLGDTSTLADP 635
Cdd:cd05968 551 ALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGK--ELGDLSSLENP 610
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
69-628 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 531.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 69 WYEDGTLNLAANCLDRHLA-ERGDQTAIIWEGDDASQSkhITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAV 147
Cdd:PRK04319 36 WLETGKVNIAYEAIDRHADgGRKDKVALRYLDASRKEK--YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 148 AMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVITADEGLRagraiplKKNVDDalknpnVNSIEHVVVLKRTGGki 227
Cdd:PRK04319 114 ALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLE-------RKPADD------LPSLKHVLLVGEDVE-- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 228 dwQEGRDLWWSDLMANASAEHRPVEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTfKYVFDYHPGDIYWCTADV 307
Cdd:PRK04319 179 --EGPGTLDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQTG-KYVLDLHEDDVYWCTADP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 308 GWVTGHSYLLYGPLACGATTLMFEGVPNwptPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVG 387
Cdd:PRK04319 256 GWVTGTSYGIFAPWLNGATNVIDGGRFS---PERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDLSSLRHILSVG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 388 EPINPEAWEWYWKKIGNekcPVMDTWWQTETGGFMITPLPgAIELKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIA 467
Cdd:PRK04319 333 EPLNPEVVRWGMKVFGL---PIHDNWWMTETGGIMIANYP-AMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 468 DSWPGQARTLFGDHERFEQtYFStfKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAV 547
Cdd:PRK04319 409 KGWPSMMRGIWNNPEKYES-YFA--GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGV 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 548 VGIPHNIKGQAIYAYVTLNHGEEPTPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK----IAAGDT 623
Cdd:PRK04319 486 IGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAwelgLPEGDL 565
|
....*
gi 839746169 624 SNLGD 628
Cdd:PRK04319 566 STMED 570
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
109-619 |
3.16e-148 |
|
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: 436.93 E-value: 3.16e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 109 TYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVITADE 188
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 189 GLRagraiplkknvddalknpnvnsiehvvvlkrtggkidwqegrdlwwsdlmanasaehrpvEMNAEDPLFILYTSGST 268
Cdd:cd05969 82 LYE------------------------------------------------------------RTDPEDPTLLHYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 269 GKPKGVLHTTGGYLVYAATTfKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNwptPARMCQVVDK 348
Cdd:cd05969 102 GTPKGVLHVHDAMIFYYFTG-KYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRFD---AESWYGIIER 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 349 HKVSILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGnekCPVMDTWWQTETGGFMITPLPG 428
Cdd:cd05969 178 VKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFG---VPIHDTWWQTETGSIMIANYPC 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 429 aIELKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIADSWPGQARTLFGDHERFEqtyfSTFKN-MYFSGDGARRDED 507
Cdd:cd05969 255 -MPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPGWPSMFRGIWNDEERYK----NSFIDgWYLTGDLAYRDED 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 508 GYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPELYAEVRNWVRKEI 587
Cdd:cd05969 330 GYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQKL 409
|
490 500 510
....*....|....*....|....*....|..
gi 839746169 588 GPLATPDVLHWTDSLPKTRSGKIMRRILRKIA 619
Cdd:cd05969 410 GAHVAPREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
109-617 |
1.11e-124 |
|
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: 375.91 E-value: 1.11e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 109 TYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVITade 188
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 189 glragraiplkknvddalknpnvnsiehvvvlkrtggkidwqegrdlwwsdlmanasaehrpvemNAEDPLFILYTSGST 268
Cdd:cd05972 79 -----------------------------------------------------------------DAEDPALIYFTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 269 GKPKGVLHTTGgYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNwpTPARMCQVVDK 348
Cdd:cd05972 94 GLPKGVLHTHS-YPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRF--DAERILELLER 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 349 HKVSILYTAPTAIRALMAEGdkaIEGTDRSSLRILGSVGEPINPEAWEWyWKKIGNEkcPVMDTWWQTETGgFMITPLPG 428
Cdd:cd05972 171 YGVTSFCGPPTAYRMLIKQD---LSSYKFSHLRLVVSAGEPLNPEVIEW-WRAATGL--PIRDGYGQTETG-LTVGNFPD 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 429 aIELKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIADSWPGQARTLFGDHERFEQTYFSTFknmYFSGDGARRDEDG 508
Cdd:cd05972 244 -MPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPPPGLFLGYVGDPEKTEASIRGDY---YLTGDRAYRDEDG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 509 YYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPELYAEVRNWVRKEIG 588
Cdd:cd05972 320 YFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKVLA 399
|
490 500
....*....|....*....|....*....
gi 839746169 589 PLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05972 400 PYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
82-523 |
3.85e-110 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 338.13 E-value: 3.85e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 82 LDRHLAERGDQTAiiWEGDDasqSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSV 161
Cdd:pfam00501 1 LERQAARTPDKTA--LEVGE---GRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 162 IFGGFSPEAVAGRIIDSSSRLVITADEglragraiPLKKNVDDALKNPNVnsIEHVVVLKRTggkiDWQEGRDLWWSDLm 241
Cdd:pfam00501 76 LNPRLPAEELAYILEDSGAKVLITDDA--------LKLEELLEALGKLEV--VKLVLVLDRD----PVLKEEPLPEEAK- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 242 ANASAEHRPVEMNAEDPLFILYTSGSTGKPKGVLHTTgGYLVYAATTFKYV----FDYHPGDIYWCTADVGWVTGHSYLL 317
Cdd:pfam00501 141 PADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTH-RNLVANVLSIKRVrprgFGLGPDDRVLSTLPLFHDFGLSLGL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 318 YGPLACGATTLMFEGVPNwPTPARMCQVVDKHKVSILYTAPTAIRALMAEGdkAIEGTDRSSLRILGSVGEPINPEAWEW 397
Cdd:pfam00501 220 LGPLLAGATVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNMLLEAG--APKRALLSSLRLVLSGGAPLPPELARR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 398 YWKKIGnekCPVMDTWWQTETGGFMITPLPGAIEL-KAGSATRPFFGVQPVLVD-NEGLPLDGATEGNLAIADswPGQAR 475
Cdd:pfam00501 297 FRELFG---GALVNGYGLTETTGVVTTPLPLDEDLrSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRG--PGVMK 371
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 839746169 476 TLFGDHERFEQTYFStfKNMYFSGDGARRDEDGYYWITGRVDDVLNVS 523
Cdd:pfam00501 372 GYLNDPELTAEAFDE--DGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
82-623 |
2.63e-106 |
|
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: 329.46 E-value: 2.63e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 82 LDRHLAERGDQTAIIWEGddasqsKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSV 161
Cdd:COG0318 5 LRRAAARHPDRPALVFGG------RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 162 IFGGFSPEAVAGRIIDSSSRLVITAdeglragraiplkknvddalknpnvnsiehvvvlkrtggkidwqegrdlwwsdlm 241
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVTA------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 242 anasaehrpvemnaedplFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPL 321
Cdd:COG0318 104 ------------------LILYTSGTTGRPKGVMLTHRN-LLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 322 ACGATTLMfegVPNWpTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEPINPEAWEWYWKK 401
Cdd:COG0318 165 LAGATLVL---LPRF-DPERVLELIERERVTVLFGVPTMLARLLRHPEFA--RYDLSSLRLVVSGGAPLPPELLERFEER 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 402 IGnekCPVMDTWWQTETGGFMITPLPGAIELKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIADswPGQARTLFGDH 481
Cdd:COG0318 239 FG---VRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRG--PNVMKGYWNDP 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 482 ERFEQTyfstFKN-MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIY 560
Cdd:COG0318 314 EATAEA----FRDgWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVV 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 839746169 561 AYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDT 623
Cdd:COG0318 390 AFVVLRPGAELDAE---ELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGA 449
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
257-611 |
5.50e-100 |
|
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: 308.83 E-value: 5.50e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 257 DPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYvFDYHPGDIYWCTADVGWVtGHSYLLYGPLACGATTLMFEGvpnw 336
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS-GGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 337 PTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEPINPEAWEWYWKKIGnekCPVMDTWWQT 416
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKAPESA--GYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 417 ETGGFMITPLPGAIELKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIADSWPGQartlfGDHERFEQTYFSTFKNMY 496
Cdd:cd04433 150 ETGGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMK-----GYWNNPEATAAVDEDGWY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 497 FSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPEly 576
Cdd:cd04433 225 RTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAE-- 302
|
330 340 350
....*....|....*....|....*....|....*
gi 839746169 577 aEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIM 611
Cdd:cd04433 303 -ELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
108-617 |
2.67e-92 |
|
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: 292.50 E-value: 2.67e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 108 ITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVITad 187
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 188 eglragraiplkknvddalknpnvnsiehvvvlkrtggkidwqegrdlwwsdlmaNASAEHRPvemnAEDPLFILYTSGS 267
Cdd:cd05973 79 -------------------------------------------------------DAANRHKL----DSDPFVMMFTSGT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 268 TGKPKGVLHTTGGYLVYAATtFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPnwpTPARMCQVVD 347
Cdd:cd05973 100 TGLPKGVPVPLRALAAFGAY-LRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGF---SVESTWRVIE 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 348 KHKVSILYTAPTAIRALMAEGdKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGnekCPVMDTWWQTETGGFMITPLP 427
Cdd:cd05973 176 RLGVTNLAGSPTAYRLLMAAG-AEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALG---VPIHDHYGQTELGMVLANHHA 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 428 GAIELKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAI-ADSWPgqaRTLFGDHERFEQTYFStfKNMYFSGDGARRDE 506
Cdd:cd05973 252 LEHPVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIdIANSP---LMWFRGYQLPDTPAID--GGYYLTGDTVEFDP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 507 DGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPELYAEVRNWVRKE 586
Cdd:cd05973 327 DGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQLHVKKR 406
|
490 500 510
....*....|....*....|....*....|.
gi 839746169 587 IGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05973 407 LSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
13-639 |
2.34e-88 |
|
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: 288.02 E-value: 2.34e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 13 IAERCLINPEQYKAQYQQSITDPDTFWGEqgkILDWI-----RPYT-RVKNTSFAPGNisiKWYEDGTLNLAANCLDRHl 86
Cdd:cd05943 8 VNARHGLSLADYAALHRWSVDDPGAFWAA---VWDFSgvrgsKPYDvVVVSGRIMPGA---RWFPGARLNYAENLLRHA- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 87 aeRGDQTAIIWEGDDASqSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGF 166
Cdd:cd05943 81 --DADDPAAIYAAEDGE-RTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 167 SPEAVAGRIIDSSSRLVITADEGLRAGRAIPLKKNVDDALKnpNVNSIEHVVVLKRTG--GKIDWQE-GRDLWWSDLMAN 243
Cdd:cd05943 158 GVPGVLDRFGQIEPKVLFAVDAYTYNGKRHDVREKVAELVK--GLPSLLAVVVVPYTVaaGQPDLSKiAKALTLEDFLAT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 244 -ASAEHRPVEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSylLYGPLA 322
Cdd:cd05943 236 gAAGELEFEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRLFYYTTCGWMMWNW--LVSGLA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 323 CGATTLMFEGVPNWPTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKI 402
Cdd:cd05943 314 VGATIVLYDGSPFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 403 GNekcpvmDTWWQTETGG------FMIT-PL----PGaiELKAgsatrPFFGVQPVLVDNEGLPLDGATeGNLAIADSWP 471
Cdd:cd05943 394 KP------DVLLASISGGtdiiscFVGGnPLlpvyRG--EIQC-----RGLGMAVEAFDEEGKPVWGEK-GELVCTKPFP 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 472 GQARTLFGDHE--RFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVG 549
Cdd:cd05943 460 SMPVGFWNDPDgsRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVG 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 550 IPHNIKGQAIYAYVTLNHGEEPTPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGdtSNLGDT 629
Cdd:cd05943 540 QEWKDGDERVILFVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKIIAG--RPVKNA 617
|
650
....*....|
gi 839746169 630 STLADPGVVE 639
Cdd:cd05943 618 GALANPESLD 627
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
13-639 |
4.68e-88 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 287.85 E-value: 4.68e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 13 IAERCLINPEQYKAQYQQSITDPDTFWGEqgkILDWI-----RPYTRVKNTSFAPGNisiKWYEDGTLNLAANCLdRHla 87
Cdd:PRK03584 25 LAARRGLSFDDYAALWRWSVEDLEAFWQS---VWDFFgvigsTPYTVVLAGRRMPGA---RWFPGARLNYAENLL-RH-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 88 ERGDQTAIIWEGDDASQSKhITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFS 167
Cdd:PRK03584 96 RRDDRPAIIFRGEDGPRRE-LSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 168 PEAVAGRIIDSSSRLVITADeGLR-AGRAIPLKKNVD---DALKnpnvnSIEHVVVLKRTGGKIDWQEG-RDLWWSDLMA 242
Cdd:PRK03584 175 VQGVLDRFGQIEPKVLIAVD-GYRyGGKAFDRRAKVAelrAALP-----SLEHVVVVPYLGPAAAAAALpGALLWEDFLA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 243 NAS-AEHRPVEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGD-IYWCTAdVGW------VTGhs 314
Cdd:PRK03584 249 PAEaAELEFEPVPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDrFFWYTT-CGWmmwnwlVSG-- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 315 yllygpLACGATTLMFEGVPNWPTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEA 394
Cdd:PRK03584 326 ------LLVGATLVLYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPLPPEG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 395 WEWYWKKIGNekcpvmDTWWQTETGG------FMI-TPL----PGaiELKAgsatrPFFGVQPVLVDNEGLPLDGATeGN 463
Cdd:PRK03584 400 FDWVYEHVKA------DVWLASISGGtdicscFVGgNPLlpvyRG--EIQC-----RGLGMAVEAWDEDGRPVVGEV-GE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 464 LAIADSWPGQARTLFGD--HERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPK 541
Cdd:PRK03584 466 LVCTKPFPSMPLGFWNDpdGSRYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPE 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 542 IAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIM----RRILRK 617
Cdd:PRK03584 546 VLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVelpvKKLLHG 625
|
650 660
....*....|....*....|..
gi 839746169 618 IAAGDTSNLGdtsTLADPGVVE 639
Cdd:PRK03584 626 RPVKKAVNRD---ALANPEALD 644
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
18-617 |
1.33e-80 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 268.15 E-value: 1.33e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 18 LINPEQYKAQYQQSITDPDTFWGEQG-KILDWIRPYTRVkntsFAPGNISIKWYEDGTLNLAANCLDRHL--AERGDQTA 94
Cdd:PTZ00237 4 LSDPFDYENDSNYANSNPESFWDEVAkKYVHWDKMYDKV----YSGDEIYPDWFKGGELNTCYNVLDIHVknPLKRDQDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 95 IIWEGDDASQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGR 174
Cdd:PTZ00237 80 LIYECPYLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 175 IIDSSSRLVITADEGLRAGRAIPLKKNVDDALK----NPNvnsieHVVVLKRTggkiDWQEGRDL--------------W 236
Cdd:PTZ00237 160 IETITPKLIITTNYGILNDEIITFTPNLKEAIElstfKPS-----NVITLFRN----DITSESDLkkietiptipntlsW 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 237 WSDLMA----NASA--EHRPVEMNaeDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWV 310
Cdd:PTZ00237 231 YDEIKKikenNQSPfyEYVPVESS--HPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 311 TGHSYLlYGPLACGATTLMFEG--VPNWPTPARMCQVVDKHKVSILYTAPTAIRALMA---EGDKAIEGTDRSSLRILGS 385
Cdd:PTZ00237 309 SFHGFL-YGSLSLGNTFVMFEGgiIKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKtdpEATIIRSKYDLSNLKEIWC 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 386 VGEPINPEAWEWYWKKIgneKCPVMDTWWQTETGgfmITPLPGAIELKAGSAT--RPFFGVQPVLVDNEGLPLDGATEGN 463
Cdd:PTZ00237 388 GGEVIEESIPEYIENKL---KIKSSRGYGQTEIG---ITYLYCYGHINIPYNAtgVPSIFIKPSILSEDGKELNVNEIGE 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 464 LAIADSWP-GQARTLFGDHERFEQTyFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKI 542
Cdd:PTZ00237 462 VAFKLPMPpSFATTFYKNDEKFKQL-FSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLV 540
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 839746169 543 AEAAVVGIPHNIKGQAIYAYVTLNHGEEPTP----ELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PTZ00237 541 LECCSIGIYDPDCYNVPIGLLVLKQDQSNQSidlnKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISK 619
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
64-616 |
8.42e-80 |
|
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: 262.82 E-value: 8.42e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 64 NISIKWYEdgTLNLAANCLDRHLAERGDQTAIIWeGDDASQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVP 143
Cdd:cd05970 7 NFSINVPE--NFNFAYDVVDAMAKEYPDKLALVW-CDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 144 EAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVITADEGLragraipLKKNVDDALknPNVNSIEhvvVLKRT 223
Cdd:cd05970 84 EFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDN-------IPEEIEKAA--PECPSKP---KLVWV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 224 GGKIdwQEGrdlwWSD---LMANASAEHRPVEMNA----EDPLFILYTSGSTGKPKGVLHTTG---GYLVyaatTFKYVF 293
Cdd:cd05970 152 GDPV--PEG----WIDfrkLIKNASPDFERPTANSypcgEDILLVYFSSGTTGMPKMVEHDFTyplGHIV----TAKYWQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 294 DYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGvpNWPTPARMCQVVDKHKVSILYTAPTAIRALMAEGdkaIE 373
Cdd:cd05970 222 NVREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVYDY--DKFDPKALLEKLSKYGVTTFCAPPTIYRFLIRED---LS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 374 GTDRSSLRILGSVGEPINPEAWEWYWKKIGNEkcpVMDTWWQTETGgFMITPLPGaIELKAGSATRPFFGVQPVLVDNEG 453
Cdd:cd05970 297 RYDLSSLRYCTTAGEALNPEVFNTFKEKTGIK---LMEGFGQTETT-LTIATFPW-MEPKPGSMGKPAPGYEIDLIDREG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 454 LPLDGATEGNLAIADSwPGQARTLFGDHERFEQTYFSTFKN-MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEI 532
Cdd:cd05970 372 RSCEAGEEGEIVIRTS-KGKPVGLFGGYYKDAEKTAEVWHDgYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEV 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 533 ESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd05970 451 ESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRR 530
|
....
gi 839746169 613 RILR 616
Cdd:cd05970 531 VEIR 534
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
78-616 |
5.99e-78 |
|
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: 257.30 E-value: 5.99e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 78 AANCLDRHLAE-RGDQTAIIwegDDASqskHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIG 156
Cdd:cd05959 5 AATLVDLNLNEgRGDKTAFI---DDAG---SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 157 AIHSVIFGGFSPEAVAGRIIDSSSRLVITADEglragraipLKKNVDDALKNpnvnSIEHVVVLKRTGGKIdwQEGRDLW 236
Cdd:cd05959 79 IVPVPVNTLLTPDDYAYYLEDSRARVVVVSGE---------LAPVLAAALTK----SEHTLVVLIVSGGAG--PEAGALL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 237 WSDLMANASAEHRPVEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYL 316
Cdd:cd05959 144 LAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 317 LYGPLACGATTLMFegvPNWPTPARMCQVVDKHKVSILYTAPTAIRALMAegDKAIEGTDRSSLRILGSVGEPINPEAWE 396
Cdd:cd05959 224 LTFPLSVGATTVLM---PERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLA--APNLPSRDLSSLRLCVSAGEALPAEVGE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 397 WYWKKIGNEkcpVMDTWWQTETGGFMITPLPGAIELkaGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIA-DSwpgqar 475
Cdd:cd05959 299 RWKARFGLD---ILDGIGSTEMLHIFLSNRPGRVRY--GTTGKPVPGYEVELRDEDGGDVADGEPGELYVRgPS------ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 476 TLFGDHERFEQTYfSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNI 554
Cdd:cd05959 368 SATMYWNNRDKTR-DTFQGEWTrTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDED 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 839746169 555 KGQAIYAYVTLNHGEEPTPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05959 447 GLTKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
105-616 |
5.29e-77 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 252.35 E-value: 5.29e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 105 SKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVI 184
Cdd:cd05971 4 PEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 185 TaDEglragraiplkknvddalknpnvnsiehvvvlkrtggkidwqegrdlwwsdlmanasaehrpvemnAEDPLFILYT 264
Cdd:cd05971 84 T-DG------------------------------------------------------------------SDDPALIIYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 265 SGSTGKPKGVLHTTGgYLVYAATTFKYVFDYHP--GDIYWCTADVGWVTGHSYLLYGPLACGATTLM-----FEgvpnwp 337
Cdd:cd05971 97 SGTTGPPKGALHAHR-VLLGHLPGVQFPFNLFPrdGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAhrmtkFD------ 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 338 tPARMCQVVDKHKVSILYTAPTAIRaLMAEGDKAIEGTDRSsLRILGSVGEPINPEAWEWYWKKIGNEkcpVMDTWWQTE 417
Cdd:cd05971 170 -PKAALDLMSRYGVTTAFLPPTALK-MMRQQGEQLKHAQVK-LRAIATGGESLGEELLGWAREQFGVE---VNEFYGQTE 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 418 tGGFMITPLPGAIELKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIADSWPGQARTLFGDHERFEQTYFSTFknmYF 497
Cdd:cd05971 244 -CNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDPVAFLGYWNNPSATEKKMAGDW---LL 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 498 SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPELYA 577
Cdd:cd05971 320 TGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALAR 399
|
490 500 510
....*....|....*....|....*....|....*....
gi 839746169 578 EVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05971 400 EIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
76-617 |
6.05e-74 |
|
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: 246.99 E-value: 6.05e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 76 NLAANCLD-----RHLAERGDQTAIIWEGDDASQSKHiTYRELHADVCRFANVLLDL-GIKKGDVVAIYMPMVPEAAVAM 149
Cdd:cd05928 6 NFASDVLDqwadkEKAGKRPPNPALWWVNGKGDEVKW-SFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 150 LACARIGAIhsVIFGGFSPEA--VAGRIIDSSSRLVITADEglragraipLKKNVDD-ALKNPNVnSIEHVVVLKRTGGK 226
Cdd:cd05928 85 VACIRTGLV--FIPGTIQLTAkdILYRLQASKAKCIVTSDE---------LAPEVDSvASECPSL-KTKLLVSEKSRDGW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 227 IDWQEgrdlwwsdLMANASAEHRPVEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTAD 306
Cdd:cd05928 153 LNFKE--------LLNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 307 VGWVTGHSYLLYGPLACGATTLMFEgVPNWpTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEgtdRSSLRILGSV 386
Cdd:cd05928 225 TGWIKSAWSSLFEPWIQGACVFVHH-LPRF-DPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYK---FPSLQHCVTG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 387 GEPINPEAWEWYWKKIGNEkcpVMDTWWQTETGgfMITPLPGAIELKAGSATR--PFFGVQpvLVDNEGLPLDGATEGNL 464
Cdd:cd05928 300 GEPLNPEVLEKWKAQTGLD---IYEGYGQTETG--LICANFKGMKIKPGSMGKasPPYDVQ--IIDDNGNVLPPGTEGDI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 465 AIADSwPGQARTLFGDHERFEQTYFSTFK-NMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIA 543
Cdd:cd05928 373 GIRVK-PIRPFGLFSGYVDNPEKTAATIRgDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVV 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 839746169 544 EAAVVGIPHNIKGQAIYAYVTLN-----HGEEptpELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05928 452 ESAVVSSPDPIRGEVVKAFVVLApqflsHDPE---QLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
72-622 |
1.46e-72 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 243.17 E-value: 1.46e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 72 DGTLNLAaNCLDRHLAERGDQTAIIWEGddasqsKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLA 151
Cdd:PRK06187 3 DYPLTIG-RILRHGARKHPDKEAVYFDG------RRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 152 CARIGAI-HSV-IFggFSPEAVAGRIIDSSSRLVITADEGLragraiPLKKNVDDALKnpnvnSIEHVVVL---KRTGGK 226
Cdd:PRK06187 76 VPKIGAVlHPInIR--LKPEEIAYILNDAEDRVVLVDSEFV------PLLAAILPQLP-----TVRTVIVEgdgPAAPLA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 227 IDWQEgrdlwWSDLMANASAEHRPVEMNAEDPLFILYTSGSTGKPKGV--------LHTTGGylvyaattfKYVFDYHPG 298
Cdd:PRK06187 143 PEVGE-----YEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVvlshrnlfLHSLAV---------CAWLKLSRD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 299 DIYWCTADV----GWVTGhsyllYGPLACGATTLM---FEgvpnwptPARMCQVVDKHKVSILYTAPTAIRALMAEgdKA 371
Cdd:PRK06187 209 DVYLVIVPMfhvhAWGLP-----YLALMAGAKQVIprrFD-------PENLLDLIETERVTFFFAVPTIWQMLLKA--PR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 372 IEGTDRSSLRILGSVGEPINPEAWEWYWKKIGnekCPVMDTWWQTETGGFM-ITPL----PGAIElKAGSATRPFFGVQP 446
Cdd:PRK06187 275 AYFVDFSSLRLVIYGGAALPPALLREFKEKFG---IDLVQGYGMTETSPVVsVLPPedqlPGQWT-KRRSAGRPLPGVEA 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 447 VLVDNEG--LPLDGATEGNLAIADSWPGQArtLFGDHERFEqtyfSTFKN-MYFSGDGARRDEDGYYWITGRVDDVLNVS 523
Cdd:PRK06187 351 RIVDDDGdeLPPDGGEVGEIIVRGPWLMQG--YWNRPEATA----ETIDGgWLHTGDVGYIDEDGYLYITDRIKDVIISG 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 524 GHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLP 603
Cdd:PRK06187 425 GENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAK---ELRAFLRGRLAKFKLPKRIAFVDELP 501
|
570 580
....*....|....*....|
gi 839746169 604 KTRSGKIMRRILR-KIAAGD 622
Cdd:PRK06187 502 RTSVGKILKRVLReQYAEGK 521
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
92-616 |
5.10e-71 |
|
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: 236.59 E-value: 5.10e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 92 QTAIIwegdDASQSkhITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAV 171
Cdd:cd05919 1 KTAFY----AADRS--VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 172 AGRIIDSSSRLVITadeglragraiplkknvddalknpnvnsiehvvvlkrtggkidwqegrdlwwsdlmanasaehrpv 251
Cdd:cd05919 75 AYIARDCEARLVVT------------------------------------------------------------------ 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 252 emNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADV--GWVTGHSylLYGPLACGATTLM 329
Cdd:cd05919 89 --SADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNS--LWFPLAVGASAVL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 330 FegvPNWPTPARMCQVVDKHKVSILYTAPTAIRALMAEGDkaIEGTDRSSLRILGSVGEPINPEAWEwYWKKIGNekCPV 409
Cdd:cd05919 165 N---PGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCA--GSPDALRSLRLCVSAGEALPRGLGE-RWMEHFG--GPI 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 410 MDTWWQTETGGFMITPLPGAIELkaGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIADswPGQARTLFGDHERFEQTYF 489
Cdd:cd05919 237 LDGIGATEVGHIFLSNRPGAWRL--GSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRG--PSAAVGYWNNPEKSRATFN 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 490 STFknmYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGE 569
Cdd:cd05919 313 GGW---YRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPA 389
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 839746169 570 EPTPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05919 390 APQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
82-612 |
8.88e-69 |
|
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: 230.57 E-value: 8.88e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 82 LDRHLAERGDQTAIIWEGddasqsKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSV 161
Cdd:cd17631 1 LRRRARRHPDRTALVFGG------RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 162 IFGGFSPEAVAGRIIDSSSRLVItadeglragraiplkknvddalknpnvnsiehvvvlkrtggkidwqegrdlwwsdlm 241
Cdd:cd17631 75 LNFRLTPPEVAYILADSGAKVLF--------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 242 anasaehrpvemnaEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPL 321
Cdd:cd17631 98 --------------DDLALLMYTSGTTGRPKGAMLTHRN-LLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTL 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 322 ACGATTLMFEGvpnwPTPARMCQVVDKHKVSILYTAPTAIRALMAEGDkaIEGTDRSSLRILGSVGEPInPEAWEWYWKK 401
Cdd:cd17631 163 LRGGTVVILRK----FDPETVLDLIERHRVTSFFLVPTMIQALLQHPR--FATTDLSSLRAVIYGGAPM-PERLLRALQA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 402 IGnekCPVMDTWWQTETGGfMITPLPGAIEL-KAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIADswPGQARtlfGD 480
Cdd:cd17631 236 RG---VKFVQGYGMTETSP-GVTFLSPEDHRrKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRG--PHVMA---GY 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 481 HERFEQTYfSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAI 559
Cdd:cd17631 307 WNRPEATA-AAFRDGWFhTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAV 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 839746169 560 YAYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17631 386 VAVVVPRPGAELDED---ELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
82-616 |
1.71e-68 |
|
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: 230.91 E-value: 1.71e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 82 LDRHLAERGDQTAIIWEGddasqsKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAI--- 158
Cdd:cd05936 5 LEEAARRFPDKTALIFMG------RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVvvp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 159 HSVIFGgfsPEAVAGRIIDSSSRLVITadeglragraiplkknvddalknpnvnsiehvvvlkrtggkidwqegrDLWWS 238
Cdd:cd05936 79 LNPLYT---PRELEHILNDSGAKALIV------------------------------------------------AVSFT 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 239 DLMANASAEHRPVEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGD-----------IYWCTAdv 307
Cdd:cd05936 108 DLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEGDdvvlaalplfhVFGLTV-- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 308 gwvtghSYLLygPLACGATTLMfegVPNwPTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKaiEGTDRSSLRILGSVG 387
Cdd:cd05936 186 ------ALLL--PLALGATIVL---IPR-FRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEF--KKRDFSSLRLCISGG 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 388 EPINPEAWEWYWKKIGnekCPVMDTWWQTETG-GFMITPLPGAIelKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAI 466
Cdd:cd05936 252 APLPVEVAERFEELTG---VPIVEGYGLTETSpVVAVNPLDGPR--KPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWV 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 467 AdswpGQARTLfGDHERFEQTYfSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEA 545
Cdd:cd05936 327 R----GPQVMK-GYWNRPEETA-EAFVDGWLrTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEA 400
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 839746169 546 AVVGIPHNIKGQAIYAYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05936 401 AVVGVPDPYSGEAVKAFVVLKEGASLTEE---EIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
28-617 |
4.14e-63 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 222.65 E-value: 4.14e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 28 YQQSITDPDTFWG---EQGKILDWIRPYTRVKNTSFA-PGNisiKWYEDGTLNLAANCLDRHLAERGDQTAIIW--EGDD 101
Cdd:PLN03052 126 QRFSVENPEVYWSivlDELSLVFSVPPRCILDTSDESnPGG---QWLPGAVLNVAECCLTPKPSKTDDSIAIIWrdEGSD 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 102 ASQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSR 181
Cdd:PLN03052 203 DLPVNRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAK 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 182 LVITADEGLRAGRAIPLKKNVDDAlKNPNvnsiehVVVLKRTGGKIDWQ-EGRDLWWSDLMANASA-----EHRPVEMNA 255
Cdd:PLN03052 283 AIFTQDVIVRGGKSIPLYSRVVEA-KAPK------AIVLPADGKSVRVKlREGDMSWDDFLARANGlrrpdEYKAVEQPV 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 256 EDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVfDYHPGDIY-WCTaDVGWVTGHsYLLYGPLACGATTLMFEGVP 334
Cdd:PLN03052 356 EAFTNILFSSGTTGEPKAIPWTQLTPLRAAADAWAHL-DIRKGDIVcWPT-NLGWMMGP-WLVYASLLNGATLALYNGSP 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 335 NWPTPARMCQvvdKHKVSILYTAPTAIRALMAEGdkAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEkcPVMDTWW 414
Cdd:PLN03052 433 LGRGFAKFVQ---DAKVTMLGTVPSIVKTWKNTN--CMAGLDWSSIRCFGSTGEASSVDDYLWLMSRAGYK--PIIEYCG 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 415 QTETGGFMIT--PL-PGAIelkaGSATRPFFGVQPVLVDNEGLPL--DGATEGNLAIADSWPGQARTLF-GDHerfEQTY 488
Cdd:PLN03052 506 GTELGGGFVTgsLLqPQAF----AAFSTPAMGCKLFILDDSGNPYpdDAPCTGELALFPLMFGASSTLLnADH---YKVY 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 489 fstFKNM-YFSGDGARRDED-------GYYWITGRVDDVLNVSGHRLGTAEIESAL-VSHPKIAEAAVVGIPHNIKGQ-- 557
Cdd:PLN03052 579 ---FKGMpVFNGKILRRHGDifertsgGYYRAHGRADDTMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPPGGGPeq 655
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 839746169 558 -AIYAYVTLNHGEEPTPELYAEVRN-WVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PLN03052 656 lVIAAVLKDPPGSNPDLNELKKIFNsAIQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQ 717
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
101-611 |
6.75e-63 |
|
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: 216.31 E-value: 6.75e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 101 DASQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSS 180
Cdd:cd05911 4 DADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 181 RLVITADEGLragraiplkKNVDDALKNpnVNSIEHVVVLkrtGGKIDWQEGRDLWWSDLmANASAEHRPVEMN--AEDP 258
Cdd:cd05911 84 KVIFTDPDGL---------EKVKEAAKE--LGPKDKIIVL---DDKPDGVLSIEDLLSPT-LGEEDEDLPPPLKdgKDDT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 259 LFILYTSGSTGKPKGVLHTTGGYLvyaaTTFKYVFDYHPGDIYWCTADVG-----WVTGHSYLLYGPLaCGATTLMFegv 333
Cdd:cd05911 149 AAILYSSGTTGLPKGVCLSHRNLI----ANLSQVQTFLYGNDGSNDVILGflplyHIYGLFTTLASLL-NGATVIIM--- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 334 pNWPTPARMCQVVDKHKVSILYTAPtAIRALMAEgDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNekCPVMDTW 413
Cdd:cd05911 221 -PKFDSELFLDLIEKYKITFLYLVP-PIAAALAK-SPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPN--ATIKQGY 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 414 WQTETGGFMITPLPGaiELKAGSATRPFFGVQPVLVDNEGLPLDGATE-GNLAIadsWPGQArtLFGDHERFEQTYFSTF 492
Cdd:cd05911 296 GMTETGGILTVNPDG--DDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEpGEICV---RGPQV--MKGYYNNPEATKETFD 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 493 KNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEP 571
Cdd:cd05911 369 EDGWLhTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKL 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 839746169 572 TPElyaEVRNWVRKEIgplatPDVLHW------TDSLPKTRSGKIM 611
Cdd:cd05911 449 TEK---EVKDYVAKKV-----ASYKQLrggvvfVDEIPKSASGKIL 486
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
108-617 |
4.22e-62 |
|
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: 214.48 E-value: 4.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 108 ITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVITAD 187
Cdd:cd05926 15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 188 EGLraGRAIPLKKNVDDALKNPNVnsiehvvvlkRTGGKIDWQEGRDLwwSDLMANASAEHRPVEMNAEDPLFILYTSGS 267
Cdd:cd05926 95 GEL--GPASRAASKLGLAILELAL----------DVGVLIRAPSAESL--SNLLADKKNAKSEGVPLPDDLALILHTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 268 TGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLM---FEGVPNWPtparmcQ 344
Cdd:cd05926 161 TGRPKGVPLTHRN-LAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLpprFSASTFWP------D 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 345 VVDKHkvSILYTA-PTAIRAL--MAEGDKAIEgtdRSSLRILGSVGEPINPEAWEWYWKKIGnekCPVMDTWWQTETGGF 421
Cdd:cd05926 234 VRDYN--ATWYTAvPTIHQILlnRPEPNPESP---PPKLRFIRSCSASLPPAVLEALEATFG---APVLEAYGMTEAAHQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 422 MIT-PLPGAIElKAGSATRPfFGVQPVLVDNEGLPLDGATEGNLAIADswPGQARTLFGDHerfEQTYFSTFKNMYF-SG 499
Cdd:cd05926 306 MTSnPLPPGPR-KPGSVGKP-VGVEVRILDEDGEILPPGVVGEICLRG--PNVTRGYLNNP---EANAEAAFKDGWFrTG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 500 DGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPElyaEV 579
Cdd:cd05926 379 DLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEE---EL 455
|
490 500 510
....*....|....*....|....*....|....*...
gi 839746169 580 RNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05926 456 RAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
82-617 |
7.56e-62 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 214.38 E-value: 7.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 82 LDRHLAERGDQTAIIWEGDDasqskhITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSV 161
Cdd:PRK07656 11 LARAARRFGDKEAYVFGDQR------LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 162 IFGGFSPEAVAGRIIDSSSRLVITADEGLragraiPLKKNVDDALknpnvNSIEHVVVLkrTGGKIDWQEGRDLWWSDLM 241
Cdd:PRK07656 85 LNTRYTADEAAYILARGDAKALFVLGLFL------GVDYSATTRL-----PALEHVVIC--ETEEDDPHTEKMKTFTDFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 242 ANASAEHRPVEMNAEDPLFILYTSGSTGKPKGVLhTTGGYLVYAATTFKYVFDYHPGDIYWCTA--------DVGWVTgh 313
Cdd:PRK07656 152 AAGDPAERAPEVDPDDVADILFTSGTTGRPKGAM-LTHRQLLSNAADWAEYLGLTEGDRYLAANpffhvfgyKAGVNA-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 314 syllygPLACGATTLMfegVPNWpTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEgtDRSSLRILGSVGEPINPE 393
Cdd:PRK07656 229 ------PLMRGATILP---LPVF-DPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAE--DLSSLRLAVTGAASMPVA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 394 AWEWYWKKIGNEKcpVMDTWWQTETGGFM-ITPLPGAIELKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIADswPG 472
Cdd:PRK07656 297 LLERFESELGVDI--VLTGYGLSEASGVTtFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRG--PN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 473 QARTLFGDHERFEQTYfsTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPH 552
Cdd:PRK07656 373 VMKGYYDDPEATAAAI--DADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPD 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 839746169 553 NIKGQAIYAYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK07656 451 ERLGEVGKAYVVLKPGAELTEE---ELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
91-624 |
9.43e-62 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 214.41 E-value: 9.43e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 91 DQTAIIWEGddasqsKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEA 170
Cdd:PRK08316 26 DKTALVFGD------RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 171 VAGRIIDSSSRLVITADEglragraipLKKNVDDALKNPNVNSIEHVVVLKRTGGkidwqEGRDLWWSDLMANASAEHRP 250
Cdd:PRK08316 100 LAYILDHSGARAFLVDPA---------LAPTAEAALALLPVDTLILSLVLGGREA-----PGGWLDFADWAEAGSVAEPD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 251 VEMNAEDPLFILYTSGSTGKPKGVLHTTGgylvyaATTFKYV-----FDYHPGDI-------YWCTADvgwvtgHSYLly 318
Cdd:PRK08316 166 VELADDDLAQILYTSGTESLPKGAMLTHR------ALIAEYVscivaGDMSADDIplhalplYHCAQL------DVFL-- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 319 GP-LACGATTLMFEGvpnwPTPARMCQVVDKHKVSILYTAPTAIRALMAEGDkaIEGTDRSSLRiLGSVGEPINPEAwew 397
Cdd:PRK08316 232 GPyLYVGATNVILDA----PDPELILRTIEAERITSFFAPPTVWISLLRHPD--FDTRDLSSLR-KGYYGASIMPVE--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 398 YWKKIgNEKCPVMDTW---WQTEtggfmITPL-----PGAIELKAGSATRPFFGVQPVLVDNEGLPldgategnlaIADS 469
Cdd:PRK08316 302 VLKEL-RERLPGLRFYncyGQTE-----IAPLatvlgPEEHLRRPGSAGRPVLNVETRVVDDDGND----------VAPG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 470 WPGQ--ART------LFGDHERFEQtyfsTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHP 540
Cdd:PRK08316 366 EVGEivHRSpqlmlgYWDDPEKTAE----AFRGGWFhSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHP 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 541 KIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAA 620
Cdd:PRK08316 442 AVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTED---ELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERYA 518
|
....
gi 839746169 621 GDTS 624
Cdd:PRK08316 519 GAFT 522
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
73-617 |
1.30e-61 |
|
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: 213.55 E-value: 1.30e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 73 GTLNLAANCLDRHLAE-RGDQTAIIwegDDASQskhITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLA 151
Cdd:TIGR02262 1 EKYNAAEDLLDRNVVEgRGGKTAFI---DDISS---LSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 152 CARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVITADEGLragraiPLKKNVddALKNPNvnsIEHVVVLKRtggkidwQE 231
Cdd:TIGR02262 75 AIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALL------PVIKAA--LGKSPH---LEHRVVVGR-------PE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 232 GRDLWWSDLMANASAEHRPVEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVT 311
Cdd:TIGR02262 137 AGEVQLAELLATESEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFAY 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 312 GHSYLLYGPLACGATTLMFegvPNWPTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGTDRssLRILGSVGEPIn 391
Cdd:TIGR02262 217 GLGNALTFPMSVGATTVLM---GERPTPDAVFDRLRRHQPTIFYGVPTLYAAMLADPNLPSEDQVR--LRLCTSAGEAL- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 392 PEAWEWYWK-KIGNEkcpVMDTWWQTETGGFMITPLPGAIELkaGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIadSW 470
Cdd:TIGR02262 291 PAEVGQRWQaRFGVD---IVDGIGSTEMLHIFLSNLPGDVRY--GTSGKPVPGYRLRLVGDGGQDVADGEPGELLI--SG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 471 PGQARTLFGDHERFEQTYFSTFKNmyfSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGI 550
Cdd:TIGR02262 364 PSSATMYWNNRAKSRDTFQGEWTR---SGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGV 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 551 P---HNIKGQaiyAYVTLNHGEEptpELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:TIGR02262 441 AdedGLIKPK---AFVVLRPGQT---ALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
109-616 |
1.12e-59 |
|
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: 206.56 E-value: 1.12e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 109 TYRELHADVCRFANVLLD-LGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAgRIIDSSSRLVITAD 187
Cdd:cd05958 12 TYRDLLALANRIANVLVGeLGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELA-YILDKARITVALCA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 188 EGLRAgraiplkknvddalknpnvnsiehvvvlkrtggkidwqegrdlwwsdlmanasaehrpvemnAEDPLFILYTSGS 267
Cdd:cd05958 91 HALTA--------------------------------------------------------------SDDICILAFTSGT 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 268 TGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVpnwpTPARMCQVVD 347
Cdd:cd05958 109 TGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEA----TPDLLLSAIA 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 348 KHKVSILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEPINPEAWEWYWKKIGnekCPVMDTWWQTETGGFMITPLP 427
Cdd:cd05958 185 RYKPTVLFTAPTAYRAMLAHPDAA--GPDLSSLRKCVSAGEALPAALHRAWKEATG---IPIIDGIGSTEMFHIFISARP 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 428 GAIelKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIADswPGQARTLFgdhERFEQTYFSTFKNmyFSGDGARRDED 507
Cdd:cd05958 260 GDA--RPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRG--PTGCRYLA---DKRQRTYVQGGWN--ITGDTYSRDPD 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 508 GYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPELYAEVRNWVRKEI 587
Cdd:cd05958 331 GYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARELQDHAKAHI 410
|
490 500
....*....|....*....|....*....
gi 839746169 588 GPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05958 411 APYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
107-616 |
1.78e-58 |
|
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: 202.52 E-value: 1.78e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 107 HITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVITa 186
Cdd:cd05934 3 RWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 187 deglragraiplkknvddalknpnvnsiehvvvlkrtggkidwqegrdlwwsdlmanasaehrpvemnaeDPLFILYTSG 266
Cdd:cd05934 82 ----------------------------------------------------------------------DPASILYTSG 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 267 STGKPKGVLhTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVpnwpTPARMCQVV 346
Cdd:cd05934 92 TTGPPKGVV-ITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRF----SASRFWSDV 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 347 DKHKVSILYTAPTAIRALMAEGDKAiegTDRSS-LRILGsvGEPINPEAWEWYWKKIGnekCPVMDTWWQTETGGFMITP 425
Cdd:cd05934 167 RRYGATVTNYLGAMLSYLLAQPPSP---DDRAHrLRAAY--GAPNPPELHEEFEERFG---VRLLEGYGMTETIVGVIGP 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 426 LPGAIelKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIAdSWPGQARTLfGDHERFEQTYfSTFKNMYF-SGDGARR 504
Cdd:cd05934 239 RDEPR--RPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIR-GLRGWGFFK-GYYNMPEATA-EAMRNGWFhTGDLGYR 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 505 DEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPElyaEVRNWVR 584
Cdd:cd05934 314 DADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPE---ELFAFCE 390
|
490 500 510
....*....|....*....|....*....|..
gi 839746169 585 KEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05934 391 GQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
82-624 |
1.11e-57 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 203.75 E-value: 1.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 82 LDRHLAERGDQTAIIWEGDDASQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAI--- 158
Cdd:PRK13295 30 LDACVASCPDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVlnp 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 159 -------HSV----------------IFGGFSPEAVAgriidsssrlvitadEGLRagRAIPlkknvddalknpnvnSIE 215
Cdd:PRK13295 110 lmpifreRELsfmlkhaeskvlvvpkTFRGFDHAAMA---------------RRLR--PELP---------------ALR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 216 HVVVLkrtGGKID-----------WQEGRDLwwsdlmANASAEHRPvemNAEDPLFILYTSGSTGKPKGVLHTT----GG 280
Cdd:PRK13295 158 HVVVV---GGDGAdsfeallitpaWEQEPDA------PAILARLRP---GPDDVTQLIYTSGTTGEPKGVMHTAntlmAN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 281 YLVYAATtfkyvFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEgvpNWpTPARMCQVVDKHKVSilYT-APT 359
Cdd:PRK13295 226 IVPYAER-----LGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQD---IW-DPARAAELIRTEGVT--FTmAST 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 360 AIRALMAEGDKAiEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEKCPVmdtWWQTETGGFMITPLPGAIELKAGSATR 439
Cdd:PRK13295 295 PFLTDLTRAVKE-SGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSA---WGMTENGAVTLTKLDDPDERASTTDGC 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 440 PFFGVQPVLVDNEGLPLDGATEGNLAIadswpgQARTLFGDHERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDV 519
Cdd:PRK13295 371 PLPGVEVRVVDADGAPLPAGQIGRLQV------RGCSNFGGYLKRPQLNGTDADGWFDTGDLARIDADGYIRISGRSKDV 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 520 LNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTpelYAEVRNWVR-KEIGPLATPDVLHW 598
Cdd:PRK13295 445 IIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLD---FEEMVEFLKaQKVAKQYIPERLVV 521
|
570 580
....*....|....*....|....*.
gi 839746169 599 TDSLPKTRSGKIMRRILRKIAAGDTS 624
Cdd:PRK13295 522 RDALPRTPSGKIQKFRLREMLRGEDA 547
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
91-613 |
4.63e-57 |
|
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: 199.29 E-value: 4.63e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 91 DQTAIIWEGddasqsKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIfggfSPEA 170
Cdd:cd05930 2 DAVAVVDGD------QSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPL----DPSY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 171 VAGRII----DSSSRLVITadeglragraiplkknvddalknpnvnsiehvvvlkrtggkidwqegrdlwwsdlmanasa 246
Cdd:cd05930 72 PAERLAyileDSGAKLVLT------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 247 ehrpvemNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTA----DVGWVTghsylLYGPLA 322
Cdd:cd05930 91 -------DPDDLAYVIYTSGSTGKPKGVMVEHRG-LVNLLLWMQEAYPLTPGDRVLQFTsfsfDVSVWE-----IFGALL 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 323 CGATTLMfegVPN--WPTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAiegtDRSSLRILGSVGEPINPEAWEwYWK 400
Cdd:cd05930 158 AGATLVV---LPEevRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELA----ALPSLRLVLVGGEALPPDLVR-RWR 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 401 KIGNEK----------CPVMDTWWQTETGGFMITPLP-GaielkagsatRPFFGVQPVLVDNEGLPL-DGATeGNLAIAD 468
Cdd:cd05930 230 ELLPGArlvnlygpteATVDATYYRVPPDDEEDGRVPiG----------RPIPNTRVYVLDENLRPVpPGVP-GELYIGG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 469 swPGQARTLFGDHE----RFEQTYFSTFKNMYFSGDGARRDEDG--YYwiTGRVDDVLNVSGHRLGTAEIESALVSHPKI 542
Cdd:cd05930 299 --AGLARGYLNRPEltaeRFVPNPFGPGERMYRTGDLVRWLPDGnlEF--LGRIDDQVKIRGYRIELGEIEAALLAHPGV 374
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 839746169 543 AEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRR 613
Cdd:cd05930 375 REAAVVAREDGDGEKRLVAYVVPDEGGELDEE---ELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRK 442
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
108-619 |
2.36e-53 |
|
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: 188.93 E-value: 2.36e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 108 ITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIhsvifggfspeavagrIIDSSSRLviTAD 187
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAV----------------VIPATTLL--TPD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 188 EglragraipLKKNVDdalknpnvnsiehvvvlkRTGGKIDWQEgrdlwwsdlmanaSAEHrpvemnAEDPLFILYTSGS 267
Cdd:cd05974 63 D---------LRDRVD------------------RGGAVYAAVD-------------ENTH------ADDPMLLYFTSGT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 268 TGKPKGVLHTTGGYLVYAATTFkYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFegvpNWP--TPARMCQV 345
Cdd:cd05974 97 TSKPKLVEHTHRSYPVGHLSTM-YWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLF----NYArfDAKRVLAA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 346 VDKHKVSILYTAPTAIRALMAEGDKAIegtdRSSLRILGSVGEPINPEAWEWYWKKIGnekCPVMDTWWQTETGGfMITP 425
Cdd:cd05974 172 LVRYGVTTLCAPPTVWRMLIQQDLASF----DVKLREVVGAGEPLNPEVIEQVRRAWG---LTIRDGYGQTETTA-LVGN 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 426 LPGAIeLKAGSATRPFFGVQPVLVDNEGLPldgATEGNLAIADSWPGQARTLFGDHERFEQTYFSTFKNMYFSGDGARRD 505
Cdd:cd05974 244 SPGQP-VKAGSMGRPLPGYRVALLDPDGAP---ATEGEVALDLGDTRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRD 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 506 EDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPELYAEVRNWVRK 585
Cdd:cd05974 320 EDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETALEIFRFSRE 399
|
490 500 510
....*....|....*....|....*....|....
gi 839746169 586 EIGPLATPDVLHWTDsLPKTRSGKIMRRILRKIA 619
Cdd:cd05974 400 RLAPYKRIRRLEFAE-LPKTISGKIRRVELRRRE 432
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
82-620 |
5.65e-53 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 192.48 E-value: 5.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 82 LDRHLAERGDQTAIIW--EGDDASQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGaIH 159
Cdd:PRK07529 31 LSRAAARHPDAPALSFllDADPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAG-IA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 160 SVIFGGFSPEAVAGRIIDSSSRLVITADEGLRAGRAIPLKKNVDDAlknPNVNSIEHVVVLKRTGGKIDWQ--------E 231
Cdd:PRK07529 110 NPINPLLEPEQIAELLRAAGAKVLVTLGPFPGTDIWQKVAEVLAAL---PELRTVVEVDLARYLPGPKRLAvplirrkaH 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 232 GRDLWWSDLMANASAEH----RPVEmnAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTADV 307
Cdd:PRK07529 187 ARILDFDAELARQPGDRlfsgRPIG--PDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDTVFCGLPL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 308 GWVTGHSYLLYGPLACGATTLmfegvpnWPTPA---------RMCQVVDKHKVSILYTAPTAIRALMaegDKAIEGTDRS 378
Cdd:PRK07529 264 FHVNALLVTGLAPLARGAHVV-------LATPQgyrgpgviaNFWKIVERYRINFLSGVPTVYAALL---QVPVDGHDIS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 379 SLRILGSVGEPINPEAWEWYWKKIGnekCPVMDTWWQTE-TGGFMITPLPGaiELKAGSATRPFFG--VQPVLVDNEG-L 454
Cdd:PRK07529 334 SLRYALCGAAPLPVEVFRRFEAATG---VRIVEGYGLTEaTCVSSVNPPDG--ERRIGSVGLRLPYqrVRVVILDDAGrY 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 455 PLDGATE--GNLAIADS--WPGQARtlfGDHER---FEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRL 527
Cdd:PRK07529 409 LRDCAVDevGVLCIAGPnvFSGYLE---AAHNKglwLEDGWLNT-------GDLGRIDADGYFWLTGRAKDLIIRGGHNI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 528 GTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPelyAEVRNWVRKEIG-PLATPDVLHWTDSLPKTR 606
Cdd:PRK07529 479 DPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATE---AELLAFARDHIAeRAAVPKHVRILDALPKTA 555
|
570
....*....|....
gi 839746169 607 SGKIMRRILRKIAA 620
Cdd:PRK07529 556 VGKIFKPALRRDAI 569
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
109-617 |
1.22e-52 |
|
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: 187.20 E-value: 1.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 109 TYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSpEAVAGRIIDSSSRLVItade 188
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFR-EHELAFILRRAKAKVF---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 189 glragraiplkknvddalknpnvnsiehvVVLKRTGGkidwqegrdlwwsdlmanasaeHRPVEMNAeDPLFILYTSGST 268
Cdd:cd05903 78 -----------------------------VVPERFRQ----------------------FDPAAMPD-AVALLLFTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 269 GKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEgvpNWpTPARMCQVVDK 348
Cdd:cd05903 106 GEPKGVMHSHNT-LSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQD---IW-DPDKALALMRE 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 349 HKVSILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEKCPVmdtWWQTETGGFMITPLPG 428
Cdd:cd05903 181 HGVTFMMGATPFLTDLLNAVEEA--GEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSA---YGSTECPGAVTSITPA 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 429 AIELKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIadswpgQARTLFGDHERFEQTYFSTFKNMYF-SGDGARRDED 507
Cdd:cd05903 256 PEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLS------RGPSVFLGYLDRPDLTADAAPEGWFrTGDLARLDED 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 508 GYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPELYAEVrnWVRKEI 587
Cdd:cd05903 330 GYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAY--LDRQGV 407
|
490 500 510
....*....|....*....|....*....|
gi 839746169 588 GPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05903 408 AKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
82-617 |
6.03e-51 |
|
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: 184.76 E-value: 6.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 82 LDRHLAERGDQTAIIWEGDDasQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSV 161
Cdd:cd12119 2 LEHAARLHGDREIVSRTHEG--EVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 162 IFGGFSPEAVAGRIIDSSSRLVITADEGLragraiPLKKNVDDALKNpnvnsIEHVVVLKRTGGKIDWQEGRDLWWSDLM 241
Cdd:cd12119 80 INPRLFPEQIAYIINHAEDRVVFVDRDFL------PLLEAIAPRLPT-----VEHVVVMTDDAAMPEPAGVGVLAYEELL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 242 ANASAEHRPVEMNAEDPLFILYTSGSTGKPKGV--------LHTTGGylvyAATTFKYVfdyHPGDIY-----------W 302
Cdd:cd12119 149 AAESPEYDWPDFDENTAAAICYTSGTTGNPKGVvyshrslvLHAMAA----LLTDGLGL---SESDVVlpvvpmfhvnaW 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 303 CTADVGWVTGHSYLLYGPlacgattlmfegvpnWPTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKaiEGTDRSSLRI 382
Cdd:cd12119 222 GLPYAAAMVGAKLVLPGP---------------YLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEA--NGRDLSSLRR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 383 LGSVGEPINPEAWEWyWKKIGnekCPVMDTWWQTETG--GFMITPLPGAIELKAG-------SATRPFFGVQPVLVDNEG 453
Cdd:cd12119 285 VVIGGSAVPRSLIEA-FEERG---VRVIHAWGMTETSplGTVARPPSEHSNLSEDeqlalraKQGRPVPGVELRIVDDDG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 454 --LPLDGATEGNLAIADSWpgQARTLFGDHER----FEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRL 527
Cdd:cd12119 361 reLPWDGKAVGELQVRGPW--VTKSYYKNDEEsealTEDGWLRT-------GDVATIDEDGYLTITDRSKDVIKSGGEWI 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 528 GTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRS 607
Cdd:cd12119 432 SSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAE---ELLEFLADKVAKWWLPDDVVFVDEIPKTST 508
|
570
....*....|
gi 839746169 608 GKIMRRILRK 617
Cdd:cd12119 509 GKIDKKALRE 518
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
91-615 |
2.14e-49 |
|
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: 178.66 E-value: 2.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 91 DQTAIIWEGDdasqskHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEA 170
Cdd:cd17643 2 EAVAVVDEDR------RLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 171 VAGRIIDSSSRLVITadeglragraiplkknvddalknpnvnsiehvvvlkrtggkidwqegrdlwwsdlmanasaehrp 250
Cdd:cd17643 76 IAFILADSGPSLLLT----------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 251 vemNAEDPLFILYTSGSTGKPKGVLHTTGGYL-VYAATTfkYVFDYHPGDIywctadvgWVTGHSYL-------LYGPLA 322
Cdd:cd17643 91 ---DPDDLAYVIYTSGSTGRPKGVVVSHANVLaLFAATQ--RWFGFNEDDV--------WTLFHSYAfdfsvweIWGALL 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 323 CGATTLMfegVPNWP--TPARMCQVVDKHKVSILYTAPTAIRALMAEGDKaiEGTDRSSLR--ILGsvGEPINPEAWEWY 398
Cdd:cd17643 158 HGGRLVV---VPYEVarSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADR--DGRDPLALRyvIFG--GEALEAAMLRPW 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 399 WKKIGNEKCPVMDTWWQTETGGFM-ITPLPGAiELKAGSAT---RPFFGVQPVLVDNEGLPLDGATEGNLAIADswPGQA 474
Cdd:cd17643 231 AGRFGLDRPQLVNMYGITETTVHVtFRPLDAA-DLPAAAASpigRPLPGLRVYVLDADGRPVPPGVVGELYVSG--AGVA 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 475 RTLFG----DHERF-EQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVG 549
Cdd:cd17643 308 RGYLGrpelTAERFvANPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIV 387
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 839746169 550 IPHNIKGQAIYAYVTLNHGEEPTPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17643 388 REDEPGDTRLVAYVVADDGAAADI---AELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
139-616 |
1.32e-48 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 177.70 E-value: 1.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 139 MPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVITADEGLRAGRAIPLKKNVDDAlkNPNVnsiehVV 218
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKVVEA--APAK-----AI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 219 VLKRTGGKIDWQ-EGRDLWWSDLMANASA-------EHRPVEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFK 290
Cdd:PLN03051 74 VLPAAGEPVAVPlREQDLSWCDFLGVAAAqgsvggnEYSPVYAPVESVTNILFSSGTTGEPKAIPWTHLSPLRCASDGWA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 291 YVfDYHPGDIYWCTADVGWVTGhSYLLYGPLACGATTLMFEGVpnwPTPARMCQVVDKHKVSILYTAPTAIRALMAEGDK 370
Cdd:PLN03051 154 HM-DIQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGA---PLGRGFGKFVQDAGVTVLGLVPSIVKAWRHTGAF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 371 AIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEKcPVMDTWWQTETGGFMI--TPL-PGAIelkaGSATRPFFGVQPV 447
Cdd:PLN03051 229 AMEGLDWSKLRVFASTGEASAVDDVLWLSSVRGYYK-PVIEYCGGTELASGYIssTLLqPQAP----GAFSTASLGTRFV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 448 LVDNEGLPL--DGATEGNLAIADSWPGQA-RTLFGDHerfEQTYFSTFKnMYFS--------GDGARRDEDGYYWITGRV 516
Cdd:PLN03051 304 LLNDNGVPYpdDQPCVGEVALAPPMLGASdRLLNADH---DKVYYKGMP-MYGSkgmplrrhGDIMKRTPGGYFCVQGRA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 517 DDVLNVSGHRLGTAEIESALVSHPK-IAEAAVVGIPhNIKGQAIYAYVTLNHGEEPT-------PELYAEVRNWVRKEIG 588
Cdd:PLN03051 380 DDTMNLGGIKTSSVEIERACDRAVAgIAETAAVGVA-PPDGGPELLVIFLVLGEEKKgfdqarpEALQKKFQEAIQTNLN 458
|
490 500
....*....|....*....|....*...
gi 839746169 589 PLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PLN03051 459 PLFKVSRVKIVPELPRNASNKLLRRVLR 486
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
84-616 |
5.28e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 176.72 E-value: 5.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 84 RHLAERGDQTAIIWegDDASqskhITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEA----AVAMLACARIGAIH 159
Cdd:PRK06188 20 SALKRYPDRPALVL--GDTR----LTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVlmaiGAAQLAGLRRTALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 160 SVIfggfSPEAVAGRIIDSSSRLVItADEGLRAGRAIPLKKNVDdalknpnvnSIEHVVVLKRTGGkidwqeGRDLWwsd 239
Cdd:PRK06188 94 PLG----SLDDHAYVLEDAGISTLI-VDPAPFVERALALLARVP---------SLKHVLTLGPVPD------GVDLL--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 240 lMANASAEHRPVEMNAE--DPLFILYTSGSTGKPKGVLHTTGGYLVYAAttfkyvfdyhpgdiyWCTADVGWVTGHSYLL 317
Cdd:PRK06188 151 -AAAAKFGPAPLVAAALppDIAGLAYTGGTTGKPKGVMGTHRSIATMAQ---------------IQLAEWEWPADPRFLM 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 318 YGPL--ACGAT---TLM----------FEgvpnwptPARMCQVVDKHKVSILYTAPTAIRALMAEGDkaIEGTDRSSLRI 382
Cdd:PRK06188 215 CTPLshAGGAFflpTLLrggtvivlakFD-------PAEVLRAIEEQRITATFLVPTMIYALLDHPD--LRTRDLSSLET 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 383 LGSVGEPINP----EAWEwywkKIGnekcPV-MDTWWQTETGGFmITPLP-----GAIELKAGSATRPFFGVQPVLVDNE 452
Cdd:PRK06188 286 VYYGASPMSPvrlaEAIE----RFG----PIfAQYYGQTEAPMV-ITYLRkrdhdPDDPKRLTSCGRPTPGLRVALLDED 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 453 GLPLDGATEGNLAIADswPGQARtlfGDHERFEQTYfSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAE 531
Cdd:PRK06188 357 GREVAQGEVGEICVRG--PLVMD---GYWNRPEETA-EAFRDGWLhTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPRE 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 532 IESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIM 611
Cdd:PRK06188 431 VEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDA---AELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPD 507
|
....*
gi 839746169 612 RRILR 616
Cdd:PRK06188 508 KKALR 512
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
82-620 |
2.39e-47 |
|
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: 174.95 E-value: 2.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 82 LDRHLAERGDQTAIIwEGDdasqsKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAI--- 158
Cdd:COG1021 31 LRRRAERHPDRIAVV-DGE-----RRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIpvf 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 159 ------HSVI--FGGFSpEAVAgriidsssrLVITADEGLRAGRAIPlkknvdDALKNpNVNSIEHVVVLKRTGGKIDWQ 230
Cdd:COG1021 105 alpahrRAEIshFAEQS-EAVA---------YIIPDRHRGFDYRALA------RELQA-EVPSLRHVLVVGDAGEFTSLD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 231 EgrdlwwsdlMANASAEHRPVEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLvYAATTFKYVFDYHPGDIYWCTADVGwv 310
Cdd:COG1021 168 A---------LLAAPADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYL-YSVRASAEICGLDADTVYLAALPAA-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 311 tgHSYllygPLAC---------GATTLMfegVPNwPTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKaiEGTDRSSLR 381
Cdd:COG1021 236 --HNF----PLSSpgvlgvlyaGGTVVL---APD-PSPDTAFPLIERERVTVTALVPPLALLWLDAAER--SRYDLSSLR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 382 ILGSVGEPINPEAWewywKKIGnekcPVMDTWWQ-----TEtGGFMITPLPGAIELKAGSATRPffgVQP---VL-VDNE 452
Cdd:COG1021 304 VLQVGGAKLSPELA----RRVR----PALGCTLQqvfgmAE-GLVNYTRLDDPEEVILTTQGRP---ISPddeVRiVDED 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 453 GLPLDGATEGNLAI-----------AdswPGQARTLFgDHERFeqtyfstfknmYFSGDGARRDEDGYYWITGRVDDVLN 521
Cdd:COG1021 372 GNPVPPGEVGELLTrgpytirgyyrA---PEHNARAF-TPDGF-----------YRTGDLVRRTPDGYLVVEGRAKDQIN 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 522 VSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNhGEEPTPelyAEVRNWVRkEIGpLAT---PDVLHW 598
Cdd:COG1021 437 RGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPR-GEPLTL---AELRRFLR-ERG-LAAfklPDRLEF 510
|
570 580
....*....|....*....|..
gi 839746169 599 TDSLPKTRSGKIMRRILRKIAA 620
Cdd:COG1021 511 VDALPLTAVGKIDKKALRAALA 532
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
87-615 |
2.72e-47 |
|
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: 173.96 E-value: 2.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 87 AERGDQTAIIwegdDASQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGF 166
Cdd:cd05904 16 SAHPSRPALI----DAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 167 SPEAVAGRIIDSSSRLVITADEGLragraiplKKNVDDALKnpnvnsiehVVVLKRTggkidwQEGRDLWWSDLMANASA 246
Cdd:cd05904 92 TPAEIAKQVKDSGAKLAFTTAELA--------EKLASLALP---------VVLLDSA------EFDSLSFSDLLFEADEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 247 EHRPVEMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFD--YHPGDIYWCTADVGWVTGHSYLLYGPLACG 324
Cdd:cd05904 149 EPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRN-LIAMVAQFVAGEGsnSDSEDVFLCVLPMFHIYGLSSFALGLLRLG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 325 ATTL---MFEGvpnwptpARMCQVVDKHKVSILYTAPTAIRAlMAEGDKAiEGTDRSSLRILGSVGEPINPEAWEWYWKK 401
Cdd:cd05904 228 ATVVvmpRFDL-------EELLAAIERYKVTHLPVVPPIVLA-LVKSPIV-DKYDLSSLRQIMSGAAPLGKELIEAFRAK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 402 IGNekCPVMDTWWQTE-TGGFMITPLPGAIELKAGSATRPFFGVQPVLVD-NEGLPLDGATEGNLaiadsW---PGQART 476
Cdd:cd05904 299 FPN--VDLGQGYGMTEsTGVVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGEL-----WirgPSIMKG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 477 LFGDHERFEQTYfsTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKG 556
Cdd:cd05904 372 YLNNPEATAATI--DKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAG 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 839746169 557 QAIYAYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05904 450 EVPMAFVVRKPGSSLTED---EIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
82-617 |
3.76e-47 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 174.20 E-value: 3.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 82 LDRHLAERG-DQTAIIWEGddasqsKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHS 160
Cdd:TIGR03098 5 LLEDAAARLpDATALVHHD------RTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 161 VIFGGFSPEAVAGRIIDSSSRLVITADEGLRAgraiplkknVDDALknPNVNSIEHVV-VLKRTGGKIDWQEGRDLWWSD 239
Cdd:TIGR03098 79 PINPLLKAEQVAHILADCNVRLLVTSSERLDL---------LHPAL--PGCHDLRTLIiVGDPAHASEGHPGEEPASWPK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 240 LMAnASAEHRPVEMNAEDPLFILYTSGSTGKPKGVL--HTTggyLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLL 317
Cdd:TIGR03098 148 LLA-LGDADPPHPVIDSDMAAILYTSGSTGRPKGVVlsHRN---LVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 318 YGPLACGATTLMfegvpNWPTPARMCQVVDKHKVSILYTAPtAIRALMAEGDkaIEGTDRSSLRILGSVGEPINPEAWEW 397
Cdd:TIGR03098 224 TAFYVGATVVLH-----DYLLPRDVLKALEKHGITGLAAVP-PLWAQLAQLD--WPESAAPSLRYLTNSGGAMPRATLSR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 398 YWKKIGNEKCPVMdtWWQTEtgGFMITPL-PGAIELKAGSATR--PFFGVQPVLVDNE----GLPLDGATEGNLAIADSW 470
Cdd:TIGR03098 296 LRSFLPNARLFLM--YGLTE--AFRSTYLpPEEVDRRPDSIGKaiPNAEVLVLREDGSecapGEEGELVHRGALVAMGYW 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 471 PGQARTlfgdHERFE-----QTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEA 545
Cdd:TIGR03098 372 NDPEKT----AERFRplppfPGELHLPELAVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEA 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 839746169 546 AVVGIPHNIKGQAIYAYVTLNHGEEPTPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:TIGR03098 448 VAFGVPDPTLGQAIVLVVTPPGGEELDR---AALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
102-616 |
2.91e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 171.24 E-value: 2.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 102 ASQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSR 181
Cdd:PRK08276 6 APSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 182 LVIT----ADEGLRAGRAIPLkknvddalknpnvnsieHVVVLKRTGGKID-WQEgrdlwWSDLMANASAEHRPVEMNAE 256
Cdd:PRK08276 86 VLIVsaalADTAAELAAELPA-----------------GVPLLLVVAGPVPgFRS-----YEEALAAQPDTPIADETAGA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 257 DplfILYTSGSTGKPKGVLHTTGGYLVYAA---TTFKYVFDYH--PGDIYWCTADvgwvtghsylLY--GPLACGATTLM 329
Cdd:PRK08276 144 D---MLYSSGTTGRPKGIKRPLPGLDPDEApgmMLALLGFGMYggPDSVYLSPAP----------LYhtAPLRFGMSALA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 330 FEGV----PNWpTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPinpeawewywkkigne 405
Cdd:PRK08276 211 LGGTvvvmEKF-DAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYDVSSLRVAIHAAAP---------------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 406 kCPV-----MDTWW---------QTETGGF-MITPlPGAIElKAGSATRPFFGVQPVLvDNEGLPLDGATEGNLAIADSW 470
Cdd:PRK08276 274 -CPVevkraMIDWWgpiiheyyaSSEGGGVtVITS-EDWLA-HPGSVGKAVLGEVRIL-DEDGNELPPGEIGTVYFEMDG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 471 PGqartlFGDHERFEQTYFSTFKNMYFS-GDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVG 549
Cdd:PRK08276 350 YP-----FEYHNDPEKTAAARNPHGWVTvGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFG 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 839746169 550 IPHNIKGQAIYAYVTLNHGEEPTPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK08276 425 VPDEEMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
91-616 |
4.41e-46 |
|
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: 169.47 E-value: 4.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 91 DQTAIIWEGddasqsKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEA 170
Cdd:cd17649 2 DAVALVFGD------QSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 171 VAGRIIDSSSRLVITadeglragraiplkknvddalknpnvnsiehvvvlkrtggkidwQEGRDLWWsdlmanasaehrp 250
Cdd:cd17649 76 LRYMLEDSGAGLLLT--------------------------------------------HHPRQLAY------------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 251 vemnaedplfILYTSGSTGKPKGVLHTTGGYLVYAATTFKYvFDYHPGDIYWCTADVGWVTGHSYLlYGPLACGATTLMf 330
Cdd:cd17649 99 ----------VIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGDRELQFASFNFDGAHEQL-LPPLICGACVVL- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 331 EGVPNWPTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGtDRSSLRILGSVGEPINPEAWeWYWKKIGnekCPVM 410
Cdd:cd17649 166 RPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDG-RPPSLRLYIFGGEALSPELL-RRWLKAP---VRLF 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 411 DTWWQTETggfMITPL--PGAIELKAGSAT----RPFFGVQPVLVDNEGLPL-DGATeGNLAIADswPGQARtlfGDHER 483
Cdd:cd17649 241 NAYGPTEA---TVTPLvwKCEAGAARAGASmpigRPLGGRSAYILDADLNPVpVGVT-GELYIGG--EGLAR---GYLGR 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 484 FEQT--------YFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIk 555
Cdd:cd17649 312 PELTaerfvpdpFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG- 390
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 839746169 556 GQAIYAYVTLNHGEEpTPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd17649 391 GKQLVAYVVLRAAAA-QPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
109-547 |
4.94e-46 |
|
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: 168.21 E-value: 4.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 109 TYRELHADVCRFANVLLDL-GIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGfSPEAVAGRII-DSSSRLVITA 186
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPA-YPAERLAFILeDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 187 DEGLRAGRAIPLkknvddalknpnvnsiEHVVVlkrtggkidwqegRDLWWSDLMANASAEHRPVEMNAEDPLFILYTSG 266
Cdd:TIGR01733 80 SALASRLAGLVL----------------PVILL-------------DPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 267 STGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTADVGWvtGHSYL-LYGPLACGATTLMFEGVPNWPTPARMCQV 345
Cdd:TIGR01733 131 STGRPKGVVVTHRS-LVNLLAWLARRYGLDPDDRVLQFASLSF--DASVEeIFGALLAGATLVVPPEDEERDDAALLAAL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 346 VDKHKVSILYTAPTAIRALMAEGDkaiegTDRSSLRILGSVGEPINPEAWEWYWKKIGNekCPVMDTWWQTE-TGGFMIT 424
Cdd:TIGR01733 208 IAEHPVTVLNLTPSLLALLAAALP-----PALASLRLVILGGEALTPALVDRWRARGPG--ARLINLYGPTEtTVWSTAT 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 425 PLPGAIELKAGSAT--RPFFGVQPVLVDNEGLPLDGATEGNLAIADswPGQARTLFGD----HERF-EQTYF-STFKNMY 496
Cdd:TIGR01733 281 LVDPDDAPRESPVPigRPLANTRLYVLDDDLRPVPVGVVGELYIGG--PGVARGYLNRpeltAERFvPDPFAgGDGARLY 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 839746169 497 FSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAV 547
Cdd:TIGR01733 359 RTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
84-616 |
5.10e-46 |
|
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: 170.22 E-value: 5.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 84 RHLAERGDQTAIIWEGDdasqskHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIF 163
Cdd:cd17651 3 RQAARTPDAPALVAEGR------RLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 164 GGFSPEAVAGRIIDSSSRLVITADE--GLRAGRAIPlkknvddalknpnvnsiehvvvlkrtGGKIDWQEGRDLwwsdlm 241
Cdd:cd17651 77 PAYPAERLAFMLADAGPVLVLTHPAlaGELAVELVA--------------------------VTLLDQPGAAAG------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 242 anASAEHRPvEMNAEDPLFILYTSGSTGKPKGVL--HTTGGYLVYAATTfkyVFDYHPGDIYWCTADVGW-VTGHSylLY 318
Cdd:cd17651 125 --ADAEPDP-ALDADDLAYVIYTSGSTGRPKGVVmpHRSLANLVAWQAR---ASSLGPGARTLQFAGLGFdVSVQE--IF 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 319 GPLACGATtLMFEGVPNWPTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEP--INPEAWE 396
Cdd:cd17651 197 STLCAGAT-LVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPL--GVRLAALRYLLTGGEQlvLTEDLRE 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 397 WYWKKIGNEkcpVMDTWWQTETGgfMITplpgAIELKAGSAT--------RPFFGVQPVLVDNEGLPLDGATEGNLAIAD 468
Cdd:cd17651 274 FCAGLPGLR---LHNHYGPTETH--VVT----ALSLPGDPAAwpapppigRPIDNTRVYVLDAALRPVPPGVPGELYIGG 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 469 swPGQARTLFGD----HERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAE 544
Cdd:cd17651 345 --AGLARGYLNRpeltAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVRE 422
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 839746169 545 AAVVGIPHNIKGQAIYAYVTLNHGEEPTPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd17651 423 AVVLAREDRPGEKRLVAYVVGDPEAPVDA---AELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
87-615 |
1.08e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 170.53 E-value: 1.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 87 AER-GDQTAIIWEGddasqsKHITYRELHADVCRFANVLLD-LGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFG 164
Cdd:PRK08314 20 ARRyPDKTAIVFYG------RAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 165 GFSPEAVAGRIIDSSSRLVITADEglRAGRAIPLKKNVddalknpnvnSIEHVVV------LKRTGGKI--DW------- 229
Cdd:PRK08314 94 MNREEELAHYVTDSGARVAIVGSE--LAPKVAPAVGNL----------RLRHVIVaqysdyLPAEPEIAvpAWlraeppl 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 230 ---QEGRDLWWSDLMANASAEhRPVEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYvFDYHPGDIYWCTAD 306
Cdd:PRK08314 162 qalAPGGVVAWKEALAAGLAP-PPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLW-SNSTPESVVLAVLP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 307 VGWVTGHSYLLYGPLACGATTLMfegVPNW--PTPARMcqvVDKHKVSILYTAPTAIRALMAEGDkaIEGTDRSSLRILG 384
Cdd:PRK08314 240 LFHVTGMVHSMNAPIYAGATVVL---MPRWdrEAAARL---IERYRVTHWTNIPTMVVDFLASPG--LAERDLSSLRYIG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 385 SVGEPInPEA-WEWYWKKIGnekCPVMDTWWQTETGGFMITPLPGAIELK-AGSatrPFFGVQPVLVDNEGL-PLDGATE 461
Cdd:PRK08314 312 GGGAAM-PEAvAERLKELTG---LDYVEGYGLTETMAQTHSNPPDRPKLQcLGI---PTFGVDARVIDPETLeELPPGEV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 462 GNLAIadSWPGQARTLFGDHERFEQTyFSTF--KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSH 539
Cdd:PRK08314 385 GEIVV--HGPQVFKGYWNRPEATAEA-FIEIdgKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKH 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 839746169 540 PKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPElYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK08314 462 PAIQEACVIATPDPRRGETVKAVVVLRPEARGKTT-EEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
90-616 |
1.60e-45 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 169.48 E-value: 1.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 90 GDQTAIIWEgDDASQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPE 169
Cdd:PRK08008 21 GHKTALIFE-SSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 170 AVAGRIIDSSSRLVITADEGLRAGRAIPLKKNvddalknpnvNSIEHVVVLKRTGGKIDwqeGRdLWWSDLMANASAE-- 247
Cdd:PRK08008 100 ESAWILQNSQASLLVTSAQFYPMYRQIQQEDA----------TPLRHICLTRVALPADD---GV-SSFTQLKAQQPATlc 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 248 -HRPVEmnAEDPLFILYTSGSTGKPKGVLHTT-----GGYlvYAATTFKYVFDyhpgDIYW-----------CTAdvgwv 310
Cdd:PRK08008 166 yAPPLS--TDDTAEILFTSGTTSRPKGVVITHynlrfAGY--YSAWQCALRDD----DVYLtvmpafhidcqCTA----- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 311 tghsylLYGPLACGATTLMFEGVpnwpTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGTD--RSSLRILgsvge 388
Cdd:PRK08008 233 ------AMAAFSAGATFVLLEKY----SARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHclREVMFYL----- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 389 PINPEAWEWYWKKIGNEkcpVMDTWWQTETGGFMITPLPGAiELKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIAD 468
Cdd:PRK08008 298 NLSDQEKDAFEERFGVR---LLTSYGMTETIVGIIGDRPGD-KRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 469 SwPGqaRTLFgdherfeQTYF----STFKNM-----YFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSH 539
Cdd:PRK08008 374 V-PG--KTIF-------KEYYldpkATAKVLeadgwLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATH 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 839746169 540 PKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK08008 444 PKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEE---EFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
82-615 |
9.72e-43 |
|
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: 160.90 E-value: 9.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 82 LDRHLAERGDQTAIIWEGddasqsKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSV 161
Cdd:cd17646 4 VAEQAARTPDAPAVVDEG------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 162 IFGGFSPEAVAGRIIDSSSRLVITADEGLRAGRAIPLKKNVDDALknpnvnsiehvvvlkrtggkidwqegrdlwwsdlM 241
Cdd:cd17646 78 LDPGYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEA----------------------------------L 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 242 ANASAEHRPVEMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTADVGW-VTGhsYLLYGP 320
Cdd:cd17646 124 AAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAG-IVNRLLWMQDEYPLGPGDRVLQKTPLSFdVSV--WELFWP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 321 LACGATTLMFEgvPNWPT-PARMCQVVDKHKVSILYTAPTAIRALMAEGDkaieGTDRSSLRILGSVGEPINPEAWEWYW 399
Cdd:cd17646 201 LVAGARLVVAR--PGGHRdPAYLAALIREHGVTTCHFVPSMLRVFLAEPA----AGSCASLRRVFCSGEALPPELAARFL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 400 KKIGNE--------KCPVMDTWWQTeTGGFMITPLP-GaielkagsatRPFFGVQPVLVDNEGLPLDGATEGNLAIADsw 470
Cdd:cd17646 275 ALPGAElhnlygptEAAIDVTHWPV-RGPAETPSVPiG----------RPVPNTRLYVLDDALRPVPVGVPGELYLGG-- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 471 PGQARTLFG----DHERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAA 546
Cdd:cd17646 342 VQLARGYLGrpalTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAV 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 839746169 547 VVGIPHNIKGQAIYAYVTLNHGEEPTPElyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17646 422 VVARAAPAGAARLVGYVVPAAGAAGPDT--AALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
108-615 |
2.70e-41 |
|
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: 155.71 E-value: 2.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 108 ITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIhsvifggfspeavagriidsssrlvitad 187
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAV----------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 188 eglragrAIPLkknvddalkNPNVNSIEHVVVLKRTGGKIdwqegrdlwwsdlmANASAEhrpvemnAEDPLFILYTSGS 267
Cdd:cd05935 53 -------VVPI---------NPMLKERELEYILNDSGAKV--------------AVVGSE-------LDDLALIPYTSGT 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 268 TGKPKGVLHTTGGYlvyAATTFKYVFDYH--PGDIYWCTADVGWVTGHSYLLYGPLACGATTLMfegVPNWPTPArMCQV 345
Cdd:cd05935 96 TGLPKGCMHTHFSA---AANALQSAVWTGltPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVL---MARWDRET-ALEL 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 346 VDKHKVSILYTAPTAIRALMAegDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEkcpVMDTWWQTETGGFMITP 425
Cdd:cd05935 169 IEKYKVTFWTNIPTMLVDLLA--TPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLR---FVEGYGLTETMSQTHTN 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 426 LPGAieLKAGSATRPFFGVQPVLVDNE-GLPLDGATEGNLAIadSWPGQARTLFGDHERFEQTYFSTFKNMYF-SGDGAR 503
Cdd:cd05935 244 PPLR--PKLQCLGIP*FGVDARVIDIEtGRELPPNEVGEIVV--RGPQIFKGYWNRPEETEESFIEIKGRRFFrTGDLGY 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 504 RDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGE--EPTPElyaEVRN 581
Cdd:cd05935 320 MDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYrgKVTEE---DIIE 396
|
490 500 510
....*....|....*....|....*....|....
gi 839746169 582 WVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05935 397 WAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
75-617 |
3.82e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 157.13 E-value: 3.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 75 LNLAaNCLDRHLAERGDQTAIIWeGDdasqsKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACAR 154
Cdd:PRK07470 7 MNLA-HFLRQAARRFPDRIALVW-GD-----RSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 155 IGAIHSVIFGGFSPEAVAGRIIDSSSRLVITAD---EGLRAGRAIPLkknvddalknpnvnSIEHVVVLKRTGGKIDWQe 231
Cdd:PRK07470 80 LGAVWVPTNFRQTPDEVAYLAEASGARAMICHAdfpEHAAAVRAASP--------------DLTHVVAIGGARAGLDYE- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 232 grdlwwsDLMA-NASAEHRPVEMNAEDPLFILYTSGSTGKPKGVLHTTGgylvyaatTFKYVFDYHPGDIYWCT--ADVG 308
Cdd:PRK07470 145 -------ALVArHLGARVANAAVDHDDPCWFFFTSGTTGRPKAAVLTHG--------QMAFVITNHLADLMPGTteQDAS 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 309 WVT-------GHSYLLygPLACGATTLMFEGVPNwpTPARMCQVVDKHKVSILYTAPTaIRALMAEgDKAIEGTDRSSLR 381
Cdd:PRK07470 210 LVVaplshgaGIHQLC--QVARGAATVLLPSERF--DPAEVWALVERHRVTNLFTVPT-ILKMLVE-HPAVDRYDHSSLR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 382 ILGSVGEPINPEAWEWYWKKIGnekcPVMDTWWQTE--TGGfmITPLPGAI-------ELKAGSATRPFFGVQPVLVDNE 452
Cdd:PRK07470 284 YVIYAGAPMYRADQKRALAKLG----KVLVQYFGLGevTGN--ITVLPPALhdaedgpDARIGTCGFERTGMEVQIQDDE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 453 GLPLDGATEGNLAIAdswpGQArtLFGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAE 531
Cdd:PRK07470 358 GRELPPGETGEICVI----GPA--VFAGYYNNPEANAKAFRDGWFrTGDLGHLDARGFLYITGRASDMYISGGSNVYPRE 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 532 IESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIM 611
Cdd:PRK07470 432 IEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEA---ELLAWLDGKVARYKLPKRFFFWDALPKSGYGKIT 508
|
....*.
gi 839746169 612 RRILRK 617
Cdd:PRK07470 509 KKMVRE 514
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
82-648 |
5.81e-41 |
|
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: 160.79 E-value: 5.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 82 LDRHLAERGDQTAIIWEGDdasqskHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGA---- 157
Cdd:COG1020 482 FEAQAARTPDAVAVVFGDQ------SLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAayvp 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 158 IhsvifggfSPEAVAGRII----DSSSRLVITaDEGLRagraiplkknvdDALKNPNVNSIEhvvvlkrtggkIDWQEgr 233
Cdd:COG1020 556 L--------DPAYPAERLAymleDAGARLVLT-QSALA------------ARLPELGVPVLA-----------LDALA-- 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 234 dlwwsdlMANASAEHRPVEMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIywctadVGWVTGH 313
Cdd:COG1020 602 -------LAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRA-LVNLLAWMQRRYGLGPGDR------VLQFASL 667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 314 S-----YLLYGPLACGATTLMF--EGVPNwptPARMCQVVDKHKVSILYTAPTAIRALMAEGdkaieGTDRSSLRILGSV 386
Cdd:COG1020 668 SfdasvWEIFGALLSGATLVLAppEARRD---PAALAELLARHRVTVLNLTPSLLRALLDAA-----PEALPSLRLVLVG 739
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 387 GEPINPEAWEWYWKKIGNekCPVMDTWWQTETGGFMITPLPGAIELKAGSAT--RPFFGVQPVLVDNEGLPL-DGATeGN 463
Cdd:COG1020 740 GEALPPELVRRWRARLPG--ARLVNLYGPTETTVDSTYYEVTPPDADGGSVPigRPIANTRVYVLDAHLQPVpVGVP-GE 816
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 464 LAIADswPGQARTLFGDH----ERFEQTYFSTFKN-MYFSGDGARRDEDG---YywiTGRVDDVLNVSGHR--LGtaEIE 533
Cdd:COG1020 817 LYIGG--AGLARGYLNRPeltaERFVADPFGFPGArLYRTGDLARWLPDGnleF---LGRADDQVKIRGFRieLG--EIE 889
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 534 SALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPELYAEVRnwvRKEIGPLATPDVLHWTDSLPKTRSGKimrr 613
Cdd:COG1020 890 AALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLAL---ALLLPPYMVPAAVVLLLPLPLTGNGK---- 962
|
570 580 590
....*....|....*....|....*....|....*
gi 839746169 614 ILRKIAAGDTSNLGDTSTLADPGVVEKLLEEKQAI 648
Cdd:COG1020 963 LDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLL 997
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
83-615 |
2.02e-40 |
|
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: 154.28 E-value: 2.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 83 DRHLAERGDQTAIIWEGDDasqskhITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVI 162
Cdd:cd12117 4 EEQAARTPDAVAVVYGDRS------LTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 163 FGGFSPEAVAGRIIDSSSRLVIT--ADEGLRAGRAIPLkknvddalknpnvnsiehvvvlkrtggkidwqegrDLWWSDL 240
Cdd:cd12117 78 DPELPAERLAFMLADAGAKVLLTdrSLAGRAGGLEVAV-----------------------------------VIDEALD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 241 MANASAEHRPVEmnAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTfKYVfDYHPGDIYWCTADVGWvTGHSYLLYGP 320
Cdd:cd12117 123 AGPAGNPAVPVS--PDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNT-NYV-TLGPDDRVLQTSPLAF-DASTFEIWGA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 321 LACGAT-TLMFEGVPnwPTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGtdrssLRILGSVGEPINPEawewyW 399
Cdd:cd12117 198 LLNGARlVLAPKGTL--LDPDALGALIAEEGVTVLWLTAALFNQLADEDPECFAG-----LRELLTGGEVVSPP-----H 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 400 KKIGNEKCP---VMDTWWQTETGGFMITPLPGAIELKAGSAT--RPFFGVQPVLVDNEGLPLDGATEGNLAIADSwpGQA 474
Cdd:cd12117 266 VRRVLAACPglrLVNGYGPTENTTFTTSHVVTELDEVAGSIPigRPIANTRVYVLDEDGRPVPPGVPGELYVGGD--GLA 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 475 RTLFGD----HERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGI 550
Cdd:cd12117 344 LGYLNRpaltAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVR 423
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 839746169 551 PHNIKGQAIYAYVTlnhGEEPTPelYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd12117 424 EDAGGDKRLVAYVV---AEGALD--AAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
84-615 |
4.80e-40 |
|
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: 152.47 E-value: 4.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 84 RHLAERGDQTAIIwegddaSQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIF 163
Cdd:cd12115 7 AQAARTPDAIALV------CGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 164 GGFSPEAVAGRIIDSSSRLVITadeglragraiplkknvddalknpnvnsiehvvvlkrtggkidwqegrdlwwsdlman 243
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVLT---------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 244 asaehrpvemNAEDPLFILYTSGSTGKPKGVL---HTTGGYLVYAATTFkyvfdyhPGDiYWctADVGWVTG-----HSY 315
Cdd:cd12115 103 ----------DPDDLAYVIYTSGSTGRPKGVAiehRNAAAFLQWAAAAF-------SAE-EL--AGVLASTSicfdlSVF 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 316 LLYGPLACGATTLMFEGVPNWPTPARMCQVvdkhkvSILYTAPTAIRALMAEGDKAiegtdrSSLRILGSVGEPINPEAW 395
Cdd:cd12115 163 ELFGPLATGGKVVLADNVLALPDLPAAAEV------TLINTVPSAAAELLRHDALP------ASVRVVNLAGEPLPRDLV 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 396 EWYWKKIGNEKC-----PVMDTWWQTetggfmITPLPGAIElKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIadSW 470
Cdd:cd12115 231 QRLYARLQVERVvnlygPSEDTTYST------VAPVPPGAS-GEVSIGRPLANTQAYVLDRALQPVPLGVPGELYI--GG 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 471 PGQARTLFGD----HERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAA 546
Cdd:cd12115 302 AGVARGYLGRpgltAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAV 381
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 839746169 547 VVGIPHNIKGQAIYAYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd12115 382 VVAIGDAAGERRLVAYIVAEPGAAGLVE---DLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
91-617 |
3.34e-39 |
|
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: 150.13 E-value: 3.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 91 DQTAIIwegddASQSKHiTYRELHADVCRFANVLLDLG-IKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPE 169
Cdd:cd05941 1 DRIAIV-----DDGDSI-TYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 170 AVAGRIIDSSSRLVItadeglragraiplkknvDDALknpnvnsiehvvvlkrtggkidwqegrdlwwsdlmanasaehr 249
Cdd:cd05941 75 ELEYVITDSEPSLVL------------------DPAL------------------------------------------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 250 pvemnaedplfILYTSGSTGKPKGVLHTTGGYLVYAATTFKYvfdyhpgdIYWCTADV-----------GWVTGhsylLY 318
Cdd:cd05941 94 -----------ILYTSGTTGRPKGVVLTHANLAANVRALVDA--------WRWTEDDVllhvlplhhvhGLVNA----LL 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 319 GPLACGATTLMfegVPNwPTPARMCQVVDKHKVSILYTAPT-------AIRALMAEGDKAIEGTDRSsLRILGSVGEPIN 391
Cdd:cd05941 151 CPLFAGASVEF---LPK-FDPKEVAISRLMPSITVFMGVPTiytrllqYYEAHFTDPQFARAAAAER-LRLMVSGSAALP 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 392 PEAWEwYWKKIGNEkcPVMDTWWQTETGGFMITPLPGaiELKAGSATRPFFGVQPVLVDNE-GLPLDGATEGNLAIAdsw 470
Cdd:cd05941 226 VPTLE-EWEAITGH--TLLERYGMTEIGMALSNPLDG--ERRPGTVGMPLPGVQARIVDEEtGEPLPRGEVGEIQVR--- 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 471 pgqARTLFGDH-ERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRV-DDVLNVSGHRLGTAEIESALVSHPKIAEAAV 547
Cdd:cd05941 298 ---GPSVFKEYwNKPEATKEEFTDDGWFkTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAV 374
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 548 VGIPHNIKGQAIYAYVTLNHGEEPTPElyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05941 375 IGVPDPDWGERVVAVVVLRAGAAALSL--EELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
109-615 |
3.72e-39 |
|
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: 150.52 E-value: 3.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 109 TYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVITADE 188
Cdd:cd12116 14 SYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTDDA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 189 ---GLRAGRAIPLKKNVDDAlknpnvnsiehvvvlkrtggkidwqegrdlwwsdlmanASAEHRPVEMNAEDPLFILYTS 265
Cdd:cd12116 94 lpdRLPAGLPVLLLALAAAA--------------------------------------AAPAAPRTPVSPDDLAYVIYTS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 266 GSTGKPKGV----------LHTTGGYL-------VYAATTfkYVFDYhpgdiywctadvgwvtghSYL-LYGPLACGATT 327
Cdd:cd12116 136 GSTGRPKGVvvshrnlvnfLHSMRERLglgpgdrLLAVTT--YAFDI------------------SLLeLLLPLLAGARV 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 328 LMFEGVPNwPTPARMCQVVDKHKVSILYTAPTAIRALMAEGdkaieGTDRSSLRIL-GsvGEPINP-----------EAW 395
Cdd:cd12116 196 VIAPRETQ-RDPEALARLIEAHSITVMQATPATWRMLLDAG-----WQGRAGLTALcG--GEALPPdlaarllsrvgSLW 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 396 EWYwkkiGnekcPVMDTWWQTETggfMITPLPGAIELkagsaTRPFFGVQPVLVDNEGLPLDGATEGNLAIADswPGQAR 475
Cdd:cd12116 268 NLY----G----PTETTIWSTAA---RVTAAAGPIPI-----GRPLANTQVYVLDAALRPVPPGVPGELYIGG--DGVAQ 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 476 TLFGD----HERFEQTYFSTF-KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGI 550
Cdd:cd12116 330 GYLGRpaltAERFVPDPFAGPgSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVR 409
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 839746169 551 PHNIKGQaIYAYVTLNHGEEPTPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd12116 410 EDGGDRR-LVAYVVLKAGAAPDA---AALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
84-618 |
1.24e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 150.46 E-value: 1.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 84 RHLAERG-DQTAIIwegDDASQskhITYRELHADVCRFANVLLDLGIKKGDVVAI----YMPMVpeaaVAMLACARIGAI 158
Cdd:PRK07788 56 AHAARRApDRAALI---DERGT---LTYAELDEQSNALARGLLALGVRAGDGVAVlarnHRGFV----LALYAAGKVGAR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 159 HSVIFGGFSPEAVAGRIIDSSSRLVITADEGLRAGRAIPlkknvddalknPNVNSIeHVVVLKRTGGKIDWQEGRDLwwS 238
Cdd:PRK07788 126 IILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALP-----------PDLGRL-RAWGGNPDDDEPSGSTDETL--D 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 239 DLMANASAEHRPVemnAEDP-LFILYTSGSTGKPKGVLHTTggylVYAATTFKYVFDYHP---GDIYWCTADVGWVTGHS 314
Cdd:PRK07788 192 DLIAGSSTAPLPK---PPKPgGIVILTSGTTGTPKGAPRPE----PSPLAPLAGLLSRVPfraGETTLLPAPMFHATGWA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 315 YLLYGpLACGATTLM---FEgvpnwptPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPIN 391
Cdd:PRK07788 265 HLTLA-MALGSTVVLrrrFD-------PEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 392 PEAWEWYWKKIGnekcPVM-DTWWQTETGgFMITPLPGAIELKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIADSW 470
Cdd:PRK07788 337 PELATRALEAFG----PVLyNLYGSTEVA-FATIATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGF 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 471 PGQARTLFGDHERFeqtyfstfKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGI 550
Cdd:PRK07788 412 PFEGYTDGRDKQII--------DGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGV 483
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 839746169 551 PHNIKGQAIYAYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKI 618
Cdd:PRK07788 484 DDEEFGQRLRAFVVKAPGAALDED---AIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
83-616 |
5.11e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 147.92 E-value: 5.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 83 DRHLAERGDQTAIIWEGDDASqskhITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVI 162
Cdd:PRK13391 4 GIHAQTTPDKPAVIMASTGEV----VTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 163 FGGFSPEAVAGRIIDSSSRLVITADEGLRAGRAIPlkKNVddalknPNVnsiEHVVVLKRTGGKIDWQEgrdlwWSDLMA 242
Cdd:PRK13391 80 NSHLTPAEAAYIVDDSGARALITSAAKLDVARALL--KQC------PGV---RHRLVLDGDGELEGFVG-----YAEAVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 243 NASAEHRPVEMNAEDplfILYTSGSTGKPKGVLH--------TTGGYLVYaattFKYVFDYHPGDIYWCTADVGwvtgHS 314
Cdd:PRK13391 144 GLPATPIADESLGTD---MLYSSGTTGRPKGIKRplpeqppdTPLPLTAF----LQRLWGFRSDMVYLSPAPLY----HS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 315 yllyGPLAC-------GATTLMFEGVpnwpTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVG 387
Cdd:PRK13391 213 ----APQRAvmlvirlGGTVIVMEHF----DAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHAA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 388 EPinpeawewywkkignekCPV-----MDTWW---------QTETGGFMITPLPGAIElKAGSATRPFFGVqPVLVDNEG 453
Cdd:PRK13391 285 AP-----------------CPPqvkeqMIDWWgpiiheyyaATEGLGFTACDSEEWLA-HPGTVGRAMFGD-LHILDDDG 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 454 LPLDGATEGNLAIADSWPGQ-----ARTlfgDHERFEQTYFSTfknmyfSGDGARRDEDGYYWITGRVDDVLNVSGHRLG 528
Cdd:PRK13391 346 AELPPGEPGTIWFEGGRPFEylndpAKT---AEARHPDGTWST------VGDIGYVDEDGYLYLTDRAAFMIISGGVNIY 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 529 TAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSG 608
Cdd:PRK13391 417 PQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTG 496
|
....*...
gi 839746169 609 KIMRRILR 616
Cdd:PRK13391 497 KLYKRLLR 504
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
79-631 |
3.64e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 146.08 E-value: 3.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 79 ANCLDRHLAERGDQTAIIWEGDDasqskhITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAI 158
Cdd:PRK07786 20 VNQLARHALMQPDAPALRFLGNT------TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 159 HSVIFGGFSPEAVAGRIIDSSSRLVITadEGLRAgraiPLKKNVDDAlknpnVNSIEHVVVLkrtGGKIDwqeGRDLWWS 238
Cdd:PRK07786 94 AVPVNFRLTPPEIAFLVSDCGAHVVVT--EAALA----PVATAVRDI-----VPLLSTVVVA---GGSSD---DSVLGYE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 239 DLMANASAEHRPVEMNAEDPLFILYTSGSTGKPKG-VL-HTTggyLVYAATTFKYVFDYH-PGDIYWCTADVGWVTGHSY 315
Cdd:PRK07786 157 DLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGaVLtHAN---LTGQAMTCLRTNGADiNSDVGFVGVPLFHIAGIGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 316 LLYGpLACGATTLMFegvpnwPT----PARMCQVVDKHKVSILYTAPTAIRALMAegDKAIEGTDRsSLRILGSVGEPIN 391
Cdd:PRK07786 234 MLPG-LLLGAPTVIY------PLgafdPGQLLDVLEAEKVTGIFLVPAQWQAVCA--EQQARPRDL-ALRVLSWGAAPAS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 392 PEAWEWYwkkigNEKCP---VMDTWWQTEtggfmITP----LPG--AIElKAGSATRPFFGVQPVLVDNEglpldgateg 462
Cdd:PRK07786 304 DTLLRQM-----AATFPeaqILAAFGQTE-----MSPvtcmLLGedAIR-KLGSVGKVIPTVAARVVDEN---------- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 463 nlaIADSWPGQ-------ARTLFGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIES 534
Cdd:PRK07786 363 ---MNDVPVGEvgeivyrAPTLMSGYWNNPEATAEAFAGGWFhSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVEN 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 535 ALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPelYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRI 614
Cdd:PRK07786 440 VLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALT--LEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTE 517
|
570
....*....|....*...
gi 839746169 615 LRK-IAAGDTSNLGDTST 631
Cdd:PRK07786 518 LRErYGACVNVERRSASA 535
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
91-617 |
1.25e-36 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 144.51 E-value: 1.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 91 DQTAIIwegDDASQSkhITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEA 170
Cdd:PRK06087 38 DKIAVV---DNHGAS--YTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 171 VAGRIIDSSSRLVI-------TADEGLragrAIPLKKNVDdalknpnvnSIEHVVVLKRTGGKIDwqegrDLWWSDLMAN 243
Cdd:PRK06087 113 LVWVLNKCQAKMFFaptlfkqTRPVDL----ILPLQNQLP---------QLQQIVGVDKLAPATS-----SLSLSQIIAD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 244 ASAEHRPVEMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLAC 323
Cdd:PRK06087 175 YEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNN-ILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 324 GATTLMFEGVpnwpTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEPInP-----EAWEWY 398
Cdd:PRK06087 254 GARSVLLDIF----TPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQ--PADLSALRFFLCGGTTI-PkkvarECQQRG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 399 WKkignekcpVMDTWWQTETGGFMITPLPGAIELKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLaiADSWPGQARTLF 478
Cdd:PRK06087 327 IK--------LLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEE--ASRGPNVFMGYL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 479 GDHERfeqtyfsTFKNM-----YFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHN 553
Cdd:PRK06087 397 DEPEL-------TARALdeegwYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDE 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 839746169 554 IKGQAIYAYVTLNhGEEPTPELyAEVRNWV-RKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK06087 470 RLGERSCAYVVLK-APHHSLTL-EEVVAFFsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
82-620 |
1.28e-36 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 144.53 E-value: 1.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 82 LDRHLAERGDQTAIIWEgddaSQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSV 161
Cdd:PRK12583 24 FDATVARFPDREALVVR----HQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 162 IFGGFSPEAVAGRIIDSSSRLVITADeGLRA-------GRAIP-LKKNVDDALKNPNVNSIEHVVVL--KRTGGKIDWQE 231
Cdd:PRK12583 100 INPAYRASELEYALGQSGVRWVICAD-AFKTsdyhamlQELLPgLAEGQPGALACERLPELRGVVSLapAPPPGFLAWHE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 232 --GRdlwwSDLMANASAEHRPVEMNAEDPLFILYTSGSTGKPKGVLHT-----TGGYLVYAATTF----KYVFdyhPGDI 300
Cdd:PRK12583 179 lqAR----GETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLShhnilNNGYFVAESLGLtehdRLCV---PVPL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 301 YWC----TADVGWVTGHSYLLY-----GPLAcgatTLmfegvpnwptparmcQVVDKHKVSILYTAPTAIRALMAEGDKA 371
Cdd:PRK12583 252 YHCfgmvLANLGCMTVGACLVYpneafDPLA----TL---------------QAVEEERCTALYGVPTMFIAELDHPQRG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 372 ieGTDRSSLRILGSVGEPINPEAWEwywKKIGNEKCP-VMDTWWQTETGGfmITPLPGA---IELKAGSATRpffgVQPV 447
Cdd:PRK12583 313 --NFDLSSLRTGIMAGAPCPIEVMR---RVMDEMHMAeVQIAYGMTETSP--VSLQTTAaddLERRVETVGR----TQPH 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 448 LvDNEGLPLDGATEGNLAIADSWPGQARTLFGDHERFEQTYFSTFKN--MYfSGDGARRDEDGYYWITGRVDDVLNVSGH 525
Cdd:PRK12583 382 L-EVKVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDgwMH-TGDLATMDEQGYVRIVGRSKDMIIRGGE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 526 RLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKT 605
Cdd:PRK12583 460 NIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEE---ELREFCKARIAHFKVPRYFRFVDEFPMT 536
|
570
....*....|....*
gi 839746169 606 RSGKIMRRILRKIAA 620
Cdd:PRK12583 537 VTGKVQKFRMREISI 551
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
82-549 |
1.32e-36 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 145.24 E-value: 1.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 82 LDRHLAERGDQTAIIWEGDDASQSkhITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSV 161
Cdd:COG1022 17 LRRRAARFPDRVALREKEDGIWQS--LTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 162 IFGGFSPEAVAGRIIDSSSRLVITADEGLRAgRAIPLKKNVDdalknpnvnSIEHVVVLKRTGGKIDwqeGRDLWWSDLM 241
Cdd:COG1022 95 IYPTSSAEEVAYILNDSGAKVLFVEDQEQLD-KLLEVRDELP---------SLRHIVVLDPRGLRDD---PRLLSLDELL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 242 ANASA-------EHRPVEMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIY-----WCtadvgW 309
Cdd:COG1022 162 ALGREvadpaelEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRN-LLSNARALLERLPLGPGDRTlsflpLA-----H 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 310 VTGHSyLLYGPLACGAT-------------------TLMFeGVP-------------------------NWPTP---ARM 342
Cdd:COG1022 236 VFERT-VSYYALAAGATvafaespdtlaedlrevkpTFML-AVPrvwekvyagiqakaeeagglkrklfRWALAvgrRYA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 343 CQVVDKHKVSILYTAPTA---------IRALMaeGDKaiegtdrssLRILGSVGEPINPEAWEWYWkKIGnekCPVMDTW 413
Cdd:COG1022 314 RARLAGKSPSLLLRLKHAladklvfskLREAL--GGR---------LRFAVSGGAALGPELARFFR-ALG---IPVLEGY 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 414 WQTETGGFMITPLPGAIelKAGSATRPFFGVQpVLVDNEGLPL-------------DGATegnlaiadswpgqARTLFGD 480
Cdd:COG1022 379 GLTETSPVITVNRPGDN--RIGTVGPPLPGVE-VKIAEDGEILvrgpnvmkgyyknPEAT-------------AEAFDAD 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 839746169 481 HerfeqtYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGhrlGT----AEIESALVSHPKIAEAAVVG 549
Cdd:COG1022 443 G------WLHT-------GDIGELDEDGFLRITGRKKDLIVTSG---GKnvapQPIENALKASPLIEQAVVVG 499
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
86-615 |
1.39e-36 |
|
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: 142.77 E-value: 1.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 86 LAERGDQTAIIWEGDDasqskhITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGG 165
Cdd:cd05945 1 AAANPDRPAVVEGGRT------LTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 166 FSPEAVAgRIIDSSSRLVITADEGlragraiplkknvddalknpnvnsiehvvvlkrtggkidwqegrdlwwsdlmanas 245
Cdd:cd05945 75 SPAERIR-EILDAAKPALLIADGD-------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 246 aehrpvemnaeDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYvFDYHPGDIYWCTADVGW---VTGhsylLYGPLA 322
Cdd:cd05945 98 -----------DNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSD-FPLGPGDVFLNQAPFSFdlsVMD----LYPALA 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 323 CGATTlmfegvpnWPTP-------ARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGTDrsSLRILGSVGEPI-NPEA 394
Cdd:cd05945 162 SGATL--------VPVPrdatadpKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLP--SLRHFLFCGEVLpHKTA 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 395 WEWywkKIGNEKCPVMDTWWQTET----GGFMITPlpgaiELKAGSAT----RPFFGVQPVLVDNEGLPLDGATEGNLAI 466
Cdd:cd05945 232 RAL---QQRFPDARIYNTYGPTEAtvavTYIEVTP-----EVLDGYDRlpigYAKPGAKLVILDEDGRPVPPGEKGELVI 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 467 ADswPGQARTLFGDHERFEQTYFSTFKN-MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEA 545
Cdd:cd05945 304 SG--PSVSKGYLNNPEKTAAAFFPDEGQrAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEA 381
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 546 AVVGIPHNIKGQAIYAYVTLNHGEEPTPElyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05945 382 VVVPKYKGEKVTELIAFVVPKPGAEAGLT--KAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
87-615 |
9.12e-36 |
|
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: 140.93 E-value: 9.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 87 AERG-DQTAIIWEGDdasqskHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIfgg 165
Cdd:cd17655 7 AEKTpDHTAVVFEDQ------TLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 166 fSPEAVAGRII----DSSSRLVITADeglragraiPLKKNVDDAlknpnvnsiehvvvlkrtgGKIDWQEGRDLwwsdlm 241
Cdd:cd17655 78 -DPDYPEERIQyileDSGADILLTQS---------HLQPPIAFI-------------------GLIDLLDEDTI------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 242 ANASAEHRPVEMNAEDPLFILYTSGSTGKPKGVLHTTGG--YLVYAATTfKYVFDYHpgdiywctADVGWVTGHSYLL-- 317
Cdd:cd17655 123 YHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGvvNLVEWANK-VIYQGEH--------LRVALFASISFDAsv 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 318 ---YGPLACGATTLMFEGVPNWPTPArMCQVVDKHKVSILYTAPTAIRALMAEGDkaiegTDRSSLRILGSVGEPINPEA 394
Cdd:cd17655 194 teiFASLLSGNTLYIVRKETVLDGQA-LTQYIRQNRITIIDLTPAHLKLLDAADD-----SEGLSLKHLIVGGEALSTEL 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 395 WEwYWKKIGNEKCPVMDTWWQTETG-GFMITPL-PGAIELKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIADSwpG 472
Cdd:cd17655 268 AK-KIIELFGTNPTITNAYGPTETTvDASIYQYePETDQQVSVPIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGE--G 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 473 QARTLFG----DHERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVV 548
Cdd:cd17655 345 VARGYLNrpelTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVI 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 839746169 549 GIPHNIKGQAIYAYVTlnhGEEPTPElyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17655 425 ARKDEQGQNYLCAYIV---SEKELPV--AQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
90-609 |
1.22e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 141.18 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 90 GDQTAIIWeGDDAsqskhITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPE 169
Cdd:PRK07798 17 PDRVALVC-GDRR-----LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVED 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 170 AVAGRIIDSSSRLVITADEglRAGRaiplkknVDDALknPNVNSIEHVVVLKRTGGKIDWQEGRDlwWSDLMANASAEHR 249
Cdd:PRK07798 91 ELRYLLDDSDAVALVYERE--FAPR-------VAEVL--PRLPKLRTLVVVEDGSGNDLLPGAVD--YEDALAAGSPERD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 250 PVEMNAEDpLFILYTSGSTGKPKGVLHTT--------GGYLVYAATTfkyvfdyhPGDIYWCTADVGWVTGHSYLLYGPL 321
Cdd:PRK07798 158 FGERSPDD-LYLLYTGGTTGMPKGVMWRQedifrvllGGRDFATGEP--------IEDEEELAKRAAAGPGMRRFPAPPL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 322 ACGATTL-----MFEG----VPNWPT--PARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPI 390
Cdd:PRK07798 229 MHGAGQWaafaaLFSGqtvvLLPDVRfdADEVWRTIEREKVNVITIVGDAMARPLLDALEARGPYDLSSLFAIASGGALF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 391 NPEAWEWYWKKIGNekCPVMDTWWQTETG-GFMITPLPGAielkaGSATRPFFGVQP--VLVDNEGLPL--DGATEGNLA 465
Cdd:PRK07798 309 SPSVKEALLELLPN--VVLTDSIGSSETGfGGSGTVAKGA-----VHTGGPRFTIGPrtVVLDEDGNPVepGSGEIGWIA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 466 IADSWP-GqartLFGDHERFEQTYFSTFKNMY-FSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIA 543
Cdd:PRK07798 382 RRGHIPlG----YYKDPEKTAETFPTIDGVRYaIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVA 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 839746169 544 EAAVVGIPHNIKGQAIYAYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGK 609
Cdd:PRK07798 458 DALVVGVPDERWGQEVVAVVQLREGARPDLA---ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
101-615 |
1.32e-35 |
|
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: 140.72 E-value: 1.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 101 DASQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIfggfSPEAVAGRIIDsss 180
Cdd:cd05923 22 DPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALI----NPRLKAAELAE--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 181 rlVITADEGLRAGRAiplkknvDDALknPNVNSIEHVVVLKRTGGKIDWQEGRDlwwsdlmANASAEHRPVEmnAEDPLF 260
Cdd:cd05923 95 --LIERGEMTAAVIA-------VDAQ--VMDAIFQSGVRVLALSDLVGLGEPES-------AGPLIEDPPRE--PEQPAF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 261 ILYTSGSTGKPKGVL---HTTGGYLVYAATTFKYVFDYH-------PgdIYWctadvgwVTGHSYLLYGPLACGATTLmf 330
Cdd:cd05923 155 VFYTSGTTGLPKGAVipqRAAESRVLFMSTQAGLRHGRHnvvlglmP--LYH-------VIGFFAVLVAALALDGTYV-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 331 egVPNWPTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEKCPVM 410
Cdd:cd05923 224 --VVEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFA--GLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 411 DTwwqTETGGFMITPLPgaielKAGSATRPFFG----VQPVLVDNEGLPLDGaTEGNL---AIADS-WPGQARtlfgdhe 482
Cdd:cd05923 300 GT---TEAMNSLYMRDA-----RTGTEMRPGFFsevrIVRIGGSPDEALANG-EEGELivaAAADAaFTGYLN------- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 483 RFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAY 562
Cdd:cd05923 364 QPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTAC 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 839746169 563 VTLNHGEEPTPELYAEVRNwvrKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05923 444 VVPREGTLSADELDQFCRA---SELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
117-616 |
5.85e-35 |
|
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: 137.96 E-value: 5.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 117 VCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEavagrIIDSSSRLVItADEGLRAgrAI 196
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPT-----LKESVLRYLV-ADAGGRI--VL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 197 PLKKNVDDALKNPNVNSIEHVVVlkrtggkidwqeGRDLWWSdlmANASAEHRPVEmnAEDPLFILYTSGSTGKPKGVL- 275
Cdd:cd05922 75 ADAGAADRLRDALPASPDPGTVL------------DADGIRA---ARASAPAHEVS--HEDLALLLYTSGSTGSPKLVRl 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 276 -HTTggyLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGpLACGATTLMFE-GVPnwptPARMCQVVDKHKVSI 353
Cdd:cd05922 138 sHQN---LLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTH-LLRGATLVLTNdGVL----DDAFWEDLREHGATG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 354 LYTAPTaIRALMAEGDKAIEGTdrSSLRILGSVGEPINPEAWEWYWKKIGNEKCPVMdtWWQTETGGFMITPLPGAIELK 433
Cdd:cd05922 210 LAGVPS-TYAMLTRLGFDPAKL--PSLRYLTQAGGRLPQETIARLRELLPGAQVYVM--YGQTEATRRMTYLPPERILEK 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 434 AGSATRPFFGVQPVLVDNEGLPL------DGATEGNLAIADSWPGQArtlfgdherfEQTYFSTFKNMYFSGDGARRDED 507
Cdd:cd05922 285 PGSIGLAIPGGEFEILDDDGTPTppgepgEIVHRGPNVMKGYWNDPP----------YRRKEGRGGGVLHTGDLARRDED 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 508 GYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIkGQAIYAYVTLNHGEEPtpelyAEVRNWVRKEI 587
Cdd:cd05922 355 GFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKIDP-----KDVLRSLAERL 428
|
490 500
....*....|....*....|....*....
gi 839746169 588 GPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05922 429 PPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
109-623 |
7.51e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 138.40 E-value: 7.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 109 TYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLvITADE 188
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRL-LLGDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 189 GLRAGRAIPLkknvddalknpnvnsiehvvvlkrtggkidwqegrDLwwSDLMANASAeHRPVE---MNAEDPLFILYTS 265
Cdd:PRK09088 103 AVAAGRTDVE-----------------------------------DL--AAFIASADA-LEPADtpsIPPERVSLILFTS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 266 GSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVpnwpTPARMCQV 345
Cdd:PRK09088 145 GTSGQPKGVMLSERN-LQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGF----EPKRTLGR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 346 VDKHKVSI--LYTAPTAIRALMAEgdkaiEGTDRSSLRILGSV---GEPiNPEAWEWYWKKIGnekCPVMDTWWQTETGG 420
Cdd:PRK09088 220 LGDPALGIthYFCVPQMAQAFRAQ-----PGFDAAALRHLTALftgGAP-HAAEDILGWLDDG---IPMVDGFGMSEAGT 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 421 FMITPL-PGAIELKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIA--DSWPGQARTLFGDHERF-EQTYFSTfknmy 496
Cdd:PRK09088 291 VFGMSVdCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRgpNLSPGYWRRPQATARAFtGDGWFRT----- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 497 fsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGeepTPELY 576
Cdd:PRK09088 366 --GDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADG---APLDL 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 839746169 577 AEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDT 623
Cdd:PRK09088 441 ERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDALAAGR 487
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
50-617 |
8.70e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 139.36 E-value: 8.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 50 RPYTRvkntSFAPGNISIKWYEDGTLnlaANCLDRHLAERGDQTAIIWEGddasqsKHITYRELHADVCRFANVLLDLGI 129
Cdd:PRK05605 13 KPWLQ----SYAPWTPHDLDYGDTTL---VDLYDNAVARFGDRPALDFFG------ATTTYAELGKQVRRAAAGLRALGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 130 KKGDVVAIYMPMVPEAAVAMLACARIGAI---HSVIFggfSPEAVAGRIIDSSSRLVITAD------EGLRagRAIPLKK 200
Cdd:PRK05605 80 RPGDRVAIVLPNCPQHIVAFYAVLRLGAVvveHNPLY---TAHELEHPFEDHGARVAIVWDkvaptvERLR--RTTPLET 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 201 NVddalknpNVNSIEHVVVLKRTGGKI---DWQEGRD---------LWWSDLMANA------SAEHRPVEmnAEDPLFIL 262
Cdd:PRK05605 155 IV-------SVNMIAAMPLLQRLALRLpipALRKARAaltgpapgtVPWETLVDAAiggdgsDVSHPRPT--PDDVALIL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 263 YTSGSTGKPKGVLHTTGGYLVYAATTfkyvfdyhpgdiywctadVGWVTG---------------HSY-----LLYGPLa 322
Cdd:PRK05605 226 YTSGTTGKPKGAQLTHRNLFANAAQG------------------KAWVPGlgdgpervlaalpmfHAYgltlcLTLAVS- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 323 CGATTLMFegvpnwPTPaRMCQVVD---KHKVSILYTAPTAIRALMAEGDKaiEGTDRSSLRILGSVGEPINPEAWEWyw 399
Cdd:PRK05605 287 IGGELVLL------PAP-DIDLILDamkKHPPTWLPGVPPLYEKIAEAAEE--RGVDLSGVRNAFSGAMALPVSTVEL-- 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 400 kkignekcpvmdtwWQTETGGFMI--------TPL----PGAIELKAGSATRPFFGVQPVLVDNEGLPLDGA--TEGNLA 465
Cdd:PRK05605 356 --------------WEKLTGGLLVegygltetSPIivgnPMSDDRRPGYVGVPFPDTEVRIVDPEDPDETMPdgEEGELL 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 466 IadswpgQARTLF-GDHERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAE 544
Cdd:PRK05605 422 V------RGPQVFkGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVED 495
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 839746169 545 AAVVGIPHNIKGQAIYAYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK05605 496 AAVVGLPREDGSEEVVAAVVLEPGAALDPE---GLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
263-620 |
2.51e-34 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 134.15 E-value: 2.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 263 YTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLmfegvpnWPTPA-- 340
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVV-------LAGPAgy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 341 -------RMCQVVDKHKVSILYTAPTAIRALMAEGDKAiegtDRSSLRILGSVGEPINPEAWEWYWKKIGnekCPVMDTW 413
Cdd:cd05944 81 rnpglfdNFWKLVERYRITSLSTVPTVYAALLQVPVNA----DISSLRFAMSGAAPLPVELRARFEDATG---LPVVEGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 414 WQTE-TGGFMITPLPGAIELKAGSATRPFFGVQPVLVDNEG---LPLDGATEGNLAIAdswpgqARTLFGDHERFEQTYF 489
Cdd:cd05944 154 GLTEaTCLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDGVGrllRDCAPDEVGEICVA------GPGVFGGYLYTEGNKN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 490 STFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHG 568
Cdd:cd05944 228 AFVADGWLnTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPG 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 839746169 569 EEPTPElyaEVRNWVRKEIGP-LATPDVLHWTDSLPKTRSGKIMRRILRKIAA 620
Cdd:cd05944 308 AVVEEE---ELLAWARDHVPErAAVPKHIEVLEELPVTAVGKVFKPALRADAI 357
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
106-615 |
3.48e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 137.47 E-value: 3.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 106 KHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVIT 185
Cdd:PRK06710 48 KDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILC 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 186 ADeglragRAIPLKKNVDDALKnpnvnsIEHVVVL-------------------KRTG--GKIDWQEGRDLWWSDLMANA 244
Cdd:PRK06710 128 LD------LVFPRVTNVQSATK------IEHVIVTriadflpfpknllypfvqkKQSNlvVKVSESETIHLWNSVEKEVN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 245 SAEHRPVEmnAEDPLFIL-YTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDiywctaDVGWVTGHSYLLYGPLAC 323
Cdd:PRK06710 196 TGVEVPCD--PENDLALLqYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGE------EVVLGVLPFFHVYGMTAV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 324 GATTLMfEG-----VPNWPTPArMCQVVDKHKVSILYTAPTAIRALMaeGDKAIEGTDRSSLRILGSVGEPINPEAWEWY 398
Cdd:PRK06710 268 MNLSIM-QGykmvlIPKFDMKM-VFEAIKKHKVTLFPGAPTIYIALL--NSPLLKEYDISSIRACISGSAPLPVEVQEKF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 399 WKKIG---------NEKCPVMDT--WWQTETGGFMITPLPGA----IELKAGSATRPffgvqpvlvdneGLPLDGATEGN 463
Cdd:PRK06710 344 ETVTGgklvegyglTESSPVTHSnfLWEKRVPGSIGVPWPDTeamiMSLETGEALPP------------GEIGEIVVKGP 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 464 LAIADSWpgqartlfgdhERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIA 543
Cdd:PRK06710 412 QIMKGYW-----------NKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQ 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 839746169 544 EAAVVGIPHNIKGQAIYAYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK06710 481 EVVTIGVPDPYRGETVKAFVVLKEGTECSEE---ELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
84-623 |
1.15e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 135.94 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 84 RHLA-ERGDQTAIIWEGDDasqskhITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVI 162
Cdd:PRK06178 40 RAWArERPQRPAIIFYGHV------ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 163 fggfSPEAVAGRII----DSSSRLVITADeglragRAIPLKKNVDDALknpnvnSIEHVVVLKRTG-----------GKI 227
Cdd:PRK06178 114 ----SPLFREHELSyelnDAGAEVLLALD------QLAPVVEQVRAET------SLRHVIVTSLADvlpaeptlplpDSL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 228 DWQEGRDLWWSDLMANASAEHRPVEMNA---EDPLFILYTSGSTGKPKGVLHTTGgYLVYAATTFKYVfdYHPGDiywcT 304
Cdd:PRK06178 178 RAPRLAAAGAIDLLPALRACTAPVPLPPpalDALAALNYTGGTTGMPKGCEHTQR-DMVYTAAAAYAV--AVVGG----E 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 305 ADVG-------WVTGHSYLLYGPLACGATTLMfegVPNWPTPARMcQVVDKHKVSILYTAPTAIRALMAEGDKAieGTDR 377
Cdd:PRK06178 251 DSVFlsflpefWIAGENFGLLFPLFSGATLVL---LARWDAVAFM-AAVERYRVTRTVMLVDNAVELMDHPRFA--EYDL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 378 SSLRILGSVG--EPINPEawewYWKKignekcpvmdtwWQTETGGFMITPLPGAIELK-AGSATRPF------FGVQPVL 448
Cdd:PRK06178 325 SSLRQVRVVSfvKKLNPD----YRQR------------WRALTGSVLAEAAWGMTETHtCDTFTAGFqdddfdLLSQPVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 449 VdneGLPLDGA----------------TEGNLAIadswpgqaRT---LFGDHERFEQTYFSTFKNMYFSGDGARRDEDGY 509
Cdd:PRK06178 389 V---GLPVPGTefkicdfetgellplgAEGEIVV--------RTpslLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 510 YWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPelyAEVRNWVRKEIGP 589
Cdd:PRK06178 458 LHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTA---AALQAWCRENMAV 534
|
570 580 590
....*....|....*....|....*....|....
gi 839746169 590 LATPDVlHWTDSLPKTRSGKIMRRILRKIAAGDT 623
Cdd:PRK06178 535 YKVPEI-RIVDALPMTATGKVRKQDLQALAEELK 567
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
91-618 |
2.20e-33 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 133.93 E-value: 2.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 91 DQTAIIWEGddasqsKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEA 170
Cdd:PRK03640 17 DRTAIEFEE------KKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 171 VAGRIIDSSSRLVITADEGLRagraiplkknvddalknpnvnsiEHVVVLKRTggkidwqegrdlwWSDLMANASAEHRP 250
Cdd:PRK03640 91 LLWQLDDAEVKCLITDDDFEA-----------------------KLIPGISVK-------------FAELMNGPKEEAEI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 251 VEMNAEDPLF-ILYTSGSTGKPKGVLHTTGGYLvYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLL----YG-PLacg 324
Cdd:PRK03640 135 QEEFDLDEVAtIMYTSGTTGKPKGVIQTYGNHW-WSAVGSALNLGLTEDDCWLAAVPIFHISGLSILMrsviYGmRV--- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 325 atTLM--FEgvpnwptPARMCQVVDKHKVSILYTAPTAIRALMAEGDkaiEGTDRSSLR--ILGsvGEPINPEAWEwywk 400
Cdd:PRK03640 211 --VLVekFD-------AEKINKLLQTGGVTIISVVSTMLQRLLERLG---EGTYPSSFRcmLLG--GGPAPKPLLE---- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 401 kIGNEK-CPVMDTWWQTETGGFMITPLPGAIELKAGSATRPFFGVQPVLVDNeGLPLDGATEGNLAIadswpgQARTLFG 479
Cdd:PRK03640 273 -QCKEKgIPVYQSYGMTETASQIVTLSPEDALTKLGSAGKPLFPCELKIEKD-GVVVPPFEEGEIVV------KGPNVTK 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 480 DHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQA 558
Cdd:PRK03640 345 GYLNREDATRETFQDGWFkTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQV 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 559 IYAYVTLnhgEEPTPElyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKI 618
Cdd:PRK03640 425 PVAFVVK---SGEVTE--EELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
79-619 |
8.69e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 132.94 E-value: 8.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 79 ANCLDRHLAERGDQTAIIWEGddasqsKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAI 158
Cdd:PRK06164 13 ASLLDAHARARPDAVALIDED------RPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 159 HSVIFGGFSPEAVAGRIIDSSSRLVITADeglrAGRAIPLKKNVDDALKNpNVNSIEHVVVLKRTGGKI-DWQEGRDLWW 237
Cdd:PRK06164 87 VIAVNTRYRSHEVAHILGRGRARWLVVWP----GFKGIDFAAILAAVPPD-ALPPLRAIAVVDDAADATpAPAPGARVQL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 238 SDLMANASAEHRPVEMNAEDPLFILY-TSGSTGKPKGVLHTTGGYLVYAATTFKyVFDYHPGDIYWCTADVGWVTGHSYL 316
Cdd:PRK06164 162 FALPDPAPPAAAGERAADPDAGALLFtTSGTTSGPKLVLHRQATLLRHARAIAR-AYGYDPGAVLLAALPFCGVFGFSTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 317 LyGPLACGATTLM---FEGvpnwptpARMCQVVDKHKVSILYTAPTAIRALMAEGDkaiEGTDRSSLRILGSVG-EPINP 392
Cdd:PRK06164 241 L-GALAGGAPLVCepvFDA-------ARTARALRRHRVTHTFGNDEMLRRILDTAG---ERADFPSARLFGFASfAPALG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 393 EAWEWywkkignekcpvmdtwwqTETGGFMITPLPGAIELKA------------------GSATRPFFGVQPVLVDNEGL 454
Cdd:PRK06164 310 ELAAL------------------ARARGVPLTGLYGSSEVQAlvalqpatdpvsvrieggGRPASPEARVRARDPQDGAL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 455 PLDGATeGNLAIadSWPGQARTLFGDHERFEQTYFStfkNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIE 533
Cdd:PRK06164 372 LPDGES-GEIEI--RAPSLMRGYLDNPDATARALTD---DGYFrTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIE 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 534 SALVSHPKIAEAAVVGIPHniKGQAI-YAYVTLNHGEEPTPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSG---K 609
Cdd:PRK06164 446 HALEALPGVAAAQVVGATR--DGKTVpVAFVIPTDGASPDE---AGLMAACREALAGFKVPARVQVVEAFPVTESAngaK 520
|
570
....*....|
gi 839746169 610 IMRRILRKIA 619
Cdd:PRK06164 521 IQKHRLREMA 530
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
108-621 |
1.36e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 135.47 E-value: 1.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 108 ITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVITAD 187
Cdd:PRK12316 4577 LTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQS 4656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 188 eglRAGRAIPLKKNVddalknpnvnsieHVVVLKRTGgkiDWqEGRdlwwsdlmanasAEHRP-VEMNAEDPLFILYTSG 266
Cdd:PRK12316 4657 ---HLLQRLPIPDGL-------------ASLALDRDE---DW-EGF------------PAHDPaVRLHPDNLAYVIYTSG 4704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 267 STGKPKGVLHTTGGYLVYAATTfkyvfdyhpGDIYWCTADVGWVTGHSYL-------LYGPLACGATTLMFEgvPNWPTP 339
Cdd:PRK12316 4705 STGRPKGVAVSHGSLVNHLHAT---------GERYELTPDDRVLQFMSFSfdgshegLYHPLINGASVVIRD--DSLWDP 4773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 340 ARMCQVVDKHKVSILYTAPTAIRALmAEGDKaiEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEKcpVMDTWWQTETg 419
Cdd:PRK12316 4774 ERLYAEIHEHRVTVLVFPPVYLQQL-AEHAE--RDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVY--LFNGYGPTET- 4847
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 420 gfMITPL---------PGAIELKAGsatRPFFGVQPVLVDNEGLPLDGATEGNLAIADSwpGQARTLFG----DHERFEQ 486
Cdd:PRK12316 4848 --TVTVLlwkardgdaCGAAYMPIG---TPLGNRSGYVLDGQLNPLPVGVAGELYLGGE--GVARGYLErpalTAERFVP 4920
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 487 TYFSTF-KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIkGQAIYAYVTL 565
Cdd:PRK12316 4921 DPFGAPgGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAV-GKQLVGYVVP 4999
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 839746169 566 NHGE-EPTPELYAEVRNWVRKEIGPlATPDVL---HWT--DSLPKTRSGKIMRRILRKIAAG 621
Cdd:PRK12316 5000 QDPAlADADEAQAELRDELKAALRE-RLPEYMvpaHLVflARMPLTPNGKLDRKALPQPDAS 5060
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
75-621 |
1.41e-32 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 132.41 E-value: 1.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 75 LNLAANCLDRhLAERGDQTAIIwegdDASQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACAR 154
Cdd:PLN02246 23 LPLHDYCFER-LSEFSDRPCLI----DGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 155 IGAIHSVIFGGFSPEAVAGRIIDSSSRLVITadeglragraipLKKNVDdalKNPNVNSIEHVVVLkrtggKIDWQEGRD 234
Cdd:PLN02246 98 RGAVTTTANPFYTPAEIAKQAKASGAKLIIT------------QSCYVD---KLKGLAEDDGVTVV-----TIDDPPEGC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 235 LWWSDLMANASAEHRPVEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAttfKYV------FDYHPGDIYWCTADVg 308
Cdd:PLN02246 158 LHFSELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVA---QQVdgenpnLYFHSDDVILCVLPM- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 309 wvtGHSYLLYGPLACG-----ATTLM--FEgvpnwptPARMCQVVDKHKVSILYTAPTAIRALmAEGDkAIEGTDRSSLR 381
Cdd:PLN02246 234 ---FHIYSLNSVLLCGlrvgaAILIMpkFE-------IGALLELIQRHKVTIAPFVPPIVLAI-AKSP-VVEKYDLSSIR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 382 ILGSVGEPINPEAWEWYWKKIGNEKcpVMDTWWQTETG-------GFMITPLPgaieLKAGSATRPFFGVQPVLVDNE-G 453
Cdd:PLN02246 302 MVLSGAAPLGKELEDAFRAKLPNAV--LGQGYGMTEAGpvlamclAFAKEPFP----VKSGSCGTVVRNAELKIVDPEtG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 454 LPLDGATEGNLAIAdswpGQ-------------ARTLfgDHERFEQTyfstfknmyfsGDGARRDEDGYYWITGRVDDVL 520
Cdd:PLN02246 376 ASLPRNQPGEICIR----GPqimkgylndpeatANTI--DKDGWLHT-----------GDIGYIDDDDELFIVDRLKELI 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 521 NVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTD 600
Cdd:PLN02246 439 KYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITED---EIKQFVAKQVVFYKRIHKVFFVD 515
|
570 580
....*....|....*....|..
gi 839746169 601 SLPKTRSGKIMRRILR-KIAAG 621
Cdd:PLN02246 516 SIPKAPSGKILRKDLRaKLAAG 537
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
102-617 |
1.27e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 132.21 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 102 ASQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSR 181
Cdd:PRK12467 532 VFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVR 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 182 LVITADEGLRagraiplKKNVDDALKnpnvnsiehVVVLKRTGgkiDWQEGRdlwwsdlmanaSAEHRPVEMNAEDPLFI 261
Cdd:PRK12467 612 LLLTQSHLLA-------QLPVPAGLR---------SLCLDEPA---DLLCGY-----------SGHNPEVALDPDNLAYV 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 262 LYTSGSTGKPKGVLHTTGGYLVYAATTFKYvfdyhpgdiYWCTADVGWVTGHSY-------LLYGPLACGATTLMFEGVP 334
Cdd:PRK12467 662 IYTSGSTGQPKGVAISHGALANYVCVIAER---------LQLAADDSMLMVSTFafdlgvtELFGALASGATLHLLPPDC 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 335 NWpTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIegtDRSSLRILgsVGEPINPEAWEWYWKKIGNEkCPVMDTWW 414
Cdd:PRK12467 733 AR-DAEAFAALMADQGVTVLKIVPSHLQALLQASRVAL---PRPQRALV--CGGEALQVDLLARVRALGPG-ARLINHYG 805
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 415 QTETG-GFMITPLPGAIELKAGSAT-RPFFGVQPVLVDNEGLPLDGATEGNLAIADSwpGQARTLFG----DHERFEQTY 488
Cdd:PRK12467 806 PTETTvGVSTYELSDEERDFGNVPIgQPLANLGLYILDHYLNPVPVGVVGELYIGGA--GLARGYHRrpalTAERFVPDP 883
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 489 FSTF-KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPhNIKGQAIYAYVTLNH 567
Cdd:PRK12467 884 FGADgGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQP-GDAGLQLVAYLVPAA 962
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 839746169 568 GEEPT--PELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK12467 963 VADGAehQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPK 1014
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
108-622 |
2.08e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 131.62 E-value: 2.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 108 ITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVITAD 187
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQS 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 188 eglRAGRAIPLKKNVDdalknpnvnsiehVVVLKRTGgkidwqegrdLWwsdlMANASAEHRPVEMNAEDPLFILYTSGS 267
Cdd:PRK12316 617 ---HLGRKLPLAAGVQ-------------VLDLDRPA----------AW----LEGYSEENPGTELNPENLAYVIYTSGS 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 268 TGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHsYLLYGPLACGATtLMFEGVPNWPTPARMCQVVD 347
Cdd:PRK12316 667 TGKPKGAGNRHRA-LSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSV-WEFFWPLMSGAR-LVVAAPGDHRDPAKLVELIN 743
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 348 KHKVSILYTAPTAIRALMAEGDKAiegtDRSSLRILGSVGEPINPEAWEWYWKKIGNekCPVMDTWWQTETggfmitplp 427
Cdd:PRK12316 744 REGVDTLHFVPSMLQAFLQDEDVA----SCTSLRRIVCSGEALPADAQEQVFAKLPQ--AGLYNLYGPTEA--------- 808
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 428 gAIEL------KAGSAT----RPFFGVQPVLVDNEGLPLDGATEGNLAIADSwpGQARTLFG----DHERFEQTYFSTFK 493
Cdd:PRK12316 809 -AIDVthwtcvEEGGDSvpigRPIANLACYILDANLEPVPVGVLGELYLAGR--GLARGYHGrpglTAERFVPSPFVAGE 885
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 494 NMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGiphnIKGQAIYAYVTLnhgEEPTP 573
Cdd:PRK12316 886 RMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVL---ESEGG 958
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 839746169 574 ELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGD 622
Cdd:PRK12316 959 DWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASV 1007
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
91-615 |
5.26e-31 |
|
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: 127.00 E-value: 5.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 91 DQTAIIwegdDASQskHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHsVIFGGFSPEA 170
Cdd:cd12114 2 DATAVI----CGDG--TLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAY-VPVDIDQPAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 171 VAGRII-DSSSRLVITADEglragraiplkknvdDALKNPNVNsiehvvvlkrtggkidwqegRDLWWSDLMANASAEHR 249
Cdd:cd12114 75 RREAILaDAGARLVLTDGP---------------DAQLDVAVF--------------------DVLILDLDALAAPAPPP 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 250 PVEMNAEDPLFILYTSGSTGKPKGVLHTTGGYL-VYAATTFKYVFDyhPGDIYWCTADVGW---VtghsYLLYGPLACGA 325
Cdd:cd12114 120 PVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALnTILDINRRFAVG--PDDRVLALSSLSFdlsV----YDIFGALSAGA 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 326 TtLMFEGVPNWPTPARMCQVVDKHKVSILYTAPTAIRALMAEGdkAIEGTDRSSLR-ILGSvGEPINPEawewywkkign 404
Cdd:cd12114 194 T-LVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVL--EAAQALLPSLRlVLLS-GDWIPLD----------- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 405 ekcpVMDTWWQTetggfmitpLPGAIELKAGSAT------------------------RPFFGVQPVLVDNEGLPLDGAT 460
Cdd:cd12114 259 ----LPARLRAL---------APDARLISLGGATeasiwsiyhpidevppdwrsipygRPLANQRYRVLDPRGRDCPDWV 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 461 EGNLAIADswPGQARTLFGDHERFEQTYFS--TFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVS 538
Cdd:cd12114 326 PGELWIGG--RGVALGYLGDPELTAARFVThpDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQA 403
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 839746169 539 HPKIAEAAVVGIPhNIKGQAIYAYVTLnhGEEPTPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd12114 404 HPGVARAVVVVLG-DPGGKRLAAFVVP--DNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
82-615 |
5.78e-31 |
|
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: 126.67 E-value: 5.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 82 LDRHLAERGDQTAIIweGDDasqsKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIhsv 161
Cdd:cd05920 21 LARSAARHPDRIAVV--DGD----RRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 162 ifggfspeavagriidsssrlVITADEGLRAgRAIplkknvdDALknpnvnsIEHV----VVLKRTGGKIDWQEgrdlww 237
Cdd:cd05920 92 ---------------------PVLALPSHRR-SEL-------SAF-------CAHAeavaYIVPDRHAGFDHRA------ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 238 sdlMANASAEHRPvemnaeDPLFILYTSGSTGKPKGVLHTTGGYlVYAATTFKYVFDYHPGDIYWCTADVGwvtgHSYLL 317
Cdd:cd05920 130 ---LARELAESIP------EVALFLLSGGTTGTPKLIPRTHNDY-AYNVRASAEVCGLDQDTVYLAVLPAA----HNFPL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 318 YGP-----LACGATTLMfegVPNwPTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKaiEGTDRSSLRILGSVGEPINP 392
Cdd:cd05920 196 ACPgvlgtLLAGGRVVL---APD-PSPDAAFPLIEREGVTVTALVPALVSLWLDAAAS--RRADLSSLRLLQVGGARLSP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 393 EAWEWYWKKIGnekCPVMDTWWQTEtGGFMITPLPGAIELKAGSATRPFFGVQPVL-VDNEGLPLDGATEGNLAIADswP 471
Cdd:cd05920 270 ALARRVPPVLG---CTLQQVFGMAE-GLLNYTRLDDPDEVIIHTQGRPMSPDDEIRvVDEEGNPVPPGEEGELLTRG--P 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 472 GQARTLFGDHERFEQTYfsTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIP 551
Cdd:cd05920 344 YTIRGYYRAPEHNARAF--TPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMP 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 839746169 552 HNIKGQAIYAYVTLNhgeePTPELYAEVRNWVRkEIGpLAT---PDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05920 422 DELLGERSCAFVVLR----DPPPSAAQLRRFLR-ERG-LAAyklPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
108-549 |
6.56e-31 |
|
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: 126.17 E-value: 6.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 108 ITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVITAD 187
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 188 eglragraiplkknvddalknpnvnsiehvvvlkrtggkidwqegrdlwwsdlmanasaehrpvemnAEDPLFILYTSGS 267
Cdd:cd05907 86 -------------------------------------------------------------------PDDLATIIYTSGT 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 268 TGKPKGVLHTTGGYLVYAATTFKYVFDYhPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNWPT------PAR 341
Cdd:cd05907 99 TGRPKGVMLSHRNILSNALALAERLPAT-EGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLLDdlsevrPTV 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 342 MCQV---VDKHKVSILYTAPTAIRALMAegDKAIEGtdrsSLRILGSVGEPINPEAWEWYwKKIGnekCPVMDTWWQTET 418
Cdd:cd05907 178 FLAVprvWEKVYAAIKVKAVPGLKRKLF--DLAVGG----RLRFAASGGAPLPAELLHFF-RALG---IPVYEGYGLTET 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 419 GGfmitplpgaielkAGSATRPffgvQPVLVDNEGLPLDGATegnLAIADSWPGQAR--TLF-GDHERFEQTYFSTFKNM 495
Cdd:cd05907 248 SA-------------VVTLNPP----GDNRIGTVGKPLPGVE---VRIADDGEILVRgpNVMlGYYKNPEATAEALDADG 307
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 839746169 496 YF-SGDGARRDEDGYYWITGRVDDVL-NVSGHRLGTAEIESALVSHPKIAEAAVVG 549
Cdd:cd05907 308 WLhTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
531-609 |
7.63e-31 |
|
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: 115.33 E-value: 7.63e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 839746169 531 EIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGK 609
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEE---ELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
87-617 |
9.03e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 129.69 E-value: 9.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 87 AERGDQTAIIWEGddasqsKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGF 166
Cdd:PRK12316 2014 ARAPEAIAVVFGD------QHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNY 2087
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 167 SPEAVAGRIIDSSSRLVITaDEGLRAGRAIPlkknvddalknpnvnsiEHVVVLKRTggkidwqegRDLWWSDlmanaSA 246
Cdd:PRK12316 2088 PAERLAYMLEDSGAALLLT-QRHLLERLPLP-----------------AGVARLPLD---------RDAEWAD-----YP 2135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 247 EHRP-VEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYvFDYHPGDIYWCTADVGWVTGHSYLLYgPLACGA 325
Cdd:PRK12316 2136 DTAPaVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGER-YELSPADCELQFMSFSFDGAHEQWFH-PLLNGA 2213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 326 TTLMFEGvPNWpTPARMCQVVDKHKVSILYTAPTAIRALMAEgdKAIEGtDRSSLRILGSVGEPINPEAWEWYWKKIGNE 405
Cdd:PRK12316 2214 RVLIRDD-ELW-DPEQLYDEMERHGVTILDFPPVYLQQLAEH--AERDG-RPPAVRVYCFGGEAVPAASLRLAWEALRPV 2288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 406 KcpVMDTWWQTETggfMITPL---------PGAIELKAGSAtrpfFGVQPVLVDNEGL-PLDGATEGNLAIADSwpGQAR 475
Cdd:PRK12316 2289 Y--LFNGYGPTEA---VVTPLlwkcrpqdpCGAAYVPIGRA----LGNRRAYILDADLnLLAPGMAGELYLGGE--GLAR 2357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 476 TLFG----DHERFEQTYFS-TFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGI 550
Cdd:PRK12316 2358 GYLNrpglTAERFVPDPFSaSGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ 2437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 839746169 551 pHNIKGQAIYAYVTlnhGEEPTPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK12316 2438 -DGASGKQLVAYVV---PDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
82-620 |
1.53e-30 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 126.46 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 82 LDRHLAERGDQTAIIwegdDASQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSV 161
Cdd:PRK08315 22 LDRTAARYPDREALV----YRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 162 IFGGFSPEAVAGRIIDSSSRLVITAD--------EGLRAgrAIP-LKKNVDDALKNPNVNSIEHVVVL--KRTGGKIDWq 230
Cdd:PRK08315 98 INPAYRLSELEYALNQSGCKALIAADgfkdsdyvAMLYE--LAPeLATCEPGQLQSARLPELRRVIFLgdEKHPGMLNF- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 231 egrdlwwSDLMANASAEHRPV------EMNAEDPLFILYTSGSTGKPKGVLHT-----TGGYLVYAATTFKyvfdyhPGD 299
Cdd:PRK08315 175 -------DELLALGRAVDDAElaarqaTLDPDDPINIQYTSGTTGFPKGATLThrnilNNGYFIGEAMKLT------EED 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 300 -------IYWCtadVGWVTGHsyllygpLAC---GATT-LMFEGVpnwpTPARMCQVVDKHKVSILYTAPTairalM--A 366
Cdd:PRK08315 242 rlcipvpLYHC---FGMVLGN-------LACvthGATMvYPGEGF----DPLATLAAVEEERCTALYGVPT-----MfiA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 367 E-GDKAIEGTDRSSLR--IL-GSVgepinpeawewywkkignekCP------VMD---------TWWQTETG-GFMITPL 426
Cdd:PRK08315 303 ElDHPDFARFDLSSLRtgIMaGSP--------------------CPievmkrVIDkmhmsevtiAYGMTETSpVSTQTRT 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 427 PGAIELKAGSATRPFFGVQPVLVDNE-GLPLDGATEGNL--------------------AI-ADSWpgqartlfgdherf 484
Cdd:PRK08315 363 DDPLEKRVTTVGRALPHLEVKIVDPEtGETVPRGEQGELctrgysvmkgywndpektaeAIdADGW-------------- 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 485 eqtyfstfknMYfSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVT 564
Cdd:PRK08315 429 ----------MH-TGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWII 497
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 839746169 565 LNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAA 620
Cdd:PRK08315 498 LRPGATLTEE---DVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMI 550
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
108-615 |
1.89e-30 |
|
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: 124.89 E-value: 1.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 108 ITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVITad 187
Cdd:cd17650 13 LTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLT-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 188 eglragraiplkknvddalknpnvnsiehvvvlkrtggkidwqegrdlwwsdlmanasaehrpvemNAEDPLFILYTSGS 267
Cdd:cd17650 91 ------------------------------------------------------------------QPEDLAYVIYTSGT 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 268 TGKPKGVLHTTGGYL-VYAATTFKYVFDYHPGDIYWctadvgwVTGHSY-LLYGPLAcgaTTLMFEG----VPN--WPTP 339
Cdd:cd17650 105 TGKPKGVMVEHRNVAhAAHAWRREYELDSFPVRLLQ-------MASFSFdVFAGDFA---RSLLNGGtlviCPDevKLDP 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 340 ARMCQVVDKHKVSILYTAPTAIRALMAEGDKaiEGTDRSSLRIL--GSVGEPINPEAWEWywKKIGnEKCPVMDTWWQTE 417
Cdd:cd17650 175 AALYDLILKSRITLMESTPALIRPVMAYVYR--NGLDLSAMRLLivGSDGCKAQDFKTLA--ARFG-QGMRIINSYGVTE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 418 T---GGFMITPLPGAIELKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIADSwpGQARTLFGD----HERFEQTYFS 490
Cdd:cd17650 250 AtidSTYYEEGRDPLGDSANVPIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGA--GVARGYLNRpeltAERFVENPFA 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 491 TFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVgIPHNIKGQA-IYAYVTLNHge 569
Cdd:cd17650 328 PGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVA-VREDKGGEArLCAYVVAAA-- 404
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 839746169 570 epTPELyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17650 405 --TLNT-AELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
102-616 |
2.34e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 125.12 E-value: 2.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 102 ASQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPeAVAGRII-DSSS 180
Cdd:PRK13390 19 AETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA-PEADYIVgDSGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 181 RLVIT--ADEGL--RAGRAIPLKKNVddalknpnvnsiehvvvlkrtGGKIDWqegrdlwWSDLMANASAEHRPVemnAE 256
Cdd:PRK13390 98 RVLVAsaALDGLaaKVGADLPLRLSF---------------------GGEIDG-------FGSFEAALAGAGPRL---TE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 257 DPL--FILYTSGSTGKPKGV--------LHTTGGYLVYAATTFkyvFDYHPGDIYWCTADVGwvtgHSyllyGPL----- 321
Cdd:PRK13390 147 QPCgaVMLYSSGTTGFPKGIqpdlpgrdVDAPGDPIVAIARAF---YDISESDIYYSSAPIY----HA----APLrwcsm 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 322 --ACGATTLM---FEGvpnwptpARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEP------- 389
Cdd:PRK13390 216 vhALGGTVVLakrFDA-------QATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVIHAAAPcpvdvkh 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 390 -----INPEAWEWYWkkignekcpvmdtwwQTETGGFMITPLPGAIElKAGSATRPFFGVQPVlVDNEGLPLDGATEGNL 464
Cdd:PRK13390 289 amidwLGPIVYEYYS---------------STEAHGMTFIDSPDWLA-HPGSVGRSVLGDLHI-CDDDGNELPAGRIGTV 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 465 AIA-DSWPgqartlFGDHERFEQTYFSTFKNMYF---SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHP 540
Cdd:PRK13390 352 YFErDRLP------FRYLNDPEKTAAAQHPAHPFwttVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHP 425
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 839746169 541 KIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK13390 426 AVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
108-617 |
4.93e-30 |
|
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: 122.84 E-value: 4.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 108 ITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIhsvifggfspeavagriidsssrlvitad 187
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAE----------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 188 eglragrAIPLKKnvddalknpnvnsiehvvvlKRTGGKIDWQegrdlwwsdlMANAsaehrpvEMNAEDPLFILYTSGS 267
Cdd:cd05912 53 -------AVLLNT--------------------RLTPNELAFQ----------LKDS-------DVKLDDIATIMYTSGT 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 268 TGKPKGVLHTTGGYLvYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLM--FEgvpnwptPARMCQV 345
Cdd:cd05912 89 TGKPKGVQQTFGNHW-WSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRSVIYGMTVYLVdkFD-------AEQVLHL 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 346 VDKHKVSILYTAPTAIRALMAEGDkaieGTDRSSLR--ILGsvGEPINPEAWEwywkkigneKC-----PVMDTWWQTET 418
Cdd:cd05912 161 INSGKVTIISVVPTMLQRLLEILG----EGYPNNLRciLLG--GGPAPKPLLE---------QCkekgiPVYQSYGMTET 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 419 GGFMITPLPGAIELKAGSATRPFFGVQPVLVDNEGLPldgATEGNL-----AIADSWPGQARTlfgDHERFEQTYFSTfk 493
Cdd:cd05912 226 CSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPP---YEVGEIllkgpNVTKGYLNRPDA---TEESFENGWFKT-- 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 494 nmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTlnhGEEPTP 573
Cdd:cd05912 298 -----GDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVV---SERPIS 369
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 839746169 574 ElyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05912 370 E--EELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
107-615 |
6.54e-30 |
|
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: 122.75 E-value: 6.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 107 HITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVITa 186
Cdd:cd17652 12 TLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLT- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 187 deglragraiplkknvddalknpnvnsiehvvvlkrtggkidwqegrdlwwsdlmanasaehrpvemNAEDPLFILYTSG 266
Cdd:cd17652 91 -------------------------------------------------------------------TPDNLAYVIYTSG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 267 STGKPKGVL--HTTGGYLVYAATTFkyvFDYHPGDIYWCTADVGWVTGHSYLLyGPLACGATTLMFEGVPNWPTPArMCQ 344
Cdd:cd17652 104 STGRPKGVVvtHRGLANLAAAQIAA---FDVGPGSRVLQFASPSFDASVWELL-MALLAGATLVLAPAEELLPGEP-LAD 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 345 VVDKHKVSILYTAPTAIRALMAEGDKAiegtdrssLRILGSVGEPINPEawewywkkignekcpVMDTWWQ--------- 415
Cdd:cd17652 179 LLREHRITHVTLPPAALAALPPDDLPD--------LRTLVVAGEACPAE---------------LVDRWAPgrrminayg 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 416 -TET--GGFMITPLPGAIELKAGsatRPFFGVQPVLVDNEGLPLDGATEGNLAIADswPGQARtlfGDH-------ERFE 485
Cdd:cd17652 236 pTETtvCATMAGPLPGGGVPPIG---RPVPGTRVYVLDARLRPVPPGVPGELYIAG--AGLAR---GYLnrpgltaERFV 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 486 QTYFSTF-KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVT 564
Cdd:cd17652 308 ADPFGAPgSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVV 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 839746169 565 LNHGEEPTPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17652 388 PAPGAAPTA---AELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
91-616 |
9.97e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 123.46 E-value: 9.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 91 DQTAIIWEGDDasqskhITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEA 170
Cdd:PRK06145 17 DRAALVYRDQE------ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 171 VAGRIIDSSSRLVITaDEGLRAGRAIPLKKNVDDALKNPNVNsiehvvvlkrtggkidwqegrdlwwsdLMANASAEHRP 250
Cdd:PRK06145 91 VAYILGDAGAKLLLV-DEEFDAIVALETPKIVIDAAAQADSR---------------------------RLAQGGLEIPP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 251 VEMNAEDPLF-ILYTSGSTGKPKGVLHTTGgylvyaattfkyvfdyhpgDIYWCTAD----VGWVTGHSYLLYGPL---- 321
Cdd:PRK06145 143 QAAVAPTDLVrLMYTSGTTDRPKGVMHSYG-------------------NLHWKSIDhviaLGLTASERLLVVGPLyhvg 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 322 AC---GATTLMFEG---VPNWPTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKaiEGTDRSSLRilgsvgepinpeaw 395
Cdd:PRK06145 204 AFdlpGIAVLWVGGtlrIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDR--DRFDLDSLA-------------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 396 ewyWKKIGNEKCP---------------VMDTWWQTET-GGFMITPLPGAIElKAGSATRPFFGVQPVLVDNEGLPLDGA 459
Cdd:PRK06145 268 ---WCIGGGEKTPesrirdftrvftrarYIDAYGLTETcSGDTLMEAGREIE-KIGSTGRALAHVEIRIADGAGRWLPPN 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 460 TEGNLAIADswPGQARTLFGDHERFEQTYFSTFknmYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSH 539
Cdd:PRK06145 344 MKGEICMRG--PKVTKGYWKDPEKTAEAFYGDW---FRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYEL 418
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 839746169 540 PKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK06145 419 PEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLE---ALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
91-616 |
1.66e-29 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 123.33 E-value: 1.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 91 DQTAIIwegDDASQskhITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAiHSVIFG-GFSPE 169
Cdd:PRK13382 58 DRPGLI---DELGT---LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGA-DILLLNtSFAGP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 170 AVAGRIIDSSSRLVITADEglragrAIPLkknVDDALKN-PNVNSIEhvvvlkrtggkiDWQEGRDLWWSDLMANASAEH 248
Cdd:PRK13382 131 ALAEVVTREGVDTVIYDEE------FSAT---VDRALADcPQATRIV------------AWTDEDHDLTVEVLIAAHAGQ 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 249 RPVEMNAEDPLfILYTSGSTGKPKGVLHT-TGGYLvyaatTFKYVFDYHPgdiywctadvgWVTGHSYLLYGPL--ACGA 325
Cdd:PRK13382 190 RPEPTGRKGRV-ILLTSGTTGTPKGARRSgPGGIG-----TLKAILDRTP-----------WRAEEPTVIVAPMfhAWGF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 326 TTLMFEGVPNWP-------TPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWY 398
Cdd:PRK13382 253 SQLVLAASLACTivtrrrfDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 399 WKKIGNekcPVMDTWWQTETGgfMI-TPLPGAIELKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIADSwpgqarTL 477
Cdd:PRK13382 333 MDQFGD---VIYNNYNATEAG--MIaTATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRND------TQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 478 F-----GDHERFEQTYFStfknmyfSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPH 552
Cdd:PRK13382 402 FdgytsGSTKDFHDGFMA-------SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDD 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 839746169 553 NIKGQAIYAYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK13382 475 EQYGQRLAAFVVLKPGASATPE---TLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
103-616 |
2.40e-29 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 122.50 E-value: 2.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 103 SQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSR- 181
Cdd:PRK12406 7 SGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 182 LVITAD--EGLRAgrAIPLKKNVDDALKNPNVNSIEHVVVLKRT--GGKIDWQEgrdlwWsdLMANASAEHRPVEmnaeD 257
Cdd:PRK12406 87 LIAHADllHGLAS--ALPAGVTVLSVPTPPEIAAAYRISPALLTppAGAIDWEG-----W--LAQQEPYDGPPVP----Q 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 258 PLFILYTSGSTGKPKGVLHT--TGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLM--FEgv 333
Cdd:PRK12406 154 PQSMIYTSGTTGHPKGVRRAapTPEQAAAAEQMRALIYGLKPGIRALLTGPLYHSAPNAYGLRAGRLGGVLVLQprFD-- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 334 pnwptPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPinpeawewywkkignekCPV---- 409
Cdd:PRK12406 232 -----PEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAP-----------------CPAdvkr 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 410 -MDTWW---------QTETGGFMITPLPGAIElKAGSATRPFFGVQPVLVDNEGLPLDGATEGNlaIADSWPGQArtLFG 479
Cdd:PRK12406 290 aMIEWWgpviyeyygSTESGAVTFATSEDALS-HPGTVGKAAPGAELRFVDEDGRPLPQGEIGE--IYSRIAGNP--DFT 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 480 DHERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAI 559
Cdd:PRK12406 365 YHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEAL 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 839746169 560 YAYVTLNHGEEPTPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK12406 445 MAVVEPQPGATLDE---ADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
82-617 |
3.90e-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: 121.25 E-value: 3.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 82 LDRHLAERGDQTAIIWEgddasqSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSV 161
Cdd:cd12118 10 LERAAAVYPDRTSIVYG------DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 162 IFGGFSPEAVAGRIIDSSSRLVItADEglragraiplkknvddalknpnvnSIEHVVVLKRTGGKIDWQEGRDLWwsdlm 241
Cdd:cd12118 84 LNTRLDAEEIAFILRHSEAKVLF-VDR------------------------EFEYEDLLAEGDPDFEWIPPADEW----- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 242 anasaehrpvemnaeDPLFILYTSGSTGKPKGVLHT-TGGYLvyAATTFKYVFDYHPGDIYWCTADV----GWVtghsyL 316
Cdd:cd12118 134 ---------------DPIALNYTSGTTGRPKGVVYHhRGAYL--NALANILEWEMKQHPVYLWTLPMfhcnGWC-----F 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 317 LYGPLACGATTLMFEGVpnwpTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGTDRsslRILGSVGEPINPEAwe 396
Cdd:cd12118 192 PWTVAAVGGTNVCLRKV----DAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPH---RVHVMTAGAPPPAA-- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 397 wYWKKIGNEKCPVMDTWWQTETGGfmitplPGAI------------ELKAGSATR---PFFGVQPVLV-DNEGL---PLD 457
Cdd:cd12118 263 -VLAKMEELGFDVTHVYGLTETYG------PATVcawkpewdelptEERARLKARqgvRYVGLEEVDVlDPETMkpvPRD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 458 GATEGNLAIadswpgQARTLFGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESAL 536
Cdd:cd12118 336 GKTIGEIVF------RGNIVMKGYLKNPEATAEAFRGGWFhSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVL 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 537 VSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDsLPKTRSGKIMRRILR 616
Cdd:cd12118 410 YKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEE---EIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVLR 485
|
.
gi 839746169 617 K 617
Cdd:cd12118 486 D 486
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
89-618 |
4.93e-29 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 121.12 E-value: 4.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 89 RGDQTAIIwegddaSQSKHITYRELHADVCRFANVLL-DLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFS 167
Cdd:PRK06839 15 HPDRIAII------TEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 168 PEAVAGRIIDSSSRLVITADEglRAGRAIPLKKnvddalknpnVNSIEHVVvlkrtggkidwqegrdlWWSDLmaNASAE 247
Cdd:PRK06839 89 ENELIFQLKDSGTTVLFVEKT--FQNMALSMQK----------VSYVQRVI-----------------SITSL--KEIED 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 248 HRP---VEMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACG 324
Cdd:PRK06839 138 RKIdnfVEKNESASFIICYTSGTTGKPKGAVLTQEN-MFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 325 ATTLmfegVPNWPTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKaiEGTDRSSLRILGSVGEPInPEAWEWYWKKIGn 404
Cdd:PRK06839 217 GVII----VPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKF--ETTNLQSVRWFYNGGAPC-PEELMREFIDRG- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 405 ekCPVMDTWWQTETGG--FMITPLPGAieLKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIadswpgQARTLFGDHE 482
Cdd:PRK06839 289 --FLFGQGFGMTETSPtvFMLSEEDAR--RKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLI------RGPNVMKEYW 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 483 RFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYA 561
Cdd:PRK06839 359 NRPDATEETIQDGWLcTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIA 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 839746169 562 YVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKI 618
Cdd:PRK06839 439 FIVKKSSSVLIEK---DVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
257-612 |
1.63e-28 |
|
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: 116.60 E-value: 1.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 257 DPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLM--FEgvp 334
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGN-LIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMekFD--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 335 nwptPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEPINPEAWEwywkkignEKCPVmdTWW 414
Cdd:cd17637 77 ----PAEALELIEEEKVTLMGSFPPILSNLLDAAEKS--GVDLSSLRHVLGLDAPETIQRFE--------ETTGA--TFW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 415 ----QTETGGFMITplpGAIELKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIadswpgQARTLFGDHERFEQTYFS 490
Cdd:cd17637 141 slygQTETSGLVTL---SPYRERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVV------RGPLVFQGYWNLPELTAY 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 491 TFKN-MYFSGDGARRDEDGYYWITGRV--DDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNH 567
Cdd:cd17637 212 TFRNgWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKP 291
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 839746169 568 GEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17637 292 GATLTAD---ELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
82-620 |
2.69e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 121.81 E-value: 2.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 82 LDRHLAERGDQTAIIWEGddasqsKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSV 161
Cdd:PRK12467 3101 IEAQVARTPEAPALVFGD------QQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVP 3174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 162 IFGGFSPEAVAGRIIDSSSRLVITADEGLRAgraIPLKKNVddalknpnvnsieHVVVLKRtggkidwqegrDLWWSDLM 241
Cdd:PRK12467 3175 LDPEYPRERLAYMIEDSGVKLLLTQAHLLEQ---LPAPAGD-------------TALTLDR-----------LDLNGYSE 3227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 242 ANASaehrpVEMNAEDPLFILYTSGSTGKPKGVLHTTGG-----------YLVYAATT----FKYVFDyhpgdiywctad 306
Cdd:PRK12467 3228 NNPS-----TRVMGENLAYVIYTSGSTGKPKGVGVRHGAlanhlcwiaeaYELDANDRvllfMSFSFD------------ 3290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 307 vgwvtGHSYLLYGPLACGATtLMFEGVPNWpTPARMCQVVDKHKVSILYTAPTAIRALMAEGDkaieGTDRSSLRILGSV 386
Cdd:PRK12467 3291 -----GAQERFLWTLICGGC-LVVRDNDLW-DPEELWQAIHAHRISIACFPPAYLQQFAEDAG----GADCASLDIYVFG 3359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 387 GEPINPEAWEWYWKKI---------GNEKCPVMDTWWQTETGGfmitpLPGAIELKAGsatRPFFGVQPVLVDNEGLPLD 457
Cdd:PRK12467 3360 GEAVPPAAFEQVKRKLkprgltngyGPTEAVVTVTLWKCGGDA-----VCEAPYAPIG---RPVAGRSIYVLDGQLNPVP 3431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 458 GATEGNLAIADSwpGQARtlfGDH-------ERFEQTYFSTF-KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGT 529
Cdd:PRK12467 3432 VGVAGELYIGGV--GLAR---GYHqrpsltaERFVADPFSGSgGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIEL 3506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 530 AEIESALVSHPKIAEAAVVGIPhNIKGQAIYAYVTLNhgeEPTPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGK 609
Cdd:PRK12467 3507 GEIEARLLQHPSVREAVVLARD-GAGGKQLVAYVVPA---DPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGK 3582
|
570
....*....|.
gi 839746169 610 IMRRILRKIAA 620
Cdd:PRK12467 3583 VDRKALPDPDA 3593
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
109-621 |
3.97e-28 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 119.35 E-value: 3.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 109 TYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVITADE 188
Cdd:PLN03102 41 TWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 189 GLRAGRAIPLKKNVDDALKNPNVNSIEHVVVLKRTGGK-IDW----QEGRDL-WWSDLMANASAEHRPVEMNaedplfil 262
Cdd:PLN03102 121 FEPLAREVLHLLSSEDSNLNLPVIFIHEIDFPKRPSSEeLDYecliQRGEPTpSLVARMFRIQDEHDPISLN-------- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 263 YTSGSTGKPKGVLHT-TGGYLVYAATTFKYVFDYHPgdIYWCTADV----GWVtghsyLLYGPLACGATTLMFEGVpnwp 337
Cdd:PLN03102 193 YTSGTTADPKGVVIShRGAYLSTLSAIIGWEMGTCP--VYLWTLPMfhcnGWT-----FTWGTAARGGTSVCMRHV---- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 338 TPARMCQVVDKHKVSILYTAPTAIRALMaEGDKAIEGTDRSSLRILGSVGEPinPEAwewYWKKIGNEKCPVMDTWWQTE 417
Cdd:PLN03102 262 TAPEIYKNIEMHNVTHMCCVPTVFNILL-KGNSLDLSPRSGPVHVLTGGSPP--PAA---LVKKVQRLGFQVMHAYGLTE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 418 TGGFMI----------TPLPGAIELKAGSATRpFFGVQPVLVDN----EGLPLDGATEGNLAIADSwpgqarTLFGDHER 483
Cdd:PLN03102 336 ATGPVLfcewqdewnrLPENQQMELKARQGVS-ILGLADVDVKNketqESVPRDGKTMGEIVIKGS------SIMKGYLK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 484 FEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAY 562
Cdd:PLN03102 409 NPKATSEAFKHGWLnTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAF 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 839746169 563 VTLNHGEEPTPE----LYAEVRN---WVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAG 621
Cdd:PLN03102 489 VVLEKGETTKEDrvdkLVTRERDlieYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAKG 554
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
257-619 |
5.20e-28 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 115.12 E-value: 5.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 257 DPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYV-FDyhPGDIYWCTADVGWVTGHSYLLYGpLACGATTLMFEgvPN 335
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLgFG--GGDSWLLSLPLYHVGGLAILVRS-LLAGAELVLLE--RN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 336 WPTPARMCQVVDKHkVSIlytAPTAIRALMAEGdkaIEGTDRSSLRILGSVGEPINPEAWEwywkKIGNEKCPVMDTWWQ 415
Cdd:cd17630 76 QALAEDLAPPGVTH-VSL---VPTQLQRLLDSG---QGPAALKSLRAVLLGGAPIPPELLE----RAADRGIPLYTTYGM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 416 TETGGfMITPLPgAIELKAGSATRPFFGVQPVLVDNEGLPLDGATegnlAIADSWPGQARTLFgdherFEQTYFSTfknm 495
Cdd:cd17630 145 TETAS-QVATKR-PDGFGRGGVGVLLPGRELRIVEDGEIWVGGAS----LAMGYLRGQLVPEF-----NEDGWFTT---- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 496 yfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPtpel 575
Cdd:cd17630 210 ---KDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADP---- 282
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 839746169 576 yAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIA 619
Cdd:cd17630 283 -AELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
109-617 |
9.83e-28 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 117.93 E-value: 9.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 109 TYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVITaDE 188
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVIT-DL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 189 GLragraIPLKKNVDDALKnpnvnSIEHVVV-----------LKRTGGKIDWQEGR--DLWWSDLMANASAEhrpvemna 255
Cdd:PRK06018 120 TF-----VPILEKIADKLP-----SVERYVVltdaahmpqttLKNAVAYEEWIAEAdgDFAWKTFDENTAAG-------- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 256 edplfILYTSGSTGKPKGVLHTTGGYLVYAATTFkyvfdyHPGDIYWCTADV-----------GWVTGHSyllyGPlACG 324
Cdd:PRK06018 182 -----MCYTSGTTGDPKGVLYSHRSNVLHALMAN------NGDALGTSAADTmlpvvplfhanSWGIAFS----AP-SMG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 325 ATTLMfegvpnwPTP----ARMCQVVDKHKVSILYTAPTAIRALMAEGDKaiegtDRSSLRILGSV--GEPINPEAWEWY 398
Cdd:PRK06018 246 TKLVM-------PGAkldgASVYELLDTEKVTFTAGVPTVWLMLLQYMEK-----EGLKLPHLKMVvcGGSAMPRSMIKA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 399 WKKIGNEkcpVMDTWWQTETGGF-MITPLPGAIELKAGSAT--------RPFFGVQPVLVDNEG--LPLDGATEGNLAIa 467
Cdd:PRK06018 314 FEDMGVE---VRHAWGMTEMSPLgTLAALKPPFSKLPGDARldvlqkqgYPPFGVEMKITDDAGkeLPWDGKTFGRLKV- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 468 dSWPGQARTLF--GDHERFEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEA 545
Cdd:PRK06018 390 -RGPAVAAAYYrvDGEILDDDGFFDT-------GDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEA 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 839746169 546 AVVGIPHNIKGQAIYAYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK06018 462 AVIGVYHPKWDERPLLIVQLKPGETATRE---EILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
106-622 |
1.56e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 119.68 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 106 KHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVIT 185
Cdd:PRK12316 3081 QRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLS 3160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 186 ADEglragraiplkknvddaLKNPNVNSIEHVVVLKRTggkidwqegrdlwwsdlmANASAEHRPVEMNAEDPLFILYTS 265
Cdd:PRK12316 3161 QSH-----------------LRLPLAQGVQVLDLDRGD------------------ENYAEANPAIRTMPENLAYVIYTS 3205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 266 GSTGKPKGVLHTTGGYLVYAATTfkyvfdyhpGDIYWCTAD--VGWVTGHSY-----LLYGPLACGATTLMfEGVPNWPT 338
Cdd:PRK12316 3206 GSTGKPKGVGIRHSALSNHLCWM---------QQAYGLGVGdrVLQFTTFSFdvfveELFWPLMSGARVVL-AGPEDWRD 3275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 339 PARMCQVVDKHKVSILYTAPTAIRALMAEGDKAiegtDRSSLRILGSVGEPINPEAWEWYwkkigNEKCPVMDTWWQTET 418
Cdd:PRK12316 3276 PALLVELINSEGVDVLHAYPSMLQAFLEEEDAH----RCTSLKRIVCGGEALPADLQQQV-----FAGLPLYNLYGPTEA 3346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 419 ggfMITPLPGAIELKAGSAT---RPFFGVQPVLVDNEGLPLDGATEGNLAIADSwpGQARTLFG----DHERFEQTYFST 491
Cdd:PRK12316 3347 ---TITVTHWQCVEEGKDAVpigRPIANRACYILDGSLEPVPVGALGELYLGGE--GLARGYHNrpglTAERFVPDPFVP 3421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 492 FKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGiphnIKGQAIYAYVTLnhgEEP 571
Cdd:PRK12316 3422 GERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVP---EDE 3494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 839746169 572 TPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGD 622
Cdd:PRK12316 3495 AGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAAL 3545
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
107-628 |
1.58e-27 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 117.17 E-value: 1.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 107 HITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVI---FGGFSPEAVAGRiidSSSRLV 183
Cdd:PRK06155 46 RWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPIntaLRGPQLEHILRN---SGARLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 184 ITADEGLRAGRAIPlkknvddalknPNVNSIEHVVVLkrtGGKIDWQEGRDLWWSDLMAnASAEHRPVEMNAEDPLFILY 263
Cdd:PRK06155 123 VVEAALLAALEAAD-----------PGDLPLPAVWLL---DAPASVSVPAGWSTAPLPP-LDAPAPAAAVQPGDTAAILY 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 264 TSGSTGKPKGVLHTTGGYLVYAATTFKyVFDYHPGDIYWCTADVGWVTGHSyLLYGPLACGATTLM---FEGVPNWPTPA 340
Cdd:PRK06155 188 TSGTTGPSKGVCCPHAQFYWWGRNSAE-DLEIGADDVLYTTLPLFHTNALN-AFFQALLAGATYVLeprFSASGFWPAVR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 341 RM-CQV--VDKHKVSILYTAPTAiralmaEGDKAiegtdrSSLRILGSVGEPinPEAWEWYWKKIGnekCPVMDTWWQTE 417
Cdd:PRK06155 266 RHgATVtyLLGAMVSILLSQPAR------ESDRA------HRVRVALGPGVP--AALHAAFRERFG---VDLLDGYGSTE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 418 TGGFMITPLPgaiELKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIADSWPGQ-ARTLFGDHERFEQTYfstfKNMY 496
Cdd:PRK06155 329 TNFVIAVTHG---SQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADEPFAfATGYFGMPEKTVEAW----RNLW 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 497 F-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPEl 575
Cdd:PRK06155 402 FhTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPV- 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 839746169 576 yaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRkiAAGDTSNLGD 628
Cdd:PRK06155 481 --ALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLR--EQGVTADTWD 529
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
91-615 |
3.42e-27 |
|
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: 115.65 E-value: 3.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 91 DQTAIIWEgddasqSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEA 170
Cdd:cd17656 3 DAVAVVFE------NQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 171 VAGRIIDSSSRLVITADEglragraiplkknvddaLKNPNVNSIEHVVvlkrtggkIDWqegrdlwwsDLMANASAEHRP 250
Cdd:cd17656 77 RIYIMLDSGVRVVLTQRH-----------------LKSKLSFNKSTIL--------LED---------PSISQEDTSNID 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 251 VEMNAEDPLFILYTSGSTGKPKGVL--HTTGGYLVyaATTFKYVFDYHPGDIYW---CTADVGWVTGHSYLLYGP---LA 322
Cdd:cd17656 123 YINNSDDLLYIIYTSGTTGKPKGVQleHKNMVNLL--HFEREKTNINFSDKVLQfatCSFDVCYQEIFSTLLSGGtlyII 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 323 CGATTLMFEgvpnwptpaRMCQVVDKHKVSILYTaPTAIRALMAEGDKAIEGTDRSSLRILgSVGEP--INPEAWEWYWK 400
Cdd:cd17656 201 REETKRDVE---------QLFDLVKRHNIEVVFL-PVAFLKFIFSEREFINRFPTCVKHII-TAGEQlvITNEFKEMLHE 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 401 KigneKCPVMDTWWQTET---GGFMITPLPGAIELKagSATRPFFGVQPVLVDNEGLPLDGATEGNLAIADSwpGQARTL 477
Cdd:cd17656 270 H----NVHLHNHYGPSEThvvTTYTINPEAEIPELP--PIGKPISNTWIYILDQEQQLQPQGIVGELYISGA--SVARGY 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 478 FGD----HERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHN 553
Cdd:cd17656 342 LNRqeltAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADD 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 839746169 554 IKGQAIYAYVTLNHgEEPTPELyaevRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17656 422 KGEKYLCAYFVMEQ-ELNISQL----REYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
256-616 |
3.59e-27 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 113.14 E-value: 3.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 256 EDPLFILYTSGSTGKPKGVLHT-----TGGYLVYAATTFKyvfdyhPGDI-------YWCTADVGwvtghsyllyGPLAC 323
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLThhnivNNGYFIGERLGLT------EQDRlcipvplFHCFGSVL----------GVLAC 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 324 ---GATTLMFEgvpnwPT--PARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIegTDRSSLR--ILGsvGEPINPEAWE 396
Cdd:cd05917 66 lthGATMVFPS-----PSfdPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDK--FDLSSLRtgIMA--GAPCPPELMK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 397 WYWKKIGNEKcpVMDTWWQTET--GGFMITPlPGAIELKAGSATRPFFGVQPVLVDNEG--LPLDGATeGNLAIAdswpG 472
Cdd:cd05917 137 RVIEVMNMKD--VTIAYGMTETspVSTQTRT-DDSIEKRVNTVGRIMPHTEAKIVDPEGgiVPPVGVP-GELCIR----G 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 473 QARTL--FGDHERFEQTYfsTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGI 550
Cdd:cd05917 209 YSVMKgyWNDPEKTAEAI--DGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGV 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 839746169 551 PHNIKGQAIYAYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05917 287 PDERYGEEVCAWIRLKEGAELTEE---DIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
91-619 |
9.79e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 114.11 E-value: 9.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 91 DQTAIIWEgddasqSKHITYRELHADVCRFANVLLDLGiKKGDVVAIYMPMVPE-----AAVAMLACARIGaihsvIFGG 165
Cdd:PRK07638 16 NKIAIKEN------DRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEflqlfAGAAMAGWTCVP-----LDIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 166 FSPEAVAGRIIDSSSRLVITadeglragraiplkknvDDALKNPnVNSIEHVVvlkrtggkIDWQEgrdlwWSDLMANAS 245
Cdd:PRK07638 84 WKQDELKERLAISNADMIVT-----------------ERYKLND-LPDEEGRV--------IEIDE-----WKRMIEKYL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 246 AEHRPVEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVY---AATTFKYVFDYH---PGDIYwctadvgwvtgHSYLLYG 319
Cdd:PRK07638 133 PTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQSWLHSfdcNVHDFHMKREDSvliAGTLV-----------HSLFLYG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 320 P---LACGAT-TLMFEGVPNwptparmcQVVDK---HKVSILYTAPTAIRALMAEgdkaiEGTDRSSLRILGSVGEpinp 392
Cdd:PRK07638 202 AistLYVGQTvHLMRKFIPN--------QVLDKletENISVMYTVPTMLESLYKE-----NRVIENKMKIISSGAK---- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 393 eawewyWKKIGNEKcpVMDTW--------WQTETGGFMITPLPGAIELKAGSATRPFFGVQpVLVDNEGlpldGATegnl 464
Cdd:PRK07638 265 ------WEAEAKEK--IKNIFpyaklyefYGASELSFVTALVDEESERRPNSVGRPFHNVQ-VRICNEA----GEE---- 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 465 aiadSWPGQARTLFGDHERFeqtyFSTFKNMYFS------------GDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEI 532
Cdd:PRK07638 328 ----VQKGEIGTVYVKSPQF----FMGYIIGGVLarelnadgwmtvRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEI 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 533 ESALVSHPKIAEAAVVGIPHNIKGQAIYAYVtlnHGEEPTPELyaevRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMR 612
Cdd:PRK07638 400 ESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---KGSATKQQL----KSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIAR 472
|
....*..
gi 839746169 613 RILRKIA 619
Cdd:PRK07638 473 MEAKSWI 479
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
109-617 |
1.21e-26 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. 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: 114.07 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 109 TYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVITADE 188
Cdd:cd05915 26 TYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 189 GLR-AGRAIPLKKNVDDalkNPNvnsiehvvvlkrtggkidwQEGRDLWWSDLMANASAEHRPVEMNAE-DPLFILYTSG 266
Cdd:cd05915 106 LLPlVEAIRGELKTVQH---FVV-------------------MDEKAPEGYLAYEEALGEEADPVRVPErAACGMAYTTG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 267 STGKPKGVLHT-TGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLlYGPLACGATTLMFEGVPNwptPARMCQV 345
Cdd:cd05915 164 TTGLPKGVVYShRALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLP-YAATLVGAKQVLPGPRLD---PASLVEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 346 VDKHKVSILYTAPTAIRaLMAEGDKAIEGTDRSSLRILGSVGEPinPEAWeWYWKKIGNEKcpVMDTWWQTETGG----- 420
Cdd:cd05915 240 FDGEGVTFTAGVPTVWL-ALADYLESTGHRLKTLRRLVVGGSAA--PRSL-IARFERMGVE--VRQGYGLTETSPvvvqn 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 421 -----FMITPLPGAIELKAGSATRPFFGVQPVL-VDNEGLPLDGAT------EGNLAIADswpgqartLFGDHERFEQTY 488
Cdd:cd05915 314 fvkshLESLSEEEKLTLKAKTGLPIPLVRLRVAdEEGRPVPKDGKAlgevqlKGPWITGG--------YYGNEEATRSAL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 489 FStfKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHG 568
Cdd:cd05915 386 TP--DGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGE 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 839746169 569 EEPTPELYaevrNWVRKEIGPLAT-PDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05915 464 KPTPEELN----EHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
261-616 |
1.77e-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: 113.24 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 261 ILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHP--GDIYWCTADVGWVTGHSYLLYGPLACGATTLM--FEgvpnw 336
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAALGFGPgaDSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMekFD----- 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 337 ptPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEwYWKKIGNEKcpVMDTWWQT 416
Cdd:cd05929 205 --PEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPCPPWVKE-QWIDWGGPI--IWEYYGGT 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 417 ETGGFmiTPLPGAIELK-AGSATRPFFGVQPVLvDNEGLPLDGATEGNLAIADSWPgqartlFGDHERFEQTYFSTFKNM 495
Cdd:cd05929 280 EGQGL--TIINGEEWLThPGSVGRAVLGKVHIL-DEDGNEVPPGEIGEVYFANGPG------FEYTNDPEKTAAARNEGG 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 496 YFS-GDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPE 574
Cdd:cd05929 351 WSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTA 430
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 839746169 575 LYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05929 431 LAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
91-617 |
4.87e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 112.47 E-value: 4.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 91 DQTAIIWEGDDASQSKHItyrelhADVCRFANVLLDLGIKKGDV-VAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPE 169
Cdd:PRK07867 18 DDRGLYFEDSFTSWREHI------RGSAARAAALRARLDPTRPPhVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 170 AVAGRIIDSSSRLVITADEGLragraiPLKKNVDDALKNPNVNSIEhvvvlkrtggkidwqegrdlwWSDLMA-NASAEH 248
Cdd:PRK07867 92 ALARDIAHADCQLVLTESAHA------ELLDGLDPGVRVINVDSPA---------------------WADELAaHRDAEP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 249 RPVEMNAEDPLFILYTSGSTGKPKGVLhTTGGYLVYAATTFKYVFDYHPGDIYWCTAD--------VGWVTGhsyllygp 320
Cdd:PRK07867 145 PFRVADPDDLFMLIFTSGTSGDPKAVR-CTHRKVASAGVMLAQRFGLGPDDVCYVSMPlfhsnavmAGWAVA-------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 321 LACGATTLM---FEGVPNWPTPARM----CQVVDKHKVSILYTAPtairalmaegdkaiEGTDRS-SLRIL-GSVGEPIN 391
Cdd:PRK07867 216 LAAGASIALrrkFSASGFLPDVRRYgatyANYVGKPLSYVLATPE--------------RPDDADnPLRIVyGNEGAPGD 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 392 PEAWEwywKKIGnekCPVMDTWWQTEtGGFMITPLPGAielKAGSATRPFFGVQpvLVDNEG--------LPLDGATEGN 463
Cdd:PRK07867 282 IARFA---RRFG---CVVVDGFGSTE-GGVAITRTPDT---PPGALGPLPPGVA--IVDPDTgtecppaeDADGRLLNAD 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 464 LAIAD----SWPGQARTLFGDHERFEQtyfSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSH 539
Cdd:PRK07867 350 EAIGElvntAGPGGFEGYYNDPEADAE---RMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRY 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 839746169 540 PKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPELYAEVRNwVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK07867 427 PDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLA-AQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
101-617 |
6.31e-26 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 112.38 E-value: 6.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 101 DASQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIhsviFGGFSPEAVAGRIID--- 177
Cdd:PLN02330 49 EAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGV----FSGANPTALESEIKKqae 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 178 -SSSRLVITADEGLRAGRAIPLKKNVDDALKNPN-VNSIEHVVVLKRTGGKIDWQEgrdLWWSDLMAnasaehrpvemna 255
Cdd:PLN02330 125 aAGAKLIVTNDTNYGKVKGLGLPVIVLGEEKIEGaVNWKELLEAADRAGDTSDNEE---ILQTDLCA------------- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 256 edplfILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIywctADVGWVTghSYLLYGPLACGATTLMFEG--- 332
Cdd:PLN02330 189 -----LPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMIGQV----VTLGLIP--FFHIYGITGICCATLRNKGkvv 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 333 VPNWPTPARMCQVVDKHKVSILYTAPTAIRALMAegDKAIEGTDRSSLRI--LGSVGEPINPEAWEWYWKKIGNEKcpVM 410
Cdd:PLN02330 258 VMSRFELRTFLNALITQEVSFAPIVPPIILNLVK--NPIVEEFDLSKLKLqaIMTAAAPLAPELLTAFEAKFPGVQ--VQ 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 411 DTWWQTETGgfMITPLPGAIELKAGSATRPFFG-VQPVL----VDNE-GLPLDGATEGNLAIADSWpgqarTLFGDHERF 484
Cdd:PLN02330 334 EAYGLTEHS--CITLTHGDPEKGHGIAKKNSVGfILPNLevkfIDPDtGRSLPKNTPGELCVRSQC-----VMQGYYNNK 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 485 EQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYV 563
Cdd:PLN02330 407 EETDRTIDEDGWLhTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACV 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 839746169 564 TLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PLN02330 487 VINPKAKESEE---DILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
82-618 |
8.89e-26 |
|
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: 111.85 E-value: 8.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 82 LDRHlAERGDQTAIIwegdDASQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSV 161
Cdd:cd17642 24 MKRY-ASVPGTIAFT----DAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 162 IFGGFSPEAVAGRIIDSSSRLVITADEGLRagRAIPLKKnvddalKNPNVNSIehvVVLKrtgGKIDWQEGRDLW---WS 238
Cdd:cd17642 99 TNDIYNERELDHSLNISKPTIVFCSKKGLQ--KVLNVQK------KLKIIKTI---IILD---SKEDYKGYQCLYtfiTQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 239 DLMANASA-EHRPVEMNAEDPL-FILYTSGSTGKPKGVLHT--------------TGGYLVYAATTFKYVFDYHPGdiYW 302
Cdd:cd17642 165 NLPPGFNEyDFKPPSFDRDEQVaLIMNSSGSTGLPKGVQLThknivarfshardpIFGNQIIPDTAILTVIPFHHG--FG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 303 CTADVGWVTghsyllygplaCGATTLM---FEgvpnwptPARMCQVVDKHKVSILYTAPTairaLMAEGDKA--IEGTDR 377
Cdd:cd17642 243 MFTTLGYLI-----------CGFRVVLmykFE-------EELFLRSLQDYKVQSALLVPT----LFAFFAKStlVDKYDL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 378 SSLRILGSVGEPINPEAWEWYWKKIgneKCP-VMDTWWQTE-TGGFMITP----LPGAIelkagSATRPFFGVQpvLVDN 451
Cdd:cd17642 301 SNLHEIASGGAPLSKEVGEAVAKRF---KLPgIRQGYGLTEtTSAILITPegddKPGAV-----GKVVPFFYAK--VVDL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 452 EGLPLDGATE-GNLAIADswPGQARTLFGDHErfeQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGT 529
Cdd:cd17642 371 DTGKTLGPNErGELCVKG--PMIMKGYVNNPE---ATKALIDKDGWLhSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPP 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 530 AEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPElyaEVRNWVRKEIGPLA-TPDVLHWTDSLPKTRSG 608
Cdd:cd17642 446 AELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEK---EVMDYVASQVSTAKrLRGGVKFVDEVPKGLTG 522
|
570
....*....|
gi 839746169 609 KIMRRILRKI 618
Cdd:cd17642 523 KIDRRKIREI 532
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
105-615 |
1.21e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 113.33 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 105 SKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVI 184
Cdd:PRK12467 1597 EQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLL 1676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 185 TAdeglragRAIPLKKNVDDALKnpnvnsiehVVVLKRTGgkiDWQEGRDlwwsdlMANasaehrPVEMNAEDPL-FILY 263
Cdd:PRK12467 1677 TQ-------SHLQARLPLPDGLR---------SLVLDQED---DWLEGYS------DSN------PAVNLAPQNLaYVIY 1725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 264 TSGSTGKPKGVLHTTGGYL-VYAATTFKYVFdyhpgdiywCTADVgWVTGHSYL-------LYGPLACGATTLMfegVPN 335
Cdd:PRK12467 1726 TSGSTGRPKGAGNRHGALVnRLCATQEAYQL---------SAADV-VLQFTSFAfdvsvweLFWPLINGARLVI---APP 1792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 336 WP--TPARMCQVVDKHKVSILYTAPTAIRALMaEGDKAIEGTdrSSLRILGSVGEPINPEAWEWYWKKIGNEKcpVMDTW 413
Cdd:PRK12467 1793 GAhrDPEQLIQLIERQQVTTLHFVPSMLQQLL-QMDEQVEHP--LSLRRVVCGGEALEVEALRPWLERLPDTG--LFNLY 1867
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 414 WQTETggfMITPLPGAIELK--AGSATRPfFGvQPV------LVDNEGLPLDGATEGNLAIADSwpGQARtlfGDH---- 481
Cdd:PRK12467 1868 GPTET---AVDVTHWTCRRKdlEGRDSVP-IG-QPIanlstyILDASLNPVPIGVAGELYLGGV--GLAR---GYLnrpa 1937
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 482 ---ERFEQTYFSTF-KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVvgIPHN-IKG 556
Cdd:PRK12467 1938 ltaERFVADPFGTVgSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVV--IAQDgANG 2015
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 839746169 557 QAIYAYVT-----LNHGEEPTPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK12467 2016 KQLVAYVVptdpgLVDDDEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
243-616 |
1.59e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 110.46 E-value: 1.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 243 NASAEHRPVEMNAEDPLFILYTSGSTGKPKGVLHTTGGYlvyAATtfkyvFDYHPGDIYWCTADV-----------GWVT 311
Cdd:PRK07787 115 HARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAI---AAD-----LDALAEAWQWTADDVlvhglplfhvhGLVL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 312 GhsylLYGPLACGATtLMFEGVPnwpTPARMCQVVDKhKVSILYTAPTAIRALMAEGDKAiegtdR--SSLRILGSVGEP 389
Cdd:PRK07787 187 G----VLGPLRIGNR-FVHTGRP---TPEAYAQALSE-GGTLYFGVPTVWSRIAADPEAA-----RalRGARLLVSGSAA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 390 INPEAWEWYWKKIGNEkcpVMDTWWQTETggFMITPLPGAIELKAGSATRPFFGVQPVLVDNEG--LPLDGATEGNLAIa 467
Cdd:PRK07787 253 LPVPVFDRLAALTGHR---PVERYGMTET--LITLSTRADGERRPGWVGLPLAGVETRLVDEDGgpVPHDGETVGELQV- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 468 dswpgQARTLF-GDHERFEQT--------YFSTfknmyfsGDGARRDEDGYYWITGRVD-DVLNVSGHRLGTAEIESALV 537
Cdd:PRK07787 327 -----RGPTLFdGYLNRPDATaaaftadgWFRT-------GDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALL 394
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 839746169 538 SHPKIAEAAVVGIPHNIKGQAIYAYVTlnHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK07787 395 GHPGVREAAVVGVPDDDLGQRIVAYVV--GADDVAAD---ELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
70-619 |
1.69e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 108.11 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 70 YEDGTLNLAANC--------LDRHLAERGDQTAIIWEGddasqsKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPM 141
Cdd:PRK08162 4 YEQGLDRNAANYvpltplsfLERAAEVYPDRPAVIHGD------RRRTWAETYARCRRLASALARRGIGRGDTVAVLLPN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 142 VPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVIT--------ADEGLRAGRAIPLKKNVDDAL--KNPNV 211
Cdd:PRK08162 78 IPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVdtefaevaREALALLPGPKPLVIDVDDPEypGGRFI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 212 NSIEHVVVLKRTGGKIDWQEGRDLWwsdlmanasaehrpvemnaeDPLFILYTSGSTGKPKGVL-HTTGGYLVYAATTFK 290
Cdd:PRK08162 158 GALDYEAFLASGDPDFAWTLPADEW--------------------DAIALNYTSGTTGNPKGVVyHHRGAYLNALSNILA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 291 YVFDYHPgdIY-W------CTadvGWvtghsyllygplaCGATTLMFEGVPN----WPTPARMCQVVDKHKVSILYTAPT 359
Cdd:PRK08162 218 WGMPKHP--VYlWtlpmfhCN---GW-------------CFPWTVAARAGTNvclrKVDPKLIFDLIREHGVTHYCGAPI 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 360 AIRALMAEGDKAIEGTDRsslRILGSVGEPINPEAWEWYWKKIGNEkcpVMDTWWQTET----------GGFMITPLPGA 429
Cdd:PRK08162 280 VLSALINAPAEWRAGIDH---PVHAMVAGAAPPAAVIAKMEEIGFD---LTHVYGLTETygpatvcawqPEWDALPLDER 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 430 IELKAGSATRpFFGVQPVLV-DNEGL---PLDGAT------EGNLAIADSWPGQARTlfgdHERFEQTYFSTfknmyfsG 499
Cdd:PRK08162 354 AQLKARQGVR-YPLQEGVTVlDPDTMqpvPADGETigeimfRGNIVMKGYLKNPKAT----EEAFAGGWFHT-------G 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 500 DGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPElyaEV 579
Cdd:PRK08162 422 DLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEE---EI 498
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 839746169 580 RNWVRKEIGPLATPDVLHWTdSLPKTRSGKIMRRILRKIA 619
Cdd:PRK08162 499 IAHCREHLAGFKVPKAVVFG-ELPKTSTGKIQKFVLREQA 537
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
257-612 |
4.45e-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: 103.64 E-value: 4.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 257 DPLFILYTSGSTGKPKGVLHTTGGYLVYaattfkyvFDYHPGDIYWCTADVGWVTG---HSYLLYGPL--------ACGA 325
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIES--------FVCNEDLFNISGEDAILAPGplsHSLFLYGAIsalylggtFIGQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 326 TTLmfegvpnwpTPARMCQVVDKHKVSILYTAPTAIRALmaegdkAIEGTDRSSLRILGSVGEPINPEAwewyWKKIGNE 405
Cdd:cd17633 73 RKF---------NPKSWIRKINQYNATVIYLVPTMLQAL------ARTLEPESKIKSIFSSGQKLFEST----KKKLKNI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 406 --KCPVMDTWWQTETGgfMITPLPGAIELKAGSATRPFFGVQPVLVDNEG-----------LPLDGATEGNLAIADSWpg 472
Cdd:cd17633 134 fpKANLIEFYGTSELS--FITYNFNQESRPPNSVGRPFPNVEIEIRNADGgeigkifvkseMVFSGYVRGGFSNPDGW-- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 473 qartlfgdherfeqtyFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPH 552
Cdd:cd17633 210 ----------------MSV-------GDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPD 266
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 553 NIKGQAIYAYVTlnhGEEPTpelYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17633 267 ARFGEIAVALYS---GDKLT---YKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
84-617 |
7.20e-24 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 106.17 E-value: 7.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 84 RHLAERGDQTAIIWEGDDASQSKHITYRELHADVCRFANVLLDLGiKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIF 163
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 164 GGFSPEA---VAGRIIDSSSRLVITADEGLRAgraiplkknvddalknpnvnsiehvvvLKRTGGKIDWQEGRDLWWSDL 240
Cdd:cd05931 80 PPTPGRHaerLAAILADAGPRVVLTTAAALAA---------------------------VRAFAASRPAAGTPRLLVVDL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 241 MANASAEH-RPVEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKyVFDYHPGDIY--W--CTADVGWVTGhsy 315
Cdd:cd05931 133 LPDTSAADwPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRR-AYGLDPGDVVvsWlpLYHDMGLIGG--- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 316 lLYGPLACGATTLMFEgvpnwPT-----PARMCQVVDKHKVSILYtAPT-----AIRALMAEGdkaIEGTDRSSLRILGS 385
Cdd:cd05931 209 -LLTPLYSGGPSVLMS-----PAaflrrPLRWLRLISRYRATISA-APNfaydlCVRRVRDED---LEGLDLSSWRVALN 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 386 VGEPINPEAWEWYWKK----------------------------IGNEKCPVMDTWWQTETGGFMITPL-PGAIELKagS 436
Cdd:cd05931 279 GAEPVRPATLRRFAEAfapfgfrpeafrpsyglaeatlfvsggpPGTGPVVLRVDRDALAGRAVAVAADdPAARELV--S 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 437 ATRPFFGVQPVLVDNEGL-PLDGATEGNLAIADS------W---PGQARTLFGDHERFEQTYFSTfknmyfsGD-GARRd 505
Cdd:cd05931 357 CGRPLPDQEVRIVDPETGrELPDGEVGEIWVRGPsvasgyWgrpEATAETFGALAATDEGGWLRT-------GDlGFLH- 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 506 eDGYYWITGRVDDVLNVSGHRLGTAEIE-SALVSHPKIAE--AAVVGIPHNIKGQ-AIYAYVTLNHGEEPTPELYAEVRN 581
Cdd:cd05931 429 -DGELYITGRLKDLIIVRGRNHYPQDIEaTAEEAHPALRPgcVAAFSVPDDGEERlVVVAEVERGADPADLAAIAAAIRA 507
|
570 580 590
....*....|....*....|....*....|....*..
gi 839746169 582 WVRKEIGpLATPDV-LHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05931 508 AVAREHG-VAPADVvLVRPGSIPRTSSGKIQRRACRA 543
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
256-609 |
8.46e-24 |
|
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: 103.62 E-value: 8.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 256 EDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDyHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPN 335
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGVMWRQEDIFRMLMGGADFGTG-EFTPSEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 336 WPT----------PARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNe 405
Cdd:cd05924 82 GGQtvvlpddrfdPEEVWRTIEKHKVTSMTIVGDAMARPLIDALRDAGPYDLSSLFAISSGGALLSPEVKQGLLELVPN- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 406 kCPVMDTWWQTETGGFMI-TPLPGAIElkagsaTRPFFGVQP--VLVDNEGLPLDGATEGNLAIADSwpGQ-ARTLFGDH 481
Cdd:cd05924 161 -ITLVDAFGSSETGFTGSgHSAGSGPE------TGPFTRANPdtVVLDDDGRVVPPGSGGVGWIARR--GHiPLGYYGDE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 482 ERFEQTYFSTFKNMY-FSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIY 560
Cdd:cd05924 232 AKTAETFPEVDGVRYaVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVV 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 839746169 561 AYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGK 609
Cdd:cd05924 312 AVVQLREGAGVDLE---ELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
48-625 |
1.10e-23 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 105.69 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 48 WIRPYTRVKNTSFAPGNISIkwyeDGTLNLAANCLDRHlaERGDQTAIIwegdDASQSKHITYRELHADVCRFANVLLD- 126
Cdd:PLN02574 17 WYSPETGIYSSKHPPVPLPS----DPNLDAVSFIFSHH--NHNGDTALI----DSSTGFSISYSELQPLVKSMAAGLYHv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 127 LGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVITADEglRAGRAIPLKKNVDDAL 206
Cdd:PLN02574 87 MGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPE--NVEKLSPLGVPVIGVP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 207 KNPNVNSiehvvvlkrtgGKIDWQEGRDLWWSDlmanASAEHRPVeMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAA 286
Cdd:PLN02574 165 ENYDFDS-----------KRIEFPKFYELIKED----FDFVPKPV-IKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 287 TTFKY---VFDYHPGD-IYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVpnwpTPARMCQVVDKHKVSILYTAPTAIR 362
Cdd:PLN02574 229 LFVRFeasQYEYPGSDnVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRF----DASDMVKVIDRFKVTHFPVVPPILM 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 363 ALMAEGdKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIgnekcPVMD---TWWQTE-----TGGFMITPLP--GAIEL 432
Cdd:PLN02574 305 ALTKKA-KGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTL-----PHVDfiqGYGMTEstavgTRGFNTEKLSkySSVGL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 433 KAGSatrpffgVQPVLVDNE-GLPLDGATEGNLAIADswPGQARTLFGDHErfeQTYFSTFKNMYF-SGDGARRDEDGYY 510
Cdd:PLN02574 379 LAPN-------MQAKVVDWStGCLLPPGNCGELWIQG--PGVMKGYLNNPK---ATQSTIDKDGWLrTGDIAYFDEDGYL 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 511 WITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPElyaEVRNWVRKEIGPL 590
Cdd:PLN02574 447 YIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQE---AVINYVAKQVAPY 523
|
570 580 590
....*....|....*....|....*....|....*
gi 839746169 591 ATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDTSN 625
Cdd:PLN02574 524 KKVRKVVFVQSIPKSPAGKILRRELKRSLTNSVSS 558
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
79-613 |
2.90e-23 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 104.20 E-value: 2.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 79 ANCLDRHLAERGDQTAIIWegddASQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAI 158
Cdd:PRK05852 19 ADLVEVAATRLPEAPALVV----TADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 159 hsvifggFSPEAVAGRIIDSSSRLvitADEGLRagraiplkknvddalknpnvnsiehvVVLKRTGGKIDWQEGRDLWWS 238
Cdd:PRK05852 95 -------VVPLDPALPIAEQRVRS---QAAGAR--------------------------VVLIDADGPHDRAEPTTRWWP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 239 ------------------DLMANASAEHR---PVEMNAEDPLfILYTSGSTGKPKGVLHTTGGYlvyAATTFKYVFDYHP 297
Cdd:PRK05852 139 ltvnvggdsgpsggtlsvHLDAATEPTPAtstPEGLRPDDAM-IMFTGGTTGLPKMVPWTHANI---ASSVRAIITGYRL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 298 GDIYWCTADVGWVTGHSYL--LYGPLACGATTLMfegvpnwPTPARMCQVV---DKHKV-SILYTA-PTAIRALMAEGDK 370
Cdd:PRK05852 215 SPRDATVAVMPLYHGHGLIaaLLATLASGGAVLL-------PARGRFSAHTfwdDIKAVgATWYTAvPTIHQILLERAAT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 371 AIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGnekCPVMDTWWQTET---------GGFMITPLPGAIELKAGSATrpf 441
Cdd:PRK05852 288 EPSGRKPAALRFIRSCSAPLTAETAQALQTEFA---APVVCAFGMTEAthqvtttqiEGIGQTENPVVSTGLVGRST--- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 442 fGVQPVLVDNEGLPLDGATEGNLAIadSWPGQARTLFGDHE----RFEQTYFSTfknmyfsGDGARRDEDGYYWITGRVD 517
Cdd:PRK05852 362 -GAQIRIVGSDGLPLPAGAVGEVWL--RGTTVVRGYLGDPTitaaNFTDGWLRT-------GDLGSLSAAGDLSIRGRIK 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 518 DVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLH 597
Cdd:PRK05852 432 ELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAE---ELVQFCRERLAAFEIPASFQ 508
|
570
....*....|....*.
gi 839746169 598 WTDSLPKTRSGKIMRR 613
Cdd:PRK05852 509 EASGLPHTAKGSLDRR 524
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
108-616 |
3.50e-23 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 103.42 E-value: 3.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 108 ITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVITAD 187
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCDP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 188 EGLRAGRAIPLKKNVddalknpnvnsiEHVVVL--KRTGGkidwqegrdlwWSDLMANASAEHRPVEMNAEDPLFILYTS 265
Cdd:PRK07514 109 ANFAWLSKIAAAAGA------------PHVETLdaDGTGS-----------LLEAAAAAPDDFETVPRGADDLAAILYTS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 266 GSTGKPKGVLHTTGGYLVYAATTFKYvFDYHPGD-------IYwctadvgwvtgHSYLLY----GPLACG---------- 324
Cdd:PRK07514 166 GTTGRSKGAMLSHGNLLSNALTLVDY-WRFTPDDvlihalpIF-----------HTHGLFvatnVALLAGasmiflpkfd 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 325 ----------ATTLMfeGVPNWPTpaRMCQ--VVDKHKVS-----ILYTAPtairaLMAEGDKAIEgtDRSSLRILgsvg 387
Cdd:PRK07514 234 pdavlalmprATVMM--GVPTFYT--RLLQepRLTREAAAhmrlfISGSAP-----LLAETHREFQ--ERTGHAIL---- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 388 epinpeawEWYwkkiGnekcpvMdtwwqTETGgfMITPLPGAIELKAGSATRPFFGVQPVLVDNE-GLPLDGATEGNLAI 466
Cdd:PRK07514 299 --------ERY----G------M-----TETN--MNTSNPYDGERRAGTVGFPLPGVSLRVTDPEtGAELPPGEIGMIEV 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 467 adswpgQARTLFGDHERF-EQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAE 544
Cdd:PRK07514 354 ------KGPNVFKGYWRMpEKTAEEFRADGFFiTGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVE 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 839746169 545 AAVVGIPHNIKGQAIYAYVTLNHGEEPTPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK07514 428 SAVIGVPHPDFGEGVTAVVVPKPGAALDE---AAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
76-616 |
6.71e-23 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 103.57 E-value: 6.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 76 NLAAnCLDRHLAERG--DQTAiiWEGDDAsqskhITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACA 153
Cdd:PRK06060 5 NLAG-LLAEQASEAGwyDRPA--FYAADV-----VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 154 RIGAIHSVIFGGFSPEAVAGRIIDSSSRLVITADeglragraiPLKknvdDALKNPNVnsiehvvvlkrtggkidwQEGR 233
Cdd:PRK06060 77 ARGVMAFLANPELHRDDHALAARNTEPALVVTSD---------ALR----DRFQPSRV------------------AEAA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 234 DLWwSDLMANASAEHRPVEMNAEdpLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGH 313
Cdd:PRK06060 126 ELM-SEAARVAPGGYEPMGGDAL--AYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 314 SYLLYGPLACGATTLmfegVPNWPTPARMCQVVD-KHKVSILYTAPTairaLMAEGDKAIEGTDRSSLRILGSVGEPINP 392
Cdd:PRK06060 203 GNSVWFPLATGGSAV----INSAPVTPEAAAILSaRFGPSVLYGVPN----FFARVIDSCSPDSFRSLRCVVSAGEALEL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 393 EAWEWYWKKIGNekCPVMDTWWQTETGGFMITPlpGAIELKAGSATRPFFGVQPVLVDNEGLPLDGATEGNL-----AIA 467
Cdd:PRK06060 275 GLAERLMEFFGG--IPILDGIGSTEVGQTFVSN--RVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLwvrgpAIA 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 468 DSWPGQARTLFGDHERFEqtyfstfknmyfSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAV 547
Cdd:PRK06060 351 KGYWNRPDSPVANEGWLD------------TRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAV 418
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 839746169 548 VGIPHNIKGQAIYAYVTLNHGEEPTPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK06060 419 VAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
256-612 |
1.19e-22 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 99.64 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 256 EDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDyhpgdiyWCTADVGWVTGHSYLLYGpLACGATTLMFEGV-- 333
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLN-------WVVGDVTYLPLPATHIGG-LWWILTCLIHGGLcv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 334 --PNWPTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGTDrsSLRILGSVGE-PINPEAWEWYWKKIGNekcpVM 410
Cdd:cd17635 73 tgGENTTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVP--SLRLIGYGGSrAIAADVRFIEATGLTN----TA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 411 DTWWQTETGGFMITPLpGAIELKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIADSWpgqarTLFGDHERFEQTYFS 490
Cdd:cd17635 147 QVYGLSETGTALCLPT-DDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPA-----NMLGYWNNPERTAEV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 491 TFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNhgEE 570
Cdd:cd17635 221 LIDGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAS--AE 298
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 839746169 571 PTPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17635 299 LDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
82-580 |
1.23e-22 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 102.65 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 82 LDRHLAERGDQTAIIWEGddasqsKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSV 161
Cdd:PRK08279 43 FEEAAARHPDRPALLFED------QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 162 IFGGFSPEAVAGRIIDSSSRLVITADEglragraipLKKNVDDALKNPNVnsieHVVVLKRTGGKIDWQEGrdlwWSDLM 241
Cdd:PRK08279 117 LNTQQRGAVLAHSLNLVDAKHLIVGEE---------LVEAFEEARADLAR----PPRLWVAGGDTLDDPEG----YEDLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 242 ANASA--EHRPVE---MNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAtTFKYVFDYHPGDIYWCT--------ADVG 308
Cdd:PRK08279 180 AAAAGapTTNPASrsgVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMG-GFGGLLRLTPDDVLYCClplyhntgGTVA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 309 WVTGhsyllygpLACGATtlmfegvpnwptparmcqVVDKHKVS--------ILYTApTAI-------RALMAEGDKAie 373
Cdd:PRK08279 259 WSSV--------LAAGAT------------------LALRRKFSasrfwddvRRYRA-TAFqyigelcRYLLNQPPKP-- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 374 gTDRS-SLRILgsVGEPINPEAWEWYWKKIGNEKcpVMDTWWQTE-TGGFMitplpgAIELKAGSATR-PFFGVQPVLV- 449
Cdd:PRK08279 310 -TDRDhRLRLM--IGNGLRPDIWDEFQQRFGIPR--ILEFYAASEgNVGFI------NVFNFDGTVGRvPLWLAHPYAIv 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 450 --DNE-GLPLDGAtEGNL-AIADSWPGQARTLFGDHERFEqTYFS-----------TFK--NMYF-SGDGARRDEDGYYW 511
Cdd:PRK08279 379 kyDVDtGEPVRDA-DGRCiKVKPGEVGLLIGRITDRGPFD-GYTDpeasekkilrdVFKkgDAWFnTGDLMRDDGFGHAQ 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 839746169 512 ITGRVDDVL-----NVSghrlgTAEIESALVSHPKIAEAAVVGIP-HNIKGQAIYAYVTLNHGEEPTP-ELYAEVR 580
Cdd:PRK08279 457 FVDRLGDTFrwkgeNVA-----TTEVENALSGFPGVEEAVVYGVEvPGTDGRAGMAAIVLADGAEFDLaALAAHLY 527
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
106-620 |
1.25e-22 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 102.26 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 106 KHITYRELHADVCRFANVLL-DLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDS-SSRLV 183
Cdd:PRK08751 49 KTITYREADQLVEQFAAYLLgELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSgASVLV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 184 ITADEGLRAGRAI---PLKKNVDD-----------ALKNPNVNSIEHVVVLKRTGGKIDWQEGRDLwwsdlmanaSAEHR 249
Cdd:PRK08751 129 VIDNFGTTVQQVIadtPVKQVITTglgdmlgfpkaALVNFVVKYVKKLVPEYRINGAIRFREALAL---------GRKHS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 250 --PVEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKyvfdyhpgdiyWCTADVGWVTGHSYL-----LYGPLA 322
Cdd:PRK08751 200 mpTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQ-----------WLAGTGKLEEGCEVVitalpLYHIFA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 323 CGATTLMFEGVPNW----PTPARMCQVVDKHKvSILYTAPTAIRALMAE--GDKAIEGTDRSSLRILGSVGEPINPEAWE 396
Cdd:PRK08751 269 LTANGLVFMKIGGCnhliSNPRDMPGFVKELK-KTRFTAFTGVNTLFNGllNTPGFDQIDFSSLKMTLGGGMAVQRSVAE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 397 wYWKKIGNekCPVMDTWWQTETG-GFMITPLpgAIELKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIADSwpgqaR 475
Cdd:PRK08751 348 -RWKQVTG--LTLVEAYGLTETSpAACINPL--TLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGP-----Q 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 476 TLFGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNI 554
Cdd:PRK08751 418 VMKGYWKRPEETAKVMDADGWLhTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEK 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 839746169 555 KGQAIYAYVTlnhgeEPTPELYAE-VRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAA 620
Cdd:PRK08751 498 SGEIVKVVIV-----KKDPALTAEdVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAAK 559
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
91-615 |
1.95e-22 |
|
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: 100.71 E-value: 1.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 91 DQTAIIWEGddasQSkhITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEA 170
Cdd:cd17645 13 DHVAVVDRG----QS--LTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGER 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 171 VAGRIIDSSSRLVITadeglragraiplkknvddalknpnvnsiehvvvlkrtggkidwqegrdlwwsdlmanasaehrp 250
Cdd:cd17645 87 IAYMLADSSAKILLT----------------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 251 vemNAEDPLFILYTSGSTGKPKGVL--HTTggyLVYAATTFKYVFDYHPGDIYWCTADVGWvTGHSYLLYGPLACGATTL 328
Cdd:cd17645 102 ---NPDDLAYVIYTSGSTGLPKGVMieHHN---LVNLCEWHRPYFGVTPADKSLVYASFSF-DASAWEIFPHLTAGAALH 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 329 MFEGVPNWPTpARMCQVVDKHKVSILYTAPTAIRALMAegdkaiegTDRSSLRILGSVGEPINPEAWEWY--WKKIGNEK 406
Cdd:cd17645 175 VVPSERRLDL-DALNDYFNQEGITISFLPTGAAEQFMQ--------LDNQSLRVLLTGGDKLKKIERKGYklVNNYGPTE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 407 CPVMDTwwqtetgGFMITPLPGAIEL-KAGSATRpffgvqpVLVDNEGLPL--DGATeGNLAIADSwpGQARTLFG---- 479
Cdd:cd17645 246 NTVVAT-------SFEIDKPYANIPIgKPIDNTR-------VYILDEALQLqpIGVA-GELCIAGE--GLARGYLNrpel 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 480 DHERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAI 559
Cdd:cd17645 309 TAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYL 388
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 839746169 560 YAYVTLNhgEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17645 389 VAYVTAP--EEIPHE---ELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
24-81 |
2.69e-22 |
|
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: 90.22 E-value: 2.69e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 839746169 24 YKAQYQQSITDPDTFWGEQGKILDWIRPYTRVKNTSFAPGnisIKWYEDGTLNLAANC 81
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKELDWFKPFDKVLDGSNGPF---AKWFVGGKLNVCYNC 55
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
76-621 |
3.24e-22 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 100.85 E-value: 3.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 76 NLAANCLDRHL--AERGDQTAIIWEGDDASQskhITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACA 153
Cdd:PRK05857 11 QLPSTVLDRVFeqARQQPEAIALRRCDGTSA---LRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 154 RIGAIHSVIFGGFSPEAVA--GRIIDSSSrlVITADEGLRAGRAIPLKKNVDDALKNpnvnSIEHVVVLKRTGGKIDWQE 231
Cdd:PRK05857 88 KLGAIAVMADGNLPIAAIErfCQITDPAA--ALVAPGSKMASSAVPEALHSIPVIAV----DIAAVTRESEHSLDAASLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 232 GRdlwwsdlmanasaehrpVEMNAEDPLFILYTSGSTGKPKGVLhttggylvYAATTFKYVFD-YHPGDIYWctadVGWV 310
Cdd:PRK05857 162 GN-----------------ADQGSEDPLAMIFTSGTTGEPKAVL--------LANRTFFAVPDiLQKEGLNW----VTWV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 311 TGHSylLYGPLACG--------ATTLMFEG--VPNWPTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAieGTDRSSL 380
Cdd:PRK05857 213 VGET--TYSPLPAThigglwwiLTCLMHGGlcVTGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSA--NATVPSL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 381 RILGSVGEpinpEAWEWYWKKIGNEKCPVMDTWWQTETGGFMITpLP---GAI-ELKAGSATRPFFGVQPVLVD-NEGLP 455
Cdd:PRK05857 289 RLVGYGGS----RAIAADVRFIEATGVRTAQVYGLSETGCTALC-LPtddGSIvKIEAGAVGRPYPGVDVYLAAtDGIGP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 456 LDGATEGNLAIADSW---PGQARTLFGDHERFEQTYFSTFKNmyfSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEI 532
Cdd:PRK05857 364 TAPGAGPSASFGTLWiksPANMLGYWNNPERTAEVLIDGWVN---TGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 533 ESALVSHPKIAEAAVVGIPHN----IKGQAIYAYVTLNhgEEPTPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSG 608
Cdd:PRK05857 441 DRIAEGVSGVREAACYEIPDEefgaLVGLAVVASAELD--ESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSG 518
|
570
....*....|...
gi 839746169 609 KIMRRILRKIAAG 621
Cdd:PRK05857 519 KVMRASLAAAATA 531
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
233-621 |
4.94e-22 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 102.17 E-value: 4.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 233 RDLWWSDLMANASAEHRPVEMNAEDPL-FILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVfDYHPGDIYWCTADVGWVT 311
Cdd:PRK05691 3845 RLLVWEEVQAGEVASHNPGIYSGPDNLaYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYL-ALSEADVIAQTASQSFDI 3923
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 312 GHSYLLYGPLAcGATTlmfEGVPNWPT--PARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGtdrssLRILGSVGEP 389
Cdd:PRK05691 3924 SVWQFLAAPLF-GARV---EIVPNAIAhdPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQALDG-----LRWMLPTGEA 3994
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 390 INPE-AWEWYWK--------KIGNEKCPVMDTWWQTETGGFMITPLPgaielkAGSATrpffgvqpvlvDNEGLPL-DGA 459
Cdd:PRK05691 3995 MPPElARQWLQRypqiglvnAYGPAECSDDVAFFRVDLASTRGSYLP------IGSPT-----------DNNRLYLlDEA 4057
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 460 TE-------GNLAIADSwpGQARTLFGDHERFEQTYF-----STFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRL 527
Cdd:PRK05691 4058 LElvplgavGELCVAGT--GVGRGYVGDPLRTALAFVphpfgAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRI 4135
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 528 GTAEIESALVSHPKIAEAAvVGIPHNIKGQAIYAYVTLNHGEEPTPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRS 607
Cdd:PRK05691 4136 ELGEIEARLHEQAEVREAA-VAVQEGVNGKHLVGYLVPHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNAN 4214
|
410
....*....|....
gi 839746169 608 GKIMRRILRKIAAG 621
Cdd:PRK05691 4215 GKLDRKALPALDIG 4228
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
254-615 |
5.61e-22 |
|
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: 99.43 E-value: 5.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 254 NAEDPLFILYTSGSTGKPKGVL--------HTTGGYLVYAATTFKYV-------FDYHPGDIYwctadVGWVTGHSYLLy 318
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMiehqslvnLSHGLIKEYGITSSDRVlqfasiaFDVAAEEIY-----VTLLSGATLVL- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 319 gplacgATTLMFegvpnwPTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKA-IEGTDRSSLRILGsvGEPINPEAWEw 397
Cdd:cd17644 178 ------RPEEMR------SSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLStIDLPSSLRLVIVG--GEAVQPELVR- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 398 YWKKIGNEKCPVMDTWWQTE----TGGFMITPLPGAIELKAgSATRPFFGVQPVLVDNEGLPLDGATEGNLAIADSwpGQ 473
Cdd:cd17644 243 QWQKNVGNFIQLINVYGPTEatiaATVCRLTQLTERNITSV-PIGRPIANTQVYILDENLQPVPVGVPGELHIGGV--GL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 474 ARTLFG----DHERFEQTYF--STFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAV 547
Cdd:cd17644 320 ARGYLNrpelTAEKFISHPFnsSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVV 399
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 839746169 548 VGIPHNIKGQAIYAYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17644 400 IVREDQPGNKRLVAYIVPHYEESPSTV---ELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
83-617 |
1.38e-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: 97.77 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 83 DRHLAERGDQTAIiwegDDASQSkhITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIhsvi 162
Cdd:cd17653 4 ERIAAAHPDAVAV----ESLGGS--LTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAA---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 163 fggfspeavagriidsssrlVITADEGLRAGRaiplkknvddalknpnvnsIEHVvvLKRTGGKIdwqegrdlwwsdLMA 242
Cdd:cd17653 74 --------------------YVPLDAKLPSAR-------------------IQAI--LRTSGATL------------LLT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 243 NASAEhrpvemnaeDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTfKYVFDYHPGD--------IYWCTADVgwvtghs 314
Cdd:cd17653 101 TDSPD---------DLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQP-PARLDVGPGSrvaqvlsiAFDACIGE------- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 315 ylLYGPLACGATTLMFEGVPNWPTPARmcqvvdkhKVSILYTAPTAIRALmaegdkaiEGTDRSSLRILGSVGEPINPea 394
Cdd:cd17653 164 --IFSTLCNGGTLVLADPSDPFAHVAR--------TVDALMSTPSILSTL--------SPQDFPNLKTIFLGGEAVPP-- 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 395 wewywkkignekcPVMDTWWQ----------TETggfmiTPLPGAIELKAGSAT---RPFFGVQPVLVDNEGLPLDGATE 461
Cdd:cd17653 224 -------------SLLDRWSPgrrlynaygpTEC-----TISSTMTELLPGQPVtigKPIPNSTCYILDADLQPVPEGVV 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 462 GNLAIADswPGQARTLFGDHE----RFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALV 537
Cdd:cd17653 286 GEICISG--VQVARGYLGNPAltasKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVL 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 538 SHPKIAEAAVVgIPHNikgQAIYAYVtlnhgeepTPELYAE--VRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17653 364 QSQPEVTQAAA-IVVN---GRLVAFV--------TPETVDVdgLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKAL 431
|
..
gi 839746169 616 RK 617
Cdd:cd17653 432 RE 433
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
90-636 |
1.83e-21 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 98.70 E-value: 1.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 90 GDQTAIIWEGDDASQskhITYRELHADVCRFANVLLD-LGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSP 168
Cdd:PRK05620 24 GDTTVTTWGGAEQEQ---TTFAAIGARAAALAHALHDeLGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 169 EAVAgRIIDSSSRLVITADEGLrAGRAIPLKKNVDdalknpnvnSIEHVVVLKRTGGKIDWQEGRD----LWWSDLMANA 244
Cdd:PRK05620 101 DQIV-HIINHAEDEVIVADPRL-AEQLGEILKECP---------CVRAVVFIGPSDADSAAAHMPEgikvYSYEALLDGR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 245 SAEHRPVEMNAEDPLFILYTSGSTGKPKGV-------------LHTTGGYLVYAATTFKY-VFDYHPgdIYWCTADVGWV 310
Cdd:PRK05620 170 STVYDWPELDETTAAAICYSTGTTGAPKGVvyshrslylqslsLRTTDSLAVTHGESFLCcVPIYHV--LSWGVPLAAFM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 311 TGhsyllygplacgaTTLMFEGVPnwPTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKaiEGTDRSSLRILGSVGEPI 390
Cdd:PRK05620 248 SG-------------TPLVFPGPD--LSAPTLAKIIATAMPRVAHGVPTLWIQLMVHYLK--NPPERMSLQEIYVGGSAV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 391 NP---EAWEwywKKIGNEkcpVMDTWWQTETG--GFMITPlPGAIELKAGSATRPFFGVQPV----LVDNEGLPLDGA-- 459
Cdd:PRK05620 311 PPiliKAWE---ERYGVD---VVHVWGMTETSpvGTVARP-PSGVSGEARWAYRVSQGRFPAsleyRIVNDGQVMESTdr 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 460 TEGNLAIADSW-------------PGQARTLFGDHERFEQTYFsTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHR 526
Cdd:PRK05620 384 NEGEIQVRGNWvtasyyhspteegGGAASTFRGEDVEDANDRF-TADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEW 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 527 LGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTR 606
Cdd:PRK05620 463 IYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTS 542
|
570 580 590
....*....|....*....|....*....|.
gi 839746169 607 SGKIMRRILRK-IAAGDTsnlgDTSTLADPG 636
Cdd:PRK05620 543 VGKFDKKDLRQhLADGDF----EIIKLKGPG 569
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
108-619 |
1.86e-21 |
|
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: 98.17 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 108 ITYRELhadvcRFANVLLDLGIKK----GDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLV 183
Cdd:cd05909 8 LTYRKL-----LTGAIALARKLAKmtkeGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 184 ITADEGLRAGraiplkknvdDALKNPNVNSIEHVVVLKRTGGKIDWQEG---------RDLWWSDLMANASAEhrpvemn 254
Cdd:cd05909 83 LTSKQFIEKL----------KLHHLFDVEYDARIVYLEDLRAKISKADKckaflagkfPPKWLLRIFGVAPVQ------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 255 AEDPLFILYTSGSTGKPKGVLHTTGGYL--VYAATTfkyVFDYHPGDIywctadvgwVTG-----HSYLLYG----PLAC 323
Cdd:cd05909 146 PDDPAVILFTSGSEGLPKGVVLSHKNLLanVEQITA---IFDPNPEDV---------VFGalpffHSFGLTGclwlPLLS 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 324 GATTLMFegvPNwPTPAR-MCQVVDKHKVSILYTAPTAIRALMaegdKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKI 402
Cdd:cd05909 214 GIKVVFH---PN-PLDYKkIPELIYDKKATILLGTPTFLRGYA----RAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKF 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 403 G---------NEKCPVMDtwwqtetggfMITPLPGAielKAGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIADSwPGQ 473
Cdd:cd05909 286 GirilegygtTECSPVIS----------VNTPQSPN---KEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRG-PNV 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 474 ARTLFGDHerfEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSH-PKIAEAAVVGIPH 552
Cdd:cd05909 352 MLGYLNEP---ELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPD 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 839746169 553 NIKGQAIYAYVTlnhGEEPTPElyaEVRNWVRK-EIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIA 619
Cdd:cd05909 429 GRKGEKIVLLTT---TTDTDPS---SLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
237-616 |
2.89e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 97.79 E-value: 2.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 237 WSDLMANASAEHRPVEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYA-ATTFKYvfDYHPGDIYWCTADVGwvtgHS- 314
Cdd:PRK13388 131 YAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGrALTERF--GLTRDDVCYVSMPLF----HSn 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 315 --YLLYGP-LACGATTLMfegvPNWPTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGTDRssLRIlgSVGEPIN 391
Cdd:PRK13388 205 avMAGWAPaVASGAAVAL----PAKFSASGFLDDVRRYGATYFNYVGKPLAYILATPERPDDADNP--LRV--AFGNEAS 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 392 PEAWEWYWKKIGnekCPVMDTWWQTETGGfMITPLPGAielKAGSATRPFFGVqpVLVDNEGLPLDGATE----GNLAIA 467
Cdd:PRK13388 277 PRDIAEFSRRFG---CQVEDGYGSSEGAV-IVVREPGT---PPGSIGRGAPGV--AIYNPETLTECAVARfdahGALLNA 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 468 DSWPG-----QARTLF--------GDHERFEQtyfstfkNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIES 534
Cdd:PRK13388 348 DEAIGelvntAGAGFFegyynnpeATAERMRH-------GMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIER 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 535 ALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPELYAEVRNwVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRI 614
Cdd:PRK13388 421 ILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAFLA-AQPDLGTKAWPRYVRIAADLPSTATNKVLKRE 499
|
..
gi 839746169 615 LR 616
Cdd:PRK13388 500 LI 501
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
104-617 |
7.40e-21 |
|
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: 95.96 E-value: 7.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 104 QSKHITYRELHADVCRFANVLLD-LGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRL 182
Cdd:cd05937 2 EGKTWTYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 183 VItadeglragraiplkknVDDalknpnvnsiehvvvlkrtggkidwqegrdlwwsdlmanasaehrpvemnaEDPLFIL 262
Cdd:cd05937 82 VI-----------------VDP---------------------------------------------------DDPAILI 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 263 YTSGSTGKPKGVLHTTGGYLVyAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLM---FEGVPNWPtp 339
Cdd:cd05937 94 YTSGTTGLPKAAAISWRRTLV-TSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALsrkFSASQFWK-- 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 340 armcQVVDKHKVSILYTAPTaIRALMAegdKAIEGTDRSSlRILGSVGEPINPEAWEWYWKKIGnekCPVMD-------- 411
Cdd:cd05937 171 ----DVRDSGATIIQYVGEL-CRYLLS---TPPSPYDRDH-KVRVAWGNGLRPDIWERFRERFN---VPEIGefyaateg 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 412 --TWWQTETGGFMItplpGAIELKaGSATRPFFGVQPVLVD---NEGLPL-DGATEGNLAIADSWPGQA--RTLFGDHER 483
Cdd:cd05937 239 vfALTNHNVGDFGA----GAIGHH-GLIRRWKFENQVVLVKmdpETDDPIrDPKTGFCVRAPVGEPGEMlgRVPFKNREA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 484 FeQTYFSTFK--------------NMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVV 548
Cdd:cd05937 314 F-QGYLHNEDatesklvrdvfrkgDIYFrTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVY 392
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 839746169 549 GI--PHNiKGQAIYAYVTL-NHGEEPTPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05937 393 GVkvPGH-DGRAGCAAITLeESSAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
108-549 |
1.52e-20 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 95.95 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 108 ITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVITAD 187
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAED 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 188 EglragraiplkKNVDDALK-NPNVNSIEHVVVLKRTGGKiDWQEGRDLWWSDLMANASAEHRP---------VEMNAED 257
Cdd:cd17641 92 E-----------EQVDKLLEiADRIPSVRYVIYCDPRGMR-KYDDPRLISFEDVVALGRALDRRdpglyerevAAGKGED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 258 PLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKyvFDY-HPGDIYWCTADVGWVTGHSYLLYGPLACG--------ATTL 328
Cdd:cd17641 160 VAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLA--ADPlGPGDEYVSVLPLPWIGEQMYSVGQALVCGfivnfpeePETM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 329 M-----------------FEGVPNwPTPARMC------QVVDKHKVSILYTA----------PTAIRALMAEGDKAIEGT 375
Cdd:cd17641 238 MedlreigptfvllpprvWEGIAA-DVRARMMdatpfkRFMFELGMKLGLRAldrgkrgrpvSLWLRLASWLADALLFRP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 376 DR-----SSLRILGSVGEPINPEAWEWYwKKIGnekCPVMDTWWQTEtggfmitpLPGAIELKAGSATRPffgvqpvlvD 450
Cdd:cd17641 317 LRdrlgfSRLRSAATGGAALGPDTFRFF-HAIG---VPLKQLYGQTE--------LAGAYTVHRDGDVDP---------D 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 451 NEGLPLDGAtegNLAIADSWPGQART--LF-GDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVS-GH 525
Cdd:cd17641 376 TVGVPFPGT---EVRIDEVGEILVRSpgVFvGYYKNPEATAEDFDEDGWLhTGDAGYFKENGHLVVIDRAKDVGTTSdGT 452
|
490 500
....*....|....*....|....
gi 839746169 526 RLGTAEIESALVSHPKIAEAAVVG 549
Cdd:cd17641 453 RFSPQFIENKLKFSPYIAEAVVLG 476
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
82-615 |
3.00e-20 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 96.39 E-value: 3.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 82 LDRHLAERGDQTAIIWEGDDasqskhITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSV 161
Cdd:PRK05691 1137 LNEQARQTPERIALVWDGGS------LDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVP 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 162 IFGGFSPEAVAGRIIDSSSRLVITADEGLRAgraiplkknvddalknpnVNSIEHVVVLKRTGGKIDWqegrdlwWSDlm 241
Cdd:PRK05691 1211 LDPDYPAERLAYMLADSGVELLLTQSHLLER------------------LPQAEGVSAIALDSLHLDS-------WPS-- 1263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 242 anasaeHRP-VEMNAEDPLFILYTSGSTGKPKGVLHTTGGY---LVYAATTfkYVFDyhPGDIYWCTADVGWVTGhSYLL 317
Cdd:PRK05691 1264 ------QAPgLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALaerLQWMQAT--YALD--DSDVLMQKAPISFDVS-VWEC 1332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 318 YGPLACGATtLMFEGVPNWPTPARMCQVVDKHKVSILYTAPTAIRALMAEGDKAiegtDRSSLRILGSVGEPINPEAWEW 397
Cdd:PRK05691 1333 FWPLITGCR-LVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAA----ACTSLRRLFSGGEALPAELRNR 1407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 398 YWKKI---------GNEKCPVMDTWWQTETGGFMITPLpgaielkagsaTRPFFGVQPVLVDNEGLPLDGATEGNLAIAD 468
Cdd:PRK05691 1408 VLQRLpqvqlhnryGPTETAINVTHWQCQAEDGERSPI-----------GRPLGNVLCRVLDAELNLLPPGVAGELCIGG 1476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 469 SwpGQARTLFG----DHERF-EQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIA 543
Cdd:PRK05691 1477 A--GLARGYLGrpalTAERFvPDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVA 1554
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 839746169 544 EAAVVgIPHNIKGQAIYAYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK05691 1555 QAAVL-VREGAAGAQLVGYYTGEAGQEAEAE---RLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
82-615 |
8.54e-20 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 94.34 E-value: 8.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 82 LDRHLAERGDQTAIIWEGDdasqskHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSV 161
Cdd:PRK10252 464 VAQQAAKTPDAPALADARY------QFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 162 IFGGFSPEAVAGRIIDSSSRLVITADEGLRAGRAIPlkknvDDALKNPNVnsiehvvvlkrtggkidwqegrdlWWSDLM 241
Cdd:PRK10252 538 LDTGYPDDRLKMMLEDARPSLLITTADQLPRFADVP-----DLTSLCYNA------------------------PLAPQG 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 242 ANASAEHRPvemnaEDPLFILYTSGSTGKPKGVL--HTTggyLV---------YAATTFKYVFDYHPgdiywCTADVG-W 309
Cdd:PRK10252 589 AAPLQLSQP-----HHTAYIIFTSGSTGRPKGVMvgQTA---IVnrllwmqnhYPLTADDVVLQKTP-----CSFDVSvW 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 310 VtghsylLYGPLACGATTLMFEgvpnwPT----PARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGTDRSSLRILGS 385
Cdd:PRK10252 656 E------FFWPFIAGAKLVMAE-----PEahrdPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVFC 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 386 VGEPINPE---AWE-WYWKKIGNEKCP----VMDTWWqtetggfmitPLPGAIELKAGSAT----RPFFGVQPVLVDNEG 453
Cdd:PRK10252 725 SGEALPADlcrEWQqLTGAPLHNLYGPteaaVDVSWY----------PAFGEELAAVRGSSvpigYPVWNTGLRILDARM 794
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 454 LPLDGATEGNLAIAdswpG-Q-ARTLFG----DHERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRL 527
Cdd:PRK10252 795 RPVPPGVAGDLYLT----GiQlAQGYLGrpdlTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRI 870
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 528 GTAEIESALVSHPKIAEAAVV------GIPHNIKGQAIYAYVTLNHGEeptPELYAEVRNWVRKEIGPLATPDVLHWTDS 601
Cdd:PRK10252 871 ELGEIDRAMQALPDVEQAVTHacvinqAAATGGDARQLVGYLVSQSGL---PLDTSALQAQLRERLPPHMVPVVLLQLDQ 947
|
570
....*....|....
gi 839746169 602 LPKTRSGKIMRRIL 615
Cdd:PRK10252 948 LPLSANGKLDRKAL 961
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
82-616 |
2.68e-19 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 91.62 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 82 LDRHLAERGDQTAIIwegddaSQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSV 161
Cdd:PRK07059 29 LEESFRQYADRPAFI------CMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 162 IFGGFSPEAVAGRIIDSSSRlvitadeglragrAIPLKKN----VDDALKNPNVnsiEHVVV--------LK-------- 221
Cdd:PRK07059 103 VNPLYTPRELEHQLKDSGAE-------------AIVVLENfattVQQVLAKTAV---KHVVVasmgdllgFKghivnfvv 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 222 RTGGKI--DWQEGRDLWWSD-LMANASAEHRPVEMNAEDPLFILYTSGSTGKPKG--VLHT--------TGGYLVYAATT 288
Cdd:PRK07059 167 RRVKKMvpAWSLPGHVRFNDaLAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGatLLHRnivanvlqMEAWLQPAFEK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 289 FKYVFD---------YHpgdIYWCTAdvgwvtghSYLLygPLACGATTLMfegVPNWPTPARMCQVVDKHKVSILYTAPT 359
Cdd:PRK07059 247 KPRPDQlnfvcalplYH---IFALTV--------CGLL--GMRTGGRNIL---IPNPRDIPGFIKELKKYQVHIFPAVNT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 360 AIRALMAEGDkaIEGTDRSSLRI-LG---SVGEPInpeAWEWYwKKIGnekCPVMDTWWQTETGGFMITPLPGAIELkAG 435
Cdd:PRK07059 311 LYNALLNNPD--FDKLDFSKLIVaNGggmAVQRPV---AERWL-EMTG---CPITEGYGLSETSPVATCNPVDATEF-SG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 436 SATRPFFGVQPVLVDNEG--LPLDGATE----GNLAIADSWpgqartlfgdhERFEQTYFSTFKNMYF-SGDGARRDEDG 508
Cdd:PRK07059 381 TIGLPLPSTEVSIRDDDGndLPLGEPGEicirGPQVMAGYW-----------NRPDETAKVMTADGFFrTGDVGVMDERG 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 509 YYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTlnhgeEPTPELY-AEVRNWVRKEI 587
Cdd:PRK07059 450 YTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVV-----KKDPALTeEDVKAFCKERL 524
|
570 580
....*....|....*....|....*....
gi 839746169 588 GPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK07059 525 TNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
261-612 |
5.22e-19 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 88.71 E-value: 5.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 261 ILYTSGSTGKPKGVL--HTTGgYLVYAAttfkyvfdyhpgdiyWCtaDVGWVT-GHSYLLYGP-----------LAC--- 323
Cdd:cd17638 5 IMFTSGTTGRSKGVMcaHRQT-LRAAAA---------------WA--DCADLTeDDRYLIINPffhtfgykagiVACllt 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 324 GATTL---MFEgvpnwptPARMCQVVDKHKVSILYTAPTAIRALMAEGDKaiEGTDRSSLRILGSVGEPINPEAWEWYWK 400
Cdd:cd17638 67 GATVVpvaVFD-------VDAILEAIERERITVLPGPPTLFQSLLDHPGR--KKFDLSSLRAAVTGAATVPVELVRRMRS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 401 KIGNEKcpVMDTWWQTETGGFMITPLPGAIELKAGSATRPFFGVQPVLVDNEGLPLDGategnlaiadswPGQARTLFGD 480
Cdd:cd17638 138 ELGFET--VLTAYGLTEAGVATMCRPGDDAETVATTCGRACPGFEVRIADDGEVLVRG------------YNVMQGYLDD 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 481 HERFEQTYFStfKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIY 560
Cdd:cd17638 204 PEATAEAIDA--DGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGK 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 839746169 561 AYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17638 282 AFVVARPGVTLTEE---DVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
82-620 |
6.87e-19 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 90.43 E-value: 6.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 82 LDRHLAerGDQTAIIwegddaSQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIhsV 161
Cdd:PRK10946 31 LTRHAA--SDAIAVI------CGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--P 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 162 IFGGFSPE-----AVAGRIidsSSRLVItadeglrAGRAIPLKKNVD--DALKNpNVNSIEHVVVLKRTGGkidwqegRD 234
Cdd:PRK10946 101 VNALFSHQrselnAYASQI---EPALLI-------ADRQHALFSDDDflNTLVA-EHSSLRVVLLLNDDGE-------HS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 235 LwwSDLMANASAEHRPVEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLvYAATTFKYVFDYHPGDIYWCTADvgwvTGHS 314
Cdd:PRK10946 163 L--DDAINHPAEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYY-YSVRRSVEICGFTPQTRYLCALP----AAHN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 315 YLLYGPLA-----CGATTLMfegVPNwPTPARMCQVVDKHKVSILYTAPTA----IRALMAEGDKAiegtDRSSLRILgS 385
Cdd:PRK10946 236 YPMSSPGAlgvflAGGTVVL---APD-PSATLCFPLIEKHQVNVTALVPPAvslwLQAIAEGGSRA----QLASLKLL-Q 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 386 VGEPINPEAWEwywKKIGNE-KCPVMDTWWQTEtGGFMITPLPGAIELKAGSATRPFFGVQPV-LVDNEGLPLDGATEGN 463
Cdd:PRK10946 307 VGGARLSETLA---RRIPAElGCQLQQVFGMAE-GLVNYTRLDDSDERIFTTQGRPMSPDDEVwVADADGNPLPQGEVGR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 464 LAIADSW--------PGQARTLFgDHERFeqtyfstfknmYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESA 535
Cdd:PRK10946 383 LMTRGPYtfrgyyksPQHNASAF-DANGF-----------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENL 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 536 LVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPtpelyAEVRNWVRKE-IGPLATPDVLHWTDSLPKTRSGKIMRRI 614
Cdd:PRK10946 451 LLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKA-----VQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQ 525
|
....*.
gi 839746169 615 LRKIAA 620
Cdd:PRK10946 526 LRQWLA 531
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
84-620 |
1.65e-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: 88.75 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 84 RHLAERGDQTAI-IWEGDdasqskhITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGaihsvi 162
Cdd:cd05918 7 ERARSQPDAPAVcAWDGS-------LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAG------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 163 fGGF---SPEAVAGR----IIDSSSRLVITADeglragraiplkknvddalknpnvnsiehvvvlkrtggkidwqegrdl 235
Cdd:cd05918 74 -GAFvplDPSHPLQRlqeiLQDTGAKVVLTSS------------------------------------------------ 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 236 wwsdlmanasaehrpvemnAEDPLFILYTSGSTGKPKGVL--HTTggyLVYAATTFKYVFDYHPG-----------DIyw 302
Cdd:cd05918 105 -------------------PSDAAYVIFTSGSTGKPKGVVieHRA---LSTSALAHGRALGLTSEsrvlqfasytfDV-- 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 303 CTADVgwvtghsyllYGPLACGATTLmfegVP-NWPTPARMCQVVDKHKVSILYTAPTAIRALMAEgdkaiegtDRSSLR 381
Cdd:cd05918 161 SILEI----------FTTLAAGGCLC----IPsEEDRLNDLAGFINRLRVTWAFLTPSVARLLDPE--------DVPSLR 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 382 ILGSVGEPINPEawewywkkignekcpVMDTWWQ----------TETGGFMITPLPGAIElKAGSATRPfFGVQPVLVDN 451
Cdd:cd05918 219 TLVLGGEALTQS---------------DVDTWADrvrlinaygpAECTIAATVSPVVPST-DPRNIGRP-LGATCWVVDP 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 452 EG----LPLdGATeGNLAIADswPGQARtlfGDHERFEQTYFSTFKN--------------MYFSGDGARRDEDG--YYw 511
Cdd:cd05918 282 DNhdrlVPI-GAV-GELLIEG--PILAR---GYLNDPEKTAAAFIEDpawlkqegsgrgrrLYRTGDLVRYNPDGslEY- 353
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 512 iTGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGI--PHNIKGQAIYAYVTLNHGEEPTPELYAEVRNWVRKEIGP 589
Cdd:cd05918 354 -VGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVvkPKDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDEFRA 432
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 839746169 590 LAT---------------PDVLHWTDSLPKTRSGKIMRRILRKIAA 620
Cdd:cd05918 433 LVAelrsklrqrlpsymvPSVFLPLSHLPLTASGKIDRRALRELAE 478
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
260-615 |
6.00e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 88.69 E-value: 6.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 260 FILYTSGSTGKPKGVLHTTGGYLVYAATTFKyVFDYHPGD----IYWCTADVGwvtghSYLLYGPLACGATtLMFEGVPN 335
Cdd:PRK05691 2337 YLIYTSGSTGKPKGVVVSHGEIAMHCQAVIE-RFGMRADDcelhFYSINFDAA-----SERLLVPLLCGAR-VVLRAQGQ 2409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 336 WPTpARMCQVVDKHKVSILYTAPT----AIRALMAEGDkaiegtdRSSLRILGSVGEPINPEawewYWKKIGNEKCP--V 409
Cdd:PRK05691 2410 WGA-EEICQLIREQQVSILGFTPSygsqLAQWLAGQGE-------QLPVRMCITGGEALTGE----HLQRIRQAFAPqlF 2477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 410 MDTWWQTETggfMITPL--PGAIELKAGSATRPF---FG--VQPVLVDNEGLPLDGATeGNLAIADSwpGQARtlfGDH- 481
Cdd:PRK05691 2478 FNAYGPTET---VVMPLacLAPEQLEEGAASVPIgrvVGarVAYILDADLALVPQGAT-GELYVGGA--GLAQ---GYHd 2548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 482 ------ERFEQTYFSTFK-NMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIpHNI 554
Cdd:PRK05691 2549 rpgltaERFVADPFAADGgRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTP 2627
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 839746169 555 KGQAIYAYV---TLNHGEEPTPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK05691 2628 SGKQLAGYLvsaVAGQDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
106-616 |
8.90e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 87.13 E-value: 8.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 106 KHITYRELHADVCRFANVLLDL-GIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSR-LV 183
Cdd:PRK05677 48 KTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKaLV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 184 ITADEGLRAGRAIP-------LKKNVDDAL---KNPNVNS-IEHVvvlKRTGGKIDWQEGRDLwwSDLMANASAEH-RPV 251
Cdd:PRK05677 128 CLANMAHLAEKVLPktgvkhvIVTEVADMLpplKRLLINAvVKHV---KKMVPAYHLPQAVKF--NDALAKGAGQPvTEA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 252 EMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVyaattfkyvfdyhpGDIYWCTADVGWVTGHS----------YLLYG-P 320
Cdd:PRK05677 203 NPQADDVAVLQYTGGTTGVAKGAMLTHRN-LV--------------ANMLQCRALMGSNLNEGceiliaplplYHIYAfT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 321 LACGATTLMFEG---VPNWPTPARMCQVVDKHKVSILYTAPTAIRALMaeGDKAIEGTDRSSLRILGSVGEPINPEAWEw 397
Cdd:PRK05677 268 FHCMAMMLIGNHnilISNPRDLPAMVKELGKWKFSGFVGLNTLFVALC--NNEAFRKLDFSALKLTLSGGMALQLATAE- 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 398 YWKKIGNekCPVMDTWWQTETGGFMITPLPGAIELkaGSATRPFFGVQPVLVDNEGLPLDGATEGNLAIADSwpgqaRTL 477
Cdd:PRK05677 345 RWKEVTG--CAICEGYGMTETSPVVSVNPSQAIQV--GTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGP-----QVM 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 478 FGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKG 556
Cdd:PRK05677 416 KGYWQRPEATDEILDSDGWLkTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSG 495
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 557 QAIYAYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK05677 496 EAIKVFVVVKPGETLTKE---QVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
82-616 |
1.25e-17 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 86.65 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 82 LDRHLAERGDQTAIIWEGddasqsKHITYRELHADVCRFANVLL-DLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHS 160
Cdd:PRK08974 29 FEQAVARYADQPAFINMG------EVMTFRKLEERSRAFAAYLQnGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 161 VIFGGFSPEAVAGRIIDSSSR-LVITADeglragRAIPLKKNVD-------------DALKNPNVNSIEHVV-VLKRTGG 225
Cdd:PRK08974 103 NVNPLYTPRELEHQLNDSGAKaIVIVSN------FAHTLEKVVFktpvkhviltrmgDQLSTAKGTLVNFVVkYIKRLVP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 226 KIDW----------QEGRDLWWSdlmanasaehRPvEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLvyaATTFKYVFDY 295
Cdd:PRK08974 177 KYHLpdaisfrsalHKGRRMQYV----------KP-ELVPEDLAFLQYTGGTTGVAKGAMLTHRNML---ANLEQAKAAY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 296 ----HPGDIYWCTAdvgwvtghsYLLYGPLACGATTLMFegvpnwptparmcqvVDKHKVSILYTAPTAIRALMAEGDK- 370
Cdd:PRK08974 243 gpllHPGKELVVTA---------LPLYHIFALTVNCLLF---------------IELGGQNLLITNPRDIPGFVKELKKy 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 371 ---AIEGT----------------DRSSLRILGSVGEPINPEAWEwYWKKIgnEKCPVMDTWWQTETGGfMITPLPGAIE 431
Cdd:PRK08974 299 pftAITGVntlfnallnneefqelDFSSLKLSVGGGMAVQQAVAE-RWVKL--TGQYLLEGYGLTECSP-LVSVNPYDLD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 432 LKAGSATRPFFGVQPVLVDNEG--LPLDGATEgnlaiadSWPGQARTLFGDHERFEQTYfSTFKNMYFS-GDGARRDEDG 508
Cdd:PRK08974 375 YYSGSIGLPVPSTEIKLVDDDGneVPPGEPGE-------LWVKGPQVMLGYWQRPEATD-EVIKDGWLAtGDIAVMDEEG 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 509 YYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHgEEPTPElyaEVRNWVRKEIG 588
Cdd:PRK08974 447 FLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKD-PSLTEE---ELITHCRRHLT 522
|
570 580
....*....|....*....|....*...
gi 839746169 589 PLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK08974 523 GYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
104-612 |
2.94e-17 |
|
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: 84.80 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 104 QSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLV 183
Cdd:cd05914 4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 184 ITADEglragraiplkknvddalknpnvnsiehvvvlkrtggkidwqegrdlwwsdlmanasaehrpvemnaEDPLFILY 263
Cdd:cd05914 84 FVSDE-------------------------------------------------------------------DDVALINY 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 264 TSGSTGKPKGVLhTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTL--------------M 329
Cdd:cd05914 97 TSGTTGNSKGVM-LTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVfldkipsakiialaF 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 330 FEGVPNWPTPaRMCQVVDKHKVSI------------LYTAPTAIRALMAEGDKAIEGTDrSSLRILGSVGEPINPEAwEW 397
Cdd:cd05914 176 AQVTPTLGVP-VPLVIEKIFKMDIipkltlkkfkfkLAKKINNRKIRKLAFKKVHEAFG-GNIKEFVIGGAKINPDV-EE 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 398 YWKKIGnekCPVMDTWWQTETGGFMITPLPGaiELKAGSATRPFFGVQpVLVDNeglPLDGATEGNLAIADSwpgqaRTL 477
Cdd:cd05914 253 FLRTIG---FPYTIGYGMTETAPIISYSPPN--RIRLGSAGKVIDGVE-VRIDS---PDPATGEGEIIVRGP-----NVM 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 478 FGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDV-LNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIK 555
Cdd:cd05914 319 KGYYKNPEATAEAFDKDGWFhTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLV 398
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 839746169 556 GQAIYAYVTLNHGEEPTPELYAEVRNWVRKEIGpLATP------DVLHWTDSLPKTRSGKIMR 612
Cdd:cd05914 399 ALAYIDPDFLDVKALKQRNIIDAIKWEVRDKVN-QKVPnykkisKVKIVKEEFEKTPKGKIKR 460
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
108-619 |
6.73e-17 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 84.10 E-value: 6.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 108 ITYRELHADVCRFANVL---LDLgiKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVI 184
Cdd:PRK12492 50 LSYAELERHSAAFAAYLqqhTDL--VPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 185 ---------------TADEGL---RAGRAIPLKKNvddALKNPNVNSIEHVV----VLKRTGGKIDWQEGRDLwwsdlma 242
Cdd:PRK12492 128 ylnmfgklvqevlpdTGIEYLieaKMGDLLPAAKG---WLVNTVVDKVKKMVpayhLPQAVPFKQALRQGRGL------- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 243 nasaEHRPVEMNAEDPLFILYTSGSTGKPKGVLHTTGGYL-----VYAA---------TTFKYVFD--------YHpgdI 300
Cdd:PRK12492 198 ----SLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVanmlqVRAClsqlgpdgqPLMKEGQEvmiaplplYH---I 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 301 YWCTADVG--WVTG-HSYLLYGPLACGAttlmfegvpnwptparMCQVVDKHKVSILYTAPTAIRALMAEGDkaIEGTDR 377
Cdd:PRK12492 271 YAFTANCMcmMVSGnHNVLITNPRDIPG----------------FIKELGKWRFSALLGLNTLFVALMDHPG--FKDLDF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 378 SSLRILGSVGEPINPEAWEwYWKKIGNekCPVMDTWWQTETGGFMITPlPGAIELKAGSATRPFFGVQPVLVDNEGLPLD 457
Cdd:PRK12492 333 SALKLTNSGGTALVKATAE-RWEQLTG--CTIVEGYGLTETSPVASTN-PYGELARLGTVGIPVPGTALKVIDDDGNELP 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 458 GATEGNLAIADSwpgqaRTLFGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESAL 536
Cdd:PRK12492 409 LGERGELCIKGP-----QVMKGYWQQPEATAEALDAEGWFkTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVV 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 537 VSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPELYAevrnWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK12492 484 MAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVEELKA----YCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
...
gi 839746169 617 KIA 619
Cdd:PRK12492 560 DIA 562
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
87-618 |
9.65e-17 |
|
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: 83.87 E-value: 9.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 87 AERGDQTAIIWEGDDASQSKhITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACarigaihsvIFGGF 166
Cdd:cd05906 20 AERGPTKGITYIDADGSEEF-QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWAC---------VLAGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 167 SPeavagriidsssrlvitadeglragraIPLKKNVDDALKNPNVNSIEHV-------VVLKRTGG--KIDWQEGRDLW- 236
Cdd:cd05906 90 VP---------------------------APLTVPPTYDEPNARLRKLRHIwqllgspVVLTDAELvaEFAGLETLSGLp 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 237 ------WSDLMANASAEHRPVEmNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKyVFDYHPGDIY--WCTAD-- 306
Cdd:cd05906 143 girvlsIEELLDTAADHDLPQS-RPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQ-HNGLTPQDVFlnWVPLDhv 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 307 VGWVTGHSYLLYgpLACG----ATTLMFEGVPNWptparmCQVVDKHKVSILYtAPTAIRALMAEGDKAIEGT--DRSSL 380
Cdd:cd05906 221 GGLVELHLRAVY--LGCQqvhvPTEEILADPLRW------LDLIDRYRVTITW-APNFAFALLNDLLEEIEDGtwDLSSL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 381 RILGSVGEPINPEAWEWYWKKIgnEKCPVMDT-----WWQTETGGFMI-------TPLPGAIELKagSATRPFFGVQPVL 448
Cdd:cd05906 292 RYLVNAGEAVVAKTIRRLLRLL--EPYGLPPDairpaFGMTETCSGVIysrsfptYDHSQALEFV--SLGRPIPGVSMRI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 449 VDNEGLPLDGATEGNLAIadswpgQARTLFGDHERFEQTYFSTFKN--MYFSGDGARRDeDGYYWITGRVDDVLNVSGHR 526
Cdd:cd05906 368 VDDEGQLLPEGEVGRLQV------RGPVVTKGYYNNPEANAEAFTEdgWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVN 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 527 LGTAEIESALVSHPKIAEAAVVGIPHNIKGQ-----AIYAYVTLNHgEEPTPELYAEVRNWVRKEIG-------PLAtpd 594
Cdd:cd05906 441 YYSHEIEAAVEEVPGVEPSFTAAFAVRDPGAeteelAIFFVPEYDL-QDALSETLRAIRSVVSREVGvspayliPLP--- 516
|
570 580
....*....|....*....|....
gi 839746169 595 vlhwTDSLPKTRSGKIMRRILRKI 618
Cdd:cd05906 517 ----KEEIPKTSLGKIQRSKLKAA 536
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
452-617 |
2.31e-16 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 81.24 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 452 EGLPLDGATegnLAIADSwpgqaRTLFG------------DHERF-EQTYFSTfknmyfsgDGARRDEDGYYWITGRVDD 518
Cdd:PRK07824 194 DGVPLDGVR---VRVEDG-----RIALGgptlakgyrnpvDPDPFaEPGWFRT--------DDLGALDDGVLTVLGRADD 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 519 VLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPElyaEVRNWVRKEIGPLATPDVLHW 598
Cdd:PRK07824 258 AISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLE---ALRAHVARTLDRTAAPRELHV 334
|
170
....*....|....*....
gi 839746169 599 TDSLPKTRSGKIMRRILRK 617
Cdd:PRK07824 335 VDELPRRGIGKVDRRALVR 353
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
261-615 |
5.19e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 81.20 E-value: 5.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 261 ILYTSGSTGKPKGVLHT--------------------TGGYLVYAATTFKyvfdyhpgdiywctadvGWVTGhsyLLYGP 320
Cdd:PRK13383 179 VLLTSGTTGKPKGVPRApqlrsavgvwvtildrtrlrTGSRISVAMPMFH-----------------GLGLG---MLMLT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 321 LACGATTLMFEgvpNWPTPARMCQVvDKHKVSILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWK 400
Cdd:PRK13383 239 IALGGTVLTHR---HFDAEAALAQA-SLHRADAFTAVPVVLARILELPPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMD 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 401 KIGNekcPVMDTWWQTETG-GFMITPlpgaIELKAGSAT--RPFFGVQPVLVDNEGLPLDGATEGNLAIADSWPGQARTL 477
Cdd:PRK13383 315 TYGD---ILYNGYGSTEVGiGALATP----ADLRDAPETvgKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTD 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 478 FGDHerfeqtyfSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQ 557
Cdd:PRK13383 388 GGGK--------AVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGH 459
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 839746169 558 AIYAYVTLNHGEEPTPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK13383 460 RLAAFVVLHPGSGVDA---AQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
84-551 |
9.44e-16 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 80.71 E-value: 9.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 84 RHL----AERGDQTAII----WEGDDASQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARI 155
Cdd:PRK09274 10 RHLpraaQERPDQLAVAvpggRGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 156 GAIHSVIFGGFSPEAVAGRIIDSSSRLVITadeglragraIPlKKNVDDALKNPNVNSIEHVVVlkrTGGKIDWqEGRDL 235
Cdd:PRK09274 90 GAVPVLVDPGMGIKNLKQCLAEAQPDAFIG----------IP-KAHLARRLFGWGKPSVRRLVT---VGGRLLW-GGTTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 236 wwSDLMA-NASAEHRPVEMNAEDPLFILYTSGSTGKPKGVLHTTGGYL--VYAAttfKYVFDYHPGDIYWCTADVgwvtg 312
Cdd:PRK09274 155 --ATLLRdGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEaqIEAL---REDYGIEPGEIDLPTFPL----- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 313 hsYLLYGPlACGATTLmfegVPNW-PT------PARMCQVVDKHKVSILYTAPTAIRALMAEGdkaiEGTDRS--SLRIL 383
Cdd:PRK09274 225 --FALFGP-ALGMTSV----IPDMdPTrpatvdPAKLFAAIERYGVTNLFGSPALLERLGRYG----EANGIKlpSLRRV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 384 GSVGEPINPEAWEWYwKKIGNEKCPVMDTWWQTETggfmitpLPGA-IELKA-----GSATRPFFGvqpVLVdneGLPLD 457
Cdd:PRK09274 294 ISAGAPVPIAVIERF-RAMLPPDAEILTPYGATEA-------LPISsIESREilfatRAATDNGAG---ICV---GRPVD 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 458 GATEGNLAIAD----SWpGQARTLF----------GDHerFEQTYF----STFKN------------MyfsGDGARRDED 507
Cdd:PRK09274 360 GVEVRIIAISDapipEW-DDALRLAtgeigeivvaGPM--VTRSYYnrpeATRLAkipdgqgdvwhrM---GDLGYLDAQ 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 839746169 508 GYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIP 551
Cdd:PRK09274 434 GRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVG 477
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
82-619 |
1.21e-15 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 80.27 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 82 LDRHLAERGDQTAIIWEgddasqSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSV 161
Cdd:PLN02479 26 LERAAVVHPTRKSVVHG------SVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNC 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 162 IFGGFSPEAVAGRIIDSSSRLVIT-------ADEGLR--AGRAI-----PL----------KKNVDDALKNpnvNSIEHV 217
Cdd:PLN02479 100 VNIRLNAPTIAFLLEHSKSEVVMVdqefftlAEEALKilAEKKKssfkpPLlivigdptcdPKSLQYALGK---GAIEYE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 218 VVLKRTGGKIDWQEGRDLWWSDLMAnasaehrpvemnaedplfilYTSGSTGKPKGV-LHTTGGYLvyAATTFKYVFDYH 296
Cdd:PLN02479 177 KFLETGDPEFAWKPPADEWQSIALG--------------------YTSGTTASPKGVvLHHRGAYL--MALSNALIWGMN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 297 PGDIYWCTADVGWVTGHSYLLYGPLACGaTTLMFEGVpnwpTPARMCQVVDKHKVSILYTAPTAIRALmaegdkaiegtd 376
Cdd:PLN02479 235 EGAVYLWTLPMFHCNGWCFTWTLAALCG-TNICLRQV----TAKAIYSAIANYGVTHFCAAPVVLNTI------------ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 377 rsslrILGSVGEPINPEAWEWYWKKIGNEKCPVMdtWWQTETGGFMITPLPGAIELKAGS---ATRPFFGVQPVL----- 448
Cdd:PLN02479 298 -----VNAPKSETILPLPRVVHVMTAGAAPPPSV--LFAMSEKGFRVTHTYGLSETYGPStvcAWKPEWDSLPPEeqarl 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 449 --------VDNEGL-----------PLDGATEGNLAIADS--WPGQARTLFGDHERFEQTYFStfknmyfSGDGARRDED 507
Cdd:PLN02479 371 narqgvryIGLEGLdvvdtktmkpvPADGKTMGEIVMRGNmvMKGYLKNPKANEEAFANGWFH-------SGDLGVKHPD 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 508 GYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPE--LYAEVRNWVRK 585
Cdd:PLN02479 444 GYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEaaLAEDIMKFCRE 523
|
570 580 590
....*....|....*....|....*....|....
gi 839746169 586 EIGPLATPDVLHWtDSLPKTRSGKIMRRILRKIA 619
Cdd:PLN02479 524 RLPAYWVPKSVVF-GPLPKTATGKIQKHVLRAKA 556
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
257-608 |
4.35e-15 |
|
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: 76.96 E-value: 4.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 257 DPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYwctadvgwvtghsyLLYGPL------ACGATTLMF 330
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQA-LLAQALVLAVLQAIDEGTVF--------------LNSGPLfhigtlMFTLATFHA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 331 EG----VPNWpTPARMCQVVDKHKVSILY-TAPT--AIRALMAEGdkaieGTDRSSLRILgsvgepinPEAWEWywkkig 403
Cdd:cd17636 66 GGtnvfVRRV-DAEEVLELIEAERCTHAFlLPPTidQIVELNADG-----LYDLSSLRSS--------PAAPEW------ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 404 NEKCPVMDTWW--------QTETGGFMITPLPGaiELKAGSATRPFFGVQPVLVDNEG--LPlDGAT-----EGNLAIAD 468
Cdd:cd17636 126 NDMATVDTSPWgrkpggygQTEVMGLATFAALG--GGAIGGAGRPSPLVQVRILDEDGreVP-DGEVgeivaRGPTVMAG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 469 SW--PG--QARTLFGDHErfeqtyfstfknmyfSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAE 544
Cdd:cd17636 203 YWnrPEvnARRTRGGWHH---------------TNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVAD 267
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 839746169 545 AAVVGIPHNIKGQAIYAYVTLNHGEEPTPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSG 608
Cdd:cd17636 268 AAVIGVPDPRWAQSVKAIVVLKPGASVTE---AELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
108-617 |
6.52e-15 |
|
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: 77.39 E-value: 6.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 108 ITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIidsssrlvitad 187
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCL------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 188 eglragraiplkknvddalknpNVNSIEHVVVlkrtggkidwqegrdlwwsdlmanasaehrpvemnaeDPLFILYTSGS 267
Cdd:cd05940 72 ----------------------NVSSAKHLVV-------------------------------------DAALYIYTSGT 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 268 TGKPKGVLHTTGGYLvYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLM---FEGVPNWPTparmcq 344
Cdd:cd05940 93 TGLPKAAIISHRRAW-RGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIrkkFSASNFWDD------ 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 345 vVDKHKVSILYTAPTAIRALMAEgdKAIEGTDRSSLRILgsVGEPINPEAWEWYWKKIGNEKcpVMDTWWQTE--TGGFM 422
Cdd:cd05940 166 -IRKYQATIFQYIGELCRYLLNQ--PPKPTERKHKVRMI--FGNGLRPDIWEEFKERFGVPR--IAEFYAATEgnSGFIN 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 423 ITPLPGAIElKAGSATRPFFGVQPVLVDNE-GLPLDGATEGNLAIADSWPGQARTLFGDHERF----------EQTYFST 491
Cdd:cd05940 239 FFGKPGAIG-RNPSLLRKVAPLALVKYDLEsGEPIRDAEGRCIKVPRGEPGLLISRINPLEPFdgytdpaateKKILRDV 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 492 FK--NMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIP-HNIKGQAIYAYVTLNH 567
Cdd:cd05940 318 FKkgDAWFnTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvPGTDGRAGMAAIVLQP 397
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 839746169 568 GEEPTPELYAevrNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05940 398 NEEFDLSALA---AHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
237-584 |
1.92e-14 |
|
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: 76.35 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 237 WSDLMANASAEHRPVEMNAEDPLFILYTSGSTGKPKGVLHTTGGYlVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYL 316
Cdd:cd05932 118 WDDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSF-AWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 317 LYGPLACGATTLMFEGVPNWPTPARMCQ-----------------VVDK---HKVSILYTAPTaIRALMaeGDKAIEGTD 376
Cdd:cd05932 197 EGGSLYGGVLVAFAESLDTFVEDVQRARptlffsvprlwtkfqqgVQDKipqQKLNLLLKIPV-VNSLV--KRKVLKGLG 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 377 RSSLRILGSVGEPINPEAWEWYwKKIGnekCPVMDTWWQTETGGFMITPLPGaiELKAGSATRPFFGVQpvlvdneglpl 456
Cdd:cd05932 274 LDQCRLAGCGSAPVPPALLEWY-RSLG---LNILEAYGMTENFAYSHLNYPG--RDKIGTVGNAGPGVE----------- 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 457 dgategnLAIADSWPGQAR---TLFGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVS-GHRLGTAE 531
Cdd:cd05932 337 -------VRISEDGEILVRspaLMMGYYKDPEATAEAFTADGFLrTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAP 409
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 839746169 532 IESALVSHPKIAEAAVVG--IPHNIkgqaiyAYVTLNhgEEPTPELYAEVRNWVR 584
Cdd:cd05932 410 IENKLAEHDRVEMVCVIGsgLPAPL------ALVVLS--EEARLRADAFARAELE 456
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
106-615 |
2.63e-14 |
|
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: 75.51 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 106 KHITYRELHADVCRFANVLLDLG-IKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVI 184
Cdd:cd17648 11 KRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDTGARVVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 185 TadeglragraiplkknvddalknpnvnsiehvvvlkrtggkidwqegrdlwwsdlmanasaehrpvemNAEDPLFILYT 264
Cdd:cd17648 91 T--------------------------------------------------------------------NSTDLAYAIYT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 265 SGSTGKPKGVLHTTGG-----------YLV----YAATTF--KYVFDYHpgdIYWCTADVgwVTGHSYLLYGPlacgatt 327
Cdd:cd17648 103 SGTTGKPKGVLVEHGSvvnlrtslserYFGrdngDEAVLFfsNYVFDFF---VEQMTLAL--LNGQKLVVPPD------- 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 328 lmfEGVPnwpTPARMCQVVDKHKVSILYTAPTAIralmaegdKAIEGTDRSSLRILGSVGEPINPEAWEwywKKIGNEKC 407
Cdd:cd17648 171 ---EMRF---DPDRFYAYINREKVTYLSGTPSVL--------QQYDLARLPHLKRVDAAGEEFTAPVFE---KLRSRFAG 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 408 PVMDTWWQTETGGF-MITPLPGAiELKAGSATRPFFGVQP-VLVDN-EGLPLdGATeGNLAIADSwpGQARtlfGDH--- 481
Cdd:cd17648 234 LIINAYGPTETTVTnHKRFFPGD-QRFDKSLGRPVRNTKCyVLNDAmKRVPV-GAV-GELYLGGD--GVAR---GYLnrp 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 482 ----ERFEQTYFST--------FKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVG 549
Cdd:cd17648 306 eltaERFLPNPFQTeqerargrNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVA 385
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 839746169 550 IPHNIKGQA-----IYAYVTLNhgEEPTPElyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17648 386 KEDASQAQSriqkyLVGYYLPE--PGHVPE--SDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
106-617 |
5.21e-14 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 74.77 E-value: 5.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 106 KHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVIT 185
Cdd:cd05939 2 RHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 186 adeglragraiplkknvddalknpnvnsiEHVVVLKRTggkidwqegrdlwwsdlmanaSAEHRP--VEMNAEDPLFILY 263
Cdd:cd05939 82 -----------------------------NLLDPLLTQ---------------------SSTEPPsqDDVNFRDKLFYIY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 264 TSGSTGKPKGVLHTTGGYLVYAATTFkYVFDYHPGDI-YWC-----TAdvGWVTGHSYLLYGplacGATTLM---FEGVP 334
Cdd:cd05939 112 TSGTTGLPKAAVIVHSRYYRIAAGAY-YAFGMRPEDVvYDClplyhSA--GGIMGVGQALLH----GSTVVIrkkFSASN 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 335 NWptpaRMCqvvDKHKVSILYTAPTAIRALMAEgdKAIEGTDRSSLRILgsVGEPINPEAWEWYWKKIGNEK-------- 406
Cdd:cd05939 185 FW----DDC---VKYNCTIVQYIGEICRYLLAQ--PPSEEEQKHNVRLA--VGNGLRPQIWEQFVRRFGIPQigefygat 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 407 ---CPVMDTWWQTETGGFMITPLPGaielkagsatrpFFGVQPVLVDNEGLPLDGATEGnLAIAdSWPGQARTLFG---- 479
Cdd:cd05939 254 egnSSLVNIDNHVGACGFNSRILPS------------VYPIRLIKVDEDTGELIRDSDG-LCIP-CQPGEPGLLVGkiiq 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 480 ---------------DHERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAE 544
Cdd:cd05939 320 ndplrrfdgyvnegaTNKKIARDVFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLED 399
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 839746169 545 AAVVG--IPHnIKGQAIYAYVTLNHGEEPTPELYAEvrnwVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05939 400 VVVYGveVPG-VEGRAGMAAIVDPERKVDLDRFSAV----LAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
429-616 |
2.28e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 73.20 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 429 AIELKAGsatRPFFGVQPVLVDNEG--LPLDGATEGNLAIADSWPGQaRTLFGDHERFEQTYFSTfknmyfsGDGARRDE 506
Cdd:PRK07008 353 KLLEKQG---RVIYGVDMKIVGDDGreLPWDGKAFGDLQVRGPWVID-RYFRGDASPLVDGWFPT-------GDVATIDA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 507 DGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPElyaEVRNWVRKE 586
Cdd:PRK07008 422 DGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTRE---ELLAFYEGK 498
|
170 180 190
....*....|....*....|....*....|
gi 839746169 587 IGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK07008 499 VAKWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
255-580 |
4.17e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 68.64 E-value: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 255 AEDPLFILYTSGSTGKPKGVLHTTgGYLVYAATTFKYVFDYHPGDIYWCTADVgwvtghsYLLYGPlACGATTLMFEGVP 334
Cdd:cd05910 84 ADEPAAILFTSGSTGTPKGVVYRH-GTFAAQIDALRQLYGIRPGEVDLATFPL-------FALFGP-ALGLTSVIPDMDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 335 NWP---TPARMCQVVDKHKVSILYTAPTAIRALMAEGdkAIEGTDRSSLRILGSVGEPINPEAWEWYwKKIGNEKCPVMD 411
Cdd:cd05910 155 TRParaDPQKLVGAIRQYGVSIVFGSPALLERVARYC--AQHGITLPSLRRVLSAGAPVPIALAARL-RKMLSDEAEILT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 412 TWWQTETggfmitpLP----GAIELKA--GSATRPFFGVqpvlvdNEGLPLDGATEGNLAIAD----SWPGQARTLFGD- 480
Cdd:cd05910 232 PYGATEA-------LPvssiGSRELLAttTAATSGGAGT------CVGRPIPGVRVRIIEIDDepiaEWDDTLELPRGEi 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 481 --------------HERFEQTYFSTFKN-----MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPK 541
Cdd:cd05910 299 geitvtgptvtptyVNRPVATALAKIDDnsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPG 378
|
330 340 350
....*....|....*....|....*....|....*....
gi 839746169 542 IAEAAVVGIPHNIKGQAIYAYVTLNHGEEPTPELYAEVR 580
Cdd:cd05910 379 VRRSALVGVGKPGCQLPVLCVEPLPGTITPRARLEQELR 417
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
79-617 |
6.07e-12 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 68.67 E-value: 6.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 79 ANCLDRHLAERGDQTAIIwegddaSQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAI 158
Cdd:PLN02860 10 CQCLTRLATLRGNAVVTI------SGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 159 HSVIFGGFSPEAVAGRIIDSSSRLVITaDEG-------LRAGRAIPLKKNV-------DDALKNPNVNSIEHVvvLKRTG 224
Cdd:PLN02860 84 VAPLNYRWSFEEAKSAMLLVRPVMLVT-DETcsswyeeLQNDRLPSLMWQVflespssSVFIFLNSFLTTEML--KQRAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 225 GKIDWqegrDLWWSdlmanasaehrpvemnAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVfDYHPGDIYWCT 304
Cdd:PLN02860 161 GTTEL----DYAWA----------------PDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIV-GYGEDDVYLHT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 305 ADVGWVTGHSYLLygplacgaTTLMFEG----VPNWPTPARMcQVVDKHKVSILYTAPTAIRALMAEGDKAIEGTDRSSL 380
Cdd:PLN02860 220 APLCHIGGLSSAL--------AMLMVGAchvlLPKFDAKAAL-QAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 381 R-IL---GSVGEPINPEAWEWYWK-KIGN-----EKC----------PVMDTWWQTETGGFMITPLPGaiELKAGS---- 436
Cdd:PLN02860 291 RkILnggGSLSSRLLPDAKKLFPNaKLFSaygmtEACssltfmtlhdPTLESPKQTLQTVNQTKSSSV--HQPQGVcvgk 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 437 -ATRPFFGVQPVLVDNEGLPLdgaTEGNLAIADSWpgqARTLFGDHERFEQTYFSTfknmyfsGDGARRDEDGYYWITGR 515
Cdd:PLN02860 369 pAPHVELKIGLDESSRVGRIL---TRGPHVMLGYW---GQNSETASVLSNDGWLDT-------GDIGWIDKAGNLWLIGR 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 516 VDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHG------EEPTPE-----------LYAE 578
Cdd:PLN02860 436 SNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGwiwsdnEKENAKknltlssetlrHHCR 515
|
570 580 590
....*....|....*....|....*....|....*....
gi 839746169 579 VRNWVRKEIGPLatpdVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PLN02860 516 EKNLSRFKIPKL----FVQWRKPFPLTTTGKIRRDEVRR 550
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
412-625 |
7.23e-11 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 64.63 E-value: 7.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 412 TWWQTETGGFMITPLPGAIELKAGSATRPFFGVQPVLVDNeglpldgaTEGNLAIadswpgQARTLF-GdherfeqtYFS 490
Cdd:PRK07445 260 TYGMTETASQIATLKPDDFLAGNNSSGQVLPHAQITIPAN--------QTGNITI------QAQSLAlG--------YYP 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 491 TFKNMY---FSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNH 567
Cdd:PRK07445 318 QILDSQgifETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKD 397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 568 GeEPTPElyaEVRNWVRKEIGPLATPDvlHW--TDSLPKTRSGKIMRRILRKIAAGDTSN 625
Cdd:PRK07445 398 P-SISLE---ELKTAIKDQLSPFKQPK--HWipVPQLPRNPQGKINRQQLQQIAVQRLGL 451
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
106-549 |
7.79e-11 |
|
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: 64.69 E-value: 7.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 106 KHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVifggfspeavagriidsssrlvit 185
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVV------------------------ 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 186 adeglRAGRAiplkkNVDDALKNpnVNSIEHVVVLkrtggkidwqegrdlwwsdlmanasaehrpVEMNAEDPLFILYTS 265
Cdd:cd17640 60 -----RGSDS-----SVEELLYI--LNHSESVALV------------------------------VENDSDDLATIIYTS 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 266 GSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTADVgWvtgHSY---LLYGPLACGATTLmfegvpnWPTPARM 342
Cdd:cd17640 98 GTTGNPKGVMLTHAN-LLHQIRSLSDIVPPQPGDRFLSILPI-W---HSYersAEYFIFACGCSQA-------YTSIRTL 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 343 CQVVDKHKVSILYTAPTAIRALMAEGDKAIEGTDRSSLRILG---SVGE---PIN-----PEAWEWYWKKIGnekCPVMD 411
Cdd:cd17640 166 KDDLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLfflSGGIfkfGISgggalPPHVDTFFEAIG---IEVLN 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 412 TWWQTETGGFMITPLPGAIelKAGSATRPFFGVQPVLVDNEG---LPldgategnlaiadswPGQARTLF--GDHerFEQ 486
Cdd:cd17640 243 GYGLTETSPVVSARRLKCN--VRGSVGRPLPGTEIKIVDPEGnvvLP---------------PGEKGIVWvrGPQ--VMK 303
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 839746169 487 TYF----STFKNM----YF-SGDGARRDEDGYYWITGRVDD--VLNvSGHRLGTAEIESALVSHPKIAEAAVVG 549
Cdd:cd17640 304 GYYknpeATSKVLdsdgWFnTGDLGWLTCGGELVLTGRAKDtiVLS-NGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
69-279 |
1.15e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 64.61 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 69 WYEDGTL--NLAANCldrhlAERGDQTAI---------------------IWEGDDASQSKHITYRELHADVCRFANVLL 125
Cdd:PTZ00216 65 WYYGPNFlqRLERIC-----KERGDRRALayrpvervekevvkdadgkerTMEVTHFNETRYITYAELWERIVNFGRGLA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 126 DLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVITAdeglragraiplKKNVDDA 205
Cdd:PTZ00216 140 ELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCN------------GKNVPNL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 206 LKNPNVNSIEHVVV--LKRTGGKIDWQEGRDLWWSDLMANASAE--HRPVEM--NAEDPLFILYTSGSTGKPKGVLHTTG 279
Cdd:PTZ00216 208 LRLMKSGGMPNTTIiyLDSLPASVDTEGCRLVAWTDVVAKGHSAgsHHPLNIpeNNDDLALIMYTSGTTGDPKGVMHTHG 287
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
497-615 |
1.63e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 63.52 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 497 FSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPtpely 576
Cdd:PRK08308 294 FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDP----- 368
|
90 100 110
....*....|....*....|....*....|....*....
gi 839746169 577 AEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK08308 369 VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
107-613 |
6.53e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 61.94 E-value: 6.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 107 HITYRELHADVCRFANVLLDLGIKKGDVVAIY--MP--MVPEAAVAMLACARIGAIHSvifggfsPEAvagriidsSSRL 182
Cdd:PRK07768 29 RHTWGEVHERARRIAGGLAAAGVGPGDAVAVLagAPveIAPTAQGLWMRGASLTMLHQ-------PTP--------RTDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 183 VITADEGLRAGRAIPLKKNVddaLKNPNVNSIEhvvVLKRTGGKIDwqEGRDLWwsdlmanASAEHRPVEMNAEDPLFIL 262
Cdd:PRK07768 94 AVWAEDTLRVIGMIGAKAVV---VGEPFLAAAP---VLEEKGIRVL--TVADLL-------AADPIDPVETGEDDLALMQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 263 YTSGSTGKPKGVLHTTG-----GYLVYAATTFKYVFDYHpgdIYW--CTADVGWVTGhsylLYGPLACGA-----TTLMF 330
Cdd:PRK07768 159 LTSGSTGSPKAVQITHGnlyanAEAMFVAAEFDVETDVM---VSWlpLFHDMGMVGF----LTVPMYFGAelvkvTPMDF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 331 EGVP-NWPtparmcQVVDKHKVSILyTAPTAIRALMAE--GDKAIEGT-DRSSLRILGSVGEPINPEAWEWYW---KKIG 403
Cdd:PRK07768 232 LRDPlLWA------ELISKYRGTMT-AAPNFAYALLARrlRRQAKPGAfDLSSLRFALNGAEPIDPADVEDLLdagARFG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 404 NEKCPVMDTWWQTET---------GGFMITPLPGAIELKA--------GSATRPFFGVQPVL-------VDNEGLPLDGA 459
Cdd:PRK07768 305 LRPEAILPAYGMAEAtlavsfspcGAGLVVDEVDADLLAAlrravpatKGNTRRLATLGPPLpglevrvVDEDGQVLPPR 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 460 TEGNLAIA-DSWPGQARTLFGdherfeqtyfstFKNM------YFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEI 532
Cdd:PRK07768 385 GVGVIELRgESVTPGYLTMDG------------FIPAqdadgwLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDI 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 533 ESALVSHPKIAEAAVVGI----PHNIKGQAIYAYVTLNHGEEPTPELYAEVRNWVRKEIGplATPDVLHWTD--SLPKTR 606
Cdd:PRK07768 453 ERAAARVEGVRPGNAVAVrldaGHSREGFAVAVESNAFEDPAEVRRIRHQVAHEVVAEVG--VRPRNVVVLGpgSIPKTP 530
|
....*..
gi 839746169 607 SGKIMRR 613
Cdd:PRK07768 531 SGKLRRA 537
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
247-610 |
1.38e-09 |
|
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: 60.56 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 247 EHRPVEMNAEDPL-FILYTSGSTGKPKGVlHTTGGYLVYAATTFKYVFDYHPGDIYWCTA----DVGWVTghsylLYGPL 321
Cdd:cd17654 108 EHRHFNIRTDECLaYVIHTSGTTGTPKIV-AVPHKCILPNIQHFRSLFNITSEDILFLTSpltfDPSVVE-----IFLSL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 322 ACGATTLMfegVPNW--PTPARMCQVVDK-HKVSILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWY 398
Cdd:cd17654 182 SSGATLLI---VPTSvkVLPSKLADILFKrHRITVLQATPTLFRRFGSQSIKSTVLSATSSLRVLALGGEPFPSLVILSS 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 399 WKKIGNeKCPVMDTWWQTETGGFMITplpgaIELKAGSATRPffGVQPVLVD-NEGLPLDGAT-EGNLAIAdswpGQART 476
Cdd:cd17654 259 WRGKGN-RTRIFNIYGITEVSCWALA-----YKVPEEDSPVQ--LGSPLLGTvIEVRDQNGSEgTGQVFLG----GLNRV 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 477 LFGDHErfEQTYFSTfknMYFSGDGARRdEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIaEAAVVGIPHNikg 556
Cdd:cd17654 327 CILDDE--VTVPKGT---MRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGV-ESCAVTLSDQ--- 396
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 839746169 557 QAIYAYVTlnhgeepTPELYAEVRNWVRKEIGPL-ATPDVLHWTDSLPKTRSGKI 610
Cdd:cd17654 397 QRLIAFIV-------GESSSSRIHKELQLTLLSShAIPDTFVQIDKLPLTSHGKV 444
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
108-322 |
1.65e-09 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 60.90 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 108 ITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVA--------------- 172
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALChslnetevttvicds 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 173 ---GRIIDSSSRL-----VITADEGlragraIPLKKNVDDALKNPNVNSIEHVVVLKRTggkidwqegrdlwwsdlmaNA 244
Cdd:PLN02387 187 kqlKKLIDISSQLetvkrVIYMDDE------GVDSDSSLSGSSNWTVSSFSEVEKLGKE-------------------NP 241
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 839746169 245 SAEHRPvemNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIywctadvgwvtghsYLLYGPLA 322
Cdd:PLN02387 242 VDPDLP---SPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDV--------------YLAYLPLA 302
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
54-277 |
5.35e-09 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 59.12 E-value: 5.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 54 RVKNTSFAPGNISIKWYEDGTLNLAAN------------CLDRHLAERGDQTAIIwEGDDASQSKHITYRELHADVCRFA 121
Cdd:PRK08180 5 RYRPVAFAPPAVEVERRADGTIYLRSAeplgdyprrltdRLVHWAQEAPDRVFLA-ERGADGGWRRLTYAEALERVRAIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 122 NVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIfggfSPeAVAGRIIDsSSRL----------VITADEGLR 191
Cdd:PRK08180 84 QALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPV----SP-AYSLVSQD-FGKLrhvlelltpgLVFADDGAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 192 AGRAIplkknvdDALKNPnvnsieHVVVLKRTGGKIDwqeGRDLWWSDLMA-----NASAEHRPVemNAEDPLFILYTSG 266
Cdd:PRK08180 158 FARAL-------AAVVPA------DVEVVAVRGAVPG---RAATPFAALLAtpptaAVDAAHAAV--GPDTIAKFLFTSG 219
|
250
....*....|.
gi 839746169 267 STGKPKGVLHT 277
Cdd:PRK08180 220 STGLPKAVINT 230
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
254-621 |
1.13e-08 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 58.40 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 254 NAEDPLFILYTSGSTGKPKGVL---HTTGGYLVYAATtfkyVFDYHPGDIywctadvgwVTG-----HSY----LLYGPL 321
Cdd:PRK08633 780 KPDDTATIIFSSGSEGEPKGVMlshHNILSNIEQISD----VFNLRNDDV---------ILSslpffHSFgltvTLWLPL 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 322 ACGATTLMfegVPNwPTPARMC-QVVDKHKVSILYTAPTAIRALMAegDKAIEGTDRSSLRILGSVGEPINPEAWEWYWK 400
Cdd:PRK08633 847 LEGIKVVY---HPD-PTDALGIaKLVAKHRATILLGTPTFLRLYLR--NKKLHPLMFASLRLVVAGAEKLKPEVADAFEE 920
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 401 KIG---------NEKCPVM----------DTWWQTETggfmitplpgaielKAGSATRPFFGVQPVLVD-NEGLPLDGAT 460
Cdd:PRK08633 921 KFGirilegygaTETSPVAsvnlpdvlaaDFKRQTGS--------------KEGSVGMPLPGVAVRIVDpETFEELPPGE 986
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 461 EGNLAIADS-----WPGQA-RTLFGDHERFEQTYfstfknmYFSGDGARRDEDGYYWITGRVDdvlnvsghRLgtAEIES 534
Cdd:PRK08633 987 DGLILIGGPqvmkgYLGDPeKTAEVIKDIDGIGW-------YVTGDKGHLDEDGFLTITDRYS--------RF--AKIGG 1049
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 535 ALVSHPKIAEA------------AVVGIPHNIKGQAIYAYVTlnHGEEPTPELYAEVRNwvrKEIGPLATPDVLHWTDSL 602
Cdd:PRK08633 1050 EMVPLGAVEEElakalggeevvfAVTAVPDEKKGEKLVVLHT--CGAEDVEELKRAIKE---SGLPNLWKPSRYFKVEAL 1124
|
410
....*....|....*....
gi 839746169 603 PKTRSGKIMRRILRKIAAG 621
Cdd:PRK08633 1125 PLLGSGKLDLKGLKELALA 1143
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
91-615 |
5.34e-08 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 55.67 E-value: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 91 DQTAIIWEGDDasqskhITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIG------AIHSvifg 164
Cdd:PRK04813 17 DFPAYDYLGEK------LTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGhayipvDVSS---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 165 gfSPEAVAgRIIDSS-SRLVITADEGLRAGRAIPLKK--NVDDALKNPNVNSIEHVVvlkrtggkidwqegrdlwwsdlm 241
Cdd:PRK04813 87 --PAERIE-MIIEVAkPSLIIATEELPLEILGIPVITldELKDIFATGNPYDFDHAV----------------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 242 anasaehrpvemNAEDPLFILYTSGSTGKPKGV--LHTTggyLVyaatTFkyvfdyhpgdIYWCTADVGWVTGHSYL--- 316
Cdd:PRK04813 141 ------------KGDDNYYIIFTSGTTGKPKGVqiSHDN---LV----SF----------TNWMLEDFALPEGPQFLnqa 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 317 ----------LYGPLACGAT------------TLMFEGVPNWP------TP--ARMCqvvdkhkvsilytaptairaLMa 366
Cdd:PRK04813 192 pysfdlsvmdLYPTLASGGTlvalpkdmtanfKQLFETLPQLPinvwvsTPsfADMC--------------------LL- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 367 egDKAIEGTDRSSLRILGSVGEPI-NPEAwewywKKIgNEKCP---VMDTWWQTETGGFM----IT--------PLPgai 430
Cdd:PRK04813 251 --DPSFNEEHLPNLTHFLFCGEELpHKTA-----KKL-LERFPsatIYNTYGPTEATVAVtsieITdemldqykRLP--- 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 431 elkAGSAtRPffGVQPVLVDNEGLPLDGATEGNLAIAdswpGQARTL--FGDHERFEQTYFsTFKNM--YFSGDGARRDe 506
Cdd:PRK04813 320 ---IGYA-KP--DSPLLIIDEEGTKLPDGEQGEIVIS----GPSVSKgyLNNPEKTAEAFF-TFDGQpaYHTGDAGYLE- 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 507 DGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGE-EPTPELYAEVRNWVRK 585
Cdd:PRK04813 388 DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDfEREFELTKAIKKELKE 467
|
570 580 590
....*....|....*....|....*....|
gi 839746169 586 EIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK04813 468 RLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
103-559 |
7.80e-08 |
|
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: 55.30 E-value: 7.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 103 SQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRL 182
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 183 VITadeglragraiplkknvddalkNPNvnsiehvvvlkrtggkidwqegrdlwwsdlmanasaehrpvemnAEDPLFIL 262
Cdd:cd17639 81 IFT----------------------DGK--------------------------------------------PDDLACIM 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 263 YTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDiywctADVgwvtghsYLLYGPLA----------C---GAT--- 326
Cdd:cd17639 95 YTSGSTGNPKGVMLTHGN-LVAGIAGLGDRVPELLGP-----DDR-------YLAYLPLAhifelaaenvClyrGGTigy 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 327 ----TL------------------MFEGVPN-WPT--PARMCQVVDK--HKVSILYTAPTAIRALMAEG------DKAIE 373
Cdd:cd17639 162 gsprTLtdkskrgckgdltefkptLMVGVPAiWDTirKGVLAKLNPMggLKRTLFWTAYQSKLKALKEGpgtpllDELVF 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 374 GTDRSS----LRILGSVGEPINPEAWEWywkkIGNEKCPVMDTWWQTETGGFMITPLPGaiELKAGSATRPFFGVQPVLV 449
Cdd:cd17639 242 KKVRAAlggrLRYMLSGGAPLSADTQEF----LNIVLCPVIQGYGLTETCAGGTVQDPG--DLETGRVGPPLPCCEIKLV 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 450 DNEglpldgatEGNLaIADSWPGQARTLFG---------------DHERFEQTYFSTfknmyfsGDGARRDEDGYYWITG 514
Cdd:cd17639 316 DWE--------EGGY-STDKPPPRGEILIRgpnvfkgyyknpektKEAFDGDGWFHT-------GDIGEFHPDGTLKIID 379
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 839746169 515 RVDD-VLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAI 559
Cdd:cd17639 380 RKKDlVKLQNGEYIALEKLESIYRSNPLVNNICVYADPDKSYPVAI 425
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
108-322 |
2.66e-07 |
|
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: 53.76 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 108 ITYRELHADVCRFANVLLDLGIK--KGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAgRIIDSSSRLVIT 185
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIE-YILNHAEISIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 186 ADEGLRagraiplkknvddalknpnvnsiehvVVLkrtggkidwqegrdlwWSDLMA-NASAEHRPVEMNAEDPLFILYT 264
Cdd:cd05927 85 CDAGVK--------------------------VYS----------------LEEFEKlGKKNKVPPPPPKPEDLATICYT 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 839746169 265 SGSTGKPKGVLHTTGGYLVYAATTFKYVFDYH---PGDIYWctadvgwvtghSYLlygPLA 322
Cdd:cd05927 123 SGTTGNPKGVMLTHGNIVSNVAGVFKILEILNkinPTDVYI-----------SYL---PLA 169
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
119-607 |
2.99e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 50.49 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 119 RFANV---LLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIhSVIFGGFSPEAVAGRIIDSSSrlVITADEGLRAGRA 195
Cdd:PRK07868 481 RINNVvrgLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAV-AVLMPPDTDLAAAVRLGGVTE--IITDPTNLEAARQ 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 196 IPlkknvddalknpnvnsiEHVVVLKrtGGkidwqEGRDLwwsDLMANAS---------------AEHRPVEMNAEDPLF 260
Cdd:PRK07868 558 LP-----------------GRVLVLG--GG-----ESRDL---DLPDDADvidmekidpdavelpGWYRPNPGLARDLAF 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 261 ILY-TSGSTGKPKGVlhTTGGYLVYAATTFKYVfDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVpnwpTP 339
Cdd:PRK07868 611 IAFsTAGGELVAKQI--TNYRWALSAFGTASAA-ALDRRDTVYCLTPLHHESGLLVSLGGAVVGGSRIALSRGL----DP 683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 340 ARMCQVVDKHKVSILYTAPTAIRALMAEGDKAIEGTDRSSLRIlGSvGEPINpeawewYWKKIGNEKCP--VMDTWWQTE 417
Cdd:PRK07868 684 DRFVQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRLFI-GS-GMPTG------LWERVVEAFAPahVVEFFATTD 755
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 418 tGGFMITPLPGAielKAGSATRPFFGVQPV------------LVDNEGLpLDGATEGNLAI--------ADSWPGQARTL 477
Cdd:PRK07868 756 -GQAVLANVSGA---KIGSKGRPLPGAGRVelaaydpehdliLEDDRGF-VRRAEVNEVGVllarargpIDPTASVKRGV 830
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 478 FGDHErfeqTYFSTfKNMYfsgdgaRRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQ 557
Cdd:PRK07868 831 FAPAD----TWIST-EYLF------RRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGVEVGGRQL 899
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 839746169 558 AIYAyVTLNHGEEPTPelyAEVRNWVRkEIGPLATPDVLHWTDSLPKTRS 607
Cdd:PRK07868 900 AVAA-VTLRPGAAITA---ADLTEALA-SLPVGLGPDIVHVVPEIPLSAT 944
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
100-275 |
7.57e-06 |
|
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: 49.29 E-value: 7.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 100 DDASQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPeavagriidss 179
Cdd:TIGR03443 263 DPSSKTRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPP----------- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 180 SRLVITAD----EGL----RAGRAIPL-KKNVDDALKnpNVNSIEHVVVLKR---TGGKIDWQEGrdlwwsDLMANASA- 246
Cdd:TIGR03443 332 ARQTIYLSvakpRALivieKAGTLDQLvRDYIDKELE--LRTEIPALALQDDgslVGGSLEGGET------DVLAPYQAl 403
|
170 180 190
....*....|....*....|....*....|.
gi 839746169 247 --EHRPVEMNAEDPLFILYTSGSTGKPKGVL 275
Cdd:TIGR03443 404 kdTPTGVVVGPDSNPTLSFTSGSEGIPKGVL 434
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
246-617 |
7.61e-06 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 49.02 E-value: 7.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 246 AEHRPVEMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIY--W--CTADVGWVTGHsyllYGPL 321
Cdd:cd05908 96 TEEEVLCELADELAFIQFSSGSTGDPKGVMLTHEN-LVHNMFAILNSTEWKTKDRIlsWmpLTHDMGLIAFH----LAPL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 322 ACGATTLMFegvpnwPT------PARMCQVVDKHKVSILYTAPTAIRALMAE-GDKAIEGTDRSSLRILGSVGEPINPEA 394
Cdd:cd05908 171 IAGMNQYLM------PTrlfirrPILWLKKASEHKATIVSSPNFGYKYFLKTlKPEKANDWDLSSIRMILNGAEPIDYEL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 395 WEWYWKKIG----NEKCpvmdtwwqtetggfmITPLPGAIELKAGS----ATRPFF-----------GVQPVLVDNE--- 452
Cdd:cd05908 245 CHEFLDHMSkyglKRNA---------------ILPVYGLAEASVGAslpkAQSPFKtitlgrrhvthGEPEPEVDKKdse 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 453 -------GLPLDGAT-----EGNLAIADSWPGQARtLFGdhERFEQTYFSTFK--NMYFSGDGARRDED------GYYWI 512
Cdd:cd05908 310 cltfvevGKPIDETDiricdEDNKILPDGYIGHIQ-IRG--KNVTPGYYNNPEatAKVFTDDGWLKTGDlgfirnGRLVI 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 513 TGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGI---PHNIKGQAIYAYVTLNHGEEPTPELYAEVRN-------W 582
Cdd:cd05908 387 TGREKDIIFVNGQNVYPHDIERIAEELEGVELGRVVACgvnNSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKhlnkrggW 466
|
410 420 430
....*....|....*....|....*....|....*
gi 839746169 583 VRKEIGPLATpdvlhwtdsLPKTRSGKIMRRILRK 617
Cdd:cd05908 467 QINEVLPIRR---------IPKTTSGKVKRYELAQ 492
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
108-612 |
1.24e-05 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 48.44 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 108 ITYRELHADVCRFANVLLD-LGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVITA 186
Cdd:cd05938 6 YTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 187 DEglragraipLKKNVDD---ALKNPNVnsieHVVVLKRTggkiDWQEG-RDLwwSDLMANASAEHRPVEMNAE----DP 258
Cdd:cd05938 86 PE---------LQEAVEEvlpALRADGV----SVWYLSHT----SNTEGvISL--LDKVDAASDEPVPASLRAHvtikSP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 259 LFILYTSGSTGKPKGVLHTTggYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGhsyLLYGPLAC---GATTLM---FEG 332
Cdd:cd05938 147 ALYIYTSGTTGLPKAARISH--LRVLQCSGFLSLCGVTADDVIYITLPLYHSSG---FLLGIGGCielGATCVLkpkFSA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 333 VPNWPTparmCQvvdKHKVS-ILYTAPTaIRALMAEGDKAIEGTDRSSLrilgSVGEPINPEAWEWYWKKIGNEKcpVMD 411
Cdd:cd05938 222 SQFWDD----CR---KHNVTvIQYIGEL-LRYLCNQPQSPNDRDHKVRL----AIGNGLRADVWREFLRRFGPIR--IRE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 412 TWWQTE-TGGFM-ITPLPGAIElKAGSATRPFFGVQPVLVDNE-GLPLDGATEGNLAIADSWPG------QARTLF---- 478
Cdd:cd05938 288 FYGSTEgNIGFFnYTGKIGAVG-RVSYLYKLLFPFELIKFDVEkEEPVRDAQGFCIPVAKGEPGllvakiTQQSPFlgya 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 479 GDHERFEQTYF-STFK--NMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIP-HN 553
Cdd:cd05938 367 GDKEQTEKKLLrDVFKkgDVYFnTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTvPG 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 554 IKGQAIYAYVTLNHGEEPTPE-LYAEVRNWvrkeIGPLATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd05938 447 HEGRIGMAAVKLKPGHEFDGKkLYQHVREY----LPAYARPRFLRIQDSLEITGTFKQQK 502
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
108-620 |
1.43e-05 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 48.42 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 108 ITYRELHADvcrfANVLLDL---GIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIfgGFSpeAVAGRIIDSSS---- 180
Cdd:PRK06814 659 LTYRKLLTG----AFVLGRKlkkNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMI--NFS--AGIANILSACKaaqv 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 181 RLVITADEGLRAGRAIPLKKNVDDALKnpnVNSIEHVVVLKRTGGKIDwqegrdlwwsDLMANASAEHRPVEMNAEDPLF 260
Cdd:PRK06814 731 KTVLTSRAFIEKARLGPLIEALEFGIR---IIYLEDVRAQIGLADKIK----------GLLAGRFPLVYFCNRDPDDPAV 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 261 ILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVfDYHPGDIYWCTADVgwvtGHSYLLYGplacGATTLMFEGVPnwptpa 340
Cdd:PRK06814 798 ILFTSGSEGTPKGVVLSHRNLLANRAQVAARI-DFSPEDKVFNALPV----FHSFGLTG----GLVLPLLSGVK------ 862
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 341 rmcqvvdkhkvSILYTAPTAIRA----LMAEGDKAIEGTD-------RS-------SLRILGSVGEPINPEAWEWYWKKI 402
Cdd:PRK06814 863 -----------VFLYPSPLHYRIipelIYDTNATILFGTDtflngyaRYahpydfrSLRYVFAGAEKVKEETRQTWMEKF 931
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 403 GNEkcpVMDTWWQTETGGF--MITPLpgaiELKAGSATRPFFGVQPVLVDNEGLPlDGateGNLAI-----------ADS 469
Cdd:PRK06814 932 GIR---ILEGYGVTETAPViaLNTPM----HNKAGTVGRLLPGIEYRLEPVPGID-EG---GRLFVrgpnvmlgylrAEN 1000
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 470 wPGQartlfgdHERFEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVG 549
Cdd:PRK06814 1001 -PGV-------LEPPADGWYDT-------GDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVS 1065
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 839746169 550 IPHNIKGQAIYAYVTLNHGEEptpelyAEVRNWVRKE-IGPLATPDVLHWTDSLPKTRSGKI----MRRILRKIAA 620
Cdd:PRK06814 1066 IPDARKGERIILLTTASDATR------AAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKIdyvaVTKLAEEAAA 1135
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
108-322 |
1.69e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 47.91 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 108 ITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIIDSSSRLVITAD 187
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 188 EGLRAGRAIpLKK---NVDDALKNPNVNSIEHVVVLKRTGGKIDWQEgrdlwwSDLMANASAEHRPveMNAEDPLFILYT 264
Cdd:PLN02861 158 SKISSILSC-LPKcssNLKTIVSFGDVSSEQKEEAEELGVSCFSWEE------FSLMGSLDCELPP--KQKTDICTIMYT 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 839746169 265 SGSTGKPKGVLHTTGGYLVYAATTFKYVFdyhpgdiywcTADVGWVTGHSYLLYGPLA 322
Cdd:PLN02861 229 SGTTGEPKGVILTNRAIIAEVLSTDHLLK----------VTDRVATEEDSYFSYLPLA 276
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
106-322 |
3.72e-05 |
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long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 47.02 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 106 KHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVagriidsssRLVIT 185
Cdd:PLN02736 77 KWMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAV---------KFIVN 147
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 186 ADEgLRAGRAIPLKKNVddaLKN--PNVNSIEHVVVL-----------KRTGGKIdwqegrdLWWSDLMANASAEHRP-V 251
Cdd:PLN02736 148 HAE-VAAIFCVPQTLNT---LLSclSEIPSVRLIVVVggadeplpslpSGTGVEI-------VTYSKLLAQGRSSPQPfR 216
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170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 839746169 252 EMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWctadvgwvtghSYLlygPLA 322
Cdd:PLN02736 217 PPKPEDVATICYTSGTTGTPKGVVLTHGN-LIANVAGSSLSTKFYPSDVHI-----------SYL---PLA 272
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| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
532-649 |
1.29e-03 |
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serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 41.67 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839746169 532 IESALVSHPKIAEAAVVGIPHNIKGQAIYAYVtlnhgEEPTPELYAEVRNWVRKEIGPLAtPDVLHWTDSLPKTRSGKIM 611
Cdd:PRK09188 245 IQAALKSDPAVSDVAIALFSLPAKGVGLYAFV-----EAELPADEKSLRARLAGAKPPKP-PEHIQPVAALPRDADGTVR 318
|
90 100 110
....*....|....*....|....*....|....*....
gi 839746169 612 RRILRKIAAGDTSNLGDTSTL-ADPGVVEKLLEEKQAIT 649
Cdd:PRK09188 319 DDILRLIAMNQIDELDDLLREpEIRGLVEAIAAHRLNLT 357
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| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
103-169 |
2.21e-03 |
|
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: 40.96 E-value: 2.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 839746169 103 SQSKHITYRELHADVCRFANVLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPE 169
Cdd:cd17647 16 SKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPA 82
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