|
Name |
Accession |
Description |
Interval |
E-value |
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
1-571 |
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: 1078.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 1 MLNMCYNAIDRHIESGKGDKVAIIYDSPVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLAC 80
Cdd:cd05967 48 RLNTCYNALDRHVEAGRGDQIALIYDSPVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLAC 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 81 ARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTASFGIEPGRKVEYMPILEEAMRIGQHKPDKVLIYNRPNMETVPLASG 160
Cdd:cd05967 128 ARIGAIHSVVFGGFAAKELASRIDDAKPKLIVTASCGIEPGKVVPYKPLLDKALELSGHKPHHVLVLNRPQVPADLTKPG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 161 RDLDWDEEMAKAQSQDCVPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLGWVVGH 240
Cdd:cd05967 208 RDLDWSELLAKAEPVDCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGH 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 241 SYICYGPLIHGNTTVLYEGKPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALGKQYSLTRFKTLFVAGERC 320
Cdd:cd05967 288 SYIVYGPLLHGATTVLYEGKPVGTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPDGKYIKKYDLSSLRTLFLAGERL 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 321 DVETLEWSKKVFRVPVLDHWWQTETGSPITASCIGLGNsKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPL 400
Cdd:cd05967 368 DPPTLEWAENTLGVPVIDHWWQTETGWPITANPVGLEP-LPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPL 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 401 PPGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVG 480
Cdd:cd05967 447 PPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVG 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 481 KEDPLKGHVPLALCVLRKDINITEGQVLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAALSALVNGKPYKVTP 560
Cdd:cd05967 527 VRDELKGQVPLGLVVLKEGVKITAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGEDYTIPS 606
|
570
....*....|.
gi 1191882763 561 TIEDPSIFGHI 571
Cdd:cd05967 607 TIEDPSVLDEI 617
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
2-573 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 698.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 2 LNMCYNAIDRHIEsGKGDKVAIIYDSpVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACA 81
Cdd:COG0365 8 LNIAYNCLDRHAE-GRGDKVALIWEG-EDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 82 RIGAIHSLIFGGFASKELSSRIDHAKPKVVVTASFGIEPGRKVEYMPILEEAMRiGQHKPDKVLIYNRPNmetVPLASGR 161
Cdd:COG0365 86 RIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALE-ELPSLEHVIVVGRTG---ADVPMEG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 162 DLDWDEEMAKAQSQ-DCVPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLGWVVGH 240
Cdd:COG0365 162 DLDWDELLAAASAEfEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGWATGH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 241 SYICYGPLIHGNTTVLYEGKPVgTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPgaALGKQYSLTRFKTLFVAGERC 320
Cdd:COG0365 242 SYIVYGPLLNGATVVLYEGRPD-FPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGD--EPLKKYDLSSLRLLGSAGEPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 321 DVETLEWSKKVFRVPVLDHWWQTETGSPITASCIGlgnskTPP-PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLP 399
Cdd:COG0365 319 NPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPG-----LPVkPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 400 LpPGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVV 479
Cdd:COG0365 394 W-PGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 480 GKEDPLKGHVPLALCVLRKDINITEGQVlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAALSALVNGKPYKVT 559
Cdd:COG0365 473 GVPDEIRGQVVKAFVVLKPGVEPSDELA-KELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGRPLGDT 551
|
570
....*....|....
gi 1191882763 560 PTIEDPSIFGHIEE 573
Cdd:COG0365 552 STLEDPEALDEIKE 565
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
3-577 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 627.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 3 NMCYNAIDRHIESgKGDKVAIIYDSPVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACAR 82
Cdd:PRK10524 53 NLCHNAVDRHLAK-RPEQLALIAVSTETDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACAR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 83 IGAIHSLIFGGFASKELSSRIDHAKPKVVVTASFGIEPGRKVEYMPILEEAMRIGQHKPDKVLIYNRpNMETVPLASGRD 162
Cdd:PRK10524 132 IGAIHSVVFGGFASHSLAARIDDAKPVLIVSADAGSRGGKVVPYKPLLDEAIALAQHKPRHVLLVDR-GLAPMARVAGRD 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 163 LDWDEEMAKAQSQDcVPVL---SEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLGWVVG 239
Cdd:PRK10524 211 VDYATLRAQHLGAR-VPVEwleSNEPSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 240 HSYICYGPLIHGNTTVLYEGKPVgTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPgaALGKQYSLTRFKTLFVAGER 319
Cdd:PRK10524 290 HSYIVYAPLLAGMATIMYEGLPT-RPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDP--ALLRKHDLSSLRALFLAGEP 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 320 CDVETLEWSKKVFRVPVLDHWWQTETGSPITASCIGLGnSKTPPPGQAGKSVPGYNVMILDDNM-QKLKARCLGNIVVKL 398
Cdd:PRK10524 367 LDEPTASWISEALGVPVIDNYWQTETGWPILAIARGVE-DRPTRLGSPGVPMYGYNVKLLNEVTgEPCGPNEKGVLVIEG 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 399 PLPPGAFSGLWKNQEAFKHLYFEKF-PGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCA 477
Cdd:PRK10524 446 PLPPGCMQTVWGDDDRFVKTYWSLFgRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVA 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 478 VVGKEDPLKGHVPLALCVLRKDINITEGQV---LE-EIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAALSALVNG 553
Cdd:PRK10524 526 VVGVKDALKGQVAVAFVVPKDSDSLADREArlaLEkEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAEG 605
|
570 580
....*....|....*....|....
gi 1191882763 554 KPYKVTPTIEDPSIFGHIEEVLKQ 577
Cdd:PRK10524 606 RDPGDLTTIEDPAALQQIRQALEE 629
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
2-564 |
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: 579.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 2 LNMCYNAIDRHIESgKGDKVAIIYDSPVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACA 81
Cdd:cd05966 52 LNISYNCLDRHLKE-RGDKVAIIWEGDEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 82 RIGAIHSLIFGGFASKELSSRIDHAKPKVVVTASFGIEPGRKVEYMPILEEAMRIGqHKPDKVLIYNRPNmETVPLASGR 161
Cdd:cd05966 131 RIGAVHSVVFAGFSAESLADRINDAQCKLVITADGGYRGGKVIPLKEIVDEALEKC-PSVEKVLVVKRTG-GEVPMTEGR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 162 DLDWDEEMAKaQSQDC--VPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLGWVVG 239
Cdd:cd05966 209 DLWWHDLMAK-QSPECepEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 240 HSYICYGPLIHGNTTVLYEGKPVgTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFVAGER 319
Cdd:cd05966 288 HSYIVYGPLANGATTVMFEGTPT-YPDPGRYWDIVEKHKVTIFYTAPTAIRALMKF--GDEWVKKHDLSSLRVLGSVGEP 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 320 CDVETLEWSKKV---FRVPVLDHWWQTETGSPITASCIGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVV 396
Cdd:cd05966 365 INPEAWMWYYEVigkERCPIVDTWWQTETGGIMITPLPGATPLK---PGSATRPFFGIEPAILDEEGNEVEGEVEGYLVI 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 397 KLPLpPGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADC 476
Cdd:cd05966 442 KRPW-PGMARTIYGDHERYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEA 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 477 AVVGKEDPLKGHVPLALCVLRKDINITEgQVLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAALSALVNG-KP 555
Cdd:cd05966 521 AVVGRPHDIKGEAIYAFVTLKDGEEPSD-ELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGeEE 599
|
....*....
gi 1191882763 556 YKVTPTIED 564
Cdd:cd05966 600 LGDTSTLAD 608
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
2-573 |
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: 565.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 2 LNMCYNAIDRHIESgKGDKVAIIYDSPVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACA 81
Cdd:TIGR02188 56 LNVSYNCVDRHLEA-RPDKVAIIWEGDEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 82 RIGAIHSLIFGGFASKELSSRIDHAKPKVVVTASFGIEPGRKVEYMPILEEAMRIGQHKPDKVLIYNRPNMETVPLASGR 161
Cdd:TIGR02188 135 RIGAIHSVVFGGFSAEALADRINDAGAKLVITADEGLRGGKVIPLKAIVDEALEKCPVSVEHVLVVRRTGNPVVPWVEGR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 162 DLDWDEEMAKaQSQDCVP--VLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLGWVVG 239
Cdd:TIGR02188 215 DVWWHDLMAK-ASAYCEPepMDSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 240 HSYICYGPLIHGNTTVLYEGKPVgTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFVAGER 319
Cdd:TIGR02188 294 HSYIVYGPLANGATTVMFEGVPT-YPDPGRFWEIIEKHKVTIFYTAPTAIRALMRL--GDEWVKKHDLSSLRLLGSVGEP 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 320 CDVETLEWSKKVF---RVPVLDHWWQTETGSPITASCIGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNI-V 395
Cdd:TIGR02188 371 INPEAWMWYYKVVgkeRCPIVDTWWQTETGGIMITPLPGATPTK---PGSATLPFFGIEPAVVDEEGNPVEGPGEGGYlV 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 396 VKLPLpPGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVAD 475
Cdd:TIGR02188 448 IKQPW-PGMLRTIYGDHERFVDTYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAE 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 476 CAVVGKEDPLKGHVPLALCVLRKDINITEgQVLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAALSALVNGKP 555
Cdd:TIGR02188 527 AAVVGIPDDIKGQAIYAFVTLKDGYEPDD-ELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEA 605
|
570 580
....*....|....*....|
gi 1191882763 556 --YKVTPTIEDPSIFGHIEE 573
Cdd:TIGR02188 606 eiLGDTSTLEDPSVVEELIE 625
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
2-577 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 562.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 2 LNMCYNAIDRHIESGkGDKVAIIY--DSPVTDTKatITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLA 79
Cdd:PRK00174 66 LNVSYNCLDRHLKTR-GDKVAIIWegDDPGDSRK--ITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 80 CARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTASFGIEPGRKVEYMPILEEAMRIGqHKPDKVLIYNRPNmETVPLAS 159
Cdd:PRK00174 143 CARIGAVHSVVFGGFSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALANC-PSVEKVIVVRRTG-GDVDWVE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 160 GRDLDWDEEMAKaQSQDC--VPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLGWV 237
Cdd:PRK00174 221 GRDLWWHELVAG-ASDECepEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWV 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 238 VGHSYICYGPLIHGNTTVLYEGKPVgTPDAGAYFRVLAEHGVAALFTAPTAIRA-IRQqdpGAALGKQYSLTRFKTLFVA 316
Cdd:PRK00174 300 TGHSYIVYGPLANGATTLMFEGVPN-YPDPGRFWEVIDKHKVTIFYTAPTAIRAlMKE---GDEHPKKYDLSSLRLLGSV 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 317 GERCDVETLEWSKKVF---RVPVLDHWWQTETGSPITASCIGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGN 393
Cdd:PRK00174 376 GEPINPEAWEWYYKVVggeRCPIVDTWWQTETGGIMITPLPGATPLK---PGSATRPLPGIQPAVVDEEGNPLEGGEGGN 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 394 IVVKLPLpPGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTV 473
Cdd:PRK00174 453 LVIKDPW-PGMMRTIYGDHERFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKV 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 474 ADCAVVGKEDPLKGHVPLALCVLRKDINITEgQVLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAALSALVNG 553
Cdd:PRK00174 532 AEAAVVGRPDDIKGQGIYAFVTLKGGEEPSD-ELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEG 610
|
570 580
....*....|....*....|....*
gi 1191882763 554 KPYKV-TPTIEDPSIFGHIEEVLKQ 577
Cdd:PRK00174 611 EEILGdTSTLADPSVVEKLIEARQN 635
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
2-542 |
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: 562.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 2 LNMCYNAIDRHIESGkGDKVAIIYDSPVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACA 81
Cdd:cd17634 52 LNLAANALDRHLREN-GDRTAIIYEGDDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 82 RIGAIHSLIFGGFASKELSSRIDHAKPKVVVTASFGIEPGRKVEYMPILEEAMRIGQHKPDKVLIYNRpnmETVPLA--S 159
Cdd:cd17634 131 RIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGVRAGRSVPLKKNVDDALNPNVTSVEHVIVLKR---TGSDIDwqE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 160 GRDLDWDEEMAKAQSQ-DCVPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLGWVV 238
Cdd:cd17634 208 GRDLWWRDLIAKASPEhQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVT 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 239 GHSYICYGPLIHGNTTVLYEGKPVGtPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALGkqYSLTRFKTLFVAGE 318
Cdd:cd17634 288 GHSYLLYGPLACGATTLLYEGVPNW-PTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEG--TDRSSLRILGSVGE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 319 RCDVETLEWSKKVF---RVPVLDHWWQTETGSPITASCIGLGNSKTpppGQAGKSVPGYNVMILDDNMQKLKARCLGNIV 395
Cdd:cd17634 365 PINPEAYEWYWKKIgkeKCPVVDTWWQTETGGFMITPLPGAIELKA---GSATRPVFGVQPAVVDNEGHPQPGGTEGNLV 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 396 VKLPLPPGAFSGLWKNQEaFKHLYFEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVAD 475
Cdd:cd17634 442 ITDPWPGQTRTLFGDHER-FEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAE 520
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191882763 476 CAVVGKEDPLKGHVPLALCVLRKdiNITEGQVL-EEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKI 542
Cdd:cd17634 521 AAVVGIPHAIKGQAPYAYVVLNH--GVEPSPELyAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
3-567 |
2.28e-127 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 388.49 E-value: 2.28e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 3 NMCYNAIDRHIESGKGDKVAIIYDSPVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACAR 82
Cdd:PLN02654 88 NICYNCLDRNVEAGNGDKIAIYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACAR 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 83 IGAIHSLIFGGFASKELSSRIDHAKPKVVVTASfGIEPGRKVEYMPILEEAMRIGQHKP----DKVLIY-NRPNM--ETV 155
Cdd:PLN02654 168 IGAVHSVVFAGFSAESLAQRIVDCKPKVVITCN-AVKRGPKTINLKDIVDAALDESAKNgvsvGICLTYeNQLAMkrEDT 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 156 PLASGRDLDWdeemakaqsQDCVP----------VLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPG 225
Cdd:PLN02654 247 KWQEGRDVWW---------QDVVPnyptkcevewVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 226 EVWWAASDLGWVVGHSYICYGPLIHGNTTVLYEGKPvGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQY 305
Cdd:PLN02654 318 DVYWCTADCGWITGHSYVTYGPMLNGATVLVFEGAP-NYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRD--GDEYVTRH 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 306 SLTRFKTLFVAGERCDVETLEWSKKVF---RVPVLDHWWQTETGSPITASCIGLGNSKtppPGQAGKSVPGYNVMILDDN 382
Cdd:PLN02654 395 SRKSLRVLGSVGEPINPSAWRWFFNVVgdsRCPISDTWWQTETGGFMITPLPGAWPQK---PGSATFPFFGVQPVIVDEK 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 383 MQKLKARCLGNIVVKLPLpPGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGA 462
Cdd:PLN02654 472 GKEIEGECSGYLCVKKSW-PGAFRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAE 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 463 IEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEgQVLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKI 542
Cdd:PLN02654 551 VESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSE-ELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKI 629
|
570 580
....*....|....*....|....*..
gi 1191882763 543 PRAALSALVNGKPYKV--TPTIEDPSI 567
Cdd:PLN02654 630 MRRILRKIASRQLDELgdTSTLADPGV 656
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
2-577 |
1.58e-123 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 377.93 E-value: 1.58e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 2 LNMCYNAIDRHIESG-KGDKVAIIYDSPVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLAC 80
Cdd:PTZ00237 58 LNTCYNVLDIHVKNPlKRDQDALIYECPYLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSC 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 81 ARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTASFGIEPGRKVEYMPILEEAMRIGQHKPDKVLIYNR----------- 149
Cdd:PTZ00237 138 ARIGATHCVLFDGYSVKSLIDRIETITPKLIITTNYGILNDEIITFTPNLKEAIELSTFKPSNVITLFRnditsesdlkk 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 150 -PNMETVPlasgRDLDWDEEMAKAQSQ------DCVPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGL 222
Cdd:PTZ00237 218 iETIPTIP----NTLSWYDEIKKIKENnqspfyEYVPVESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEK 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 223 KPGEVWWAASDLGWVVGHSYIcYGPLIHGNTTVLYEGKPVGTPDAGAYF-RVLAEHGVAALFTAPTAIRAIRQQDPGAA- 300
Cdd:PTZ00237 294 DIPTVVFSHSSIGWVSFHGFL-YGSLSLGNTFVMFEGGIIKNKHIEDDLwNTIEKHKVTHTLTLPKTIRYLIKTDPEATi 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 301 LGKQYSLTRFKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQTETGspiTASCIGLGNSKTpPPGQAGKSVPGYNVMILD 380
Cdd:PTZ00237 373 IRSKYDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGYGQTEIG---ITYLYCYGHINI-PYNATGVPSIFIKPSILS 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 381 DNMQKLKARCLGNIVVKLPLPPGAFSGLWKNQEAFKHLyFEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISA 460
Cdd:PTZ00237 449 EDGKELNVNEIGEVAFKLPMPPSFATTFYKNDEKFKQL-FSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQL 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 461 GAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDI---NITEGQVLEEIVQHVRQSIGPVAAFRKAVFVQQLPKT 537
Cdd:PTZ00237 528 NTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQsnqSIDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKT 607
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1191882763 538 RSGKIPRAALSALVNGKPYKVTPTIEDPSIFGHIEEVLKQ 577
Cdd:PTZ00237 608 KTGKIPRQIISKFLNDSNYQLPDNVNDSEIFYKIKELYMK 647
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
2-564 |
7.42e-120 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 366.14 E-value: 7.42e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 2 LNMCYNAIDRHIESGKGDKVAIIYDSPvtDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACA 81
Cdd:PRK04319 42 VNIAYEAIDRHADGGRKDKVALRYLDA--SRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGAL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 82 RIGAIHSLIFGGFASKELSSRIDHAKPKVVVTAsfgiepgrkveympileeaMRIGQHKPDKVLiynrPNMETVPL---- 157
Cdd:PRK04319 120 KNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITT-------------------PALLERKPADDL----PSLKHVLLvged 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 158 --ASGRDLDWDEEMAKAQSQ-DCVPVLSEHPLYILYTSGTTGLPKGVVRPTGgyAVMLNWtMSSIYGL--KPGEVWWAAS 232
Cdd:PRK04319 177 veEGPGTLDFNALMEQASDEfDIEWTDREDGAILHYTSGSTGKPKGVLHVHN--AMLQHY-QTGKYVLdlHEDDVYWCTA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 233 DLGWVVGHSYICYGPLIHGNTTVLYEGKPvgtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKt 312
Cdd:PRK04319 254 DPGWVTGTSYGIFAPWLNGATNVIDGGRF----SPERWYRILEDYKVTVWYTAPTAIRMLMGA--GDDLVKKYDLSSLR- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 313 lFVA--GERCDVETLEWSKKVFRVPVLDHWWQTETGspitasCIGLGNSKTPP--PGQAGKSVPGYNVMILDDNMQKLKA 388
Cdd:PRK04319 327 -HILsvGEPLNPEVVRWGMKVFGLPIHDNWWMTETG------GIMIANYPAMDikPGSMGKPLPGIEAAIVDDQGNELPP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 389 RCLGNIVVKLPLPpGAFSGLWKNQEAFKHlYFEkfPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLL 468
Cdd:PRK04319 400 NRMGNLAIKKGWP-SMMRGIWNNPEKYES-YFA--GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLM 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 469 SHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEgQVLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAALS 548
Cdd:PRK04319 476 EHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSE-ELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK 554
|
570
....*....|....*.
gi 1191882763 549 ALVNGKPYKVTPTIED 564
Cdd:PRK04319 555 AWELGLPEGDLSTMED 570
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
37-549 |
1.27e-107 |
|
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: 329.68 E-value: 1.27e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 37 TYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTASf 116
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 117 giepgrkveympileeamrigqhkpdkvliynrpnmetvplasgrdldwdeemakaqsqdcvpvlsEHPLYILYTSGTTG 196
Cdd:cd05972 81 ------------------------------------------------------------------EDPALIYFTSGTTG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 197 LPKGVVRPTG-GYAVMLnwTMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLYEGKPVgtpDAGAYFRVLA 275
Cdd:cd05972 95 LPKGVLHTHSyPLGHIP--TAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRF---DAERILELLE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 276 EHGVAALFTAPTAIRAIRQQDPgaalgKQYSLTRFKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQTETGspitascIG 355
Cdd:cd05972 170 RYGVTSFCGPPTAYRMLIKQDL-----SSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETG-------LT 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 356 LGNSKTPP--PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPlPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAG 433
Cdd:cd05972 238 VGNFPDMPvkPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLP-PPGLFLGYVGDPEKTEASIRG---DYYLTGDRA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 434 YMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEgQVLEEIVQ 513
Cdd:cd05972 314 YRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSE-ELAEELQG 392
|
490 500 510
....*....|....*....|....*....|....*.
gi 1191882763 514 HVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAALSA 549
Cdd:cd05972 393 HVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
37-549 |
4.12e-104 |
|
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: 320.99 E-value: 4.12e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 37 TYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTAsf 116
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 117 giepgrkveympilEEamrigqhkpdkvlIYNRPNMETvplasgrdldwdeemakaqsqdcvpvlsehPLYILYTSGTTG 196
Cdd:cd05969 80 --------------EE-------------LYERTDPED------------------------------PTLLHYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 197 LPKGVVRPTGgyAVMLNW-TMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLYEGKPvgtpDAGAYFRVLA 275
Cdd:cd05969 103 TPKGVLHVHD--AMIFYYfTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRF----DAESWYGIIE 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 276 EHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQTETGSPITASCIG 355
Cdd:cd05969 177 RVKVTVWYTAPTAIRMLMKE--GDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYPC 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 356 LgnskTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlPLPPGAFSGLWKNQEAFKhLYFEKfpGYYDTMDAGYM 435
Cdd:cd05969 255 M----PIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALK-PGWPSMFRGIWNDEERYK-NSFID--GWYLTGDLAYR 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 436 DEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEgQVLEEIVQHV 515
Cdd:cd05969 327 DEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSD-ELKEEIINFV 405
|
490 500 510
....*....|....*....|....*....|....
gi 1191882763 516 RQSIGPVAAFRKAVFVQQLPKTRSGKIPRAALSA 549
Cdd:cd05969 406 RQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKA 439
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
2-565 |
8.74e-98 |
|
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: 310.19 E-value: 8.74e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 2 LNMCYNAIDRHIESGKgDKVAIIYDSPVTDTKaTITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACA 81
Cdd:cd05968 60 MNIVEQLLDKWLADTR-TRPALRWEGEDGTSR-TLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 82 RIGAIHSLIFGGFASKELSSRIDHAKPKVVVTASFGIEPGRKVEYMPILEEAMRigqHKP--DKVLIYNRPNMEtVPLAS 159
Cdd:cd05968 138 RIGGIVVPIFSGFGKEAAATRLQDAEAKALITADGFTRRGREVNLKEEADKACA---QCPtvEKVVVVRHLGND-FTPAK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 160 GRDLDWDEEMAKAQSQdCVPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLGWVVG 239
Cdd:cd05968 214 GRDLSYDEEKETAGDG-AERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 240 hSYICYGPLIHGNTTVLYEGKPvGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFVAGER 319
Cdd:cd05968 293 -PWLIFGGLILGATMVLYDGAP-DHPKADRLWRMVEDHEITHLGLSPTLIRALKPR--GDAPVNAHDLSSLRVLGSTGEP 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 320 CDVETLEWSKKVF---RVPVLDHWWQTETGSPItascigLGNSKTPP--PGQAGKSVPGYNVMILDDNMQKLKARcLGNI 394
Cdd:cd05968 369 WNPEPWNWLFETVgkgRNPIINYSGGTEISGGI------LGNVLIKPikPSSFNGPVPGMKADVLDESGKPARPE-VGEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 395 VVKLPLpPGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVA 474
Cdd:cd05968 442 VLLAPW-PGMTRGFWRDEDRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVL 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 475 DCAVVGKEDPLKGHVPLALCVLRKDINITEGqVLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAALSALVNGK 554
Cdd:cd05968 521 ESAAIGVPHPVKGEAIVCFVVLKPGVTPTEA-LAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGK 599
|
570
....*....|.
gi 1191882763 555 PYKVTPTIEDP 565
Cdd:cd05968 600 ELGDLSSLENP 610
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
18-551 |
2.37e-92 |
|
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: 290.94 E-value: 2.37e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 18 GDKVAIIYDSpvtdtkATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 97
Cdd:COG0318 13 PDRPALVFGG------RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 98 ELSSRIDHAKPKVVVTAsfgiepgrkveympileeamrigqhkpdkvliynrpnmetvplasgrdldwdeemakaqsqdc 177
Cdd:COG0318 87 ELAYILEDSGARALVTA--------------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 178 vpvlsehplYILYTSGTTGLPKGVVRPTGgyAVMLN-WTMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVL 256
Cdd:COG0318 104 ---------LILYTSGTTGRPKGVMLTHR--NLLANaAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVL 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 257 YEGkpvgtPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdPGAAlgkQYSLTRFKTLFVAGERCDVETLEWSKKVFRVPV 336
Cdd:COG0318 173 LPR-----FDPERVLELIERERVTVLFGVPTMLARLLRH-PEFA---RYDLSSLRLVVSGGAPLPPELLERFEERFGVRI 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 337 LDHWWQTETGSPITascIGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFK 416
Cdd:COG0318 244 VEGYGLTETSPVVT---VNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVR---GPNVMKGYWNDPEATA 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 417 hlyfEKFP-GYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCV 495
Cdd:COG0318 318 ----EAFRdGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVV 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1191882763 496 LRKDINITEgqvlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAALSALV 551
Cdd:COG0318 394 LRPGAELDA----EELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERY 445
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
16-454 |
2.03e-87 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 276.89 E-value: 2.03e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 16 GKGDKVAIIYDSPVTdtkatITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFA 95
Cdd:pfam00501 7 RTPDKTALEVGEGRR-----LTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 96 SKELSSRIDHAKPKVVVTASFGIepgrkveyMPILEEAMRIGQHKPDKVLIYNrpnmetVPLASGRDLDWDEEMAKAQSQ 175
Cdd:pfam00501 82 AEELAYILEDSGAKVLITDDALK--------LEELLEALGKLEVVKLVLVLDR------DPVLKEEPLPEEAKPADVPPP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 176 DCVPVLSEHPLYILYTSGTTGLPKGVVRPTGG--YAVMLNWTMS-SIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGN 252
Cdd:pfam00501 148 PPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNlvANVLSIKRVRpRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 253 TTVLYEGKPvgTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPgaalGKQYSLTRFKTLFVAGERCDVETLEWSKKVF 332
Cdd:pfam00501 228 TVVLPPGFP--ALDPAALLELIERYKVTVLYGVPTLLNMLLEAGA----PKRALLSSLRLVLSGGAPLPPELARRFRELF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 333 RVPVLDHWWQTETGSPITasCIGLGNSKTPPPGQAGKSVPGYNVMILDDN-MQKLKARCLGNIVVKlplPPGAFSGLWKN 411
Cdd:pfam00501 302 GGALVNGYGLTETTGVVT--TPLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVR---GPGVMKGYLND 376
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1191882763 412 QEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVA 454
Cdd:pfam00501 377 PELTAEAFDED--GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
184-542 |
2.00e-84 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 266.46 E-value: 2.00e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 184 HPLYILYTSGTTGLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVvGHSYICYGPLIHGNTTVLYEGkpvg 263
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAA-LAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 264 tPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAAlgkqYSLTRFKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQT 343
Cdd:cd04433 75 -FDPEAALELIEREKVTILLGVPTLLARLLKAPESAG----YDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 344 ETGSPITASCIGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPpgaFSGLWKNQEAFkhlYFEKF 423
Cdd:cd04433 150 ETGGTVATGPPDDDARK---PGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSV---MKGYWNNPEAT---AAVDE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 424 PGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINIT 503
Cdd:cd04433 221 DGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLD 300
|
330 340 350
....*....|....*....|....*....|....*....
gi 1191882763 504 EgqvlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKI 542
Cdd:cd04433 301 A----EELRAHVRERLAPYKVPRRVVFVDALPRTASGKI 335
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
36-547 |
4.57e-74 |
|
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: 242.81 E-value: 4.57e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 36 ITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTas 115
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 116 fgiepgrkveympilEEAMRigqHKpdkvliynrpnmetvplasgrdldwdeemakaqsqdcvpvLSEHPLYILYTSGTT 195
Cdd:cd05973 79 ---------------DAANR---HK----------------------------------------LDSDPFVMMFTSGTT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 196 GLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLYEGKpvGTPDAgaYFRVLA 275
Cdd:cd05973 101 GLPKGVPVPLRALAAFGAY-LRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGG--FSVES--TWRVIE 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 276 EHGVAALFTAPTAIRAIRQQDPGAALGKQYSLTRFKTlfvAGERCDVETLEWSKKVFRVPVLDHWWQTETGSPItasCIG 355
Cdd:cd05973 176 RLGVTNLAGSPTAYRLLMAAGAEVPARPKGRLRRVSS---AGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVL---ANH 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 356 LGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGA-FSGLWK-NQEAFKHlyfekfpGYYDTMDAG 433
Cdd:cd05973 250 HALEHPVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIDIANSPLMwFRGYQLpDTPAIDG-------GYYLTGDTV 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 434 YMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEgQVLEEIVQ 513
Cdd:cd05973 323 EFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTP-ALADELQL 401
|
490 500 510
....*....|....*....|....*....|....
gi 1191882763 514 HVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:cd05973 402 HVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLL 435
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
37-549 |
8.00e-72 |
|
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: 236.95 E-value: 8.00e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 37 TYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTasf 116
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 117 giepgrkveympileeamrigqhkpdkvliynrpnmetvplasgrdldwDEemakaqsqdcvpvlSEHPLYILYTSGTTG 196
Cdd:cd05971 85 -------------------------------------------------DG--------------SDDPALIIYTSGTTG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 197 LPKGVVRptgGYAVML----NWTMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLYEGKPVgtpDAGAYFR 272
Cdd:cd05971 102 PPKGALH---AHRVLLghlpGVQFPFNLFPRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKF---DPKAALD 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 273 VLAEHGVAALFTAPTAIRAIRQQdpgaalGKQYSLT--RFKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQTETGSpIT 350
Cdd:cd05971 176 LMSRYGVTTAFLPPTALKMMRQQ------GEQLKHAqvKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNL-VI 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 351 ASCIGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPlPPGAFSGLWKNQEAFKhlyfEKFPG-YYDT 429
Cdd:cd05971 249 GNCSALFPIK---PGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELP-DPVAFLGYWNNPSATE----KKMAGdWLLT 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 430 MDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEgQVLE 509
Cdd:cd05971 321 GDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSD-ALAR 399
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1191882763 510 EIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAALSA 549
Cdd:cd05971 400 EIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
3-547 |
9.35e-65 |
|
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: 220.83 E-value: 9.35e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 3 NMCYNAIDRHIESgKGDKVAIIYDSPVTDTKaTITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACAR 82
Cdd:cd05970 17 NFAYDVVDAMAKE-YPDKLALVWCDDAGEER-IFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 83 IGAIHSLIFGGFASKELSSRIDHAKPKVVVTASFGIEPGRkveympiLEEAMRIGQHKPDKVLIYNrpnmetvPLASGRd 162
Cdd:cd05970 95 LGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDNIPEE-------IEKAAPECPSKPKLVWVGD-------PVPEGW- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 163 LDWDEEMAKA-----QSQDCVPVLSEHPLYILYTSGTTGLPKGV----VRPTGGYAVMLNWtmssiYGLKPGEVWWAASD 233
Cdd:cd05970 160 IDFRKLIKNAspdfeRPTANSYPCGEDILLVYFSSGTTGMPKMVehdfTYPLGHIVTAKYW-----QNVREGGLHLTVAD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 234 LGWVVGHSYICYGPLIHGNTTVLYEgkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPgaalgKQYSLTRFKTL 313
Cdd:cd05970 235 TGWGKAVWGKIYGQWIAGAAVFVYD---YDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDL-----SRYDLSSLRYC 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 314 FVAGERCDVETLEWSKKVFRVPVLDHWWQTETgspitASCIGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGN 393
Cdd:cd05970 307 TTAGEALNPEVFNTFKEKTGIKLMEGFGQTET-----TLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 394 IVVKLP--LPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHG 471
Cdd:cd05970 382 IVIRTSkgKPVGLFGGYYKDAEKTAEVWHD---GYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHP 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191882763 472 TVADCAVVGKEDPLKGHVPLALCVLRKDinITEGQVLE-EIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:cd05970 459 AVLECAVTGVPDPIRGQVVKATIVLAKG--YEPSEELKkELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEI 533
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
31-542 |
2.44e-64 |
|
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: 218.62 E-value: 2.44e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 31 DTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKV 110
Cdd:cd05911 6 DTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 111 VVTASFGIE----------PGRKVEYMPILEEAMrigqhkpdkvliynrPNMETVPLASGRDLDWDEEMAKAQSQDcvpv 180
Cdd:cd05911 86 IFTDPDGLEkvkeaakelgPKDKIIVLDDKPDGV---------------LSIEDLLSPTLGEEDEDLPPPLKDGKD---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 181 lseHPLYILYTSGTTGLPKGVVRPtggYAVMLNWTMSSIYGLK----PGEVWWAASDLGWVVG-HSYICYgpLIHGNTTV 255
Cdd:cd05911 147 ---DTAAILYSSGTTGLPKGVCLS---HRNLIANLSQVQTFLYgndgSNDVILGFLPLYHIYGlFTTLAS--LLNGATVI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 256 LYEGkpvgtPDAGAYFRVLAEHGVAALFTAPtAIRAIRQQDPgaaLGKQYSLTRFKTLFVAGERCDVETLEWSKKVFRVP 335
Cdd:cd05911 219 IMPK-----FDSELFLDLIEKYKITFLYLVP-PIAAALAKSP---LLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 336 VLDHWW-QTETGSPITASCIGlgnskTPPPGQAGKSVPGYNVMILDDN-MQKLKARCLGNIVVKLPLppgAFSGLWKNQE 413
Cdd:cd05911 290 TIKQGYgMTETGGILTVNPDG-----DDKPGSVGRLLPNVEAKIVDDDgKDSLGPNEPGEICVRGPQ---VMKGYYNNPE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 414 AFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLAL 493
Cdd:cd05911 362 ATKETFDED--GWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAY 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1191882763 494 CVLRKDINITEgqvlEEIVQHVRQSIGPVAAFRKAV-FVQQLPKTRSGKI 542
Cdd:cd05911 440 VVRKPGEKLTE----KEVKDYVAKKVASYKQLRGGVvFVDEIPKSASGKI 485
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
18-547 |
3.07e-63 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 216.59 E-value: 3.07e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 18 GDKVAiiydspVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAI-HSL-IFggFA 95
Cdd:PRK06187 20 PDKEA------VYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVlHPInIR--LK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 96 SKELSSRIDHAKPKVVVTASfgiepgrkvEYMPILEEAMRIGQHKPDKVLIYNRPNMETVPLAsgrdLDWDEEMAKAQSQ 175
Cdd:PRK06187 92 PEEIAYILNDAEDRVVLVDS---------EFVPLLAAILPQLPTVRTVIVEGDGPAAPLAPEV----GEYEELLAAASDT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 176 DCVPVLSEHPLY-ILYTSGTTGLPKGVVRptgGYAVMLNWTMSSIYGLKpgevwWAASDLGWVV---GHSY---ICYGPL 248
Cdd:PRK06187 159 FDFPDIDENDAAaMLYTSGTTGHPKGVVL---SHRNLFLHSLAVCAWLK-----LSRDDVYLVIvpmFHVHawgLPYLAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 249 IHGNTTVLyegkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQqdpgAALGKQYSLTRFKTLFVAGERCDVETLEWS 328
Cdd:PRK06187 231 MAGAKQVI-----PRRFDPENLLDLIETERVTFFFAVPTIWQMLLK----APRAYFVDFSSLRLVIYGGAALPPALLREF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 329 KKVFRVPVLDHWWQTETGSPITASciglgnsktPPPGQ----------AGKSVPGYNVMILDDNMQKLKARC--LGNIVV 396
Cdd:PRK06187 302 KEKFGIDLVQGYGMTETSPVVSVL---------PPEDQlpgqwtkrrsAGRPLPGVEARIVDDDGDELPPDGgeVGEIIV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 397 KlplPPGAFSGLWKNQEAFKhlyfEKFP-GYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVAD 475
Cdd:PRK06187 373 R---GPWLMQGYWNRPEATA----ETIDgGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAE 445
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1191882763 476 CAVVGKEDPLKGHVPLALCVLRKDINITEgqvlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:PRK06187 446 VAVIGVPDEKWGERPVAVVVLKPGATLDA----KELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
18-544 |
4.66e-63 |
|
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: 213.63 E-value: 4.66e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 18 GDKVAIIYDSpvtdtkATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 97
Cdd:cd17631 9 PDRTALVFGG------RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 98 ELSSRIDHAKPKVVVtasfgiepgrkveympileeamrigqhkpdkvliynrpnmetvplasgrdldwdeemakaqsqdc 177
Cdd:cd17631 83 EVAYILADSGAKVLF----------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 178 vpvlsEHPLYILYTSGTTGLPKGVVRPTGG-YAVMLNWTMSsiYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVL 256
Cdd:cd17631 98 -----DDLALLMYTSGTTGRPKGAMLTHRNlLWNAVNALAA--LDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVI 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 257 YEGkpvgtPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdPGAAlgkQYSLTRFKTLFVAGERCDVETLE-WskKVFRVP 335
Cdd:cd17631 171 LRK-----FDPETVLDLIERHRVTSFFLVPTMIQALLQH-PRFA---TTDLSSLRAVIYGGAPMPERLLRaL--QARGVK 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 336 VLDHWWQTETGSPITAsciglgnskTPP------PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLW 409
Cdd:cd17631 240 FVQGYGMTETSPGVTF---------LSPedhrrkLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVR---GPHVMAGYW 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 410 KNQEA----FKHlyfekfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPL 485
Cdd:cd17631 308 NRPEAtaaaFRD-------GWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEK 380
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1191882763 486 KGHVPLALCVLRKDINITEgqvlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPR 544
Cdd:cd17631 381 WGEAVVAVVVPRPGAELDE----DELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
37-547 |
1.96e-58 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 203.85 E-value: 1.96e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 37 TYKEVLEQVSRLAGVLVKH-GVSKGDTVVIYMPMIPQAMYTMLACARIGAIhsLIFGG--FASKELSSRIDHAKPKVVVT 113
Cdd:cd05928 43 SFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLV--FIPGTiqLTAKDILYRLQASKAKCIVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 114 ASfgiepgrkvEYMPILEEamrigqhkpdkvLIYNRPNMETVPLAS--GRD--LDWDEEMAKA-QSQDCVPVLSEHPLYI 188
Cdd:cd05928 121 SD---------ELAPEVDS------------VASECPSLKTKLLVSekSRDgwLNFKELLNEAsTEHHCVETGSQEPMAI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 189 LYTSGTTGLPKGVVRPTGGYAvmLNWTMSSIY--GLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLYEGKPVgtpD 266
Cdd:cd05928 180 YFTSGTTGSPKMAEHSHSSLG--LGLKVNGRYwlDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGACVFVHHLPRF---D 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 267 AGAYFRVLAEHGVAALFTAPTAIRAIRQQDPgaalgKQYSLTRFKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQTETG 346
Cdd:cd05928 255 PLVILKTLSSYPITTFCGAPTVYRMLVQQDL-----SSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 347 spitascIGLGNSKTPP--PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKL-PLPP-GAFSGLWKNQEAFKHLYFEK 422
Cdd:cd05928 330 -------LICANFKGMKikPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVkPIRPfGLFSGYVDNPEKTAATIRGD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 423 FpgyYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINI 502
Cdd:cd05928 403 F---YLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLS 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1191882763 503 TE-GQVLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:cd05928 480 HDpEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
6-547 |
2.82e-52 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 186.42 E-value: 2.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 6 YNAI---DRHIESGKGDKVAIIYDSpvtdtkATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACAR 82
Cdd:cd05959 3 YNAAtlvDLNLNEGRGDKTAFIDDA------GSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 83 IGAIHSLIFGGFASKELSSRIDHAKPKVVVTASfgiepgrkvEYMPILEEAMRIGQHKpDKVLIYNRPNMETVPLASGRD 162
Cdd:cd05959 77 AGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSG---------ELAPVLAAALTKSEHT-LVVLIVSGGAGPEAGALLLAE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 163 LdWDEEmakAQSQDCVPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLGWVVGHSY 242
Cdd:cd05959 147 L-VAAE---AEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 243 ICYGPLIHGNTTVLYEGKPvgTPDAgaYFRVLAEHGVAALFTAPTaIRAIRQQDPGAalgKQYSLTRFKTLFVAGERCDV 322
Cdd:cd05959 223 SLTFPLSVGATTVLMPERP--TPAA--VFKRIRRYRPTVFFGVPT-LYAAMLAAPNL---PSRDLSSLRLCVSAGEALPA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 323 ETLEWSKKVFRVPVLDHWWQTETGSpitascIGLGNskTP---PPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlp 399
Cdd:cd05959 295 EVGERWKARFGLDILDGIGSTEMLH------IFLSN--RPgrvRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVR-- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 400 lPPGAFSGLWKNQEAFKhlyfEKFPGY-YDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAV 478
Cdd:cd05959 365 -GPSSATMYWNNRDKTR----DTFQGEwTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAV 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191882763 479 VGKEDPLKGHVPLALCVLRKDINITEgQVLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:cd05959 440 VGVEDEDGLTKPKAFVVLRPGYEDSE-ALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
19-565 |
4.89e-52 |
|
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: 188.25 E-value: 4.89e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIIYDSpvTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 98
Cdd:cd05943 84 DPAAIYAAE--DGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 99 LSSRIDHAKPKVVVTASFGIEPGRKVEYMP-ILEEAMRIGQHKPDKVLIYNRPNMETVPLASGRDLDWDEEMAKAQSQ-- 175
Cdd:cd05943 162 VLDRFGQIEPKVLFAVDAYTYNGKRHDVREkVAELVKGLPSLLAVVVVPYTVAAGQPDLSKIAKALTLEDFLATGAAGel 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 176 DCVPVLSEHPLYILYTSGTTGLPKGVVRPTGGY------AVMLNWtmssiyGLKPGEVWWAASDLGWVVGHSYIcyGPLI 249
Cdd:cd05943 242 EFEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTllqhlkEHILHC------DLRPGDRLFYYTTCGWMMWNWLV--SGLA 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 250 HGNTTVLYEGKPvGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFVAGERCDVETLEW-S 328
Cdd:cd05943 314 VGATIVLYDGSP-FYPDTNALWDLADEEGITVFGTSAKYLDALEKA--GLKPAETHDLSSLRTILSTGSPLKPESFDYvY 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 329 KKVFRvpvlDHWWQTETGSPITASCIGLGNSKTPP-PGQAGKSVPGYNVMILDDNMQKLKARcLGNIVVKLPLP--PGAF 405
Cdd:cd05943 391 DHIKP----DVLLASISGGTDIISCFVGGNPLLPVyRGEIQCRGLGMAVEAFDEEGKPVWGE-KGELVCTKPFPsmPVGF 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 406 sglWKNQEA--FKHLYFEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKED 483
Cdd:cd05943 466 ---WNDPDGsrYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEW 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 484 P-LKGHVPLALcVLRKDINITEgQVLEEIVQHVRQSIGP--VAAfrKAVFVQQLPKTRSGKIPRAALSALVNGKPYKVTP 560
Cdd:cd05943 543 KdGDERVILFV-KLREGVELDD-ELRKRIRSTIRSALSPrhVPA--KIIAVPDIPRTLSGKKVEVAVKKIIAGRPVKNAG 618
|
....*
gi 1191882763 561 TIEDP 565
Cdd:cd05943 619 ALANP 623
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
16-555 |
4.74e-51 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 186.15 E-value: 4.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 16 GKGDKVAIIYDSPvTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFA 95
Cdd:PRK03584 96 RRDDRPAIIFRGE-DGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 96 SKELSSRIDHAKPKVVVTA---SFGiepGRKVEYMPILEEamrIGQHKPD--KVLIYNRPNMETVPLASGRDLDWDEEMA 170
Cdd:PRK03584 175 VQGVLDRFGQIEPKVLIAVdgyRYG---GKAFDRRAKVAE---LRAALPSleHVVVVPYLGPAAAAAALPGALLWEDFLA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 171 KAQSQ--DCVPVLSEHPLYILYTSGTTGLPKGVVRPTGG------YAVMLNWtmssiyGLKPGE-VWWAASdLGWV---- 237
Cdd:PRK03584 249 PAEAAelEFEPVPFDHPLWILYSSGTTGLPKCIVHGHGGillehlKELGLHC------DLGPGDrFFWYTT-CGWMmwnw 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 238 -VGhsyicyGPLIhGNTTVLYEGKPvGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFVA 316
Cdd:PRK03584 322 lVS------GLLV-GATLVLYDGSP-FYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKA--GLVPGETHDLSALRTIGST 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 317 GERCDVETLEWskkVFRVPVLDHWWQTETGSPITASCIGLGNSKTPP-PGQAGKSVPGYNVMILDDNMQKLKARcLGNIV 395
Cdd:PRK03584 392 GSPLPPEGFDW---VYEHVKADVWLASISGGTDICSCFVGGNPLLPVyRGEIQCRGLGMAVEAWDEDGRPVVGE-VGELV 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 396 VKLPLP--PgafSGLW--KNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAG-------AIE 464
Cdd:PRK03584 468 CTKPFPsmP---LGFWndPDGSRYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAeiyrqveALP 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 465 EsllshgtVADCAVVGKEDPLKG-HVPLaLCVLRKDINITEGqVLEEIVQHVRQSIGP--VAAfrKAVFVQQLPKTRSGK 541
Cdd:PRK03584 545 E-------VLDSLVIGQEWPDGDvRMPL-FVVLAEGVTLDDA-LRARIRTTIRTNLSPrhVPD--KIIAVPDIPRTLSGK 613
|
570
....*....|....
gi 1191882763 542 IPRAALSALVNGKP 555
Cdd:PRK03584 614 KVELPVKKLLHGRP 627
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
36-547 |
3.13e-50 |
|
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: 179.02 E-value: 3.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 36 ITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTAs 115
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 116 fgiepgrkveympileeamrigqhkpdkvliynrpnmetvplasgrdldwdeemakaqsqdcvpvlsehPLYILYTSGTT 195
Cdd:cd05934 83 ---------------------------------------------------------------------PASILYTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 196 GLPKGVVRPtggYAVMLNW--TMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLYEgkpvgTPDAGAYFRV 273
Cdd:cd05934 94 GPPKGVVIT---HANLTFAgyYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLP-----RFSASRFWSD 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 274 LAEHGVAALFTAPTAIRAIRQQDPGAalgkQYSLTRFKTLFVAGERCDVETlEWSKKvFRVPVLDHWWQTETGSPITASc 353
Cdd:cd05934 166 VRRYGATVTNYLGAMLSYLLAQPPSP----DDRAHRLRAAYGAPNPPELHE-EFEER-FGVRLLEGYGMTETIVGVIGP- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 354 iglgNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWKNQEA----FKHlyfekfpGYYDT 429
Cdd:cd05934 239 ----RDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRGLRGWGFFKGYYNMPEAtaeaMRN-------GWFHT 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 430 MDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEgqvlE 509
Cdd:cd05934 308 GDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDP----E 383
|
490 500 510
....*....|....*....|....*....|....*...
gi 1191882763 510 EIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:cd05934 384 ELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQL 421
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
17-547 |
2.35e-49 |
|
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: 177.76 E-value: 2.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 17 KGDKVAIIYDspvtdtKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAI---HSLIFGG 93
Cdd:cd05936 12 FPDKTALIFM------GRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVvvpLNPLYTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 94 fasKELSSRIDHAKPKVVVTA-SF--GIEPGRKVEYMPILeeamrigqHKPDKVLIynrpnmetvplasgrdldwdeema 170
Cdd:cd05936 86 ---RELEHILNDSGAKALIVAvSFtdLLAAGAPLGERVAL--------TPEDVAVL------------------------ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 171 kaqsqdcvpvlsehplyiLYTSGTTGLPKGVvrptggyavMLnwTMSSIYGLKPGEVWWAASDLgwVVGHSYICYGPLIH 250
Cdd:cd05936 131 ------------------QYTSGTTGVPKGA---------ML--THRNLVANALQIKAWLEDLL--EGDDVVLAALPLFH 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 251 --------------GNTTVLyegkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGaalgKQYSLTRFKTLFVA 316
Cdd:cd05936 180 vfgltvalllplalGATIVL-----IPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEF----KKRDFSSLRLCISG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 317 GERCDVETLEWSKKVFRVPVLDHWWQTETgSPITASCIGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVV 396
Cdd:cd05936 251 GAPLPVEVAERFEELTGVPIVEGYGLTET-SPVVAVNPLDGPRK---PGSIGIPLPGTEVKIVDDDGEELPPGEVGELWV 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 397 KlplPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADC 476
Cdd:cd05936 327 R---GPQVMKGYWNRPEETAEAFVD---GWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEA 400
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191882763 477 AVVGKEDPLKGHVPLALCVLRKDINITEgqvlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:cd05936 401 AVVGVPDPYSGEAVKAFVVLKEGASLTE----EEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
19-548 |
2.40e-49 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 178.27 E-value: 2.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIIydspVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 98
Cdd:cd05926 2 DAPALV----VPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 99 LSSRIDHAKPKVVVTASFGIEP---GRKVEYMPILEEAMrigqhkpDKVLIYNRPNMETVPLASGrDLDWDEEMAKAQSQ 175
Cdd:cd05926 78 FEFYLADLGSKLVLTPKGELGPasrAASKLGLAILELAL-------DVGVLIRAPSAESLSNLLA-DKKNAKSEGVPLPD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 176 DcvPVLsehplyILYTSGTTGLPKGV-VRPTGGYAVMLNwtMSSIYGLKPgevwwaaSDLGWVVGhsyicygPLIHGN-- 252
Cdd:cd05926 150 D--LAL------ILHTSGTTGRPKGVpLTHRNLAASATN--ITNTYKLTP-------DDRTLVVM-------PLFHVHgl 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 253 -----TTVLYEGKPVGTP--DAGAYFRVLAEHGvAALFTA-PTaIRAIRQQDPGAALGKQYSLTRFktLFVAGERCDVET 324
Cdd:cd05926 206 vasllSTLAAGGSVVLPPrfSASTFWPDVRDYN-ATWYTAvPT-IHQILLNRPEPNPESPPPKLRF--IRSCSASLPPAV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 325 LEWSKKVFRVPVLDHWWQTETGSPITASCIglgNSKTPPPGQAGKSVpGYNVMILDDNMQKLKARCLGNIVVKlplPPGA 404
Cdd:cd05926 282 LEALEATFGAPVLEAYGMTEAAHQMTSNPL---PPGPRKPGSVGKPV-GVEVRILDEDGEILPPGVVGEICLR---GPNV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 405 FSGLWKNQEAFKHlYFEKFpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDP 484
Cdd:cd05926 355 TRGYLNNPEANAE-AAFKD-GWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDE 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191882763 485 LKGHVPLALCVLRKDINITEgqvlEEIVQHVRQSIgpvAAF---RKAVFVQQLPKTRSGKIPRAALS 548
Cdd:cd05926 433 KYGEEVAAAVVLREGASVTE----EELRAFCRKHL---AAFkvpKKVYFVDELPKTATGKIQRRKVA 492
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
19-542 |
1.74e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 176.66 E-value: 1.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIIYDSpvtdtkATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 98
Cdd:PRK08316 26 DKTALVFGD------RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 99 LSSRIDHAKPKVVVTASfgiepgrkvEYMPILEEAMRIGQHKPDKVliynrPNMETVPLASGRDLDWDEeMAKAQSQDC- 177
Cdd:PRK08316 100 LAYILDHSGARAFLVDP---------ALAPTAEAALALLPVDTLIL-----SLVLGGREAPGGWLDFAD-WAEAGSVAEp 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 178 -VPVLSEHPLYILYTSGTTGLPKGVVRPTGgyAVMLNWtMSSIYGLKpgevwWAASDlgwVVGHS---YIC------YGP 247
Cdd:PRK08316 165 dVELADDDLAQILYTSGTESLPKGAMLTHR--ALIAEY-VSCIVAGD-----MSADD---IPLHAlplYHCaqldvfLGP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 248 LIH-GNTTVLYEGkpvgtPDAGAYFRVLAEHGVAALFTAPTA-IRAIRQQDPGaalgkQYSLTRFKTLFVAGERCDVETL 325
Cdd:PRK08316 234 YLYvGATNVILDA-----PDPELILRTIEAERITSFFAPPTVwISLLRHPDFD-----TRDLSSLRKGYYGASIMPVEVL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 326 EWSKKvfRVPVLDHW---WQTETGSpiTASCIGLGNSKTPPpGQAGKsvPGYNV--MILDDNMQKLKARCLGNIVVKlpl 400
Cdd:PRK08316 304 KELRE--RLPGLRFYncyGQTEIAP--LATVLGPEEHLRRP-GSAGR--PVLNVetRVVDDDGNDVAPGEVGEIVHR--- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 401 PPGAFSGLWKN----QEAFKHlyfekfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADC 476
Cdd:PRK08316 374 SPQLMLGYWDDpektAEAFRG-------GWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEV 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191882763 477 AVVGKEDPLKGHVPLALCVLRKDINITEgqvlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKI 542
Cdd:PRK08316 447 AVIGLPDPKWIEAVTAVVVPKAGATVTE----DELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
35-547 |
2.73e-47 |
|
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: 171.51 E-value: 2.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 35 TITYKEVLEQVSRLAGVLV-KHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVT 113
Cdd:cd05958 10 EWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVALC 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 114 ASfgiepgrkveympileeamrigqhkpdkvliynrpnmetvplasgrdldwdeemaKAQSQDCVPVLSehplyilYTSG 193
Cdd:cd05958 90 AH-------------------------------------------------------ALTASDDICILA-------FTSG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 194 TTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLYEGKpvgTPDAgaYFRV 273
Cdd:cd05958 108 TTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEA---TPDL--LLSA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 274 LAEHGVAALFTAPTAIRAIRQQDPGAalgkQYSLTRFKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQTEtgspitASC 353
Cdd:cd05958 183 IARYKPTVLFTAPTAYRAMLAHPDAA----GPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTE------MFH 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 354 IGLGNSKTPP-PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPlppgafSGLWKNQEAFKHLYFEKfpGYYDTMDA 432
Cdd:cd05958 253 IFISARPGDArPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP------TGCRYLADKRQRTYVQG--GWNITGDT 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 433 GYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEgQVLEEIV 512
Cdd:cd05958 325 YSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGP-VLARELQ 403
|
490 500 510
....*....|....*....|....*....|....*
gi 1191882763 513 QHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:cd05958 404 DHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
19-547 |
1.01e-46 |
|
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: 170.02 E-value: 1.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIIYDSpvtdtkATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 98
Cdd:cd05930 2 DAVAVVDGD------QSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 99 LSSRIDHAKPKVVVTASfgiepgrkveympileeamrigqhkpdkvliynrpnmetvplasgrdldwdeemakaqsqdcv 178
Cdd:cd05930 76 LAYILEDSGAKLVLTDP--------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 179 pvlsEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVVGHSYIcYGPLIHGNTTVLYE 258
Cdd:cd05930 93 ----DDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW-MQEAYPLTPGDRVLQFTSFSFDVSVWEI-FGALLAGATLVVLP 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 259 GKPVGTPDAgaYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALgkqyslTRFKTLFVAGERCDVETLE-WSKKVFRVPVL 337
Cdd:cd05930 167 EEVRKDPEA--LADLLAEEGITVLHLTPSLLRLLLQELELAAL------PSLRLVLVGGEALPPDLVRrWRELLPGARLV 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 338 DHWWQTETGSPITASCIGLGN-SKTPPPgqAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGLW------- 409
Cdd:cd05930 239 NLYGPTEATVDATYYRVPPDDeEDGRVP--IGRPIPNTRVYVLDENLR--------------PVPPGVPGELYiggagla 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 410 --------KNQEAFKHLYFekFPG--YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVV 479
Cdd:cd05930 303 rgylnrpeLTAERFVPNPF--GPGerMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVV 380
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191882763 480 GKEDPLKGHVPLALCVLRKDINITEgqvlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:cd05930 381 AREDGDGEKRLVAYVVPDEGGELDE----EELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
18-544 |
1.41e-45 |
|
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: 168.18 E-value: 1.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 18 GDKVAIIyDSPvtdTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 97
Cdd:cd05904 19 PSRPALI-DAA---TGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 98 ELSSRIDHAKPKVVVTASfgiepgrkvEYMPILEEAMRigqhkpdKVLIYNRPnmETVPLASGRDLDWDEEMAKAQsqdc 177
Cdd:cd05904 95 EIAKQVKDSGAKLAFTTA---------ELAEKLASLAL-------PVVLLDSA--EFDSLSFSDLLFEADEAEPPV---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 178 VPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSI-YGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVL 256
Cdd:cd05904 153 VVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEgSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 257 yegkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpgaALGKQYSLTRFKTLFVAGERCDVETLEWSKKVF-RVP 335
Cdd:cd05904 233 -----MPRFDLEELLAAIERYKVTHLPVVPPIVLALVKS----PIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFpNVD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 336 VLDHWWQTETgSPITASCigLGNSKTP-PPGQAGKSVPGYNVMILDdnmqklkarclgnIVVKLPLPPGaFSG-LW---- 409
Cdd:cd05904 304 LGQGYGMTES-TGVVAMC--FAPEKDRaKYGSVGRLVPNVEAKIVD-------------PETGESLPPN-QTGeLWirgp 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 410 -------KNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKE 482
Cdd:cd05904 367 simkgylNNPEATAATIDKE--GWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYP 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1191882763 483 DPLKGHVPLALCVLRKDINITEgqvlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPR 544
Cdd:cd05904 445 DEEAGEVPMAFVVRKPGSSLTE----DEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILR 502
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
26-547 |
1.42e-45 |
|
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: 166.48 E-value: 1.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 26 DSPVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDH 105
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 106 AKPKVVVTasfgiepgrkveympileeamrigqhkpdkvliynrpnmetvplasgrdldwdeemakaqSQDCVpvlsehp 185
Cdd:cd05919 81 CEARLVVT------------------------------------------------------------SADDI------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 186 LYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDL--GWVVGHSYIcyGPLIHGNTTVLYEGKPvg 263
Cdd:cd05919 94 AYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNSLW--FPLAVGASAVLNPGWP-- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 264 tpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpgaALGKQYSLTRFKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQT 343
Cdd:cd05919 170 --TAERVLATLARFRPTVLYGVPTFYANLLDS----CAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGAT 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 344 ETGSPITASCIGLGNsktppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPlppGAFSGLWKNQEAFKHLYFEkf 423
Cdd:cd05919 244 EVGHIFLSNRPGAWR-----LGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGP---SAAVGYWNNPEKSRATFNG-- 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 424 pGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDpLKGHVPLALCVLRKDINIT 503
Cdd:cd05919 314 -GWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPE-STGLSRLTAFVVLKSPAAP 391
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1191882763 504 EGQVLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:cd05919 392 QESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
35-542 |
3.83e-43 |
|
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: 159.85 E-value: 3.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 35 TITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTA 114
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 115 SfgiepgrkveympileeamRIGQHKPdkvliynrpnmetvplasgrdldwdEEMAKAqsqdcvpvlsehPLYILYTSGT 194
Cdd:cd05903 81 E-------------------RFRQFDP-------------------------AAMPDA------------VALLLFTSGT 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 195 TGLPKGVVRPTggyavmlNWTMSSI------YGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLYEgkpVGTPDAG 268
Cdd:cd05903 105 TGEPKGVMHSH-------NTLSASIrqyaerLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQD---IWDPDKA 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 269 AyfRVLAEHGVAALFTAPT----AIRAIRQQDPgaalgkqySLTRFKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQTE 344
Cdd:cd05903 175 L--ALMREHGVTFMMGATPfltdLLNAVEEAGE--------PLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTE 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 345 TGSpitasciGLGNSKTPPPGQA----GKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQeafkHLYF 420
Cdd:cd05903 245 CPG-------AVTSITPAPEDRRlytdGRPLPGVEIKVVDDTGATLAPGVEGELLSR---GPSVFLGYLDRP----DLTA 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 421 EKFP-GYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKD 499
Cdd:cd05903 311 DAAPeGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSG 390
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1191882763 500 INITegqvLEEIVQHV-RQSIGPVAAFRKAVFVQQLPKTRSGKI 542
Cdd:cd05903 391 ALLT----FDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
19-554 |
7.31e-43 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 160.13 E-value: 7.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIIYDspvtdtKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 98
Cdd:PRK03640 17 DRTAIEFE------EKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 99 LSSRIDHAKPKVVVTASfgiepgrkvEYMPileeamrigQHKPDKVLIYnrpnmetvplasgrdldwdEEMAKAQSQDcV 178
Cdd:PRK03640 91 LLWQLDDAEVKCLITDD---------DFEA---------KLIPGISVKF-------------------AELMNGPKEE-A 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 179 PVLSEHPL----YILYTSGTTGLPKGVVRPTGgyavmlNWTMSSI-----YGLKPGEVWWAASDLGWVVGHSyICYGPLI 249
Cdd:PRK03640 133 EIQEEFDLdevaTIMYTSGTTGKPKGVIQTYG------NHWWSAVgsalnLGLTEDDCWLAAVPIFHISGLS-ILMRSVI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 250 HGNTTVLYEgkpvgTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAalgkQYSLTrFKTLFVAGERCDVETLEWSK 329
Cdd:PRK03640 206 YGMRVVLVE-----KFDAEKINKLLQTGGVTIISVVSTMLQRLLERLGEG----TYPSS-FRCMLLGGGPAPKPLLEQCK 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 330 KvFRVPVLDHWWQTETGSPITasciglgnskTPPP-------GQAGKSVPGYNVMILDDNmQKLKARCLGNIVVKLP-LP 401
Cdd:PRK03640 276 E-KGIPVYQSYGMTETASQIV----------TLSPedaltklGSAGKPLFPCELKIEKDG-VVVPPFEEGEIVVKGPnVT 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 402 PGAFSGLWKNQEAFKHlyfekfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGK 481
Cdd:PRK03640 344 KGYLNREDATRETFQD-------GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGV 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191882763 482 EDPLKGHVPLALCVlrKDINITEgqvlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAALSALVNGK 554
Cdd:PRK03640 417 PDDKWGQVPVAFVV--KSGEVTE----EELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVEEM 483
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
18-550 |
9.37e-42 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 159.35 E-value: 9.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 18 GDKVAIIY--DSPVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIG---AIHSLIFG 92
Cdd:PRK07529 39 PDAPALSFllDADPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGianPINPLLEP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 93 GfaskELSSRIDHAKPKVVVTAsfGIEPG----RKVEYM--------PILEEAM--RIGQHKPDKVLIYNRPnmetvplA 158
Cdd:PRK07529 119 E----QIAELLRAAGAKVLVTL--GPFPGtdiwQKVAEVlaalpelrTVVEVDLarYLPGPKRLAVPLIRRK-------A 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 159 SGRDLDWDEEMAK--AQSQDCVPVLSEHPLYILY-TSGTTGLPKgVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLG 235
Cdd:PRK07529 186 HARILDFDAELARqpGDRLFSGRPIGPDDVAAYFhTGGTTGMPK-LAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 236 WVVGHSYICYGPLIHGNTTVLyeGKPVGTPDAGAY---FRVLAEHGVAALFTAPTAIRAIRQQDPGAAlgkqySLTRFKT 312
Cdd:PRK07529 265 HVNALLVTGLAPLARGAHVVL--ATPQGYRGPGVIanfWKIVERYRINFLSGVPTVYAALLQVPVDGH-----DISSLRY 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 313 LFVAGERCDVETLEWSKKVFRVPVLDHWWQTETGSPITASCIG----LGNSKTPPPGQAGKsvpgynVMILDDN---MQK 385
Cdd:PRK07529 338 ALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPDgerrIGSVGLRLPYQRVR------VVILDDAgryLRD 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 386 LKARCLGNIVVKlplPPGAFSGlWKNQEAFKHLYFEkfPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 465
Cdd:PRK07529 412 CAVDEVGVLCIA---GPNVFSG-YLEAAHNKGLWLE--DGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEE 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 466 SLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEGQVLEeivqHVRQSIGPVAAFRKAV-FVQQLPKTRSGKIPR 544
Cdd:PRK07529 486 ALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAELLA----FARDHIAERAAVPKHVrILDALPKTAVGKIFK 561
|
....*.
gi 1191882763 545 AALSAL 550
Cdd:PRK07529 562 PALRRD 567
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
37-478 |
6.01e-41 |
|
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: 153.19 E-value: 6.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 37 TYKEVLEQVSRLAGVLVK-HGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTAS 115
Cdd:TIGR01733 1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 116 fgiepgrkveymPILEEAMRIGQhkpdkvLIYNRPNMETVPLASGRDLDWDEemakaqsqdcVPVLSEHPLYILYTSGTT 195
Cdd:TIGR01733 81 ------------ALASRLAGLVL------PVILLDPLELAALDDAPAPPPPD----------APSGPDDLAYVIYTSGST 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 196 GLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVVGHSYIcYGPLIHGNTTVLYEGKPVGtPDAGAYFRVLA 275
Cdd:TIGR01733 133 GRPKGVVVTHRSLVNLLAW-LARRYGLDPDDRVLQFASLSFDASVEEI-FGALLAGATLVVPPEDEER-DDAALLAALIA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 276 EHGVAALFTAPTAIRAIRQQDPGAalgkqysLTRFKTLFVAGERCDVETLE-WSKKVFRVPVLDHWWQTETgsPITASCI 354
Cdd:TIGR01733 210 EHPVTVLNLTPSLLALLAAALPPA-------LASLRLVILGGEALTPALVDrWRARGPGARLINLYGPTET--TVWSTAT 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 355 GLGNSKTPPPGQA--GKSVPGYNVMILDDNMQKLKARCLGNIVVklpLPPGAFSGLW----KNQEAFKHLYFEKFPGY-- 426
Cdd:TIGR01733 281 LVDPDDAPRESPVpiGRPLANTRLYVLDDDLRPVPVGVVGELYI---GGPGVARGYLnrpeLTAERFVPDPFAGGDGArl 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1191882763 427 YDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAV 478
Cdd:TIGR01733 358 YRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
36-550 |
3.24e-40 |
|
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: 151.57 E-value: 3.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 36 ITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAihslifggfaskelssridhakpkVVVTAS 115
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGA------------------------VVIPAT 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 116 FGIEPGRkveympiLEEAMRIGQHKPDKVliynrpnmetvplasgrdldwdEEMAKAqsqdcvpvlsEHPLYILYTSGTT 195
Cdd:cd05974 57 TLLTPDD-------LRDRVDRGGAVYAAV----------------------DENTHA----------DDPMLLYFTSGTT 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 196 GLPKGVVRPTGGYAVMLNWTMSSIyGLKPGEVWWAASDLGWVvGHSYIC-YGPLIHGNTTVLYEGKPVgtpDAGAYFRVL 274
Cdd:cd05974 98 SKPKLVEHTHRSYPVGHLSTMYWI-GLKPGDVHWNISSPGWA-KHAWSCfFAPWNAGATVFLFNYARF---DAKRVLAAL 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 275 AEHGVAALFTAPTAIRAIRQQDpgaalgkqysLTRFKT----LFVAGERCDVETLEWSKKVFRVPVLDHWWQTETGSPIt 350
Cdd:cd05974 173 VRYGVTTLCAPPTVWRMLIQQD----------LASFDVklreVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALV- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 351 asciglGNSKTPP--PGQAGKSVPGYNVMILDDNMQKLKArclGNIVVKL--PLPPGAFSGLWKNQEAFKHLYFEkfpGY 426
Cdd:cd05974 242 ------GNSPGQPvkAGSMGRPLPGYRVALLDPDGAPATE---GEVALDLgdTRPVGLMKGYAGDPDKTAHAMRG---GY 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 427 YDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEGQ 506
Cdd:cd05974 310 YRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPET 389
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1191882763 507 VLeEIVQHVRQSIGPVAAFRKAVFVqQLPKTRSGKIPRAALSAL 550
Cdd:cd05974 390 AL-EIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRRVELRRR 431
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
7-547 |
1.01e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 152.24 E-value: 1.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 7 NAIDRHIESgKGDKVAIIYdspvtdTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAI 86
Cdd:PRK07786 21 NQLARHALM-QPDAPALRF------LGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 87 HSLIFGGFASKELSSRIDHAKPKVVVTASFGIEPGRKV-EYMPILEEAMRIGQHKPDKVLIYNRPNMETVPLASGRDLDW 165
Cdd:PRK07786 94 AVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAPVATAVrDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 166 DEemakaqsqdcvpvlsehPLYILYTSGTTGLPKGVVRPtggYAVMLNWTMSSIYGLK---PGEVWWAASDLGWVVGHSY 242
Cdd:PRK07786 174 DS-----------------PALIMYTSGTTGRPKGAVLT---HANLTGQAMTCLRTNGadiNSDVGFVGVPLFHIAGIGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 243 ICYGPLIhGNTTVLYegkPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIrQQDPGAAlGKQYSLtRFKTlFVAGERCDV 322
Cdd:PRK07786 234 MLPGLLL-GAPTVIY---PLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAV-CAEQQAR-PRDLAL-RVLS-WGAAPASDT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 323 ETLEWSKKVFRVPVLDHWWQTETgSPITasCIGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPP 402
Cdd:PRK07786 306 LLRQMAATFPEAQILAAFGQTEM-SPVT--CMLLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYR---AP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 403 GAFSGLWKNQEAFKhlyfEKFPG-YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGK 481
Cdd:PRK07786 380 TLMSGYWNNPEATA----EAFAGgWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGR 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191882763 482 EDPLKGHVPLALCVLRKDINITEGQVLEEIVQhvrqsiGPVAAFR--KAV-FVQQLPKTRSGKIPRAAL 547
Cdd:PRK07786 456 ADEKWGEVPVAVAAVRNDDAALTLEDLAEFLT------DRLARYKhpKALeIVDALPRNPAGKVLKTEL 518
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
10-547 |
2.88e-39 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 150.97 E-value: 2.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 10 DRHIESgKGDKVAIIYDSPVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSL 89
Cdd:PRK13295 31 DACVAS-CPDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 90 IFGGFASKELSSRIDHAKPKV-VVTASFgiepgRKVEYmpileEAMRIGQHkPDkvliynRPNMETVPLASGRDLD-WDE 167
Cdd:PRK13295 110 LMPIFRERELSFMLKHAESKVlVVPKTF-----RGFDH-----AAMARRLR-PE------LPALRHVVVVGGDGADsFEA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 168 ---EMAKAQSQDCVPVLSEHPL------YILYTSGTTGLPKGVVRPTggyavmlNWTMSSIY------GLKPGEVWWAAS 232
Cdd:PRK13295 173 lliTPAWEQEPDAPAILARLRPgpddvtQLIYTSGTTGEPKGVMHTA-------NTLMANIVpyaerlGLGADDVILMAS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 233 DLGWVVGHSYICYGPLIHGNTTVLYEgkpVGTPDAGAyfRVLAEHGVAalFT---APTAIRAIRQQDPGAalgkqYSLTR 309
Cdd:PRK13295 246 PMAHQTGFMYGLMMPVMLGATAVLQD---IWDPARAA--ELIRTEGVT--FTmasTPFLTDLTRAVKESG-----RPVSS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 310 FKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQTETGSpitASCIGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKAR 389
Cdd:PRK13295 314 LRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA---VTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 390 CLGNIVVKlplPPGAFSGLWKNQeafkHLYFEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLS 469
Cdd:PRK13295 391 QIGRLQVR---GCSNFGGYLKRP----QLNGTDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 470 HGTVADCAVVGKEDPLKGHVPLALCVLRKDINITegqvLEEIV-----QHVRQSIGPvaafRKAVFVQQLPKTRSGKIPR 544
Cdd:PRK13295 464 HPAIAQVAIVAYPDERLGERACAFVVPRPGQSLD----FEEMVeflkaQKVAKQYIP----ERLVVRDALPRTPSGKIQK 535
|
...
gi 1191882763 545 AAL 547
Cdd:PRK13295 536 FRL 538
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
7-549 |
1.55e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 148.60 E-value: 1.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 7 NAIDRHiesgkGDKVAIIydspvtDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQA----MYTMLACAR 82
Cdd:PRK06188 20 SALKRY-----PDRPALV------LGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVlmaiGAAQLAGLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 83 IGAIHSLifggfaskelSSRIDH------AKPKVVVtasfgIEPGrkveymPILEEAMRIGQHKPdkvliyNRPNMETV- 155
Cdd:PRK06188 89 RTALHPL----------GSLDDHayvledAGISTLI-----VDPA------PFVERALALLARVP------SLKHVLTLg 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 156 PLASGRDLDwdEEMAKAQSQDCVPV-LSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSsiyglkpgevwwaasDL 234
Cdd:PRK06188 142 PVPDGVDLL--AAAAKFGPAPLVAAaLPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLA---------------EW 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 235 GWVVGHSYICYGPLIH------------GNTTVLYEGKpvgtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAAlg 302
Cdd:PRK06188 205 EWPADPRFLMCTPLSHaggafflptllrGGTVIVLAKF-----DPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRT-- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 303 kqYSLTRFKTLFVAGERCDVETLEWSKKVFRvPVL-DHWWQTETGSPIT---------------ASCiglgnsktpppgq 366
Cdd:PRK06188 278 --RDLSSLETVYYGASPMSPVRLAEAIERFG-PIFaQYYGQTEAPMVITylrkrdhdpddpkrlTSC------------- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 367 aGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGafsGLWK----NQEAFKHlyfekfpGYYDTMDAGYMDEEGYVY 442
Cdd:PRK06188 342 -GRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMD---GYWNrpeeTAEAFRD-------GWLHTGDVAREDEDGFYY 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 443 VMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEgqvlEEIVQHVRQSIGPV 522
Cdd:PRK06188 411 IVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDA----AELQAHVKERKGSV 486
|
570 580
....*....|....*....|....*..
gi 1191882763 523 AAFRKAVFVQQLPKTRSGKIPRAALSA 549
Cdd:PRK06188 487 HAPKQVDFVDSLPLTALGKPDKKALRA 513
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
37-547 |
3.29e-38 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 147.98 E-value: 3.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 37 TYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTASF 116
Cdd:PRK06155 48 TYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 117 GIEpgrKVEYMPILEEAMRigqhkpdKVLIYNRPNMETVPLAsgrdLDWDEEMAKAQSQDCVPVLSEHPLYILYTSGTTG 196
Cdd:PRK06155 128 LLA---ALEAADPGDLPLP-------AVWLLDAPASVSVPAG----WSTAPLPPLDAPAPAAAVQPGDTAAILYTSGTTG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 197 LPKGVVRPTGGYavmlnwtmssiyglkpgeVWW---AASDLGWVVGHSYICYGPLIHGNT------TVLYEGKPVGTP-- 265
Cdd:PRK06155 194 PSKGVCCPHAQF------------------YWWgrnSAEDLEIGADDVLYTTLPLFHTNAlnaffqALLAGATYVLEPrf 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 266 DAGAYFRVLAEHGvAALFTAPTAIRAIRQQDPGAALGKQYSLT---------RFKTLFvaGERcdvetlewskkvFRVPV 336
Cdd:PRK06155 256 SASGFWPAVRRHG-ATVTYLLGAMVSILLSQPARESDRAHRVRvalgpgvpaALHAAF--RER------------FGVDL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 337 LDHWWQTETGSPITASciglgnSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPlPPGAF-SGLW----KN 411
Cdd:PRK06155 321 LDGYGSTETNFVIAVT------HGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRAD-EPFAFaTGYFgmpeKT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 412 QEAFKHLYFEkfpgyydTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPL 491
Cdd:PRK06155 394 VEAWRNLWFH-------TGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVM 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1191882763 492 ALCVLRkdinitEGQVLE--EIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:PRK06155 467 AAVVLR------DGTALEpvALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
19-549 |
6.23e-37 |
|
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: 147.31 E-value: 6.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIIYDSpvtdtkATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMP----MIPqamyTMLACARIGAIHslifggf 94
Cdd:COG1020 491 DAVAVVFGD------QSLTYAELNARANRLAHHLRALGVGPGDLVGVCLErsleMVV----ALLAVLKAGAAY------- 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 95 askeLSsrIDHAKPkvvvtasfgiePGRkVEYMpiLEEAmrigqhKPdKVLIYNRPNMETVPLASGRDLDWDEEMAKAQS 174
Cdd:COG1020 554 ----VP--LDPAYP-----------AER-LAYM--LEDA------GA-RLVLTQSALAARLPELGVPVLALDALALAAEP 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 175 QD--CVPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVVGHSYIcYGPLIHGN 252
Cdd:COG1020 607 ATnpPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAW-MQRRYGLGPGDRVLQFASLSFDASVWEI-FGALLSGA 684
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 253 TTVLYEgkPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAalgkqysLTRFKTLFVAGERCDVETLE-WSKKV 331
Cdd:COG1020 685 TLVLAP--PEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEA-------LPSLRLVLVGGEALPPELVRrWRARL 755
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 332 FRVPVLDHWWQTETGspITASCiglgnSKTPPPGQAGKSVP------GYNVMILDDNMQklkarclgnivvklPLPPGAf 405
Cdd:COG1020 756 PGARLVNLYGPTETT--VDSTY-----YEVTPPDADGGSVPigrpiaNTRVYVLDAHLQ--------------PVPVGV- 813
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 406 SG-LW---------------KNQEAFKHLYFEkFPG--YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESL 467
Cdd:COG1020 814 PGeLYiggaglargylnrpeLTAERFVADPFG-FPGarLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAAL 892
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 468 LSHGTVADCAVVGKEDPLkGHVPLALCVLRKDINITEGQVLEEIVQHVRQSIGPVAAFrkaVFVQQLPKTRSGKIPRAAL 547
Cdd:COG1020 893 LQHPGVREAVVVAREDAP-GDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAV---VLLLPLPLTGNGKLDRLAL 968
|
..
gi 1191882763 548 SA 549
Cdd:COG1020 969 PA 970
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
35-547 |
1.11e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 140.56 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 35 TITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAihslifggfaskelssridhakpkVVVTA 114
Cdd:PRK07470 32 SWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGA------------------------VWVPT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 115 SFGIEPGrKVEYMpileeamriGQHKPDKVLIYNRPNMETVPL--ASGRDLDW-------------DEEMAKAQSQDCVP 179
Cdd:PRK07470 88 NFRQTPD-EVAYL---------AEASGARAMICHADFPEHAAAvrAASPDLTHvvaiggaragldyEALVARHLGARVAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 180 VLSEH--PLYILYTSGTTGLPKGVVRPTGGYAVMLNwtmSSIYGLKPGEvwwAASDLGWVVGhsyicygPLIHGN----- 252
Cdd:PRK07470 158 AAVDHddPCWFFFTSGTTGRPKAAVLTHGQMAFVIT---NHLADLMPGT---TEQDASLVVA-------PLSHGAgihql 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 253 -------TTVLYEGKPVgtpDAGAYFRVLAEHGVAALFTAPTaIRAIRQQDPGAALGKQYSLtrfKTLFVAGE---RCDv 322
Cdd:PRK07470 225 cqvargaATVLLPSERF---DPAEVWALVERHRVTNLFTVPT-ILKMLVEHPAVDRYDHSSL---RYVIYAGApmyRAD- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 323 etlewSKKVFRV--PVLDHWWqtetgspitasciGL----GNSKTPPP-------------GQAGKSVPGYNVMILDDNM 383
Cdd:PRK07470 297 -----QKRALAKlgKVLVQYF-------------GLgevtGNITVLPPalhdaedgpdariGTCGFERTGMEVQIQDDEG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 384 QKLKARCLGNIVVklpLPPGAFSGLWKNQEA----FKHlyfekfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRIS 459
Cdd:PRK07470 359 RELPPGETGEICV---IGPAVFAGYYNNPEAnakaFRD-------GWFRTGDLGHLDARGFLYITGRASDMYISGGSNVY 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 460 AGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEgqvlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRS 539
Cdd:PRK07470 429 PREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDE----AELLAWLDGKVARYKLPKRFFFWDALPKSGY 504
|
....*...
gi 1191882763 540 GKIPRAAL 547
Cdd:PRK07470 505 GKITKKMV 512
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
36-547 |
3.43e-35 |
|
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: 137.61 E-value: 3.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 36 ITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTAS 115
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 116 fgiepgrkveympileeamrigqhkpdkvliynrpNMETVPLasgrdldwdeemakaqsqdcvpvlsehplyILYTSGTT 195
Cdd:cd05935 82 -----------------------------------ELDDLAL------------------------------IPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 196 GLPKGVVRpTGGYAVMLNWTMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLyegkpVGTPDAGAYFRVLA 275
Cdd:cd05935 97 GLPKGCMH-THFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVL-----MARWDRETALELIE 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 276 EHGVAALFTAPTAIRAIrQQDPGAalgKQYSLTRFKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQTETGSPITascig 355
Cdd:cd05935 171 KYKVTFWTNIPTMLVDL-LATPEF---KTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTH----- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 356 lgnskTPPPGQAGKS---VPGYNV--MILD-DNMQKLKARCLGNIVVKlplPPGAFSGLWK----NQEAFKHLYFEKFpg 425
Cdd:cd05935 242 -----TNPPLRPKLQclgIP*FGVdaRVIDiETGRELPPNEVGEIVVR---GPQIFKGYWNrpeeTEESFIEIKGRRF-- 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 426 yYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDI--NIT 503
Cdd:cd05935 312 -FRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYrgKVT 390
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1191882763 504 EgqvlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:cd05935 391 E----EDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
35-547 |
4.29e-35 |
|
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: 136.71 E-value: 4.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 35 TITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTA 114
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKLDDIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 115 SfgiepgrkveympileeamrigqhkpdkvliynrpnmetvplasgrdldwdeemakaqsqdcvpvlsehplyILYTSGT 194
Cdd:cd05912 81 T------------------------------------------------------------------------IMYTSGT 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 195 TGLPKGVVRPTGGY-----AVMLNwtmssiYGLKPGEVWWAASDLGWVVGHSYICYGpLIHGNTTVLYEgkpvgTPDAGA 269
Cdd:cd05912 89 TGKPKGVQQTFGNHwwsaiGSALN------LGLTEDDNWLCALPLFHISGLSILMRS-VIYGMTVYLVD-----KFDAEQ 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 270 YFRVLAEHGVAALFTAPTAIRAIRQQDPGAalgkqYSLTrFKTLFVAGERCDVETLEWSKKvFRVPVLDHWWQTETGSPI 349
Cdd:cd05912 157 VLHLINSGKVTIISVVPTMLQRLLEILGEG-----YPNN-LRCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTETCSQI 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 350 TASCIGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKarcLGNIVVKLP-LPPGAFSGLWKNQEAFKHlyfekfpGYYD 428
Cdd:cd05912 230 VTLSPEDALNK---IGSAGKPLFPVELKIEDDGQPPYE---VGEILLKGPnVTKGYLNRPDATEESFEN-------GWFK 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 429 TMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINitegqvL 508
Cdd:cd05912 297 TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPIS------E 370
|
490 500 510
....*....|....*....|....*....|....*....
gi 1191882763 509 EEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:cd05912 371 EELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
19-547 |
1.34e-34 |
|
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: 136.87 E-value: 1.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIIydspVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 98
Cdd:cd05923 16 DACAIA----DPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 99 LSSRIDHAKPKVVVtasfgiepgrkveympileeamrigqHKPDkvliynRPNMETVPLASGRDLDWDEEMAKAQSQDCV 178
Cdd:cd05923 92 LAELIERGEMTAAV--------------------------IAVD------AQVMDAIFQSGVRVLALSDLVGLGEPESAG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 179 PVLS------EHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWtMSSIYGLKPG--EVWWAASDLGWVVGHSYICYGPLIH 250
Cdd:cd05923 140 PLIEdpprepEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLF-MSTQAGLRHGrhNVVLGLMPLYHVIGFFAVLVAALAL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 251 GNTTVlyegkPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIrqqdPGAALGKQYSLTRFKTLFVAGERCDVETLEWSKK 330
Cdd:cd05923 219 DGTYV-----VVEEFDPADALKLIEQERVTSLFATPTHLDAL----AAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 331 VFRVPVLDHWWQTETGSPITAsciglgnsKTPPPGQAGKsvPGYN-----VMILDDNMQKLKARCLGNIVVKLPlPPGAF 405
Cdd:cd05923 290 HLPGEKVNIYGTTEAMNSLYM--------RDARTGTEMR--PGFFsevriVRIGGSPDEALANGEEGELIVAAA-ADAAF 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 406 SGLWKNQEA-FKHLYFekfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDP 484
Cdd:cd05923 359 TGYLNQPEAtAKKLQD----GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADE 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191882763 485 LKGHVPLAlCVLRKDINITEgqvlEEIVQHVRQSigPVAAF---RKAVFVQQLPKTRSGKIPRAAL 547
Cdd:cd05923 435 RWGQSVTA-CVVPREGTLSA----DELDQFCRAS--ELADFkrpRRYFFLDELPKNAMNKVLRRQL 493
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
32-547 |
7.70e-34 |
|
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: 135.35 E-value: 7.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 32 TKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVV 111
Cdd:cd17642 41 TGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 112 VTASFGIEPGRKVEY-MPILEeamrigqhkpdKVLIynrpnmetvpLASGRDLDWDEEMAKAQSQDCVPVLSEHPL---- 186
Cdd:cd17642 121 FCSKKGLQKVLNVQKkLKIIK-----------TIII----------LDSKEDYKGYQCLYTFITQNLPPGFNEYDFkpps 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 187 --------YILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLGWVvgHSYICY---GPLIHGNTTV 255
Cdd:cd17642 180 fdrdeqvaLIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNQIIPDTAILTVIPFH--HGFGMFttlGYLICGFRVV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 256 LyegkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIrqqdPGAALGKQYSLTRFKTLFVAGERCDVETLEWSKKVFRVP 335
Cdd:cd17642 258 L-----MYKFEEELFLRSLQDYKVQSALLVPTLFAFF----AKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 336 -VLDHWWQTETGSPITASciglgNSKTPPPGQAGKSVPGYNVMILD-DNMQKLKARCLGNIVVKlplPPGAFSGLWKNQE 413
Cdd:cd17642 329 gIRQGYGLTETTSAILIT-----PEGDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVK---GPMIMKGYVNNPE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 414 AFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLAL 493
Cdd:cd17642 401 ATKALIDKD--GWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAV 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1191882763 494 CVLRKDINITEgqvlEEIVQHVRQSIGPVAAFRKAV-FVQQLPKTRSGKIPRAAL 547
Cdd:cd17642 479 VVLEAGKTMTE----KEVMDYVASQVSTAKRLRGGVkFVDEVPKGLTGKIDRRKI 529
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
37-547 |
2.31e-33 |
|
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: 133.52 E-value: 2.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 37 TYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAI-HSLIFGGFAsKELSSRIDHAKPKVVVtas 115
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVlHTINPRLFP-EQIAYIINHAEDRVVF--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 116 fgIEPgrkvEYMPILEEAMriGQHKPDKVLIYNRPNMETVPLASGRDLDWDEEMAKAQSQDCVPVLSEH-PLYILYTSGT 194
Cdd:cd12119 103 --VDR----DFLPLLEAIA--PRLPTVEHVVVMTDDAAMPEPAGVGVLAYEELLAAESPEYDWPDFDENtAAAICYTSGT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 195 TGLPKGVV---RPTGGYAVMLNwtMSSIYGLKPGEVwwaasdlgwvvghsYICYGPLIHGN------TTVLYEGK---PV 262
Cdd:cd12119 175 TGNPKGVVyshRSLVLHAMAAL--LTDGLGLSESDV--------------VLPVVPMFHVNawglpyAAAMVGAKlvlPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 263 GTPDAGAYFRVLAEHGVAalFTA--PTAIRAIRQQdPGAALGKQYSLTRfktLFVAGERCDVETLEWSKKVFrVPVLDHW 340
Cdd:cd12119 239 PYLDPASLAELIEREGVT--FAAgvPTVWQGLLDH-LEANGRDLSSLRR---VVIGGSAVPRSLIEAFEERG-VRVIHAW 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 341 WQTETgSPI-TASCIGLGNSKTPPPGQA------GKSVPGYNVMILDDNMQKLKA--RCLGNIVVKLP-LPPGAFsglwK 410
Cdd:cd12119 312 GMTET-SPLgTVARPPSEHSNLSEDEQLalrakqGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPwVTKSYY----K 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 411 NQEAfKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVP 490
Cdd:cd12119 387 NDEE-SEALTED--GWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERP 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1191882763 491 LALCVLRKDINITEgqvlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:cd12119 464 LAVVVLKEGATVTA----EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
18-547 |
3.22e-33 |
|
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: 132.41 E-value: 3.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 18 GDKVAIIYDSpvtdtkATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHslifggfask 97
Cdd:cd12116 1 PDATAVRDDD------RSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAY---------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 98 elssridhakpkVVVTASFgiePGRKVEYMpiLEEAmrigqhKPdKVLIYNRPNMETVPLASGRDLDWDEEMAKAQSQDC 177
Cdd:cd12116 65 ------------VPLDPDY---PADRLRYI--LEDA------EP-ALVLTDDALPDRLPAGLPVLLLALAAAAAAPAAPR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 178 VPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNwTMSSIYGLKPGEVWWAASDLGWVVGHSYIcYGPLIHGNTTVLY 257
Cdd:cd12116 121 TPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLH-SMRERLGLGPGDRLLAVTTYAFDISLLEL-LLPLLAGARVVIA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 258 EGKpvGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALGKqysltrfkTLFVAGERCDVETLEwsKKVFRVPVL 337
Cdd:cd12116 199 PRE--TQRDPEALARLIEAHSITVMQATPATWRMLLDAGWQGRAGL--------TALCGGEALPPDLAA--RLLSRVGSL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 338 dhwWQ----TETgsPITASCIGLGNSKTPPPgqAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGLWKNQE 413
Cdd:cd12116 267 ---WNlygpTET--TIWSTAARVTAAAGPIP--IGRPLANTQVYVLDAALR--------------PVPPGVPGELYIGGD 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 414 AFKHLYF-------EKF-------PG--YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCA 477
Cdd:cd12116 326 GVAQGYLgrpaltaERFvpdpfagPGsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAA 405
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 478 VVGKEDPLKGHVpLALCVLRKDINITEGQVLEEIVQHVRQSIGPVAAFRkavfVQQLPKTRSGKIPRAAL 547
Cdd:cd12116 406 VVVREDGGDRRL-VAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVR----LDALPLTANGKLDRKAL 470
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
36-547 |
1.36e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 132.08 E-value: 1.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 36 ITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMytmlacarIGAIHSLIFGG--------FASKELSSRIDHAK 107
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAV--------IGYYGTLLAGGivvqtnplYTERELEYQLHDSG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 108 PKVVVTASF------GIEPGRKVEYMPIleeaMRIGQHKP-DKVLIY-----NRPNMETVPLASGRDLDWDEEMAKAQSQ 175
Cdd:PRK06710 122 AKVILCLDLvfprvtNVQSATKIEHVIV----TRIADFLPfPKNLLYpfvqkKQSNLVVKVSESETIHLWNSVEKEVNTG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 176 DCVPVLSEHPLYIL-YTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEvwwaasDLGWVVGHSYICYGPLIHGNTT 254
Cdd:PRK06710 198 VEVPCDPENDLALLqYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGE------EVVLGVLPFFHVYGMTAVMNLS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 255 VLYEGKPVGTP--DAGAYFRVLAEHGVAALFTAPTAIRAIRQqdpgAALGKQYSLTRFKTLFVAGERCDVETLEWSKKVF 332
Cdd:PRK06710 272 IMQGYKMVLIPkfDMKMVFEAIKKHKVTLFPGAPTIYIALLN----SPLLKEYDISSIRACISGSAPLPVEVQEKFETVT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 333 RVPVLDHWWQTETgSPITASCIgLGNSKTPppGQAGKSVPGYNVMILD-DNMQKLKARCLGNIVVKlplPPGAFSGLWKN 411
Cdd:PRK06710 348 GGKLVEGYGLTES-SPVTHSNF-LWEKRVP--GSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVK---GPQIMKGYWNK 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 412 QEAFKHLYFEkfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPL 491
Cdd:PRK06710 421 PEETAAVLQD---GWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVK 497
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1191882763 492 ALCVLRKDINITEgqvlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:PRK06710 498 AFVVLKEGTECSE----EELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
19-547 |
3.56e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 130.43 E-value: 3.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIIydspvtDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIyMPMIPQAM-YTMLACARIGAIHSLIFGGFASK 97
Cdd:PRK07788 64 DRAALI------DERGTLTYAELDEQSNALARGLLALGVRAGDGVAV-LARNHRGFvLALYAAGKVGARIILLNTGFSGP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 98 ELSSRIDHAKPKVVVTASfgiepgrkvEYMPILEEAmrigqhKPD----KVLIYNRPNMETVPlASGRDLDwdeEMAKAQ 173
Cdd:PRK07788 137 QLAEVAAREGVKALVYDD---------EFTDLLSAL------PPDlgrlRAWGGNPDDDEPSG-STDETLD---DLIAGS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 174 SQDCVPVLSEHPLYILYTSGTTGLPKGVVRPT----GGYAVMLNWTmssiyGLKPGEVWWAASDL--GWVVGHSYICYGp 247
Cdd:PRK07788 198 STAPLPKPPKPGGIVILTSGTTGTPKGAPRPEpsplAPLAGLLSRV-----PFRAGETTLLPAPMfhATGWAHLTLAMA- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 248 liHGNTTVLYEgkpvgTPDAGAYFRVLAEHGVAALFTAPTAIRaiRQQDPGAALGKQYSLTRFKTLFVAGERCDVETLEW 327
Cdd:PRK07788 272 --LGSTVVLRR-----RFDPEATLEDIAKHKATALVVVPVMLS--RILDLGPEVLAKYDTSSLKIIFVSGSALSPELATR 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 328 SKKVFRvPVLDHWW-QTETGSPITAsciglgnskTPP-----PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLP 401
Cdd:PRK07788 343 ALEAFG-PVLYNLYgSTEVAFATIA---------TPEdlaeaPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFP 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 402 pgaFSGlwknqeafkhlYF-----EKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADC 476
Cdd:PRK07788 413 ---FEG-----------YTdgrdkQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEA 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191882763 477 AVVGKEDPLKGHVPLALCVLRKDINITEgqvlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:PRK07788 479 AVIGVDDEEFGQRLRAFVVKAPGAALDE----DAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKREL 545
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
29-549 |
8.70e-32 |
|
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: 129.13 E-value: 8.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 29 VTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKP 108
Cdd:TIGR03098 19 LVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 109 KVVVTASfgiepgrkvEYMPILEEAMRiGQHKPDKVLIYNRPNMETVPLASGRDLDWDEEMAKAQSQDCVPVLSEHPLYI 188
Cdd:TIGR03098 99 RLLVTSS---------ERLDLLHPALP-GCHDLRTLIIVGDPAHASEGHPGEEPASWPKLLALGDADPPHPVIDSDMAAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 189 LYTSGTTGLPKGVVRP-----TGGYAVmlnwtmSSIYGLKPGEVWWAASDLGWVVGHSYICYGpLIHGNTTVLYE---GK 260
Cdd:TIGR03098 169 LYTSGSTGRPKGVVLShrnlvAGAQSV------ATYLENRPDDRLLAVLPLSFDYGFNQLTTA-FYVGATVVLHDyllPR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 261 PVGT--------------------------PDAGAYFRVLAEHGVAalfTAPTAIRAIRQQDPGAALGKQYSLTR-FKTL 313
Cdd:TIGR03098 242 DVLKalekhgitglaavpplwaqlaqldwpESAAPSLRYLTNSGGA---MPRATLSRLRSFLPNARLFLMYGLTEaFRST 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 314 FVAGERCDVEtlewskkvfrvpvldhwwqtetgspitasciglgnsktppPGQAGKSVPGYNVMILDDnmqkLKARCL-- 391
Cdd:TIGR03098 319 YLPPEEVDRR----------------------------------------PDSIGKAIPNAEVLVLRE----DGSECApg 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 392 --GNIVVKLPLppgAFSGLWKNQEAFKHLyFEKFPGYYDTM----------DAGYMDEEGYVYVMSRVDDVINVAGHRIS 459
Cdd:TIGR03098 355 eeGELVHRGAL---VAMGYWNDPEKTAER-FRPLPPFPGELhlpelavwsgDTVRRDEEGFLYFVGRRDEMIKTSGYRVS 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 460 AGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEGQVLEEIVQHVRQSIGPvaafRKAVFVQQLPKTRS 539
Cdd:TIGR03098 431 PTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGEELDRAALLAECRARLPNYMVP----ALIHVRQALPRNAN 506
|
570
....*....|
gi 1191882763 540 GKIPRAALSA 549
Cdd:TIGR03098 507 GKIDRKALAK 516
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
11-550 |
1.42e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 129.01 E-value: 1.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 11 RHIESGKGDKVAIIYdspvtdTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLI 90
Cdd:PRK06178 40 RAWARERPQRPAIIF------YGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 91 FGGFASKELSSRIDHAKPKVVVTASFGIEPGRKVEYMPILEEAMRIGQHKpdkVLiynrPNMETVPL------ASGRDLD 164
Cdd:PRK06178 114 SPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSLRHVIVTSLAD---VL----PAEPTLPLpdslraPRLAAAG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 165 WDEEMA-----KAQSQDCVPVLSEhPLYILYTSGTTGLPKGVVRpTGGYAVmlnWTMSSIYGLKPG------------EV 227
Cdd:PRK06178 187 AIDLLPalracTAPVPLPPPALDA-LAALNYTGGTTGMPKGCEH-TQRDMV---YTAAAAYAVAVVggedsvflsflpEF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 228 WWAASDLGWVVghsyicygPLIHGNTTVLyegkpVGTPDAGAYFRVLAEHGVAALF-TAPTAIRAIrqQDPGAAlgkQYS 306
Cdd:PRK06178 262 WIAGENFGLLF--------PLFSGATLVL-----LARWDAVAFMAAVERYRVTRTVmLVDNAVELM--DHPRFA---EYD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 307 LTRFKTLFVAgercdvetlEWSKKVfrVPVLDHWWQTETGSPITASCIGLGNSKT----------------PPPGQAGKS 370
Cdd:PRK06178 324 LSSLRQVRVV---------SFVKKL--NPDYRQRWRALTGSVLAEAAWGMTETHTcdtftagfqdddfdllSQPVFVGLP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 371 VPGYNVMILD-DNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYVYVMSRVDD 449
Cdd:PRK06178 393 VPGTEFKICDfETGELLPLGAEGEIVVR---TPSLLKGYWNKPEATAEALRD---GWLHTGDIGKIDEQGFLHYLGRRKE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 450 VINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEgqvlEEIVQHVRQSIGP--VAAFRk 527
Cdd:PRK06178 467 MLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTA----AALQAWCRENMAVykVPEIR- 541
|
570 580
....*....|....*....|...
gi 1191882763 528 avFVQQLPKTRSGKIPRAALSAL 550
Cdd:PRK06178 542 --IVDALPMTATGKVRKQDLQAL 562
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
19-542 |
4.34e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 127.38 E-value: 4.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIIYdspvtdTKATITYKEVLEQVSRLAGVLV-KHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 97
Cdd:PRK08314 25 DKTAIVF------YGRAISYRELLEEAERLAGYLQqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 98 ELSSRIDHAKPKVVVTASfgiepgrkvEYMPILEEA---MRIG------------QHKPDKVLIYNRPNMETVPLASGRD 162
Cdd:PRK08314 99 ELAHYVTDSGARVAIVGS---------ELAPKVAPAvgnLRLRhvivaqysdylpAEPEIAVPAWLRAEPPLQALAPGGV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 163 LDWDEEMAkaqSQDCVPVLSEHP--LYIL-YTSGTTGLPKGVVRPTGgyAVMLNWTMSSI-YGLKPGEVWWAASDLGWVV 238
Cdd:PRK08314 170 VAWKEALA---AGLAPPPHTAGPddLAVLpYTSGTTGVPKGCMHTHR--TVMANAVGSVLwSNSTPESVVLAVLPLFHVT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 239 GHSYICYGPLIHGNTTVLYegkPVGTPDAGAyfRVLAEHGVAALFTAPT------AIRAIRQQD---------PGAALGK 303
Cdd:PRK08314 245 GMVHSMNAPIYAGATVVLM---PRWDREAAA--RLIERYRVTHWTNIPTmvvdflASPGLAERDlsslryiggGGAAMPE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 304 qysltrfktlfVAGERCdvetlewsKKVFRVPVLDHWWQTETGSPITASciglgnsktPP--PGQAGKSVPGYNV--MIL 379
Cdd:PRK08314 320 -----------AVAERL--------KELTGLDYVEGYGLTETMAQTHSN---------PPdrPKLQCLGIPTFGVdaRVI 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 380 D-DNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEkFPG--YYDTMDAGYMDEEGYVYVMSRVDDVINVAGH 456
Cdd:PRK08314 372 DpETLEELPPGEVGEIVVH---GPQVFKGYWNRPEATAEAFIE-IDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGF 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 457 RISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKD--INITEgqvlEEIVQHVRQSIGPVAAFRKAVFVQQL 534
Cdd:PRK08314 448 KVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEarGKTTE----EEIIAWAREHMAAYKYPRIVEFVDSL 523
|
....*...
gi 1191882763 535 PKTRSGKI 542
Cdd:PRK08314 524 PKSGSGKI 531
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
17-547 |
4.44e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 126.94 E-value: 4.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 17 KGDKVAIIYDSpvtdtkATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFAS 96
Cdd:PRK07656 18 FGDKEAYVFGD------QRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 97 KELSSRIDHAKPKVVVTASfgiepgrkvEYMPILEEAMrigQHKPDKVLIYNRPNMETVPLASgRDLDWDEEMA-KAQSQ 175
Cdd:PRK07656 92 DEAAYILARGDAKALFVLG---------LFLGVDYSAT---TRLPALEHVVICETEEDDPHTE-KMKTFTDFLAaGDPAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 176 DCVPVLSEHPLYILYTSGTTGLPKGVvrptggyavMLN----------WtmSSIYGLKPGEVWWAASDLGWVVGHSYICY 245
Cdd:PRK07656 159 RAPEVDPDDVADILFTSGTTGRPKGA---------MLThrqllsnaadW--AEYLGLTEGDRYLAANPFFHVFGYKAGVN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 246 GPLIHGNTTVlyegkPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAAlgkqyslTRFKTLFVA---GERCDV 322
Cdd:PRK07656 228 APLMRGATIL-----PLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSA-------EDLSSLRLAvtgAASMPV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 323 ETLEWSKKVFRVP-VLDHWWQTETgSPITASCiGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplP 401
Cdd:PRK07656 296 ALLERFESELGVDiVLTGYGLSEA-SGVTTFN-RLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVR---G 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 402 PGAFSGLWKNQEAFKHLYfeKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGK 481
Cdd:PRK07656 371 PNVMKGYYDDPEATAAAI--DADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGV 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191882763 482 EDPLKGHVPLALCVLRKDINITEgqvlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:PRK07656 449 PDERLGEVGKAYVVLKPGAELTE----EELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
29-547 |
5.56e-31 |
|
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: 126.30 E-value: 5.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 29 VTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKP 108
Cdd:cd17651 14 LVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 109 KVVVTASfgiepgrkvEYMPILEeamrigqhkpdkvliynrpnmetVPLASGRDLDWDEEMAKAQSQDCVPVLSEHPLYI 188
Cdd:cd17651 94 VLVLTHP---------ALAGELA-----------------------VELVAVTLLDQPGAAAGADAEPDPALDADDLAYV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 189 LYTSGTTGLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVVGHSYIcYGPLIHGNTTVLyeGKPVGTPDAG 268
Cdd:cd17651 142 IYTSGSTGRPKGVVMPHRSLANLVAW-QARASSLGPGARTLQFAGLGFDVSVQEI-FSTLCAGATLVL--PPEEVRTDPP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 269 AYFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQysLTRFKTLFVAGER--CDVETLEWSKKVFRVPVLDHWWQTETG 346
Cdd:cd17651 218 ALAAWLDEQRISRVFLPTVALRALAEH--GRPLGVR--LAALRYLLTGGEQlvLTEDLREFCAGLPGLRLHNHYGPTETH 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 347 SpitASCIGLGNSKTPPPGQA--GKSVPGYNVMILDDNMQklkarclgnivvklPLPPG-------AFSGLWKNQEAFKH 417
Cdd:cd17651 294 V---VTALSLPGDPAAWPAPPpiGRPIDNTRVYVLDAALR--------------PVPPGvpgelyiGGAGLARGYLNRPE 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 418 LYFEKF------PG--YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHV 489
Cdd:cd17651 357 LTAERFvpdpfvPGarMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKR 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1191882763 490 PLALCVLRKDinitEGQVLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:cd17651 437 LVAYVVGDPE----APVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
26-547 |
5.64e-31 |
|
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: 125.82 E-value: 5.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 26 DSPVTDTK-ATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRID 104
Cdd:cd05945 6 DRPAVVEGgRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 105 HAKPKVVVTAsfgiepgrkveympileeamrigqhkPDkvliynrpnmetvPLAsgrdldwdeemakaqsqdcvpvlseh 184
Cdd:cd05945 86 AAKPALLIAD--------------------------GD-------------DNA-------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 185 plYILYTSGTTGLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVVGHSYIcYGPLIHGNTTVlyegkPVG- 263
Cdd:cd05945 101 --YIIFTSGSTGRPKGVQISHDNLVSFTNW-MLSDFPLGPGDVFLNQAPFSFDLSVMDL-YPALASGATLV-----PVPr 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 264 --TPDAGAYFRVLAEHGVAALFTAPTAIRAIRQqDPGAALGKQYSLTRFktLFvAGERCDVETLE-WSKKVFRVPVLDHW 340
Cdd:cd05945 172 daTADPKQLFRFLAEHGITVWVSTPSFAAMCLL-SPTFTPESLPSLRHF--LF-CGEVLPHKTARaLQQRFPDARIYNTY 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 341 WQTETGSPITASCIglgnskTPPPGQAGKSVP-GY-----NVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEa 414
Cdd:cd05945 248 GPTEATVAVTYIEV------TPEVLDGYDRLPiGYakpgaKLVILDEDGRPVPPGEKGELVIS---GPSVSKGYLNNPE- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 415 fKHLY-FEKFPGY--YDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPL 491
Cdd:cd05945 318 -KTAAaFFPDEGQraYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELI 396
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1191882763 492 ALCVLRKDiniTEGQVLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:cd05945 397 AFVVPKPG---AEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
18-542 |
8.30e-31 |
|
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: 125.87 E-value: 8.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 18 GDKVAIIYDSPVtdtkatITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPqAMYTM-LACARIGAIHSLIFGGFAS 96
Cdd:cd12118 18 PDRTSIVYGDRR------YTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTP-AMYELhFGVPMAGAVLNALNTRLDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 97 KELSSRIDHAKPKVVVTasfgiepGRKVEYmpilEEAMRIGqhKPDKVLIynRPNMEtvplasgrdldWDeemakaqsqd 176
Cdd:cd12118 91 EEIAFILRHSEAKVLFV-------DREFEY----EDLLAEG--DPDFEWI--PPADE-----------WD---------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 177 cvpvlsehPLYILYTSGTTGLPKGVVRPTGGyaVMLNwTMSSIY--GLKPGEVwwaasdlgwvvghsYICYGPLIHGN-- 252
Cdd:cd12118 135 --------PIALNYTSGTTGRPKGVVYHHRG--AYLN-ALANILewEMKQHPV--------------YLWTLPMFHCNgw 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 253 ----TTVLYEGKPVGTP--DAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALgkqySLTRFKTLFVAGERCDVETLE 326
Cdd:cd12118 190 cfpwTVAAVGGTNVCLRkvDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDAR----PLPHRVHVMTAGAPPPAAVLA 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 327 WSK----KVFRVPVLdhwwqTETGSPITAsCIGLGNSKT-PPPGQA------GKSVPGYN-VMILDDNMQKLKAR----- 389
Cdd:cd12118 266 KMEelgfDVTHVYGL-----TETYGPATV-CAWKPEWDElPTEERArlkarqGVRYVGLEeVDVLDPETMKPVPRdgkti 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 390 ----CLGNIVVKlplppgafsGLWKN----QEAFKHlyfekfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAG 461
Cdd:cd12118 340 geivFRGNIVMK---------GYLKNpeatAEAFRG-------GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSV 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 462 AIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEgqvlEEIVQHVRQSIgpvAAFR--KAVFVQQLPKTRS 539
Cdd:cd12118 404 EVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTE----EEIIAFCREHL---AGFMvpKTVVFGELPKTST 476
|
...
gi 1191882763 540 GKI 542
Cdd:cd12118 477 GKI 479
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
18-551 |
1.03e-30 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 126.03 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 18 GDKVAIIydspvtDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHslIFGGFA-- 95
Cdd:COG1021 39 PDRIAVV------DGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIP--VFALPAhr 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 96 SKELSSRIDHAKPKVVVTASFGiepgRKVEYMPILEEAMRIGQHkPDKVLIYNRPNmETVPLASGRDLDWDEEMAKAQSQ 175
Cdd:COG1021 111 RAEISHFAEQSEAVAYIIPDRH----RGFDYRALARELQAEVPS-LRHVLVVGDAG-EFTSLDALLAAPADLSEPRPDPD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 176 DcvpvlsehPLYILYTSGTTGLPKGVVRPTGGYAvmLNWTMSS-IYGLKPGEVWWAASDlgwvVGHSY--IC---YGPLI 249
Cdd:COG1021 185 D--------VAFFQLSGGTTGLPKLIPRTHDDYL--YSVRASAeICGLDADTVYLAALP----AAHNFplSSpgvLGVLY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 250 HGNTTVLyegkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQqdpgAALGKQYSLTRFKTLFVAGERCDVETLEwsk 329
Cdd:COG1021 251 AGGTVVL-----APDPSPDTAFPLIERERVTVTALVPPLALLWLD----AAERSRYDLSSLRVLQVGGAKLSPELAR--- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 330 kvfRV-PVLDHWWQ------------TETGSP--ITASCIGLGNSktpppgqagksvPGYNVMILDDNmqklkarclGNi 394
Cdd:COG1021 319 ---RVrPALGCTLQqvfgmaeglvnyTRLDDPeeVILTTQGRPIS------------PDDEVRIVDED---------GN- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 395 vvklPLPPGA-----------FSGLWK----NQEAFKHlyfekfPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRIS 459
Cdd:COG1021 374 ----PVPPGEvgelltrgpytIRGYYRapehNARAFTP------DGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIA 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 460 AGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDiNITegqvLEEIVQHVRQSiGpVAAFR---KAVFVQQLPK 536
Cdd:COG1021 444 AEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRGE-PLT----LAELRRFLRER-G-LAAFKlpdRLEFVDALPL 516
|
570
....*....|....*
gi 1191882763 537 TRSGKIPRAALSALV 551
Cdd:COG1021 517 TAVGKIDKKALRAAL 531
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
17-547 |
2.11e-30 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 126.35 E-value: 2.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 17 KGDKVAIIY------DSPVTdtkaTITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLI 90
Cdd:PLN03052 188 TDDSIAIIWrdegsdDLPVN----RMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSI 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 91 FGGFASKELSSRIDHAKPKVVVTASFGIEPGRKVE-YMPILEEAmrigqhKPDKVLIYNRPNMETVPLASGrDLDWDEEM 169
Cdd:PLN03052 264 ADSFAPSEIATRLKISKAKAIFTQDVIVRGGKSIPlYSRVVEAK------APKAIVLPADGKSVRVKLREG-DMSWDDFL 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 170 AKA----QSQDCVPVlsEHPL----YILYTSGTTGLPKGVvrPtggyavmlnWTMSSiyGLKPGEVWWAASD-------- 233
Cdd:PLN03052 337 ARAnglrRPDEYKAV--EQPVeaftNILFSSGTTGEPKAI--P---------WTQLT--PLRAAADAWAHLDirkgdivc 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 234 ----LGWVVGHsYICYGPLIHGNTTVLYEGKPVGTpdagAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALgkqySLTR 309
Cdd:PLN03052 402 wptnLGWMMGP-WLVYASLLNGATLALYNGSPLGR----GFAKFVQDAKVTMLGTVPSIVKTWKNTNCMAGL----DWSS 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 310 FKTLFVAGERCDVETLEW-SKKVFRVPVLDHWWQTETGSPItascigLGNSKTPPPGQAGKSVP--GYNVMILDDNMQKL 386
Cdd:PLN03052 473 IRCFGSTGEASSVDDYLWlMSRAGYKPIIEYCGGTELGGGF------VTGSLLQPQAFAAFSTPamGCKLFILDDSGNPY 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 387 --KARCLGNIVVkLPLPPGAFSGLWkNQEAFKhLYFEKFPGYYDTMDAGYMDE-----EGYVYVMSRVDDVINVAGHRIS 459
Cdd:PLN03052 547 pdDAPCTGELAL-FPLMFGASSTLL-NADHYK-VYFKGMPVFNGKILRRHGDIfertsGGYYRAHGRADDTMNLGGIKVS 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 460 AGAIEESL-LSHGTVADCAVVGKEDPLKGHVPLALCVLRKDIN--ITEGQVLEEIVQ-HVRQSIGPVAAFRKAVFVQQLP 535
Cdd:PLN03052 624 SVEIERVCnAADESVLETAAIGVPPPGGGPEQLVIAAVLKDPPgsNPDLNELKKIFNsAIQKKLNPLFKVSAVVIVPSFP 703
|
570
....*....|..
gi 1191882763 536 KTRSGKIPRAAL 547
Cdd:PLN03052 704 RTASNKVMRRVL 715
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
29-547 |
2.30e-30 |
|
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: 123.96 E-value: 2.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 29 VTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAihslifggfaskelssridhakp 108
Cdd:cd17643 6 VVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGG----------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 109 kvvvtASFGIEPGRKVEYMP-ILEEAmrigqhkpDKVLIYNRPnmetvplasgrdldwdeemakaqsqdcvpvlsEHPLY 187
Cdd:cd17643 63 -----AYVPIDPAYPVERIAfILADS--------GPSLLLTDP--------------------------------DDLAY 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 188 ILYTSGTTGLPKGVVRPTGGyAVMLNWTMSSIYGLKPGEVWWAAsdlgwvvgHSYI-------CYGPLIHGNTTVLYEGK 260
Cdd:cd17643 98 VIYTSGSTGRPKGVVVSHAN-VLALFAATQRWFGFNEDDVWTLF--------HSYAfdfsvweIWGALLHGGRLVVVPYE 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 261 PVGTPDagAYFRVLAEHGVAALFTAPTAIRAIRQ---QDPGAALGKQYsltrfktLFVAGERCDVETLE-WSKKVF--RV 334
Cdd:cd17643 169 VARSPE--DFARLLRDEGVTVLNQTPSAFYQLVEaadRDGRDPLALRY-------VIFGGEALEAAMLRpWAGRFGldRP 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 335 PVLDHWWQTETG-----SPITASCIGLGNSKTpppgqAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGLW 409
Cdd:cd17643 240 QLVNMYGITETTvhvtfRPLDAADLPAAAASP-----IGRPLPGLRVYVLDADGR--------------PVPPGVVGELY 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 410 ----------KNQEAfkhLYFEKF-------PG--YYDTMD-AGYMDEEGYVYvMSRVDDVINVAGHRISAGAIEESLLS 469
Cdd:cd17643 301 vsgagvargyLGRPE---LTAERFvanpfggPGsrMYRTGDlARRLPDGELEY-LGRADEQVKIRGFRIELGEIEAALAT 376
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 470 HGTVADCAVVGKEDPLKGHVpLALCVLRKDiniTEGQVLEEIVQHVRQSIgPvAAFRKAVFVQ--QLPKTRSGKIPRAAL 547
Cdd:cd17643 377 HPSVRDAAVIVREDEPGDTR-LVAYVVADD---GAAADIAELRALLKELL-P-DYMVPARYVPldALPLTVNGKLDRAAL 450
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
190-550 |
5.33e-30 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 121.05 E-value: 5.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 190 YTSGTTGLPKgVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLgWVVGHSYICYGPLIHGNTTVLYEGkPVGTPDAGA 269
Cdd:cd05944 9 HTGGTTGTPK-LAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPL-FHVNGSVVTLLTPLASGAHVVLAG-PAGYRNPGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 270 Y---FRVLAEHGVAALFTAPTAIRAIRQQDPGAALGkqySLtrfKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQTEtg 346
Cdd:cd05944 86 FdnfWKLVERYRITSLSTVPTVYAALLQVPVNADIS---SL---RFAMSGAAPLPVELRARFEDATGLPVVEGYGLTE-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 347 spitASCiglGNSKTPP-----PGQAGKSVPGYNVMIL-DDNMQKLKARC----LGNIVVKlplPPGAFsGLWKNQEAFK 416
Cdd:cd05944 158 ----ATC---LVAVNPPdgpkrPGSVGLRLPYARVRIKvLDGVGRLLRDCapdeVGEICVA---GPGVF-GGYLYTEGNK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 417 HLYFEkfPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVL 496
Cdd:cd05944 227 NAFVA--DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQL 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1191882763 497 RKDINITEgqvlEEIVQHVRQSIGPVAAFRKAVFV-QQLPKTRSGKIPRAALSAL 550
Cdd:cd05944 305 KPGAVVEE----EELLAWARDHVPERAAVPKHIEVlEELPVTAVGKVFKPALRAD 355
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
19-553 |
1.14e-29 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 123.59 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIIYDspvtdtKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPqAMYTM-LACARIGAIHSLIFGGFASK 97
Cdd:PLN03102 29 NRTSIIYG------KTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTP-AMYEMhFAVPMAGAVLNPINTRLDAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 98 ELSSRIDHAKPKVVVTASfgiepgrkvEYMPILEEAMRI---GQHKPD-KVLIYNRPNMETVPlaSGRDLDWDEEMAKAQ 173
Cdd:PLN03102 102 SIAAILRHAKPKILFVDR---------SFEPLAREVLHLlssEDSNLNlPVIFIHEIDFPKRP--SSEELDYECLIQRGE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 174 -----SQDCVPVLSEH-PLYILYTSGTTGLPKGVV-RPTGGY----AVMLNWTMssiyGLKPGEVWWAA--SDLGWVvgh 240
Cdd:PLN03102 171 ptpslVARMFRIQDEHdPISLNYTSGTTADPKGVViSHRGAYlstlSAIIGWEM----GTCPVYLWTLPmfHCNGWT--- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 241 syICYGPLIHGNTTVLYegKPVGTPDAgayFRVLAEHGVAALFTAPTAIRAIRQQD-------------------PGAAL 301
Cdd:PLN03102 244 --FTWGTAARGGTSVCM--RHVTAPEI---YKNIEMHNVTHMCCVPTVFNILLKGNsldlsprsgpvhvltggspPPAAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 302 GKQYSLTRFKTLFVAGER---CDVETLEWSKKVFRVPvlDHWwQTETGSPITASCIGLG-----NSKTPppgqagKSVPg 373
Cdd:PLN03102 317 VKKVQRLGFQVMHAYGLTeatGPVLFCEWQDEWNRLP--ENQ-QMELKARQGVSILGLAdvdvkNKETQ------ESVP- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 374 ynvmilddnmqkLKARCLGNIVVKlplPPGAFSGLWKN----QEAFKHlyfekfpGYYDTMDAGYMDEEGYVYVMSRVDD 449
Cdd:PLN03102 387 ------------RDGKTMGEIVIK---GSSIMKGYLKNpkatSEAFKH-------GWLNTGDVGVIHPDGHVEIKDRSKD 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 450 VINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEGQVLE------EIVQHVRQSIGPVA 523
Cdd:PLN03102 445 IIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKlvtrerDLIEYCRENLPHFM 524
|
570 580 590
....*....|....*....|....*....|
gi 1191882763 524 AFRKAVFVQQLPKTRSGKIPRAALSALVNG 553
Cdd:PLN03102 525 CPRKVVFLQELPKNGNGKILKPKLRDIAKG 554
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
18-480 |
1.17e-29 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 123.67 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 18 GDKVAIIYdsPVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 97
Cdd:COG1022 25 PDRVALRE--KEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 98 ELSSRIDHAKPKVVVtasfgiepgrkVEYMPILEEAMRIGQHKPD--KVLIYNRPNMETVP--------LASGRDLDWDE 167
Cdd:COG1022 103 EVAYILNDSGAKVLF-----------VEDQEQLDKLLEVRDELPSlrHIVVLDPRGLRDDPrllsldelLALGREVADPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 168 EMAKAQSQdcvpVLSEHPLYILYTSGTTGLPKGVvrptggyavML---NWT-----MSSIYGLKPGEVW-----WAasdl 234
Cdd:COG1022 172 ELEARRAA----VKPDDLATIIYTSGTTGRPKGV---------MLthrNLLsnaraLLERLPLGPGDRTlsflpLA---- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 235 gWVVGHSyICYGPLIHGNTTVLYEG-----------KP---VGTPD------AGAYFRVLAEHGVA-ALFTA--PTAIRA 291
Cdd:COG1022 235 -HVFERT-VSYYALAAGATVAFAESpdtlaedlrevKPtfmLAVPRvwekvyAGIQAKAEEAGGLKrKLFRWalAVGRRY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 292 IRQQD----PGAALGKQYSL--------------TRFKTLFVAGERCDVETLEWskkvFR---VPVLDHWWQTETGSPIT 350
Cdd:COG1022 313 ARARLagksPSLLLRLKHALadklvfsklrealgGRLRFAVSGGAALGPELARF----FRalgIPVLEGYGLTETSPVIT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 351 ASCigLGNSKtppPGQAGKSVPGYNVMILDDnmqklkarclGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTM 430
Cdd:COG1022 389 VNR--PGDNR---IGTVGPPLPGVEVKIAED----------GEILVR---GPNVMKGYYKNPEATAEAFDAD--GWLHTG 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1191882763 431 DAGYMDEEGYVYVMSRVDDVINVA-GHRISAGAIEESLLSHGTVADCAVVG 480
Cdd:COG1022 449 DIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
38-542 |
2.56e-29 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 121.73 E-value: 2.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 38 YKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTASFG 117
Cdd:PRK12406 14 FDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 118 IEPGRKV--EYMPILEEAmrigqhKPDKVLIYNRPNMETVPLASGrDLDWDEEMAKAQSQDCVPVlsEHPLYILYTSGTT 195
Cdd:PRK12406 94 LHGLASAlpAGVTVLSVP------TPPEIAAAYRISPALLTPPAG-AIDWEGWLAQQEPYDGPPV--PQPQSMIYTSGTT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 196 GLPKGVVR--PTGGYAVMLNWTMSSIYGLKPGEVwwaasdlgwvvghsYICYGPLIHG--NTTVLYEGKPVGT----P-- 265
Cdd:PRK12406 165 GHPKGVRRaaPTPEQAAAAEQMRALIYGLKPGIR--------------ALLTGPLYHSapNAYGLRAGRLGGVlvlqPrf 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 266 DAGAYFRVLAEHGVAALFTAPTAIraIRQQDPGAALGKQYSLTRFKTLFVAGERCDVET----LEWSKKVfrvpVLDHWW 341
Cdd:PRK12406 231 DPEELLQLIERHRITHMHMVPTMF--IRLLKLPEEVRAKYDVSSLRHVIHAAAPCPADVkramIEWWGPV----IYEYYG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 342 QTETGSPITASciglGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGaFSglWKNQEAfKHLYFE 421
Cdd:PRK12406 305 STESGAVTFAT----SEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPD-FT--YHNKPE-KRAEID 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 422 KfPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHvplALCVLrkdIN 501
Cdd:PRK12406 377 R-GGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGE---ALMAV---VE 449
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1191882763 502 ITEGQVLEE--IVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKI 542
Cdd:PRK12406 450 PQPGATLDEadIRAQLKARLAGYKVPKHIEIMAELPREDSGKI 492
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
19-553 |
4.16e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 120.76 E-value: 4.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIIYDSpvtdtkATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 98
Cdd:PRK06145 17 DRAALVYRD------QEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 99 LSSRIDHAKPKVV-VTASFGIEPGrkveympILEEAMRIGQHKPDKVLIYNRPNMETVPLASGRDLDwdeemakaqsqdc 177
Cdd:PRK06145 91 VAYILGDAGAKLLlVDEEFDAIVA-------LETPKIVIDAAAQADSRRLAQGGLEIPPQAAVAPTD------------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 178 vpvlsehpLY-ILYTSGTTGLPKGVvrptggyavMLNWtmssiyglkpGEVWWAASD----LGWVVGHSYICYGPLIH-- 250
Cdd:PRK06145 151 --------LVrLMYTSGTTDRPKGV---------MHSY----------GNLHWKSIDhviaLGLTASERLLVVGPLYHvg 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 251 ----GNTTVLYEGKPVGTP---DAGAYFRVLAEHGVAALFTAP---TAIRAIRQQDpgaalgkQYSLTRFKTLFVAGERC 320
Cdd:PRK06145 204 afdlPGIAVLWVGGTLRIHrefDPEAVLAAIERHRLTCAWMAPvmlSRVLTVPDRD-------RFDLDSLAWCIGGGEKT 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 321 DVETLEWSKKVF-RVPVLDHWWQTETGSPITASCIGLGNSKTpppGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlp 399
Cdd:PRK06145 277 PESRIRDFTRVFtRARYIDAYGLTETCSGDTLMEAGREIEKI---GSTGRALAHVEIRIADGAGRWLPPNMKGEICMR-- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 400 lPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVV 479
Cdd:PRK06145 352 -GPKVTKGYWKDPEKTAEAFYG---DWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVI 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1191882763 480 GKEDPLKGHVPLALCVLRKDINITegqvLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAALSALVNG 553
Cdd:PRK06145 428 GVHDDRWGERITAVVVLNPGATLT----LEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDELNG 497
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
18-547 |
6.96e-29 |
|
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: 120.00 E-value: 6.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 18 GDKVAIIYDspvtdtKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAihslifggfask 97
Cdd:cd12117 11 PDAVAVVYG------DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGA------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 98 elssridhakpkvvvtASFGIEPGRKVEYMP-ILEEAmrigqhkPDKVLIYNRPNMETVPLASGRDLDWDEEMAKAQSQD 176
Cdd:cd12117 73 ----------------AYVPLDPELPAERLAfMLADA-------GAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 177 CVPVLSEHPLYILYTSGTTGLPKGV----------VRPTggyavmlNWTmssiyGLKPGEVWWAASDLGWVVGhSYICYG 246
Cdd:cd12117 130 AVPVSPDDLAYVMYTSGSTGRPKGVavthrgvvrlVKNT-------NYV-----TLGPDDRVLQTSPLAFDAS-TFEIWG 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 247 PLIHGNTTVLYEGKPVGTPDAGAyfRVLAEHGVAALFTAPTAIRAIRQQDPGAalgkqysLTRFKTLFVAGERCDVetlE 326
Cdd:cd12117 197 ALLNGARLVLAPKGTLLDPDALG--ALIAEEGVTVLWLTAALFNQLADEDPEC-------FAGLRELLTGGEVVSP---P 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 327 WSKKVFR----VPVLDHWWQTETGSPITASCIglgnskTPPPGQA-----GKSVPGYNVMILDDNMQklkarclgnivvk 397
Cdd:cd12117 265 HVRRVLAacpgLRLVNGYGPTENTTFTTSHVV------TELDEVAgsipiGRPIANTRVYVLDEDGR------------- 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 398 lPLPPGAF-------SGLWK---NQEAfkhLYFEKF------PG--YYDTMD-AGYMDEEGYVYVmSRVDDVINVAGHRI 458
Cdd:cd12117 326 -PVPPGVPgelyvggDGLALgylNRPA---LTAERFvadpfgPGerLYRTGDlARWLPDGRLEFL-GRIDDQVKIRGFRI 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 459 SAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINitegqvLEEIVQHVRQSIgPvAAFRKAVFVQ--QLPK 536
Cdd:cd12117 401 ELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALD------AAELRAFLRERL-P-AYMVPAAFVVldELPL 472
|
570
....*....|.
gi 1191882763 537 TRSGKIPRAAL 547
Cdd:cd12117 473 TANGKVDRRAL 483
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
35-500 |
7.21e-29 |
|
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: 119.62 E-value: 7.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 35 TITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTa 114
Cdd:cd05907 5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 115 sfgiepgrkveympileeamrigqhkpdkvliynrpnmetvplasgrdlDWDEEMAKaqsqdcvpvlsehplyILYTSGT 194
Cdd:cd05907 84 -------------------------------------------------EDPDDLAT----------------IIYTSGT 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 195 TGLPKGVVRPTGGYAvmlnWTMSSIY---GLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLYEGKPVGTPDagayf 271
Cdd:cd05907 99 TGRPKGVMLSHRNIL----SNALALAerlPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLLDD----- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 272 rvLAEHGVAALFTAPTAIR----AIRQQDPGAALGKQY---SLTRFKTLFVAGERCDVETLEWSKKvFRVPVLDHWWQTE 344
Cdd:cd05907 170 --LSEVRPTVFLAVPRVWEkvyaAIKVKAVPGLKRKLFdlaVGGRLRFAASGGAPLPAELLHFFRA-LGIPVYEGYGLTE 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 345 TGSPITASCIGlgnskTPPPGQAGKSVPGYNVMILDDnmqklkarclGNIVVKlplPPGAFSGLWKNQEAFKHLYFEkfP 424
Cdd:cd05907 247 TSAVVTLNPPG-----DNRIGTVGKPLPGVEVRIADD----------GEILVR---GPNVMLGYYKNPEATAEALDA--D 306
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191882763 425 GYYDTMDAGYMDEEGYVYVMSRVDDVI-NVAGHRISAGAIEESLLSHGTVADCAVVGKEDPlkghVPLALCVLRKDI 500
Cdd:cd05907 307 GWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIGDGRP----FLVALIVPDPEA 379
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
67-547 |
1.09e-28 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 119.54 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 67 MPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTASFGIEPGRKveyMPILEEAMRIGQHKPDKVLI 146
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRA---LPLYSKVVEAAPAKAIVLPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 147 YNRPNmeTVPLASGrDLDWDEEMAKAQSQDCV------PVL--SEHPLYILYTSGTTGLPKGVvrptggyavmlNWTMSS 218
Cdd:PLN03051 78 AGEPV--AVPLREQ-DLSWCDFLGVAAAQGSVggneysPVYapVESVTNILFSSGTTGEPKAI-----------PWTHLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 219 -IYG---------LKPGEVWWAASDLGWVVGhSYICYGPLIHGNTTVLYEGKPVGtpdaGAYFRVLAEHGVAALFTAPTA 288
Cdd:PLN03051 144 pLRCasdgwahmdIQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGAPLG----RGFGKFVQDAGVTVLGLVPSI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 289 IRAIRQQdpGAALGKQYSLTRFKTLFVAGERCDVETLEW--SKKVFRVPVLDHWWQTETGSPITASCIGLGNSktppPGQ 366
Cdd:PLN03051 219 VKAWRHT--GAFAMEGLDWSKLRVFASTGEASAVDDVLWlsSVRGYYKPVIEYCGGTELASGYISSTLLQPQA----PGA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 367 AGKSVPGYNVMILDDNMQKL--KARCLGNIVVKLPLPPGAFSGLWKNQEAfkhLYFEKFPGYY----------DTMDAgy 434
Cdd:PLN03051 293 FSTASLGTRFVLLNDNGVPYpdDQPCVGEVALAPPMLGASDRLLNADHDK---VYYKGMPMYGskgmplrrhgDIMKR-- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 435 mDEEGYVYVMSRVDDVINVAGHRISAGAIEESLL-SHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEGQVLEEIVQ 513
Cdd:PLN03051 368 -TPGGYFCVQGRADDTMNLGGIKTSSVEIERACDrAVAGIAETAAVGVAPPDGGPELLVIFLVLGEEKKGFDQARPEALQ 446
|
490 500 510
....*....|....*....|....*....|....*....
gi 1191882763 514 H-----VRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:PLN03051 447 KkfqeaIQTNLNPLFKVSRVKIVPELPRNASNKLLRRVL 485
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
45-547 |
1.64e-28 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 118.70 E-value: 1.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 45 VSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIF----GGFASKELSSRIDHAKPKVVvtasfgiep 120
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFvplnPTLKESVLRYLVADAGGRIV--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 121 grkveympILEEAMRigqHKPDKVLIYNrPNMETVplasgrdLDWDEEMAKAQSQDCVPVLSEHPLYILYTSGTTGLPKG 200
Cdd:cd05922 74 --------LADAGAA---DRLRDALPAS-PDPGTV-------LDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 201 VVRPTggYAVMLNW-TMSSIYGLKPGEVWWAASDLGWvvghsyiCYG------PLIHGNTTVLYEGkpvGTPDAGaYFRV 273
Cdd:cd05922 135 VRLSH--QNLLANArSIAEYLGITADDRALTVLPLSY-------DYGlsvlntHLLRGATLVLTND---GVLDDA-FWED 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 274 LAEHGVAALFTAPT--AI--RAIRQQDPGAAL-------GK--QYSLTRFKTLFVAGercdvetlewskkvfRVPVLdhW 340
Cdd:cd05922 202 LREHGATGLAGVPStyAMltRLGFDPAKLPSLryltqagGRlpQETIARLRELLPGA---------------QVYVM--Y 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 341 WQTETGSPITAsciglgnskTPP------PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLppgAFSGLWkNQEA 414
Cdd:cd05922 265 GQTEATRRMTY---------LPPerilekPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPN---VMKGYW-NDPP 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 415 FKhLYFEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVplALC 494
Cdd:cd05922 332 YR-RKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKL--ALF 408
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1191882763 495 VLRKDiniteGQVLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:cd05922 409 VTAPD-----KIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
188-547 |
2.02e-28 |
|
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: 118.16 E-value: 2.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 188 ILYTSGTTGLPKGVVRPTGGYAVMLNwTMSsiyglkpgEVW-WAASDlgwVVGHSYicygPLIHGNTTV------LYEGK 260
Cdd:cd05941 94 ILYTSGTTGRPKGVVLTHANLAANVR-ALV--------DAWrWTEDD---VLLHVL----PLHHVHGLVnallcpLFAGA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 261 PV---GTPDAGAYFRVLAEHGVAALFTAPTA----IRAIRQQDPGAALGKQYSLTRFKtLFVAGERC-DVETLEWSKKVF 332
Cdd:cd05941 158 SVeflPKFDPKEVAISRLMPSITVFMGVPTIytrlLQYYEAHFTDPQFARAAAAERLR-LMVSGSAAlPVPTLEEWEAIT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 333 RVPVLDHWWQTETGspITASCiGLGNSKTppPGQAGKSVPGYNVMILDDNMQK-LKARCLGNIVVKlplPPGAFSGLWKN 411
Cdd:cd05941 237 GHTLLERYGMTEIG--MALSN-PLDGERR--PGTVGMPLPGVQARIVDEETGEpLPRGEVGEIQVR---GPSVFKEYWNK 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 412 QEAFKhlyfEKFP--GYYDTMDAGYMDEEGYVYVMSRV-DDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGH 488
Cdd:cd05941 309 PEATK----EEFTddGWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGE 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1191882763 489 VPLALCVLRKDiniTEGQVLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:cd05941 385 RVVAVVVLRAG---AAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
184-544 |
3.29e-28 |
|
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: 115.20 E-value: 3.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 184 HPLYILYTSGTTGLPKGVVRptggyavmlnwtmssiyglkpGEVWWAAS-----DLGWVVGHSYICY-GPLIH-----GN 252
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYR---------------------SERSWIESfvcneDLFNISGEDAILApGPLSHslflyGA 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 253 TTVLYEGKPV---GTPDAGAYFRVLAEHGVAALFTAPTAIRA-IRQQDPgaalgkqysLTRFKTLFVAGERCDVETLEWS 328
Cdd:cd17633 60 ISALYLGGTFigqRKFNPKSWIRKINQYNATVIYLVPTMLQAlARTLEP---------ESKIKSIFSSGQKLFESTKKKL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 329 KKVFRVPVLDHWWQTETGSPITASCiglgNSKTPPPGQAGKSVPGYNVMILDDNmqklkARCLGNIVVKLPLppgAFSGL 408
Cdd:cd17633 131 KNIFPKANLIEFYGTSELSFITYNF----NQESRPPNSVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEM---VFSGY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 409 WKNQEAFKHlyfekfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGH 488
Cdd:cd17633 199 VRGGFSNPD-------GWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGE 271
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1191882763 489 VPLALCVLRKdinITEGQVLEEIVQHV-RQSIgPvaafRKAVFVQQLPKTRSGKIPR 544
Cdd:cd17633 272 IAVALYSGDK---LTYKQLKRFLKQKLsRYEI-P----KKIIFVDSLPYTSSGKIAR 320
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
188-551 |
5.61e-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: 114.74 E-value: 5.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 188 ILYTSGTTGLPKgvvrptggyAVMLNW---TMS-----SIYGLKPGEVWWAASDLGWVVGhsyicYGPLIHGnttvLYEG 259
Cdd:cd17630 5 VILTSGSTGTPK---------AVVHTAanlLASaaglhSRLGFGGGDSWLLSLPLYHVGG-----LAILVRS----LLAG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 260 KP--VGTPDAGAYFRvLAEHGVAALFTAPTAIRAIRQQDPGAAlgkqySLTRFKTLFVAGERCDVETLEWSKKVfRVPVL 337
Cdd:cd17630 67 AElvLLERNQALAED-LAPPGVTHVSLVPTQLQRLLDSGQGPA-----ALKSLRAVLLGGAPIPPELLERAADR-GIPLY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 338 DHWWQTETGSPITASCIGLgnsktPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWknqeafkh 417
Cdd:cd17630 140 TTYGMTETASQVATKRPDG-----FGRGGVGVLLPGRELRIVEDGEIWVGGASLAMGYLRGQLVPEFNEDGW-------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 418 lyfekfpgyYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLR 497
Cdd:cd17630 207 ---------FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGR 277
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1191882763 498 kdinitEGQVLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAALSALV 551
Cdd:cd17630 278 ------GPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
18-548 |
5.84e-28 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 117.86 E-value: 5.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 18 GDKVAIIYDSPVTDTKaTITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 97
Cdd:PRK08008 21 GHKTALIFESSGGVVR-RYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 98 ELSSRIDHAKPKVVVTASfgiepgrkvEYMPILEEAMRIGQHKPDKVLIyNRPNMETVPLASgrdlDWDEEMAKAQSQDC 177
Cdd:PRK08008 100 ESAWILQNSQASLLVTSA---------QFYPMYRQIQQEDATPLRHICL-TRVALPADDGVS----SFTQLKAQQPATLC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 178 --VPVLSEHPLYILYTSGTTGLPKGVVrptggyAVMLNWTMSSIYGlkpgeVWWAA---SDLgwvvghsYICYGPLIH-- 250
Cdd:PRK08008 166 yaPPLSTDDTAEILFTSGTTSRPKGVV------ITHYNLRFAGYYS-----AWQCAlrdDDV-------YLTVMPAFHid 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 251 ------------GNTTVLYEGKpvgtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdPGAALGKQYSLTRFktLFVAG- 317
Cdd:PRK08008 228 cqctaamaafsaGATFVLLEKY-----SARAFWGQVCKYRATITECIPMMIRTLMVQ-PPSANDRQHCLREV--MFYLNl 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 318 ---ERCDVETLewskkvFRVPVLDHWWQTETgspitascigLGNSKTPPPGQA------GKSVPGYNVMILDDNMQKLKA 388
Cdd:PRK08008 300 sdqEKDAFEER------FGVRLLTSYGMTET----------IVGIIGDRPGDKrrwpsiGRPGFCYEAEIRDDHNRPLPA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 389 RCLGNIVVKlpLPPGA--FSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEES 466
Cdd:PRK08008 364 GEIGEICIK--GVPGKtiFKEYYLDPKATAKVLEAD--GWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENI 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 467 LLSHGTVADCAVVGKEDPLKGHVPLALCVLrkdiniTEGQVL--EEIVQHVRQSIgpvAAFRKAVFV---QQLPKTRSGK 541
Cdd:PRK08008 440 IATHPKIQDIVVVGIKDSIRDEAIKAFVVL------NEGETLseEEFFAFCEQNM---AKFKVPSYLeirKDLPRNCSGK 510
|
....*..
gi 1191882763 542 IPRAALS 548
Cdd:PRK08008 511 IIKKNLK 517
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
18-547 |
7.02e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 117.74 E-value: 7.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 18 GDKVAIIYDspvtdtKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPqAMYTM-LACARIGAIHSLIFGGFAS 96
Cdd:PRK08162 32 PDRPAVIHG------DRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIP-AMVEAhFGVPMAGAVLNTLNTRLDA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 97 KELSSRIDHAKPKVVVTASfgiepgrkvEYMPILEEAMRIGQHKPDKVLIYNRPNMETVPLASGRDLD-----WDEEMAK 171
Cdd:PRK08162 105 ASIAFMLRHGEAKVLIVDT---------EFAEVAREALALLPGPKPLVIDVDDPEYPGGRFIGALDYEaflasGDPDFAW 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 172 AQSQDCVPVLSehplyILYTSGTTGLPKGVV---RptGGYavmLNwTMSSI--YGLKPGEVWWaasdlgWVVghsyicyg 246
Cdd:PRK08162 176 TLPADEWDAIA-----LNYTSGTTGNPKGVVyhhR--GAY---LN-ALSNIlaWGMPKHPVYL------WTL-------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 247 PLIHGN------TTVLYEGKPVGTP--DAGAYFRVLAEHGVAALFTAPTAIRAIRQqdpgAALGKQYSLTRFKTLFVAGE 318
Cdd:PRK08162 231 PMFHCNgwcfpwTVAARAGTNVCLRkvDPKLIFDLIREHGVTHYCGAPIVLSALIN----APAEWRAGIDHPVHAMVAGA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 319 RCDVETLEWSKKV-FRVpvlDHWWQ-TETGSPITASCIGLGNSKTPPPGQAG-KSVPGYN------VMILD-DNMQKLKA 388
Cdd:PRK08162 307 APPAAVIAKMEEIgFDL---THVYGlTETYGPATVCAWQPEWDALPLDERAQlKARQGVRyplqegVTVLDpDTMQPVPA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 389 ----------RclGNIVVKlplppgafsGLWKNQEAFKhlyfEKFP-GYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHR 457
Cdd:PRK08162 384 dgetigeimfR--GNIVMK---------GYLKNPKATE----EAFAgGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGEN 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 458 ISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEgqvlEEIVQHVRQSIgpvAAFR--KAVFVQQLP 535
Cdd:PRK08162 449 ISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATE----EEIIAHCREHL---AGFKvpKAVVFGELP 521
|
570
....*....|..
gi 1191882763 536 KTRSGKIPRAAL 547
Cdd:PRK08162 522 KTSTGKIQKFVL 533
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
182-547 |
1.03e-27 |
|
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: 116.26 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 182 SEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSiyglkpgevwWAASDLGWVVGHSYICY--------GPLIHGNT 253
Cdd:cd12115 104 PDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAA----------FSAEELAGVLASTSICFdlsvfelfGPLATGGK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 254 TVLYEgkpvgtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQD--PGAAlgkqysltrfKTLFVAGE---RCDVETLEWS 328
Cdd:cd12115 174 VVLAD-------NVLALPDLPAAAEVTLINTVPSAAAELLRHDalPASV----------RVVNLAGEplpRDLVQRLYAR 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 329 KKVFRVPVLdhWWQTETGSPITASCIGLGNSKTPPpgqAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGL 408
Cdd:cd12115 237 LQVERVVNL--YGPSEDTTYSTVAPVPPGASGEVS---IGRPLANTQAYVLDRALQ--------------PVPLGVPGEL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 409 WKNQEAFKHLYF-------EKF------PG--YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTV 473
Cdd:cd12115 298 YIGGAGVARGYLgrpgltaERFlpdpfgPGarLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGV 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1191882763 474 ADCAVVGKEDPLKGHVPLALCVLRKDINITegqvLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:cd12115 378 REAVVVAIGDAAGERRLVAYIVAEPGAAGL----VEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
18-547 |
1.42e-27 |
|
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: 116.27 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 18 GDKVAIIydspvtDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 97
Cdd:cd05920 29 PDRIAVV------DGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 98 ELSSRIDHAKPKVVVTAsfgiepgrkveympileeamriGQHKPDkvliynrpnmETVPLAsgrdldwdEEMAKAQSQdc 177
Cdd:cd05920 103 ELSAFCAHAEAVAYIVP----------------------DRHAGF----------DHRALA--------RELAESIPE-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 178 vpvlsehPLYILYTSGTTGLPKGVVRPTGGYAVMLNwTMSSIYGLKPGEVWWAASDlgwvVGHSYICYGPLIHGntTVLY 257
Cdd:cd05920 141 -------VALFLLSGGTTGTPKLIPRTHNDYAYNVR-ASAEVCGLDQDTVYLAVLP----AAHNFPLACPGVLG--TLLA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 258 EGKPV--GTPDAGAYFRVLAEHGVaalfTAPTAIRAIRQQDPGAALGKQYSLTRFKTLFVAGERCDVETLEWSKKVFRVP 335
Cdd:cd05920 207 GGRVVlaPDPSPDAAFPLIEREGV----TVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 336 VLDHWWQTEtgspitasciGLGNSKTP--PP----GQAGKSV-PGYNVMILDDNmqklkarclGNivvklPLPPGA---- 404
Cdd:cd05920 283 LQQVFGMAE----------GLLNYTRLddPDeviiHTQGRPMsPDDEIRVVDEE---------GN-----PVPPGEegel 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 405 -------FSGLWK----NQEAFKHlyfekfPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTV 473
Cdd:cd05920 339 ltrgpytIRGYYRapehNARAFTP------DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAV 412
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191882763 474 ADCAVVGKEDPLKGHVPLALCVLRkdinitEGQV-LEEIVQHVRQSigPVAAFR---KAVFVQQLPKTRSGKIPRAAL 547
Cdd:cd05920 413 HDAAVVAMPDELLGERSCAFVVLR------DPPPsAAQLRRFLRER--GLAAYKlpdRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
19-550 |
1.88e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 116.11 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIIydspvtDTKATITYKEVLEQVSRLAGVLVKH-GVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 97
Cdd:PRK06839 17 DRIAII------TEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 98 ELSSRI-DHAKPKVVVTASFG-----IEPGRKVEYMPILEEAMRIGQHKPDkvliynrpnmetvplasgrdldwdeemak 171
Cdd:PRK06839 91 ELIFQLkDSGTTVLFVEKTFQnmalsMQKVSYVQRVISITSLKEIEDRKID----------------------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 172 aqsqDCVPVLSEHPLYILYTSGTTGLPKGVVrptggyAVMLNWTMSSIYGLkpgevwwAASDLgwVVGHSYICYGPLIH- 250
Cdd:PRK06839 142 ----NFVEKNESASFIICYTSGTTGKPKGAV------LTQENMFWNALNNT-------FAIDL--TMHDRSIVLLPLFHi 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 251 GNTTV-----LYEGKPVGTP---DAGAYFRVLAEHGVAALFTAPTAIRAIRQqdpgAALGKQYSLTRFKTLFVAGERCDV 322
Cdd:PRK06839 203 GGIGLfafptLFAGGVIIVPrkfEPTKALSMIEKHKVTVVMGVPTIHQALIN----CSKFETTNLQSVRWFYNGGAPCPE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 323 ETLewskKVFRvpvldhwwqtETGSPITAsciGLGNSKTPP-------------PGQAGKSVPGYNVMILDDNMQKLKAR 389
Cdd:PRK06839 279 ELM----REFI----------DRGFLFGQ---GFGMTETSPtvfmlseedarrkVGSIGKPVLFCDYELIDENKNKVEVG 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 390 CLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLS 469
Cdd:PRK06839 342 EVGELLIR---GPNVMKEYWNRPDATEETIQD---GWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINK 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 470 HGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEgqvlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAALSA 549
Cdd:PRK06839 416 LSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIE----KDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVN 491
|
.
gi 1191882763 550 L 550
Cdd:PRK06839 492 Q 492
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
37-542 |
3.05e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 116.03 E-value: 3.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 37 TYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTA-S 115
Cdd:PRK12583 47 TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICAdA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 116 FgiepgRKVEYMPILEEAMRIGQHKPDKVLIYNR-PNMETVPLASGRD----LDWDEEMAKAQS---QDCVPV---LSEH 184
Cdd:PRK12583 127 F-----KTSDYHAMLQELLPGLAEGQPGALACERlPELRGVVSLAPAPppgfLAWHELQARGETvsrEALAERqasLDRD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 185 -PLYILYTSGTTGLPKGVVrpTGGYAVMLNWTMSSI-YGLKPGEVWWAASDLgwvvghsYICYGPLI-------HGNTTV 255
Cdd:PRK12583 202 dPINIQYTSGTTGFPKGAT--LSHHNILNNGYFVAEsLGLTEHDRLCVPVPL-------YHCFGMVLanlgcmtVGACLV 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 256 LyegkPVGTPDAGAYFRVLAEHGVAALFTAPTA-IRAIRQQDPGAalgkqYSLTRFKTLFVAGERCDVETLEWSKKVFRV 334
Cdd:PRK12583 273 Y----PNEAFDPLATLQAVEEERCTALYGVPTMfIAELDHPQRGN-----FDLSSLRTGIMAGAPCPIEVMRRVMDEMHM 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 335 P-VLDHWWQTETgSPITASCiGLGNSKTPPPGQAGKSVPGYNVMILDDnmqklkarcLGNIVvklplPPGA--------- 404
Cdd:PRK12583 344 AeVQIAYGMTET-SPVSLQT-TAADDLERRVETVGRTQPHLEVKVVDP---------DGATV-----PRGEigelctrgy 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 405 --FSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKE 482
Cdd:PRK12583 408 svMKGYWNNPEATAESIDED--GWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVP 485
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 483 DPLKGHVPLALCVLRKDINITEgqvlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKI 542
Cdd:PRK12583 486 DEKYGEEIVAWVRLHPGHAASE----EELREFCKARIAHFKVPRYFRFVDEFPMTVTGKV 541
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
19-547 |
4.16e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 117.18 E-value: 4.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIIYDspvtdtKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAihslifggfASKE 98
Cdd:PRK12467 527 ERPALVFG------EQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGG---------AYVP 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 99 LSSRidhakpkvvvtasfgiEPGRKVEYMpILEEAMRIGQHKPDKVLIYNRP-NMETVPLASgrDLDWDEEMAKAQSQdc 177
Cdd:PRK12467 592 LDPE----------------YPQDRLAYM-LDDSGVRLLLTQSHLLAQLPVPaGLRSLCLDE--PADLLCGYSGHNPE-- 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 178 VPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVVGHSYIcYGPLIHGNTTVLY 257
Cdd:PRK12467 651 VALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCV-IAERLQLAADDSMLMVSTFAFDLGVTEL-FGALASGATLHLL 728
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 258 EgkPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIrQQDPGAALgkqysLTRFKTLFVAGERCDVETL-EWSKKVFRVPV 336
Cdd:PRK12467 729 P--PDCARDAEAFAALMADQGVTVLKIVPSHLQAL-LQASRVAL-----PRPQRALVCGGEALQVDLLaRVRALGPGARL 800
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 337 LDHWWQTETGSPITASCIGLGN--SKTPPPGQAgksVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGLWKNQEA 414
Cdd:PRK12467 801 INHYGPTETTVGVSTYELSDEErdFGNVPIGQP---LANLGLYILDHYLN--------------PVPVGVVGELYIGGAG 863
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 415 FKHLYF-------EKF-------PG--YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADcAV 478
Cdd:PRK12467 864 LARGYHrrpaltaERFvpdpfgaDGgrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVRE-AV 942
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 479 VGKEDPLKGHVPLALCVLRKDINITEGQVL-EEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:PRK12467 943 VLAQPGDAGLQLVAYLVPAAVADGAEHQATrDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
29-547 |
7.77e-27 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 113.91 E-value: 7.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 29 VTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKP 108
Cdd:cd17646 17 VVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 109 KVVVTASfgiepgrkveympilEEAMRIGQHKPDKVLIYNRPnmetvPLASGRDLDwdeemakaqsqdcVPVLSEHPLYI 188
Cdd:cd17646 97 AVVLTTA---------------DLAARLPAGGDVALLGDEAL-----AAPPATPPL-------------VPPRPDNLAYV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 189 LYTSGTTGLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVVGHSYIcYGPLIHGNTTVLYEgkPVGTPDAG 268
Cdd:cd17646 144 IYTSGSTGRPKGVMVTHAGIVNRLLW-MQDEYPLGPGDRVLQKTPLSFDVSVWEL-FWPLVAGARLVVAR--PGGHRDPA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 269 AYFRVLAEHGVAALFTAPTAIRA-IRQQDPGAALgkqySLTRfktLFVAGERCDVETLEWSKKVFRVPVLDHWWQTETGS 347
Cdd:cd17646 220 YLAALIREHGVTTCHFVPSMLRVfLAEPAAGSCA----SLRR---VFCSGEALPPELAARFLALPGAELHNLYGPTEAAI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 348 PITA-SCIGlgnSKTPPPGQAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGL----------WKNQEAfk 416
Cdd:cd17646 293 DVTHwPVRG---PAETPSVPIGRPVPNTRLYVLDDALR--------------PVPVGVPGELylggvqlargYLGRPA-- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 417 hLYFEKF------PG--YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGH 488
Cdd:cd17646 354 -LTAERFvpdpfgPGsrMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAA 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 489 VPLALCVLRKDiniTEGQVLEEIVQHVRQSIgPVAAFRKA-VFVQQLPKTRSGKIPRAAL 547
Cdd:cd17646 433 RLVGYVVPAAG---AAGPDTAALRAHLAERL-PEYMVPAAfVVLDALPLTANGKLDRAAL 488
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
19-547 |
1.73e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 113.18 E-value: 1.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIIydspVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 98
Cdd:PRK13390 12 DRPAVI----VAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 99 LSSRIDHAKPKVVVtASFGIEpgrkveympilEEAMRIGQHKPdkvliynrpnmetVPLASGRDLDW--DEEMAKAQSQd 176
Cdd:PRK13390 88 ADYIVGDSGARVLV-ASAALD-----------GLAAKVGADLP-------------LRLSFGGEIDGfgSFEAALAGAG- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 177 cvPVLSEHPL--YILYTSGTTGLPKGV--------VRPTGGYAVMLnwtMSSIYGLKPGEVWWA------ASDLGWvvgh 240
Cdd:PRK13390 142 --PRLTEQPCgaVMLYSSGTTGFPKGIqpdlpgrdVDAPGDPIVAI---ARAFYDISESDIYYSsapiyhAAPLRW---- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 241 syiCygPLIH--GNTTVLYEgkpvgTPDAGAYFRVLAEHGVAALFTAPTAIraIRQQDPGAALGKQYSLTRFKTLFVAGE 318
Cdd:PRK13390 213 ---C--SMVHalGGTVVLAK-----RFDAQATLGHVERYRITVTQMVPTMF--VRLLKLDADVRTRYDVSSLRAVIHAAA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 319 RCDVET----LEWSKKVfrvpVLDHWWQTET-GSPITASCIGLGNsktppPGQAGKSVPGyNVMILDDNMQKLKARCLGN 393
Cdd:PRK13390 281 PCPVDVkhamIDWLGPI----VYEYYSSTEAhGMTFIDSPDWLAH-----PGSVGRSVLG-DLHICDDDGNELPAGRIGT 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 394 IVVKLPLPPGAFSGLWKNQEAFKHlyfEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTV 473
Cdd:PRK13390 351 VYFERDRLPFRYLNDPEKTAAAQH---PAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAV 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1191882763 474 ADCAVVGKEDPLKGHVPLALCVLRKDINITEgQVLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:PRK13390 428 HDVAVIGVPDPEMGEQVKAVIQLVEGIRGSD-ELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
32-542 |
2.08e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 112.69 E-value: 2.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 32 TKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVV 111
Cdd:PRK08276 8 SGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 112 VT-ASFgiepgrkveympiLEEAMRIGQHKPDKVliynrPNMETVPLASGRDLDWDEEMAkAQSQDCVPVLSEHPLyILY 190
Cdd:PRK08276 88 IVsAAL-------------ADTAAELAAELPAGV-----PLLLVVAGPVPGFRSYEEALA-AQPDTPIADETAGAD-MLY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 191 TSGTTGLPKGVVRPTGGYAVMLNWTMSsiyglkpgeVWWAASDLGWVVGHSYICYGPLIH-------------GNTTVLY 257
Cdd:PRK08276 148 SSGTTGRPKGIKRPLPGLDPDEAPGMM---------LALLGFGMYGGPDSVYLSPAPLYHtaplrfgmsalalGGTVVVM 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 258 EG-KPVGTPDAGAYFRVLAEHGVAALFTA----PTAIRAirqqdpgaalgkQYSLTRFKTLFVAGERCDVET----LEWS 328
Cdd:PRK08276 219 EKfDAEEALALIERYRVTHSQLVPTMFVRmlklPEEVRA------------RYDVSSLRVAIHAAAPCPVEVkramIDWW 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 329 KkvfrvPVLDHWWQTETGSPITASciglgNSKT--PPPGQAGKSVPGyNVMILDDNMQKLKARCLGNIVVKLPLPPgaFS 406
Cdd:PRK08276 287 G-----PIIHEYYASSEGGGVTVI-----TSEDwlAHPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYP--FE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 407 GLwKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVInvaghrISAGA------IEESLLSHGTVADCAVVG 480
Cdd:PRK08276 354 YH-NDPEKTAAARNPH--GWVTVGDVGYLDEDGYLYLTDRKSDMI------ISGGVniypqeIENLLVTHPKVADVAVFG 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191882763 481 KEDP-----LKGHVPLALCVLRKDinitegQVLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKI 542
Cdd:PRK08276 425 VPDEemgerVKAVVQPADGADAGD------ALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
37-555 |
3.51e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 112.21 E-value: 3.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 37 TYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTasf 116
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLG--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 117 giepgrkveympileeamrigqhkpDKVLIYNRPNMEtvplasgrDLDWDEEMAKAQSQDCVPVL-SEHPLYILYTSGTT 195
Cdd:PRK09088 101 -------------------------DDAVAAGRTDVE--------DLAAFIASADALEPADTPSIpPERVSLILFTSGTS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 196 GLPKGV-VRPTGGYAVMLNWtmssiyglkpgevwwaaSDLGWVVGHS-YICYGPLIH--GNTT----VLYEGKPVGTPD- 266
Cdd:PRK09088 148 GQPKGVmLSERNLQQTAHNF-----------------GVLGRVDAHSsFLCDAPMFHiiGLITsvrpVLAVGGSILVSNg 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 267 --AGAYFRVLAEH--GVAALFTAPTAIRAIRQQdPGAALGkqySLTRFKTLFVAGERCDVETLEWSKKVfRVPVLDHWWQ 342
Cdd:PRK09088 211 fePKRTLGRLGDPalGITHYFCVPQMAQAFRAQ-PGFDAA---ALRHLTALFTGGAPHAAEDILGWLDD-GIPMVDGFGM 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 343 TETGS----PITASCIglgNSKTpppGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHL 418
Cdd:PRK09088 286 SEAGTvfgmSVDCDVI---RAKA---GAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLR---GPNLSPGYWRRPQATARA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 419 YFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRK 498
Cdd:PRK09088 357 FTGD--GWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPAD 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1191882763 499 DINITegqvLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL-SALVNGKP 555
Cdd:PRK09088 435 GAPLD----LERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLrDALAAGRK 488
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
120-547 |
2.33e-25 |
|
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: 109.39 E-value: 2.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 120 PGRKVEYMPILEEAMRIGQHKPDKVLIynrpnMETVPLASGRDLDWDEEMAkAQSQDCVPVLSEhPLYILYTSGTTGLPK 199
Cdd:cd05929 69 PAYKSSRAPRAEACAIIEIKAAALVCG-----LFTGGGALDGLEDYEAAEG-GSPETPIEDEAA-GWKMLYSGGTTGRPK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 200 GVVRPTGGyavmlnwtmssiyGLKPGEVWWAASDL-GWVVGHSYICYGPLIHG------NTTVLYEGKPVGTP--DAGAY 270
Cdd:cd05929 142 GIKRGLPG-------------GPPDNDTLMAAALGfGPGADSVYLSPAPLYHAapfrwsMTALFMGGTLVLMEkfDPEEF 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 271 FRVLAEHGVAALFTAPTAIRAIRQQdPGAALGKqYSLTRFKTLFVAGERCDVETLE-----WSKKVfrvpvldhwWQTET 345
Cdd:cd05929 209 LRLIERYRVTFAQFVPTMFVRLLKL-PEAVRNA-YDLSSLKRVIHAAAPCPPWVKEqwidwGGPII---------WEYYG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 346 GSPITASCIGLGNSKTPPPGQAGKSVPGyNVMILDDNMQklkarclgnivvklPLPPGAFSGLW-KNQEAFK-HLYFEKF 423
Cdd:cd05929 278 GTEGQGLTIINGEEWLTHPGSVGRAVLG-KVHILDEDGN--------------EVPPGEIGEVYfANGPGFEyTNDPEKT 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 424 P-----GYYDTM-DAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALcVLR 497
Cdd:cd05929 343 AaarneGGWSTLgDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAV-VQP 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1191882763 498 KDINITEGQVLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:cd05929 422 APGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
18-549 |
4.65e-25 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 109.30 E-value: 4.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 18 GDKVAIIyDSPvtdTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 97
Cdd:PLN02246 37 SDRPCLI-DGA---TGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 98 ELSSRIDHAKPKVVVTASFGIEPGRKVEYMPILEeAMRIGQHkPDKVLIYNrpnmetvplasgrdldwdeEMAKAQSQDC 177
Cdd:PLN02246 113 EIAKQAKASGAKLIITQSCYVDKLKGLAEDDGVT-VVTIDDP-PEGCLHFS-------------------ELTQADENEL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 178 --VPVLSEHPLYILYTSGTTGLPKGVVRPTGGYavmlnwtMSSIYGLKPGEVwwaaSDLGWVVGHSYICYGPLIH--GNT 253
Cdd:PLN02246 172 peVEISPDDVVALPYSSGTTGLPKGVMLTHKGL-------VTSVAQQVDGEN----PNLYFHSDDVILCVLPMFHiySLN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 254 TVLYEGKPVGTP-------DAGAYFRVLAEHGV-AALFTAP----------------TAIR---------------AIRQ 294
Cdd:PLN02246 241 SVLLCGLRVGAAilimpkfEIGALLELIQRHKVtIAPFVPPivlaiakspvvekydlSSIRmvlsgaaplgkeledAFRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 295 QDPGAALGKQYSLTRfktlfvAGercdvetlewskkvfrvPVLdhwwqtetgspitASCigLGNSKTP---PPGQAGKSV 371
Cdd:PLN02246 321 KLPNAVLGQGYGMTE------AG-----------------PVL-------------AMC--LAFAKEPfpvKSGSCGTVV 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 372 PGYNVMILDDNMQKLKARCL-GNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDV 450
Cdd:PLN02246 363 RNAELKIVDPETGASLPRNQpGEICIR---GPQIMKGYLNDPEATANTIDKD--GWLHTGDIGYIDDDDELFIVDRLKEL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 451 INVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEgqvlEEIVQHVRQSIGPVAAFRKAVF 530
Cdd:PLN02246 438 IKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITE----DEIKQFVAKQVVFYKRIHKVFF 513
|
570
....*....|....*....
gi 1191882763 531 VQQLPKTRSGKIPRAALSA 549
Cdd:PLN02246 514 VDSIPKAPSGKILRKDLRA 532
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
463-541 |
7.54e-25 |
|
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: 98.00 E-value: 7.54e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191882763 463 IEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEgqvlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGK 541
Cdd:pfam13193 2 VESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLE----EELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
12-541 |
2.31e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 106.89 E-value: 2.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 12 HIESGKGDKVAIIYDSpvtdtkATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIF 91
Cdd:PRK07798 11 AVADAVPDRVALVCGD------RRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 92 GGFASKELSSRIDHAKPKVVVtasFGIEPGRKVEymPILEEAMRIgqhkpdKVLIynrpnmeTVPLASGRDLDWD----E 167
Cdd:PRK07798 85 YRYVEDELRYLLDDSDAVALV---YEREFAPRVA--EVLPRLPKL------RTLV-------VVEDGSGNDLLPGavdyE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 168 EMAKAQSQDCVPVL-SEHPLYILYTSGTTGLPKGVV--------------RPTGGYAVMLNWTMSSIYGLKPGEVWWAAS 232
Cdd:PRK07798 147 DALAAGSPERDFGErSPDDLYLLYTGGTTGMPKGVMwrqedifrvllggrDFATGEPIEDEEELAKRAAAGPGMRRFPAP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 233 dlgwvvghsyicygPLIH-------------GNTTVLYegkPVGTPDAGAYFRVLAEHGVAALFTAPTA-----IRAIRQ 294
Cdd:PRK07798 227 --------------PLMHgagqwaafaalfsGQTVVLL---PDVRFDADEVWRTIEREKVNVITIVGDAmarplLDALEA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 295 qdpgaalGKQYSLTRFKTLFVAGercdvetLEWSKKVFR--------VPVLDHWWQTETGSpitascIGLGNSKTPPPGQ 366
Cdd:PRK07798 290 -------RGPYDLSSLFAIASGG-------ALFSPSVKEallellpnVVLTDSIGSSETGF------GGSGTVAKGAVHT 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 367 AGKSV-PGYNVMILDDNMQKLK---------ARClGNIvvklPLppgafsGLWKNQEAFKHLYFEK------FPGYYDTM 430
Cdd:PRK07798 350 GGPRFtIGPRTVVLDEDGNPVEpgsgeigwiARR-GHI----PL------GYYKDPEKTAETFPTIdgvryaIPGDRARV 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 431 DAgymdeEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEgqvlEE 510
Cdd:PRK07798 419 EA-----DGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDL----AE 489
|
570 580 590
....*....|....*....|....*....|.
gi 1191882763 511 IVQHVRQSIGPVAAFRKAVFVQQLPKTRSGK 541
Cdd:PRK07798 490 LRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
35-549 |
2.36e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 108.89 E-value: 2.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 35 TITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAihslifggfaskelssridhakpkvvvtA 114
Cdd:PRK12316 536 TLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGG----------------------------A 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 115 SFGIEPGRKVEYMPILEEAMRIGqhkpdkVLIYNRPNMETVPLASGRD-LDWDEEMAKAQSQ-DCVPVLS---EHPLYIL 189
Cdd:PRK12316 588 YVPLDPEYPAERLAYMLEDSGVQ------LLLSQSHLGRKLPLAAGVQvLDLDRPAAWLEGYsEENPGTElnpENLAYVI 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 190 YTSGTTGLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVVGHsYICYGPLIHGNTTVLyeGKPVGTPDAGA 269
Cdd:PRK12316 662 YTSGSTGKPKGAGNRHRALSNRLCW-MQQAYGLGVGDTVLQKTPFSFDVSV-WEFFWPLMSGARLVV--AAPGDHRDPAK 737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 270 YFRVLAEHGVAALFTAPTAIRAIrQQDPGAAlgkqySLTRFKTLFVAGERCDVETLEwskKVF-RVP---VLDHWWQTET 345
Cdd:PRK12316 738 LVELINREGVDTLHFVPSMLQAF-LQDEDVA-----SCTSLRRIVCSGEALPADAQE---QVFaKLPqagLYNLYGPTEA 808
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 346 GSPIT-ASCIGLGNSKTPppgqAGKSVPGYNVMILDDNMQKLKARCLGNIVVklplppgAFSGLWKNQEAFKHLYFEKF- 423
Cdd:PRK12316 809 AIDVThWTCVEEGGDSVP----IGRPIANLACYILDANLEPVPVGVLGELYL-------AGRGLARGYHGRPGLTAERFv 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 424 PG-------YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEdplkGHVPLALCVL 496
Cdd:PRK12316 878 PSpfvagerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVL 953
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1191882763 497 RkdiniTEGQVLEEIVQ-HVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAALSA 549
Cdd:PRK12316 954 E-----SEGGDWREALKaHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPA 1002
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
25-555 |
7.69e-24 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 106.27 E-value: 7.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 25 YDSPVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGaihslIFGGFASKELSsRID 104
Cdd:PRK06060 20 YDRPAFYAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARG-----VMAFLANPELH-RDD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 105 HAKPKVVVTASFGIEPGrkveymPILEeamrigQHKPDKVLiynrpnmETVPLASgrdldwdeEMAKAQSQDCVPVLSEH 184
Cdd:PRK06060 94 HALAARNTEPALVVTSD------ALRD------RFQPSRVA-------EAAELMS--------EAARVAPGGYEPMGGDA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 185 PLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPgevwwaaSDLGWVVGHSYICYG-------PLIHGNTTVLy 257
Cdd:PRK06060 147 LAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTP-------EDTGLCSARMYFAYGlgnsvwfPLATGGSAVI- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 258 EGKPVGTPDAG---AYFRVLAEHGVAALFT------APTAIRAIRqqdpgaalgkqysltrfkTLFVAGERCDVETLEWS 328
Cdd:PRK06060 219 NSAPVTPEAAAilsARFGPSVLYGVPNFFArvidscSPDSFRSLR------------------CVVSAGEALELGLAERL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 329 KKVFR-VPVLDHWWQTETGSPITASCIGLGNsktppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSG 407
Cdd:PRK06060 281 MEFFGgIPILDGIGSTEVGQTFVSNRVDEWR-----LGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVR---GPAIAKG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 408 LWKNQEAFkhLYFEkfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDpLKG 487
Cdd:PRK06060 353 YWNRPDSP--VANE---GWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRE-STG 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191882763 488 HVPLALCVLRKDINITEGQVLEEIvqHvRQSIGPVAAFR---KAVFVQQLPKTRSGKIPRAALSALVNGKP 555
Cdd:PRK06060 427 ASTLQAFLVATSGATIDGSVMRDL--H-RGLLNRLSAFKvphRFAVVDRLPRTPNGKLVRGALRKQSPTKP 494
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
19-542 |
1.27e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 104.39 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIIYDSpvtdTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 98
Cdd:PRK13391 12 DKPAVIMAS----TGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 99 LSSRIDHAKPKVVVTASfgiepgRKVEYMPILEEAmrigqhkpdkvliynrpnmetVPLASGR-DLDWDEEMAKAQS-QD 176
Cdd:PRK13391 88 AAYIVDDSGARALITSA------AKLDVARALLKQ---------------------CPGVRHRlVLDGDGELEGFVGyAE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 177 CVPVLSEHPL-------YILYTSGTTGLPKGVVRP--------TGGYAVMLNwtmsSIYGLKPGEVwwaasdlgwvvghs 241
Cdd:PRK13391 141 AVAGLPATPIadeslgtDMLYSSGTTGRPKGIKRPlpeqppdtPLPLTAFLQ----RLWGFRSDMV-------------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 242 YICYGPLIH-------------GNTTVLYEgkpvgTPDAGAYFRVLAEHGVAALFTAPTA-IRAIRQQDpgaALGKQYSL 307
Cdd:PRK13391 203 YLSPAPLYHsapqravmlvirlGGTVIVME-----HFDAEQYLALIEEYGVTHTQLVPTMfSRMLKLPE---EVRDKYDL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 308 TRFKTLFVAGERCDVETLEwskkvfrvPVLDhWWqtetgSPIT----ASCIGLGNSKTPP------PGQAGKSVPGyNVM 377
Cdd:PRK13391 275 SSLEVAIHAAAPCPPQVKE--------QMID-WW-----GPIIheyyAATEGLGFTACDSeewlahPGTVGRAMFG-DLH 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 378 ILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWKNQEAfKHlyfeKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHR 457
Cdd:PRK13391 340 ILDDDGAELPPGEPGTIWFEGGRPFEYLNDPAKTAEA-RH----PDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVN 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 458 ISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEGqVLEEIVQHVRQSIGPVAAFRKAVFVQQLPKT 537
Cdd:PRK13391 415 IYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPA-LAAELIAFCRQRLSRQKCPRSIDFEDELPRL 493
|
....*
gi 1191882763 538 RSGKI 542
Cdd:PRK13391 494 PTGKL 498
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
19-547 |
1.61e-23 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 104.68 E-value: 1.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIIYDSpvtdTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 98
Cdd:PLN02330 43 DKVAFVEAV----TGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 99 LSSRIDHAKPKVVVTASFGIEPGRKVEyMPILEeamrIGQHKpdkvlIYNRPNMETVPLASGRDLDWDEEMAKAQSQDCV 178
Cdd:PLN02330 119 IKKQAEAAGAKLIVTNDTNYGKVKGLG-LPVIV----LGEEK-----IEGAVNWKELLEAADRAGDTSDNEEILQTDLCA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 179 pvlsehplyILYTSGTTGLPKGVVRPTGGYAVMLnwtMSSIYGLKPgEVWWAASDLGWV-VGHSY----ICYGPLIHGNT 253
Cdd:PLN02330 189 ---------LPFSSGTTGISKGVMLTHRNLVANL---CSSLFSVGP-EMIGQVVTLGLIpFFHIYgitgICCATLRNKGK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 254 TVLyegkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIrQQDPgaaLGKQYSLTRFK--TLFVAGERCDVETLE-WSKK 330
Cdd:PLN02330 256 VVV-----MSRFELRTFLNALITQEVSFAPIVPPIILNL-VKNP---IVEEFDLSKLKlqAIMTAAAPLAPELLTaFEAK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 331 VFRVPVLDHWWQTEtgspitASCIGLGNSKtPPPGQA-------GKSVPGYNVMILD-DNMQKLKARCLGNIVVKlplPP 402
Cdd:PLN02330 327 FPGVQVQEAYGLTE------HSCITLTHGD-PEKGHGiakknsvGFILPNLEVKFIDpDTGRSLPKNTPGELCVR---SQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 403 GAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKE 482
Cdd:PLN02330 397 CVMQGYYNNKEETDRTIDED--GWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLP 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1191882763 483 DPLKGHVPLALCVLRKDINITEgqvlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:PLN02330 475 DEEAGEIPAACVVINPKAKESE----EDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
19-547 |
1.64e-23 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 104.44 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIiydspVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 98
Cdd:PRK06087 38 DKIAV-----VDNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 99 LSSRIDHAKPKVVVTASFGiepgRKVEYMP-ILEEAMRIGQHKPDKVLIYNRPNMETVPLAsgrdldwdEEMAKAQS-QD 176
Cdd:PRK06087 113 LVWVLNKCQAKMFFAPTLF----KQTRPVDlILPLQNQLPQLQQIVGVDKLAPATSSLSLS--------QIIADYEPlTT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 177 CVPVLSEHPLYILYTSGTTGLPKGV-------VRPTGGYAVMLNWTMSSIYglkpgevwWAASDLGWVVGHSYICYGPLI 249
Cdd:PRK06087 181 AITTHGDELAAVLFTSGTEGLPKGVmlthnniLASERAYCARLNLTWQDVF--------MMPAPLGHATGFLHGVTAPFL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 250 HGNTTVLYEgkpvgtpdagayfrvlaehgvaaLFTAPTAIRAIRQQDPGAALGKqysltrfkTLFVAGERC-------DV 322
Cdd:PRK06087 253 IGARSVLLD-----------------------IFTPDACLALLEQQRCTCMLGA--------TPFIYDLLNllekqpaDL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 323 ETLEW--------SKKVFR------VPVLDHWWQTETgSPitASCIGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKA 388
Cdd:PRK06087 302 SALRFflcggttiPKKVARecqqrgIKLLSVYGSTES-SP--HAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 389 RCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLL 468
Cdd:PRK06087 379 GCEGEEASR---GPNVFMGYLDEPELTARALDEE--GWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILL 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 469 SHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEgqvLEEIVQHV-RQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:PRK06087 454 QHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLT---LEEVVAFFsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
19-547 |
2.19e-23 |
|
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: 103.10 E-value: 2.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIIYDSpvtdtkATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIhslifggfaske 98
Cdd:cd17652 2 DAPAVVFGD------ETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAA------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 99 lssridhakpkvvvtasfgiepgrkveYMPIleeamrigqhkpdkvliynrpnmetvplasgrDLDWDEEMAKAQSQDCV 178
Cdd:cd17652 64 ---------------------------YLPL--------------------------------DPAYPAERIAYMLADAR 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 179 PVL----SEHPLYILYTSGTTGLPKGVVRPTGGYAvmlNWTMSSI--YGLKPGEVWWAASDLGWVVGHSYICyGPLIHGN 252
Cdd:cd17652 85 PALllttPDNLAYVIYTSGSTGRPKGVVVTHRGLA---NLAAAQIaaFDVGPGSRVLQFASPSFDASVWELL-MALLAGA 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 253 TTVLYEGKPVGTPDAGAyfRVLAEHGVAALFTAPTAIRAIrqqDPGAALGkqysltrFKTLFVAGERCDVETLE-WSKKv 331
Cdd:cd17652 161 TLVLAPAEELLPGEPLA--DLLREHRITHVTLPPAALAAL---PPDDLPD-------LRTLVVAGEACPAELVDrWAPG- 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 332 fRVpVLDHWWQTETgsPITASCIGLGNSKTPPPgqAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPG-------A 404
Cdd:cd17652 228 -RR-MINAYGPTET--TVCATMAGPLPGGGVPP--IGRPVPGTRVYVLDARLR--------------PVPPGvpgelyiA 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 405 FSGLWK---NQEAfkhLYFEKF-------PG--YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGT 472
Cdd:cd17652 288 GAGLARgylNRPG---LTAERFvadpfgaPGsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPG 364
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1191882763 473 VADCAVVGKEDPLKGHVPLALCVLRKDINITEGQVLEEIVQHVRQSIGPvAAFrkaVFVQQLPKTRSGKIPRAAL 547
Cdd:cd17652 365 VAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVP-AAF---VVLDALPLTPNGKLDRRAL 435
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1-544 |
2.84e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 103.93 E-value: 2.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 1 MLNMCYNAIDRHiesgkGDKVAIIYdspvtdTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLAC 80
Cdd:PRK05605 34 LVDLYDNAVARF-----GDRPALDF------FGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 81 ARIGAI---HSLIFggfASKELSSR-IDHAkPKVVV---TASFGIE------PGRKV------EYMPILeeaMRIGQHKP 141
Cdd:PRK05605 103 LRLGAVvveHNPLY---TAHELEHPfEDHG-ARVAIvwdKVAPTVErlrrttPLETIvsvnmiAAMPLL---QRLALRLP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 142 DKVLIYNR-----PNMETVP----LASGRDLDWDEEMAKAQSQDCVPVlsehplyILYTSGTTGLPKGVVRPTGGyaVML 212
Cdd:PRK05605 176 IPALRKARaaltgPAPGTVPwetlVDAAIGGDGSDVSHPRPTPDDVAL-------ILYTSGTTGKPKGAQLTHRN--LFA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 213 NWTMSS--IYGLKPG-EVWWAASDLGwvvgHSY-----ICYGPLIhGNTTVLYegkPvgTPDAGAYFRVLAEHGVAALFT 284
Cdd:PRK05605 247 NAAQGKawVPGLGDGpERVLAALPMF----HAYgltlcLTLAVSI-GGELVLL---P--APDIDLILDAMKKHPPTWLPG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 285 APTAIRAIRQqdpgAALGKQYSLTRFKTLFVAGERCDVETLE-WSKKVFRVPVlDHWWQTETgSPITascigLGN--SKT 361
Cdd:PRK05605 317 VPPLYEKIAE----AAEERGVDLSGVRNAFSGAMALPVSTVElWEKLTGGLLV-EGYGLTET-SPII-----VGNpmSDD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 362 PPPGQAGKSVPGYNVMILD-DNMQKLKARC-LGNIVVKlplPPGAFSGLWKNQEAFKHLYFekfPGYYDTMDAGYMDEEG 439
Cdd:PRK05605 386 RRPGYVGVPFPDTEVRIVDpEDPDETMPDGeEGELLVR---GPQVFKGYWNRPEETAKSFL---DGWFRTGDVVVMEEDG 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 440 YVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLrkdiniTEGQVLEE--IVQHVRQ 517
Cdd:PRK05605 460 FIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVL------EPGAALDPegLRAYCRE 533
|
570 580
....*....|....*....|....*..
gi 1191882763 518 SIGPVAAFRKAVFVQQLPKTRSGKIPR 544
Cdd:PRK05605 534 HLTRYKVPRRFYHVDELPRDQLGKVRR 560
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
19-550 |
3.57e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 105.04 E-value: 3.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIIYDspvtdtKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHslifggfaske 98
Cdd:PRK12316 4566 DAVAVVFD------EEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAY----------- 4628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 99 lssridhakpkvvvtASFGIE-PGRKVEYMpiLEEAmRIGqhkpdkVLIYNRPNMETVPLASGRD---LDWDEEMAKAQS 174
Cdd:PRK12316 4629 ---------------VPLDPEyPRERLAYM--MEDS-GAA------LLLTQSHLLQRLPIPDGLAslaLDRDEDWEGFPA 4684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 175 QDcvPVLSEHP---LYILYTSGTTGLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVVGHSYIcYGPLIHG 251
Cdd:PRK12316 4685 HD--PAVRLHPdnlAYVIYTSGSTGRPKGVAVSHGSLVNHLHA-TGERYELTPDDRVLQFMSFSFDGSHEGL-YHPLING 4760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 252 NTTVLyegKPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAAlgkqySLTRFKTLFVAGERCDVETL-EWSKK 330
Cdd:PRK12316 4761 ASVVI---RDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDG-----EPPSLRVYCFGGEAVAQASYdLAWRA 4832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 331 VFRVPVLDHWWQTETG-SPITASCiglgnSKTPPPGQA----GKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAF 405
Cdd:PRK12316 4833 LKPVYLFNGYGPTETTvTVLLWKA-----RDGDACGAAympiGTPLGNRSGYVLDGQLN--------------PLPVGVA 4893
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 406 SGLWKNQEAFKHLYF-------EKF-------PG--YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLS 469
Cdd:PRK12316 4894 GELYLGGEGVARGYLerpaltaERFvpdpfgaPGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLRE 4973
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 470 HGTVADCAVVGKEDPLKGH-----VPLALCVLrkDINITEGQVLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPR 544
Cdd:PRK12316 4974 HPAVREAVVIAQEGAVGKQlvgyvVPQDPALA--DADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDR 5051
|
....*.
gi 1191882763 545 AALSAL 550
Cdd:PRK12316 5052 KALPQP 5057
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
180-547 |
8.62e-23 |
|
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: 101.29 E-value: 8.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 180 VLSEHP---LYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSsIYGLKPGEVWWAASDLGWVVGHSYIcYGPLIHGNTTVL 256
Cdd:cd17649 88 LLTHHPrqlAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAE-RYGLTPGDRELQFASFNFDGAHEQL-LPPLICGACVVL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 257 YEGKPVGTPDAgaYFRVLAEHGVAALFTAPT-------AIRAIRQQDPGAalgkqysltrFKTLFVAGERCDVETLeWSK 329
Cdd:cd17649 166 RPDELWASADE--LAEMVRELGVTVLDLPPAylqqlaeEADRTGDGRPPS----------LRLYIFGGEALSPELL-RRW 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 330 KVFRVPVLDHWWQTETGSPITASCIGLGNSKTPPPGQAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGLW 409
Cdd:cd17649 233 LKAPVRLFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRPLGGRSAYILDADLN--------------PVPVGVTGELY 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 410 KNQEAFKHLYF-------EKF-------PG--YYDTMD-AGYMDEeGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGT 472
Cdd:cd17649 299 IGGEGLARGYLgrpeltaERFvpdpfgaPGsrLYRTGDlARWRDD-GVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPG 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1191882763 473 VADCAVVGKEDPLkGHVPLALCVLRKDinITEGQVLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:cd17649 378 VREAAVVALDGAG-GKQLVAYVVLRAA--AAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKAL 449
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
19-549 |
2.19e-22 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 100.99 E-value: 2.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIIydspvtDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 98
Cdd:PRK13382 58 DRPGLI------DELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 99 LSSRIDHAKPKVVVTASfgiepgrkvEYMPILEEAMRigqHKPDKVLIYNRPNMETVPLAsgrdldwdEEMAKAQSQDCV 178
Cdd:PRK13382 132 LAEVVTREGVDTVIYDE---------EFSATVDRALA---DCPQATRIVAWTDEDHDLTV--------EVLIAAHAGQRP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 179 PVLSEHPLYILYTSGTTGLPKGVVRP-TGGYAvmlnwTMSSIYGLKPgevwWAASDLGWVVGhsyicygPLIH--GNTTV 255
Cdd:PRK13382 192 EPTGRKGRVILLTSGTTGTPKGARRSgPGGIG-----TLKAILDRTP----WRAEEPTVIVA-------PMFHawGFSQL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 256 LYEGKPVGTP------DAGAYFRVLAEHGVAALFTAPTAIRaiRQQDPGAALGKQYSLTRFKTLFVAGERCDVETLEWSK 329
Cdd:PRK13382 256 VLAASLACTIvtrrrfDPEATLDLIDRHRATGLAVVPVMFD--RIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFM 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 330 KVFRVPVLDHWWQTETGSPITAsciglgnskTPP-----PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVK-LPLPPG 403
Cdd:PRK13382 334 DQFGDVIYNNYNATEAGMIATA---------TPAdlraaPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRnDTQFDG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 404 AFSGLWKNQEAfkhlyfekfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKED 483
Cdd:PRK13382 405 YTSGSTKDFHD----------GFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDD 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191882763 484 PLKGHVPLALCVLRKDINITEgqvlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAALSA 549
Cdd:PRK13382 475 EQYGQRLAAFVVLKPGASATP----ETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
183-544 |
5.07e-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: 97.33 E-value: 5.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 183 EHPLYILYTSGTTGLPKGVV--------RPTGGYAVMLNWTMSSI-YGLKP----GEVWWAASDL----GWVVGHSYICY 245
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLlanktffaVPDILQKEGLNWVVGDVtYLPLPathiGGLWWILTCLihggLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 246 GPLihgnttvlyegkpvgtpdagayFRVLAEHGVAALFTAPTAIRAIRQQDPGAAlgkQYSlTRFKTLFVAGERC---DV 322
Cdd:cd17635 81 KSL----------------------FKILTTNAVTTTCLVPTLLSKLVSELKSAN---ATV-PSLRLIGYGGSRAiaaDV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 323 ETLEWSKKVfrvPVLDHWWQTETGspiTASCIGLGNSkTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPP 402
Cdd:cd17635 135 RFIEATGLT---NTAQVYGLSETG---TALCLPTDDD-SIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIK---SP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 403 GAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKE 482
Cdd:cd17635 205 ANMLGYWNNPERTAEVLID---GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEIS 281
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1191882763 483 DPLKGHVPLALCVLR--KDINITEGQVLEeivqhVRQSIGPVAAFRKAVFVQQLPKTRSGKIPR 544
Cdd:cd17635 282 DEEFGELVGLAVVASaeLDENAIRALKHT-----IRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
30-558 |
2.51e-21 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 97.77 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 30 TDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPK 109
Cdd:PRK05857 36 CDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 110 VVVTAsfgiePGRKV--EYMPILEEAMRIGQHKPDKVLIYNRPNMETVPLASGRDLDWDEemakaqsqdcvpvlsehPLY 187
Cdd:PRK05857 116 AALVA-----PGSKMasSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNADQGSED-----------------PLA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 188 ILYTSGTTGLPKGVVRPTGGYAVM--------LNW--------TMSSIYGLKPGEVWWAASdlgwvvghsyiCygpLIHG 251
Cdd:PRK05857 174 MIFTSGTTGEPKAVLLANRTFFAVpdilqkegLNWvtwvvgetTYSPLPATHIGGLWWILT-----------C---LMHG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 252 NTTVlyegkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALgkqySLTRFKTLFVAGER---CDVETLEWS 328
Cdd:PRK05857 240 GLCV------TGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANA----TVPSLRLVGYGGSRaiaADVRFIEAT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 329 KkvfrVPVLDHWWQTETGSpiTASCIGLGNSKTP--PPGQAGKSVPGYNVMILDDN------MQKLKARCLGNIVVKlpl 400
Cdd:PRK05857 310 G----VRTAQVYGLSETGC--TALCLPTDDGSIVkiEAGAVGRPYPGVDVYLAATDgigptaPGAGPSASFGTLWIK--- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 401 PPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVG 480
Cdd:PRK05857 381 SPANMLGYWNNPERTAEVLID---GWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 481 KEDPLKGH-VPLALcVLRKDINITEGQVLEE-IVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAALSALVNGKPYKV 558
Cdd:PRK05857 458 IPDEEFGAlVGLAV-VASAELDESAARALKHtIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAATADKARV 536
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
36-550 |
2.99e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 97.51 E-value: 2.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 36 ITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVtas 115
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLV--- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 116 fgIEPG-RKVEYMPILEEAM--------------RIGQHKPD-----KVLIYNRPNMETVPLASGRdldwdeemakaQSQ 175
Cdd:PRK06164 113 --VWPGfKGIDFAAILAAVPpdalpplraiavvdDAADATPApapgaRVQLFALPDPAPPAAAGER-----------AAD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 176 DCVPVLsehplyILYTSGTTGLPKGVVRPTGGYaVMLNWTMSSIYGLKPGEVWWAASDLGWVVGHSYICYGplIHGNTTV 255
Cdd:PRK06164 180 PDAGAL------LFTTSGTTSGPKLVLHRQATL-LRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGA--LAGGAPL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 256 LYEgkPVGtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALGKQYSLTRFKTlFVAGERcdvETLEWskkvfrvp 335
Cdd:PRK06164 251 VCE--PVF--DAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLFGFAS-FAPALG---ELAAL-------- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 336 VLDHwwqtetGSPITasciGL-GNSK----------TPP------PGQAGKSvPGYNVMILD-DNMQKLKARCLGNIVVK 397
Cdd:PRK06164 315 ARAR------GVPLT----GLyGSSEvqalvalqpaTDPvsvrieGGGRPAS-PEARVRARDpQDGALLPDGESGEIEIR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 398 lplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEG-YVYVmSRVDDVINVAGHRISAGAIEESLLSHGTVADC 476
Cdd:PRK06164 384 ---APSLMRGYLDNPDATARALTDD--GYFRTGDLGYTRGDGqFVYQ-TRMGDSLRLGGFLVNPAEIEHALEALPGVAAA 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 477 AVVGKEdpLKGH-VPLALCVLrkdiniTEGQVL--EEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSG---KIPRAALSAL 550
Cdd:PRK06164 458 QVVGAT--RDGKtVPVAFVIP------TDGASPdeAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREM 529
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
37-542 |
2.99e-21 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 97.57 E-value: 2.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 37 TYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTA-S 115
Cdd:PRK08315 45 TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAAdG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 116 F-----------------GIEPGR-KVEYMPILEEAMRIGQHKPdkvliynrPNMETVP--LASGRDLDwDEEMAKAQSQ 175
Cdd:PRK08315 125 FkdsdyvamlyelapelaTCEPGQlQSARLPELRRVIFLGDEKH--------PGMLNFDelLALGRAVD-DAELAARQAT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 176 dcvpvLSEH-PLYILYTSGTTGLPKGvvrptggyaVMLnwTMSSIyglkpgevwwaaSDLGWVVGHS------------- 241
Cdd:PRK08315 196 -----LDPDdPINIQYTSGTTGFPKG---------ATL--THRNI------------LNNGYFIGEAmklteedrlcipv 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 242 --YICYG-------PLIHGNTTVLyegkPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIrQQDPGAAlgkQYSLTRFKT 312
Cdd:PRK08315 248 plYHCFGmvlgnlaCVTHGATMVY----PGEGFDPLATLAAVEEERCTALYGVPTMFIAE-LDHPDFA---RFDLSSLRT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 313 LFVAGERCDVETLewsKKVFRV----------------PVLdhwWQTETGSPITASC--------------IGLGNSKTP 362
Cdd:PRK08315 320 GIMAGSPCPIEVM---KRVIDKmhmsevtiaygmtetsPVS---TQTRTDDPLEKRVttvgralphlevkiVDPETGETV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 363 PPGQAGKSVP-GYNVMilddnmqklkarclgnivvklplppgafSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYV 441
Cdd:PRK08315 394 PRGEQGELCTrGYSVM----------------------------KGYWNDPEKTAEAIDAD--GWMHTGDLAVMDEEGYV 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 442 YVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEgqvlEEIVQHVRqsiGP 521
Cdd:PRK08315 444 NIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTE----EDVRDFCR---GK 516
|
570 580
....*....|....*....|....
gi 1191882763 522 VAAF---RKAVFVQQLPKTRSGKI 542
Cdd:PRK08315 517 IAHYkipRYIRFVDEFPMTVTGKI 540
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
19-547 |
3.22e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 97.16 E-value: 3.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIIYDSPVtdtkatITYKEVLEQVSRLAGVLvKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 98
Cdd:PRK07638 16 NKIAIKENDRV------LTYKDWFESVCKVANWL-NEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 99 LSSRIDHAKPKVVVTASFGIEPgrkveympILEEAMRIgqhkpdkvliynrpnmetvplasgrdLDWDE--EMAKAQSQD 176
Cdd:PRK07638 89 LKERLAISNADMIVTERYKLND--------LPDEEGRV--------------------------IEIDEwkRMIEKYLPT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 177 CVPV--LSEHPLYILYTSGTTGLPKGVVRptggyaVMLNWTMS-----SIYGLKPGEVWWAASDLGwvvgHSYICYGPL- 248
Cdd:PRK07638 135 YAPIenVQNAPFYMGFTSGSTGKPKAFLR------AQQSWLHSfdcnvHDFHMKREDSVLIAGTLV----HSLFLYGAIs 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 249 -IHGNTTVLYEGK--PVGTPDAgayfrvLAEHGVAALFTAPTAIRAIrqqdpgaalgkqYSLTRFK----TLFVAGERCD 321
Cdd:PRK07638 205 tLYVGQTVHLMRKfiPNQVLDK------LETENISVMYTVPTMLESL------------YKENRVIenkmKIISSGAKWE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 322 VETLEWSKKVFRVPVLDHWWQTETGSPITAScigLGNSKTPPPGQAGKsvPGYNVMILDDNM--QKLKARCLGNIVVKLP 399
Cdd:PRK07638 267 AEAKEKIKNIFPYAKLYEFYGASELSFVTAL---VDEESERRPNSVGR--PFHNVQVRICNEagEEVQKGEIGTVYVKSP 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 400 LppgAFSGlWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVV 479
Cdd:PRK07638 342 Q---FFMG-YIIGGVLARELNAD--GWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVI 415
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191882763 480 GKEDPLKGHVPLAlcvlrkdinITEGQV-LEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:PRK07638 416 GVPDSYWGEKPVA---------IIKGSAtKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
26-547 |
3.13e-20 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 94.52 E-value: 3.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 26 DSPVTD--TKATITYKEVLEQVSRLA-GVLVKHGVSKGDTVV------IYMPMIpqamytMLACARIGAIHSLIFGGFAS 96
Cdd:PLN02574 55 DTALIDssTGFSISYSELQPLVKSMAaGLYHVMGVRQGDVVLlllpnsVYFPVI------FLAVLSLGGIVTTMNPSSSL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 97 KELSSRIDHAKPKVVVTASfgiepgRKVEYMPILEEAMrIGQhkPDKVlIYNRPNMETVPLASGRDLDWDEEMAKAQSQD 176
Cdd:PLN02574 129 GEIKKRVVDCSVGLAFTSP------ENVEKLSPLGVPV-IGV--PENY-DFDSKRIEFPKFYELIKEDFDFVPKPVIKQD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 177 CVPVlsehplyILYTSGTTGLPKGVVRPTGGYAVMLNWTM---SSIYGLKPGE-VWWAASDLGWVVGHSYICYGPLIHGN 252
Cdd:PLN02574 199 DVAA-------IMYSSGTTGASKGVVLTHRNLIAMVELFVrfeASQYEYPGSDnVYLAALPMFHIYGLSLFVVGLLSLGS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 253 TTVLYEgkpvgTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALGKQYSLTRFKTLFVAGERCDVEtlEWSKKVF 332
Cdd:PLN02574 272 TIVVMR-----RFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQ--DFVQTLP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 333 RVPVLDHWWQTETGSPITAsciGLGNSKTPPPGQAGKSVPGYNVMILDdnmqkLKARCLgnivvklpLPPGAFSGLW--- 409
Cdd:PLN02574 345 HVDFIQGYGMTESTAVGTR---GFNTEKLSKYSSVGLLAPNMQAKVVD-----WSTGCL--------LPPGNCGELWiqg 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 410 --------KNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGK 481
Cdd:PLN02574 409 pgvmkgylNNPKATQSTIDKD--GWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAV 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191882763 482 EDPLKGHVPLALCVLRKDINITEgqvlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:PLN02574 487 PDKECGEIPVAFVVRRQGSTLSQ----EAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRREL 548
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
29-548 |
8.33e-20 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 93.03 E-value: 8.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 29 VTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKP 108
Cdd:PRK05852 37 VTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 109 KVVVTASFGiePG-RKVEYMPILEEAMRIGQhkpdkvliyNRPNMETVPLAsgrDLDWDEEMAKAQSQDcvPVLSEHPLY 187
Cdd:PRK05852 117 RVVLIDADG--PHdRAEPTTRWWPLTVNVGG---------DSGPSGGTLSV---HLDAATEPTPATSTP--EGLRPDDAM 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 188 ILYTSGTTGLPKgvvrptggyavMLNWTMSSIYGLKPGEVwwAASDLGwvVGHSYICYGPLIHGNTTV------LYEGKP 261
Cdd:PRK05852 181 IMFTGGTTGLPK-----------MVPWTHANIASSVRAII--TGYRLS--PRDATVAVMPLYHGHGLIaallatLASGGA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 262 VGTPDAGAY----FRVLAEHGVAALFTAPTAIRAIRQQDPGAalgKQYSLTRFKTLFVagERC----DVETLEWSKKVFR 333
Cdd:PRK05852 246 VLLPARGRFsahtFWDDIKAVGATWYTAVPTIHQILLERAAT---EPSGRKPAALRFI--RSCsaplTAETAQALQTEFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 334 VPVLDHWWQTETGSPITASCI-GLGNSKTP--PPGQAGKSVpGYNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWK 410
Cdd:PRK05852 321 APVVCAFGMTEATHQVTTTQIeGIGQTENPvvSTGLVGRST-GAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 411 NQEA-FKHlyfekfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHV 489
Cdd:PRK05852 400 ITAAnFTD-------GWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEA 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1191882763 490 PLALCVLRKDINITEgqvlEEIVQHVRQSIGPV---AAFRKAvfvQQLPKTRSGKIPRAALS 548
Cdd:PRK05852 473 VAAVIVPRESAPPTA----EELVQFCRERLAAFeipASFQEA---SGLPHTAKGSLDRRAVA 527
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
19-549 |
1.01e-19 |
|
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: 92.39 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIIYDSpvtdtkATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGaihslifGGFASke 98
Cdd:cd17655 12 DHTAVVFED------QTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAG-------GAYLP-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 99 lssrIDHAKPKvvvtasfgiepgRKVEYMpiLEE---AMRIGQHKpdkvLIYNRPNMETVPLasgrdLDWDEEMAKAQSQ 175
Cdd:cd17655 77 ----IDPDYPE------------ERIQYI--LEDsgaDILLTQSH----LQPPIAFIGLIDL-----LDEDTIYHEESEN 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 176 DCVPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYglkPGEvwwaASDLGWVVGHSY------IcYGPLI 249
Cdd:cd17655 130 LEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIY---QGE----HLRVALFASISFdasvteI-FASLL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 250 HGNTTVLYEGKPVGtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALgkqysltRFKTLFVAGERCDVETLEWSK 329
Cdd:cd17655 202 SGNTLYIVRKETVL--DGQALTQYIRQNRITIIDLTPAHLKLLDAADDSEGL-------SLKHLIVGGEALSTELAKKII 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 330 KVFR--VPVLDHWWQTETgsPITAS---CIGLGNSKTPPPgqAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGA 404
Cdd:cd17655 273 ELFGtnPTITNAYGPTET--TVDASiyqYEPETDQQVSVP--IGKPLGNTRIYILDQYGRPQPVGVAGELYIG---GEGV 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 405 FSGLWKNQEafkhLYFEKF------PG--YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADC 476
Cdd:cd17655 346 ARGYLNRPE----LTAEKFvddpfvPGerMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEA 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1191882763 477 AVVGKEDPLKGHVPLALCVLRKDINITegQVLEEIVQHVRQSIGPvaafrkAVFVQ--QLPKTRSGKIPRAALSA 549
Cdd:cd17655 422 VVIARKDEQGQNYLCAYIVSEKELPVA--QLREFLARELPDYMIP------SYFIKldEIPLTPNGKVDRKALPE 488
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
35-544 |
1.25e-19 |
|
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: 91.73 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 35 TITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTA 114
Cdd:cd05914 7 PLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 115 sfgiepgrkveympileeamrigqhKPDKVLIynrpnmetvplasgrdldwdeemakaqsqdcvpvlsehplyILYTSGT 194
Cdd:cd05914 87 -------------------------DEDDVAL-----------------------------------------INYTSGT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 195 TGLPKGVVRPtgGYAVMLNWTMSSIYG-LKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLYEGKPVGTPDAGAYFRV 273
Cdd:cd05914 101 TGNSKGVMLT--YRNIVSNVDGVKEVVlLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAKIIALAFAQV 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 274 LAEHGVAALF-----------------------TAPTAIRAIRQQdPGAALGKQYSlTRFKTLFVAGERCDVETLEWSKK 330
Cdd:cd05914 179 TPTLGVPVPLviekifkmdiipkltlkkfkfklAKKINNRKIRKL-AFKKVHEAFG-GNIKEFVIGGAKINPDVEEFLRT 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 331 VfRVPVLDHWWQTETGsPITASciglgnskTPPP----GQAGKSVPGYNVMILDDNMQKLKarclGNIVVKlplPPGAFS 406
Cdd:cd05914 257 I-GFPYTIGYGMTETA-PIISY--------SPPNrirlGSAGKVIDGVEVRIDSPDPATGE----GEIIVR---GPNVMK 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 407 GLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVI-NVAGHRISAGAIEESLLSHGTVADCAVVGKEDPL 485
Cdd:cd05914 320 GYYKNPEATAEAFDKD--GWFHTGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKL 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191882763 486 KGHV---PLALCVLRKDINITEGQVLEEIVQHVRQSigpVAAFRKAVFVQ----QLPKTRSGKIPR 544
Cdd:cd05914 398 VALAyidPDFLDVKALKQRNIIDAIKWEVRDKVNQK---VPNYKKISKVKivkeEFEKTPKGKIKR 460
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
35-551 |
2.72e-19 |
|
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: 90.85 E-value: 2.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 35 TITYKEVLEQVSRLaGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTA 114
Cdd:cd05909 7 SLTYRKLLTGAIAL-ARKLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 115 S-----FGIEPGRKVEYMP--ILEEAMRIGQHKPDKVLIYNRpnmetvplASGRDLDWDEEMAkaqsqdCVPVLSEHPLY 187
Cdd:cd05909 86 KqfiekLKLHHLFDVEYDAriVYLEDLRAKISKADKCKAFLA--------GKFPPKWLLRIFG------VAPVQPDDPAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 188 ILYTSGTTGLPKGVVRP-----TGGYAVmlnwtmSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLY----E 258
Cdd:cd05909 152 ILFTSGSEGLPKGVVLShknllANVEQI------TAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHpnplD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 259 GKPVGtpdagayfRVLAEHGVAALFTAPTAIRAIrqqdpgAALGKQYSLTRFKTLFVAGERCDVETLEWSKKVFRVPVLD 338
Cdd:cd05909 226 YKKIP--------ELIYDKKATILLGTPTFLRGY------ARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 339 HWWQTETgSPITASciglgNSKTPP--PGQAGKSVPGYNVMILD-DNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAF 415
Cdd:cd05909 292 GYGTTEC-SPVISV-----NTPQSPnkEGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVR---GPNVMLGYLNEPELT 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 416 KHLYFEkfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSH-GTVADCAVVGKEDPLKGHVpLALC 494
Cdd:cd05909 363 SFAFGD---GWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEK-IVLL 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1191882763 495 VLRKDINItegqvlEEIVQHVRQS-IGPVAAFRKAVFVQQLPKTRSGKIPRAALSALV 551
Cdd:cd05909 439 TTTTDTDP------SSLNDILKNAgISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
340-544 |
3.41e-19 |
|
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: 88.87 E-value: 3.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 340 WW----QTETGSPITascIGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLppgAFSGLWKNQEAF 415
Cdd:cd17637 139 FWslygQTETSGLVT---LSPYRER---PGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPL---VFQGYWNLPELT 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 416 KHLYFEkfpGYYDTMDAGYMDEEGYVYVMSRV--DDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLAL 493
Cdd:cd17637 210 AYTFRN---GWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAV 286
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1191882763 494 CVLRKDINITEgqvlEEIVQHVRQSIgpvAAFRK---AVFVQQLPKTRSGKIPR 544
Cdd:cd17637 287 CVLKPGATLTA----DELIEFVGSRI---ARYKKpryVVFVEALPKTADGSIDR 333
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
36-550 |
4.06e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 92.15 E-value: 4.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 36 ITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHslifggfaskelssridhakpkvvvtAS 115
Cdd:PRK12467 1600 LTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAY--------------------------VP 1653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 116 FGIE-PGRKVEYMPileEAMRIGqhkpdkVLIYNRPNMETVPLASG-RDLDWDEEMAKAQSQDCV-PVLSEHP---LYIL 189
Cdd:PRK12467 1654 LDPEyPRERLAYMI---EDSGIE------LLLTQSHLQARLPLPDGlRSLVLDQEDDWLEGYSDSnPAVNLAPqnlAYVI 1724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 190 YTSGTTGLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVVGHSYIcYGPLIHGNTTVLyeGKPVGTPDAGA 269
Cdd:PRK12467 1725 YTSGSTGRPKGAGNRHGALVNRLCA-TQEAYQLSAADVVLQFTSFAFDVSVWEL-FWPLINGARLVI--APPGAHRDPEQ 1800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 270 YFRVLAEHGVAALFTAPTAIRAIRQQDPgaALGKQYSLTRfktLFVAGERCDVETLE-WSKKVFRVPVLDHWWQTETGSP 348
Cdd:PRK12467 1801 LIQLIERQQVTTLHFVPSMLQQLLQMDE--QVEHPLSLRR---VVCGGEALEVEALRpWLERLPDTGLFNLYGPTETAVD 1875
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 349 ITASCIGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplppGAfsGLWKNQEAFKHLYFEKF----- 423
Cdd:PRK12467 1876 VTHWTCRRKDLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLG-----GV--GLARGYLNRPALTAERFvadpf 1948
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 424 --PG--YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDP----LKGH-VPLALC 494
Cdd:PRK12467 1949 gtVGsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGAngkqLVAYvVPTDPG 2028
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1191882763 495 VLRKDINITEGQvlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAALSAL 550
Cdd:PRK12467 2029 LVDDDEAQVALR--AILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAP 2082
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
26-573 |
4.86e-19 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 90.61 E-value: 4.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 26 DSPVT----DTKATITYKEVLEQVSRLAGVLVKH-GVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELS 100
Cdd:PRK05620 25 DTTVTtwggAEQEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 101 SRIDHAKPKVVVT-ASFGIEPGRKVEYMPILEEAMRIGQHKPDKVLIYNRPNMETVPLAS---GR--DLDWdeemakaqs 174
Cdd:PRK05620 105 HIINHAEDEVIVAdPRLAEQLGEILKECPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEAlldGRstVYDW--------- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 175 qdcvPVLSEH-PLYILYTSGTTGLPKGVVrptggYAVMLNWTMSsiYGLKpgevwwAASDLGWVVGHSYICYGPLIHgnt 253
Cdd:PRK05620 176 ----PELDETtAAAICYSTGTTGAPKGVV-----YSHRSLYLQS--LSLR------TTDSLAVTHGESFLCCVPIYH--- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 254 tVLYEGKPVGTPDAGAYFrVLAEHGVaalfTAPTAIRAIRQQDPGAALG-----------------KQYSLTrfkTLFVA 316
Cdd:PRK05620 236 -VLSWGVPLAAFMSGTPL-VFPGPDL----SAPTLAKIIATAMPRVAHGvptlwiqlmvhylknppERMSLQ---EIYVG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 317 GERCDVETLE-WSKKvFRVPVLDHWWQTETgSPItasciglGNSKTPPPGQAGKSVPGYNV------------MILDDNM 383
Cdd:PRK05620 307 GSAVPPILIKaWEER-YGVDVVHVWGMTET-SPV-------GTVARPPSGVSGEARWAYRVsqgrfpasleyrIVNDGQV 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 384 QKLKARCLGNIVVKLPLPPGAFSGLWKNQEAFKHLYF---------EKFP--GYYDTMDAGYMDEEGYVYVMSRVDDVIN 452
Cdd:PRK05620 378 MESTDRNEGEIQVRGNWVTASYYHSPTEEGGGAASTFrgedvedanDRFTadGWLRTGDVGSVTRDGFLTIHDRARDVIR 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 453 VAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEgQVLEEIVQHVRQSIGPVAAFRKAVFVQ 532
Cdd:PRK05620 458 SGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTR-ETAERLRDQLRDRLPNWMLPEYWTFVD 536
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1191882763 533 QLPKTRSGKIPRAALSALVNGKPYKVTpTIEDPSIFGHIEE 573
Cdd:PRK05620 537 EIDKTSVGKFDKKDLRQHLADGDFEII-KLKGPGESGESDS 576
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
17-546 |
5.62e-19 |
|
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: 90.38 E-value: 5.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 17 KGDKVAIIYDSPVTDTKATITYKEVLEQVSRLAGVLVKHGvSKGDTVVIympMIPQAM---YTMLACARIGAIHSLIF-- 91
Cdd:cd05931 6 RPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLL---LAPPGLdfvAAFLGCLYAGAIAVPLPpp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 92 -GGFASKELSSRIDHAKPKVVVTASfgiepgrkveympileeamriGQHKPDKVLIYNRPNMETVPLasgRDLDWDEEMA 170
Cdd:cd05931 82 tPGRHAERLAAILADAGPRVVLTTA---------------------AALAAVRAFAASRPAAGTPRL---LVVDLLPDTS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 171 KAQSQDCVPVLSEhPLYILYTSGTTGLPKGVVRPTGgyAVMLN-WTMSSIYGLKPGEVWwaAS------DLGWVVGhsyI 243
Cdd:cd05931 138 AADWPPPSPDPDD-IAYLQYTSGSTGTPKGVVVTHR--NLLANvRQIRRAYGLDPGDVV--VSwlplyhDMGLIGG---L 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 244 CyGPLIHGNTTVL-----YEGKPVGTPDAGAYFRvlAEHGVAALFTAPTAIRAIRQQDPGAalgkqYSLTRFKTLFVAGE 318
Cdd:cd05931 210 L-TPLYSGGPSVLmspaaFLRRPLRWLRLISRYR--ATISAAPNFAYDLCVRRVRDEDLEG-----LDLSSWRVALNGAE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 319 RCDVETLE----------WSKKVFR-------------VPVLDHWWQTETGSPITASCIGLGNSKTPPPGQA----GKSV 371
Cdd:cd05931 282 PVRPATLRrfaeafapfgFRPEAFRpsyglaeatlfvsGGPPGTGPVVLRVDRDALAGRAVAVAADDPAARElvscGRPL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 372 PGYNVMILDDN-MQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKFP----GYYDTMDAGYMDEeGYVYVMSR 446
Cdd:cd05931 362 PDQEVRIVDPEtGRELPDGEVGEIWVR---GPSVASGYWGRPEATAETFGALAAtdegGWLRTGDLGFLHD-GELYITGR 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 447 VDDVINVAGHRISAGAIEESLLSH------GTVADCAVVGKEDplkGHVPLALCVLRKDINITEGQVLEEIVQHVRQSIG 520
Cdd:cd05931 438 LKDLIIVRGRNHYPQDIEATAEEAhpalrpGCVAAFSVPDDGE---ERLVVVAEVERGADPADLAAIAAAIRAAVAREHG 514
|
570 580
....*....|....*....|....*...
gi 1191882763 521 pVAAfRKAVFVQQ--LPKTRSGKIPRAA 546
Cdd:cd05931 515 -VAP-ADVVLVRPgsIPRTSSGKIQRRA 540
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
26-547 |
7.74e-19 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 90.87 E-value: 7.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 26 DSP-VTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRID 104
Cdd:PRK10252 473 DAPaLADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLE 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 105 HAKPKVVVTASfgiepgrkveympilEEAMRIgQHKPDKVLiynrpnmetvplasgrdLDWDEEMAKAQSQDCVPVLSEH 184
Cdd:PRK10252 553 DARPSLLITTA---------------DQLPRF-ADVPDLTS-----------------LCYNAPLAPQGAAPLQLSQPHH 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 185 PLYILYTSGTTGLPKGVVrpTGGYAVM--LNWtMSSIYGLKPG----------------EVWWaasdlgwvvghsyicyg 246
Cdd:PRK10252 600 TAYIIFTSGSTGRPKGVM--VGQTAIVnrLLW-MQNHYPLTADdvvlqktpcsfdvsvwEFFW----------------- 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 247 PLIHGNTTVLyeGKPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQ-DPGAALGKQYSLTRfktLFVAGERCDVEtl 325
Cdd:PRK10252 660 PFIAGAKLVM--AEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASlTPEGARQSCASLRQ---VFCSGEALPAD-- 732
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 326 ewskkvfrvpVLDHWWQTeTGSPI------TASCIGLgnSKTPPPGQA-----GKSVP-GYNV-----MILDDNMQklka 388
Cdd:PRK10252 733 ----------LCREWQQL-TGAPLhnlygpTEAAVDV--SWYPAFGEElaavrGSSVPiGYPVwntglRILDARMR---- 795
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 389 rclgnivvklPLPPGAfSGlwknqeafkHLYF-----------------EKF------PG--YYDTMDAGYMDEEGYVYV 443
Cdd:PRK10252 796 ----------PVPPGV-AG---------DLYLtgiqlaqgylgrpdltaSRFiadpfaPGerMYRTGDVARWLDDGAVEY 855
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 444 MSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVV-----------GKEDPLKGHVPlALCVLRKDINITEGQVLEEIV 512
Cdd:PRK10252 856 LGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHacvinqaaatgGDARQLVGYLV-SQSGLPLDTSALQAQLRERLP 934
|
570 580 590
....*....|....*....|....*....|....*..
gi 1191882763 513 QHVRqsigPVAafrkavFVQ--QLPKTRSGKIPRAAL 547
Cdd:PRK10252 935 PHMV----PVV------LLQldQLPLSANGKLDRKAL 961
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
35-484 |
1.22e-18 |
|
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: 89.40 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 35 TITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVta 114
Cdd:cd17641 11 EFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVI-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 115 sfgIEPGRKVEymPILEEAMRIgqHKPDKVLI--------YNRPNMETVP--LASGRDLD------WDEEMAKAQSQDcV 178
Cdd:cd17641 89 ---AEDEEQVD--KLLEIADRI--PSVRYVIYcdprgmrkYDDPRLISFEdvVALGRALDrrdpglYEREVAAGKGED-V 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 179 PVLSehplyilYTSGTTGLPKGVVRPTGGYAvmlnwTMSSIY----GLKPGEVWWAASDLGWVVGHSYICYGPLIHGN-- 252
Cdd:cd17641 161 AVLC-------TTSGTTGKPKLAMLSHGNFL-----GHCAAYlaadPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFiv 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 253 ------TTVLYEGKPVG------TP---------------DAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGA------ 299
Cdd:cd17641 229 nfpeepETMMEDLREIGptfvllPPrvwegiaadvrarmmDATPFKRFMFELGMKLGLRALDRGKRGRPVSLWLrlaswl 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 300 -------ALGKQYSLTRFKTLFVAGERCDVETLewskKVFR---VPVLDHWWQTETGSPITASCIGlgnskTPPPGQAGK 369
Cdd:cd17641 309 adallfrPLRDRLGFSRLRSAATGGAALGPDTF----RFFHaigVPLKQLYGQTELAGAYTVHRDG-----DVDPDTVGV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 370 SVPGYNVMIldDNMqklkarclGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDD 449
Cdd:cd17641 380 PFPGTEVRI--DEV--------GEILVR---SPGVFVGYYKNPEATAEDFDED--GWLHTGDAGYFKENGHLVVIDRAKD 444
|
490 500 510
....*....|....*....|....*....|....*.
gi 1191882763 450 VINVA-GHRISAGAIEESLLSHGTVADCAVVGKEDP 484
Cdd:cd17641 445 VGTTSdGTRFSPQFIENKLKFSPYIAEAVVLGAGRP 480
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
183-549 |
1.95e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 88.12 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 183 EHPLYILYTSGTTGLPKGVVRPTGGYAVMLNwtmssiyGLkpGEVW-WAASDL-----------GWVVGhsyiCYGPLIH 250
Cdd:PRK07787 128 DAPALIVYTSGTTGPPKGVVLSRRAIAADLD-------AL--AEAWqWTADDVlvhglplfhvhGLVLG----VLGPLRI 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 251 GNTtVLYEGKPvgTPDAgaYFRVLAEHGvAALFTAPTAIRAIrQQDPGAAlgKQYSLTRfktLFVAGE----RCDVETLE 326
Cdd:PRK07787 195 GNR-FVHTGRP--TPEA--YAQALSEGG-TLYFGVPTVWSRI-AADPEAA--RALRGAR---LLVSGSaalpVPVFDRLA 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 327 wskKVFRVPVLDHWWQTETgsPITASCIGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKA--RCLGNIVVKlplPPGA 404
Cdd:PRK07787 263 ---ALTGHRPVERYGMTET--LITLSTRADGERR---PGWVGLPLAGVETRLVDEDGGPVPHdgETVGELQVR---GPTL 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 405 FSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVD-DVINVAGHRISAGAIEESLLSHGTVADCAVVGKED 483
Cdd:PRK07787 332 FDGYLNRPDATAAAFTAD--GWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPD 409
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191882763 484 PLKGHVPLALCVLRKDINitegqvLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAALSA 549
Cdd:PRK07787 410 DDLGQRIVAYVVGADDVA------ADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
37-549 |
2.09e-18 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 88.75 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 37 TYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPqAMY-TMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTAS 115
Cdd:PLN02479 47 TWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIP-AMYeAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 116 fgiepgrkvEYMPILEEAMRI------GQHKPDKVLIYNRPNMETVPL--ASGRDL--------DWDEEMAKAQSQDcvp 179
Cdd:PLN02479 126 ---------EFFTLAEEALKIlaekkkSSFKPPLLIVIGDPTCDPKSLqyALGKGAieyekfleTGDPEFAWKPPAD--- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 180 vlSEHPLYILYTSGTTGLPKGVV-RPTGGYAVMLNWTMssIYGLKPGEVWWaasdlgWVVghsyicygPLIHGN------ 252
Cdd:PLN02479 194 --EWQSIALGYTSGTTASPKGVVlHHRGAYLMALSNAL--IWGMNEGAVYL------WTL--------PMFHCNgwcftw 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 253 TTVLYEGKPV--GTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALgkqYSLTRFKTLFVAGERCDVETL-EWSK 329
Cdd:PLN02479 256 TLAALCGTNIclRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETI---LPLPRVVHVMTAGAAPPPSVLfAMSE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 330 KVFRVPvldHWWQ-TETGSPITASCIGLGNSKTPPPGQA------GKSVPGYNVMILDD--NMQKLKA--RCLGNIVVKl 398
Cdd:PLN02479 333 KGFRVT---HTYGlSETYGPSTVCAWKPEWDSLPPEEQArlnarqGVRYIGLEGLDVVDtkTMKPVPAdgKTMGEIVMR- 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 399 plPPGAFSGLWKNQEAFKhlyfEKFP-GYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCA 477
Cdd:PLN02479 409 --GNMVMKGYLKNPKANE----EAFAnGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEAS 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191882763 478 VVGKEDPLKGHVPLALCVLRKDINIT-EGQVLEEIVQHVRQSIgPVAAFRKAVFVQQLPKTRSGKIPRAALSA 549
Cdd:PLN02479 483 VVARPDERWGESPCAFVTLKPGVDKSdEAALAEDIMKFCRERL-PAYWVPKSVVFGPLPKTATGKIQKHVLRA 554
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
341-547 |
3.53e-18 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 87.77 E-value: 3.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 341 WQTETGSPITAsciGLGNSKTPP------------PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGL 408
Cdd:PRK07059 347 WLEMTGCPITE---GYGLSETSPvatcnpvdatefSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIR---GPQVMAGY 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 409 WKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGH 488
Cdd:PRK07059 421 WNRPDETAKVMTAD--GFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGE 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1191882763 489 VpLALCVLRKDINITEgqvlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:PRK07059 499 A-VKLFVVKKDPALTE----EDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
19-547 |
3.61e-18 |
|
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: 87.87 E-value: 3.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIIYDSPvTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 98
Cdd:cd05915 9 GRKEVVSRLH-TGEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 99 LSSRIDHAKPKVVVTASfgiepgrkvEYMPILEEAMRIgqhkpdkvliynRPNMETVPLASGRDLDWDEEMAKAQS--QD 176
Cdd:cd05915 88 IAYILNHAEDKVLLFDP---------NLLPLVEAIRGE------------LKTVQHFVVMDEKAPEGYLAYEEALGeeAD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 177 CVPVLSEHPLYILYTSGTTGLPKGVVRPTGGyaVMLNWTMSSIY---GLKPGEVWWAASDLGWVVGHSYICYGPLIHGNT 253
Cdd:cd05915 147 PVRVPERAACGMAYTTGTTGLPKGVVYSHRA--LVLHSLAASLVdgtALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 254 TVLYEgkpvgTPDAGAYFRVLAEHGVAALFTAPTAIRAIrqQDPGAALGKQYSLTrfkTLFVAGERCDVETLEWSKKVFR 333
Cdd:cd05915 225 VLPGP-----RLDPASLVELFDGEGVTFTAGVPTVWLAL--ADYLESTGHRLKTL---RRLVVGGSAAPRSLIARFERMG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 334 VPVLDHWWQTETGSPITAsCIGLGNSKTPPPGQAG--KSVPGYN-----VMILDDNMQKLKARclGNIVVKLPLPPGA-F 405
Cdd:cd05915 295 VEVRQGYGLTETSPVVVQ-NFVKSHLESLSEEEKLtlKAKTGLPiplvrLRVADEEGRPVPKD--GKALGEVQLKGPWiT 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 406 SGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPL 485
Cdd:cd05915 372 GGYYGNEEATRSALTPD--GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPK 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1191882763 486 KGHvplALCVLrkdINITEGQVL-EEIVQHVRQSIGPVAAFRKA-VFVQQLPKTRSGKIPRAAL 547
Cdd:cd05915 450 WQE---RPLAV---VVPRGEKPTpEELNEHLLKAGFAKWQLPDAyVFAEEIPRTSAGKFLKRAL 507
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
185-544 |
4.92e-18 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 85.79 E-value: 4.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 185 PLYILYTSGTTGLPKGVvrptggyavMLnwTMSSIY--GLKPGEVwwaasdLGWVVGHSYICYGPLIH------GNTTVL 256
Cdd:cd05917 4 VINIQFTSGTTGSPKGA---------TL--THHNIVnnGYFIGER------LGLTEQDRLCIPVPLFHcfgsvlGVLACL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 257 YEGKPVGTP----DAGAYFRVLAEHGVAALFTAPTA-IRAIRQQDPgaalgKQYSLTRFKTLFVAGERCDVETLEWSKKV 331
Cdd:cd05917 67 THGATMVFPspsfDPLAVLEAIEKEKCTALHGVPTMfIAELEHPDF-----DKFDLSSLRTGIMAGAPCPPELMKRVIEV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 332 FRVP-VLDHWWQTETgSPIT------------------------ASCIGLGNSKTPPPGQAGK-SVPGYNVMIlddnmqk 385
Cdd:cd05917 142 MNMKdVTIAYGMTET-SPVStqtrtddsiekrvntvgrimphteAKIVDPEGGIVPPVGVPGElCIRGYSVMK------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 386 lkarclgnivvklplppgafsGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 465
Cdd:cd05917 214 ---------------------GYWNDPEKTAEAIDGD--GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEE 270
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191882763 466 SLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEgqvlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPR 544
Cdd:cd05917 271 FLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTE----EDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
27-549 |
1.10e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 86.20 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 27 SPVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHA 106
Cdd:PRK13383 52 TAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 107 KPKVVVTASfgiepgrkveympilEEAMRIGQhKPDKVLIYnrpnmetvplasgrdldwDEEMAKAQSQDCVPVLSEHPL 186
Cdd:PRK13383 132 HISTVVADN---------------EFAERIAG-ADDAVAVI------------------DPATAGAEESGGRPAVAAPGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 187 YILYTSGTTGLPKGVVR-PTGGYAVMLNWTMSSIYGLKPGEVWWAASdlgwvvghsyicygPLIHGN-----TTVLYEGK 260
Cdd:PRK13383 178 IVLLTSGTTGKPKGVPRaPQLRSAVGVWVTILDRTRLRTGSRISVAM--------------PMFHGLglgmlMLTIALGG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 261 PVGTP---DAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPgaALGKQYSLTRFKTLFVAGERCDVETLEWSKKVFRVPVL 337
Cdd:PRK13383 244 TVLTHrhfDAEAALAQASLHRADAFTAVPVVLARILELPP--RVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 338 DHWWQTEtgspitascIGLGNSKTPP-----PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGlwKNQ 412
Cdd:PRK13383 322 NGYGSTE---------VGIGALATPAdlrdaPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTD--GGG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 413 EAFkhlyfekFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLA 492
Cdd:PRK13383 391 KAV-------VDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAA 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1191882763 493 LCVLRKDINITEGQVLEEIVQHVRQSIGPvaafRKAVFVQQLPKTRSGKIPRAALSA 549
Cdd:PRK13383 464 FVVLHPGSGVDAAQLRDYLKDRVSRFEQP----RDINIVSSIPRNPTGKVLRKELPG 516
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
1-547 |
1.55e-17 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 85.70 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 1 MLNMCYNAIDRHIESGkgDKVAIIydspvTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLAC 80
Cdd:PRK07514 1 MNNNLFDALRAAFADR--DAPFIE-----TPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLAT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 81 ARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTAsfgiePGRKVEYMPILEEAmrigqhkpdkvliyNRPNMETVPLASG 160
Cdd:PRK07514 74 LRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCD-----PANFAWLSKIAAAA--------------GAPHVETLDADGT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 161 RDLdwdEEMAKAQSQD--CVPVLSEHPLYILYTSGTTGLPKGvvrptggyAVMLNWTMSS-------IYGLKPGEVwwaa 231
Cdd:PRK07514 135 GSL---LEAAAAAPDDfeTVPRGADDLAAILYTSGTTGRSKG--------AMLSHGNLLSnaltlvdYWRFTPDDV---- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 232 sdlgwvvghsyicygpLIH-------------GNTTVLYEGKPVGTP--DAGAYFRVLAE----HGVAALFTaptaiRAI 292
Cdd:PRK07514 200 ----------------LIHalpifhthglfvaTNVALLAGASMIFLPkfDPDAVLALMPRatvmMGVPTFYT-----RLL 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 293 rqQDPGaaLGKQysLTRFKTLFVAGER-CDVETL-EWSKKVFRvPVLDHWWQTETGSpitasciglgNSKTP-----PPG 365
Cdd:PRK07514 259 --QEPR--LTRE--AAAHMRLFISGSApLLAETHrEFQERTGH-AILERYGMTETNM----------NTSNPydgerRAG 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 366 QAGKSVPGYNVMILD-DNMQKLKARCLGNIVVKlplPPGAFSGLW----KNQEAFKHlyfekfPGYYDTMDAGYMDEEGY 440
Cdd:PRK07514 322 TVGFPLPGVSLRVTDpETGAELPPGEIGMIEVK---GPNVFKGYWrmpeKTAEEFRA------DGFFITGDLGKIDERGY 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 441 VYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEGQVLEEIVqhvrqsiG 520
Cdd:PRK07514 393 VHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAILAALK-------G 465
|
570 580 590
....*....|....*....|....*....|
gi 1191882763 521 PVAAF---RKAVFVQQLPKTRSGKIPRAAL 547
Cdd:PRK07514 466 RLARFkqpKRVFFVDELPRNTMGKVQKNLL 495
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
8-548 |
2.13e-17 |
|
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: 84.67 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 8 AIDRHIESGKgDKVAiiydspVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIH 87
Cdd:cd17653 2 AFERIAAAHP-DAVA------VESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 88 SLIFGGFASkelsSRIDHakpkvvvtasfgiepgrkveympILEEAmrigqhkpDKVLIynrpnmetVPLASGRDLdwde 167
Cdd:cd17653 75 VPLDAKLPS----ARIQA-----------------------ILRTS--------GATLL--------LTTDSPDDL---- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 168 emakaqsqdcvpvlsehpLYILYTSGTTGLPKGVVRPTGGYAVMLnWTMSSIYGLKPG----EVWWAASDLG-WVVghsy 242
Cdd:cd17653 108 ------------------AYIIFTSGSTGIPKGVMVPHRGVLNYV-SQPPARLDVGPGsrvaQVLSIAFDACiGEI---- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 243 icYGPLIHGNTTVLyegkpvgtPDAGAYFRVLAEHgVAALFTAPTAIRAIRQQDpgaalgkqysLTRFKTLFVAGERCdv 322
Cdd:cd17653 165 --FSTLCNGGTLVL--------ADPSDPFAHVART-VDALMSTPSILSTLSPQD----------FPNLKTIFLGGEAV-- 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 323 etlewSKkvfrvPVLDHWWQ----------TETgspitaSCIGLGNSKTppPGQA---GKSVPGYNVMILDDNMQKLKAR 389
Cdd:cd17653 222 -----PP-----SLLDRWSPgrrlynaygpTEC------TISSTMTELL--PGQPvtiGKPIPNSTCYILDADLQPVPEG 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 390 CLGNIVVklpLPPGAFSGLWKNQEA----FKHLYFEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 465
Cdd:cd17653 284 VVGEICI---SGVQVARGYLGNPALtaskFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEE 360
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 466 S-LLSHGTVADCAVVGKEDPLKGHV-PLALCVLRkdinitegqVLEEIVQHVRQSIGPvaafRKAVFVQQLPKTRSGKIP 543
Cdd:cd17653 361 VvLQSQPEVTQAAAIVVNGRLVAFVtPETVDVDG---------LRSELAKHLPSYAVP----DRIIALDSFPLTANGKVD 427
|
....*
gi 1191882763 544 RAALS 548
Cdd:cd17653 428 RKALR 432
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
19-549 |
4.40e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 85.78 E-value: 4.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIIYDspvtdtKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHslifggfaske 98
Cdd:PRK12316 2018 EAIAVVFG------DQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAY----------- 2080
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 99 lssridhakpkVVVTASFgiePGRKVEYMpiLEEAmRIGqhkpdkVLIYNRPNMETVPLASG---RDLDWDEEMAKAQSQ 175
Cdd:PRK12316 2081 -----------VPLDPNY---PAERLAYM--LEDS-GAA------LLLTQRHLLERLPLPAGvarLPLDRDAEWADYPDT 2137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 176 DCVPVLSEHPL-YILYTSGTTGLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVVGHSYiCYGPLIHGNTT 254
Cdd:PRK12316 2138 APAVQLAGENLaYVIYTSGSTGLPKGVAVSHGALVAHCQA-AGERYELSPADCELQFMSFSFDGAHEQ-WFHPLLNGARV 2215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 255 VLyegKPVGTPDAGAYFRVLAEHGVAALFTAPT-----AIRAIRQQDPGAAlgkqysltrfKTLFVAGERCDVETLE-WS 328
Cdd:PRK12316 2216 LI---RDDELWDPEQLYDEMERHGVTILDFPPVylqqlAEHAERDGRPPAV----------RVYCFGGEAVPAASLRlAW 2282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 329 KKVFRVPVLDHWWQTETG-SPITASC--IGLGNSKTPPPGQAGKSVPGYnvmILDDNMQklkarclgnivvklPLPPGAF 405
Cdd:PRK12316 2283 EALRPVYLFNGYGPTEAVvTPLLWKCrpQDPCGAAYVPIGRALGNRRAY---ILDADLN--------------LLAPGMA 2345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 406 SGLWKNQEAFKHLYFEKfPG-----------------YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLL 468
Cdd:PRK12316 2346 GELYLGGEGLARGYLNR-PGltaerfvpdpfsasgerLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQ 2424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 469 SHGTVADCAVVGKEDPlkGHVPLALCVLRKDInitEGQVLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAALS 548
Cdd:PRK12316 2425 AHPAVREAVVVAQDGA--SGKQLVAYVVPDDA---AEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALP 2499
|
.
gi 1191882763 549 A 549
Cdd:PRK12316 2500 K 2500
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
7-213 |
5.36e-17 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 84.16 E-value: 5.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 7 NAIDRHiesgkGDKVAIIYDSpvtdtkATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAI 86
Cdd:PRK08279 45 EAAARH-----PDRPALLFED------QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 87 HSLIFGGFASKELSSRIDHAKPKVVVTASfgiepgrkvEYMPILEEAMriGQHKPDKVLIYNRPNMETVPLASgRDLDwd 166
Cdd:PRK08279 114 VALLNTQQRGAVLAHSLNLVDAKHLIVGE---------ELVEAFEEAR--ADLARPPRLWVAGGDTLDDPEGY-EDLA-- 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1191882763 167 eEMAKAQSQDCVP----VLSEHPLYILYTSGTTGLPKGVV-------RPTGGYAVMLN 213
Cdd:PRK08279 180 -AAAAGAPTTNPAsrsgVTAKDTAFYIYTSGTTGLPKAAVmshmrwlKAMGGFGGLLR 236
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
19-547 |
8.61e-17 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 83.09 E-value: 8.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIIYDSPvtdtkaTITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHslifggfaske 98
Cdd:cd12114 2 DATAVICGDG------TLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAY----------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 99 lssridhakpkvvVTASFGIEPGRKVEympILEEAMR---IGQHKPDKVLIynRPNMETVPLASGRDLDWDEEMAKAQSQ 175
Cdd:cd12114 65 -------------VPVDIDQPAARREA---ILADAGArlvLTDGPDAQLDV--AVFDVLILDLDALAAPAPPPPVDVAPD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 176 DcvpvlsehPLYILYTSGTTGLPKGVVRPTGGyavMLNwTMSSI---YGLKPGEVWWAASDLGW---VvghsYICYGPLI 249
Cdd:cd12114 127 D--------LAYVIFTSGSTGTPKGVMISHRA---ALN-TILDInrrFAVGPDDRVLALSSLSFdlsV----YDIFGALS 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 250 HGNTTVLYEGKPVGTPDAGAyfRVLAEHGV--------------AALFTAPTAIRAIRQQ---------DPGAALGKQYS 306
Cdd:cd12114 191 AGATLVLPDEARRRDPAHWA--ELIERHGVtlwnsvpallemllDVLEAAQALLPSLRLVllsgdwiplDLPARLRALAP 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 307 LTRFKTLFVAgercdVETLEWSKkVFRV-PVLDHWWQTETGSPItasciglgnsktppPGQAgksvpgYNVMildDNMQK 385
Cdd:cd12114 269 DARLISLGGA-----TEASIWSI-YHPIdEVPPDWRSIPYGRPL--------------ANQR------YRVL---DPRGR 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 386 lkarclgnivvklPLPP-----------GAFSGLWKNQEAFKHLYFEKFPG--YYDTMDAGYMDEEGYVYVMSRVDDVIN 452
Cdd:cd12114 320 -------------DCPDwvpgelwiggrGVALGYLGDPELTAARFVTHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVK 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 453 VAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEGQVLEEIVQHVRQSIGPvaafRKAVFVQ 532
Cdd:cd12114 387 VRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTPIAPDALRAFLAQTLPAYMIP----SRVIALE 462
|
570
....*....|....*
gi 1191882763 533 QLPKTRSGKIPRAAL 547
Cdd:cd12114 463 ALPLTANGKVDRAAL 477
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
36-549 |
8.78e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 84.62 E-value: 8.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 36 ITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTas 115
Cdd:PRK12316 3083 LSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLS-- 3160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 116 fgiepgrkveympilEEAMRIGQHKPDKVLiynrpnmetvplasgrDLDWDEEMAKAQSQDcVPVLSEHPLYILYTSGTT 195
Cdd:PRK12316 3161 ---------------QSHLRLPLAQGVQVL----------------DLDRGDENYAEANPA-IRTMPENLAYVIYTSGST 3208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 196 GLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVVGHSYIcYGPLIHGNTTVLyeGKPVGTPDAGAYFRVLA 275
Cdd:PRK12316 3209 GKPKGVGIRHSALSNHLCW-MQQAYGLGVGDRVLQFTTFSFDVFVEEL-FWPLMSGARVVL--AGPEDWRDPALLVELIN 3284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 276 EHGVAALFTAPTAIRAIrQQDPGAAlgkqySLTRFKTLFVAGERCDVETLEwsKKVFRVPVLDHWWQTETGSPITASCIG 355
Cdd:PRK12316 3285 SEGVDVLHAYPSMLQAF-LEEEDAH-----RCTSLKRIVCGGEALPADLQQ--QVFAGLPLYNLYGPTEATITVTHWQCV 3356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 356 LGNSKTPPpgqAGKSVPGYNVMILDDNMQKLKARCLGNIVVK-LPLPPGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAGY 434
Cdd:PRK12316 3357 EEGKDAVP---IGRPIANRACYILDGSLEPVPVGALGELYLGgEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLAR 3433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 435 MDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKE-DPLKGHVPLalcvlrkdiNITEGQVLEEIVQ 513
Cdd:PRK12316 3434 YRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDgRQLVAYVVP---------EDEAGDLREALKA 3504
|
490 500 510
....*....|....*....|....*....|....*.
gi 1191882763 514 HVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAALSA 549
Cdd:PRK12316 3505 HLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPR 3540
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
35-553 |
1.20e-16 |
|
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: 83.10 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 35 TITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAK------- 107
Cdd:cd05906 39 FQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPNARLRKLRhiwqllg 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 108 -PKVVVTasfgiePGRKVEYMPILEEAmrigQHKPDKVLIynrpnMETVpLASGRDLDWdeemakaqsqdcVPVLSEHPL 186
Cdd:cd05906 119 sPVVLTD------AELVAEFAGLETLS----GLPGIRVLS-----IEEL-LDTAADHDL------------PQSRPDDLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 187 YILYTSGTTGLPKGVVRPTGGYAVMLNWTMSsIYGLKPGEVWwaasdLGWVvghsyicygPLIHGNTTVLYEGKPVgtpD 266
Cdd:cd05906 171 LLMLTSGSTGFPKAVPLTHRNILARSAGKIQ-HNGLTPQDVF-----LNWV---------PLDHVGGLVELHLRAV---Y 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 267 AGA----------------YFRVLAEHGVAALFtAPT-AIRAIRQQDPGAAlGKQYSLTRFKTLFVAGERCDVET----L 325
Cdd:cd05906 233 LGCqqvhvpteeiladplrWLDLIDRYRVTITW-APNfAFALLNDLLEEIE-DGTWDLSSLRYLVNAGEAVVAKTirrlL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 326 EWSKK------VFRvPVldhWWQTETGSPIT--ASCIGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVK 397
Cdd:cd05906 311 RLLEPyglppdAIR-PA---FGMTETCSGVIysRSFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVR 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 398 LPLppgAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEeGYVYVMSRVDDVINVAGHRISAGAIEESL-----LSHGT 472
Cdd:cd05906 387 GPV---VTKGYYNNPEANAEAFTED--GWFRTGDLGFLDN-GNLTITGRTKDTIIVNGVNYYSHEIEAAVeevpgVEPSF 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 473 VADCAVvgkEDPLKGHVPLALC-VLRKDINITEGQVLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL-SAL 550
Cdd:cd05906 461 TAAFAV---RDPGAETEELAIFfVPEYDLQDALSETLRAIRSVVSREVGVSPAYLIPLPKEEIPKTSLGKIQRSKLkAAF 537
|
...
gi 1191882763 551 VNG 553
Cdd:cd05906 538 EAG 540
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
98-549 |
1.21e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 82.81 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 98 ELSSRIDHAKPKVVVTASfgiepgrkvEYMPILEEAmrigqhkpdkvliynRPNMETVPLASgrdLDWDEEMAKAQSQDC 177
Cdd:PRK07867 92 ALARDIAHADCQLVLTES---------AHAELLDGL---------------DPGVRVINVDS---PAWADELAAHRDAEP 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 178 VP--VLSEHPLYILYTSGTTGLPKGVvRPTGGYAVMLNWTMSSIYGLKPGEVwwaasdlgwvvghSYICYgPLIHGNTTV 255
Cdd:PRK07867 145 PFrvADPDDLFMLIFTSGTSGDPKAV-RCTHRKVASAGVMLAQRFGLGPDDV-------------CYVSM-PLFHSNAVM 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 256 lyegkpvgtpdaGAYFRVLAEHGVAAL---FTAPTAIRAIRQQdpGAA----LGK--QYSLT-------RFKTLFVA--- 316
Cdd:PRK07867 210 ------------AGWAVALAAGASIALrrkFSASGFLPDVRRY--GATyanyVGKplSYVLAtperpddADNPLRIVygn 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 317 -GERCDVETLEwskKVFRVPVLDHWWQTETGSPITasciglgnsKTP--PPGQAGKSVPGYNVM-----------ILDDN 382
Cdd:PRK07867 276 eGAPGDIARFA---RRFGCVVVDGFGSTEGGVAIT---------RTPdtPPGALGPLPPGVAIVdpdtgtecppaEDADG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 383 MQKLKARCLGNIVVklPLPPGAFSGLWKNQEAFKhlyfEKF-PGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAG 461
Cdd:PRK07867 344 RLLNADEAIGELVN--TAGPGGFEGYYNDPEADA----ERMrGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTA 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 462 AIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEGQVLEEIvqHVRQSIGPVAAFRKAVFVQQLPKTRSGK 541
Cdd:PRK07867 418 PIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFL--AAQPDLGPKQWPSYVRVCAELPRTATFK 495
|
....*...
gi 1191882763 542 IPRAALSA 549
Cdd:PRK07867 496 VLKRQLSA 503
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
182-541 |
1.31e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 81.66 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 182 SEHPLYILYTSGTTGLPKGVVRPTGGYAVML---------NWTMSSIYGLK----PGEVWWAASdlgwvvghsyicygPL 248
Cdd:cd05924 2 SADDLYILYTGGTTGMPKGVMWRQEDIFRMLmggadfgtgEFTPSEDAHKAaaaaAGTVMFPAP--------------PL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 249 IHGNTTVLYEGKPVGTP---------DAGAYFRVLAEHGVAALFTAPTA-----IRAIRqqDPGAalgkqYSLTRFKTLF 314
Cdd:cd05924 68 MHGTGSWTAFGGLLGGQtvvlpddrfDPEEVWRTIEKHKVTSMTIVGDAmarplIDALR--DAGP-----YDLSSLFAIS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 315 VAGercdvetLEWSKKVfRVPVLDHWWQ---------TETGSpitascIGLGNSKTPPPGQAGKSVPGYNVMILDDNMQK 385
Cdd:cd05924 141 SGG-------ALLSPEV-KQGLLELVPNitlvdafgsSETGF------TGSGHSAGSGPETGPFTRANPDTVVLDDDGRV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 386 LK--ARCLGNIVVKLPLPPGAFSGLWKNQEAFKHLYFEK--FPGYYDTMDAGymdeeGYVYVMSRVDDVINVAGHRISAG 461
Cdd:cd05924 207 VPpgSGGVGWIARRGHIPLGYYGDEAKTAETFPEVDGVRyaVPGDRATVEAD-----GTVTLLGRGSVCINTGGEKVFPE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 462 AIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEgqvlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGK 541
Cdd:cd05924 282 EVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREGAGVDL----EELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
162-549 |
2.13e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 82.38 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 162 DLDWDEEMAKAQsqDCVP---VLSEHPLYILYTSGTTGLPKGVvRPTGGYAVMLNWTMSSIYGLKPGEVwwaasdlgwvv 238
Cdd:PRK13388 128 TPAYAELVAAAG--ALTPhreVDAMDPFMLIFTSGTTGAPKAV-RCSHGRLAFAGRALTERFGLTRDDV----------- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 239 ghSYICYgPLIHGNTTV------LYEGKPVGTPDAGAYFRVLA---EHGvAALFT----APTAIRAIRQQDPGAalgkQY 305
Cdd:PRK13388 194 --CYVSM-PLFHSNAVMagwapaVASGAAVALPAKFSASGFLDdvrRYG-ATYFNyvgkPLAYILATPERPDDA----DN 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 306 SLTR-FKTlfVAGERcDVEtlEWSKKvFRVPVLDHWWQTETGSPITASciglgnsKTPPPGQAGKSVPGynVMILDDNMQ 384
Cdd:PRK13388 266 PLRVaFGN--EASPR-DIA--EFSRR-FGCQVEDGYGSSEGAVIVVRE-------PGTPPGSIGRGAPG--VAIYNPETL 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 385 KLKARC--------------LGNIVVKLPlpPGAFSGLWKNQEA----FKHlyfekfpGYYDTMDAGYMDEEGYVYVMSR 446
Cdd:PRK13388 331 TECAVArfdahgallnadeaIGELVNTAG--AGFFEGYYNNPEAtaerMRH-------GMYWSGDLAYRDADGWIYFAGR 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 447 VDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEGQvLEEIVqHVRQSIGPVAAFR 526
Cdd:PRK13388 402 TADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDA-FAAFL-AAQPDLGTKAWPR 479
|
410 420
....*....|....*....|...
gi 1191882763 527 KAVFVQQLPKTRSGKIPRAALSA 549
Cdd:PRK13388 480 YVRIAADLPSTATNKVLKRELIA 502
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
37-517 |
2.23e-16 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 82.13 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 37 TYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTAsf 116
Cdd:cd05932 8 TWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVG-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 117 giepgrKVEYMPileeAMRIGQhkPDKVLIYNRPnmetvPLASGRDLD-WDEEMAKAQ-SQDCVPVLSEHPLYILYTSGT 194
Cdd:cd05932 86 ------KLDDWK----AMAPGV--PEGLISISLP-----PPSAANCQYqWDDLIAQHPpLEERPTRFPEQLATLIYTSGT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 195 TGLPKGVVRPTGGYAvmlnWTMSSI---YGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLYE-----------GK 260
Cdd:cd05932 149 TGQPKGVMLTFGSFA----WAAQAGiehIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAEsldtfvedvqrAR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 261 P---VGTPDAGAYF--RVLAEHGVAA---LFTAPTAIRAIRQQdpgaaLGKQYSLTRFKTLFVAGERCDVETLEWSKKVf 332
Cdd:cd05932 225 PtlfFSVPRLWTKFqqGVQDKIPQQKlnlLLKIPVVNSLVKRK-----VLKGLGLDQCRLAGCGSAPVPPALLEWYRSL- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 333 RVPVLDHWWQTETG--SPITASciglGNSKTpppGQAGKSVPGYNVMILDDnmqklkarclGNIVVKlplPPGAFSGLWK 410
Cdd:cd05932 299 GLNILEAYGMTENFaySHLNYP----GRDKI---GTVGNAGPGVEVRISED----------GEILVR---SPALMMGYYK 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 411 NQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVA-GHRISAGAIEESLLSHGTVADCAVVGKEDPlkghV 489
Cdd:cd05932 359 DPEATAEAFTAD--GFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSGLP----A 432
|
490 500 510
....*....|....*....|....*....|...
gi 1191882763 490 PLALCVL-----RKDINITEGQVLEEIVQHVRQ 517
Cdd:cd05932 433 PLALVVLseearLRADAFARAELEASLRAHLAR 465
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
365-547 |
2.67e-16 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 82.02 E-value: 2.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 365 GQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYVYVM 444
Cdd:PRK08974 378 GSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVK---GPQVMLGYWQRPEATDEVIKD---GWLATGDIAVMDEEGFLRIV 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 445 SRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVpLALCVLRKDINITEgqvlEEIVQHVRQSIGPVAA 524
Cdd:PRK08974 452 DRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEA-VKIFVVKKDPSLTE----EELITHCRRHLTGYKV 526
|
170 180
....*....|....*....|...
gi 1191882763 525 FRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:PRK08974 527 PKLVEFRDELPKSNVGKILRREL 549
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
29-547 |
3.88e-16 |
|
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: 80.97 E-value: 3.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 29 VTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKP 108
Cdd:cd17650 6 VSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 109 KVVVTasfgiEPgrkveympileeamrigqhkpdkvliynrpnmetvplasgrdldwdeemakaqsqdcvpvlsEHPLYI 188
Cdd:cd17650 86 KLLLT-----QP--------------------------------------------------------------EDLAYV 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 189 LYTSGTTGLPKGVVRPTGGYAVM-LNWtmSSIYGL--KPGEVWWAASdLGWVVGHSYICYGpLIHGNTTVLYegkPVGTP 265
Cdd:cd17650 99 IYTSGTTGKPKGVMVEHRNVAHAaHAW--RREYELdsFPVRLLQMAS-FSFDVFAGDFARS-LLNGGTLVIC---PDEVK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 266 -DAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpgaALGKQYSLTRFKTLFVAGERCDVETLEWSKKVF--RVPVLDHWWQ 342
Cdd:cd17650 172 lDPAALYDLILKSRITLMESTPALIRPVMAY----VYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFgqGMRIINSYGV 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 343 TET---GSPITASCIGLGNSKTPPpgqAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGLW---------- 409
Cdd:cd17650 248 TEAtidSTYYEEGRDPLGDSANVP---IGRPLPNTAMYVLDERLQ--------------PQPVGVAGELYiggagvargy 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 410 -----KNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDP 484
Cdd:cd17650 311 lnrpeLTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDK 390
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191882763 485 lKGHVPL-ALCVLRKDINITEgqVLEEIVQHVRQSIGPvaafrkAVFVQ--QLPKTRSGKIPRAAL 547
Cdd:cd17650 391 -GGEARLcAYVVAAATLNTAE--LRAFLAKELPSYMIP------SYYVQldALPLTPNGKVDRRAL 447
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
188-542 |
4.55e-16 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 79.47 E-value: 4.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 188 ILYTSGTTGLPKGVV---RPTggyavmlnwtmssiygLKPGEVWwaaSDLGWVV-GHSYICYGPLIH------GNTTVLY 257
Cdd:cd17638 5 IMFTSGTTGRSKGVMcahRQT----------------LRAAAAW---ADCADLTeDDRYLIINPFFHtfgykaGIVACLL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 258 EGK---PVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdPGAalgKQYSLTRFKTLFVAGERCDVETLEWSKKVFRV 334
Cdd:cd17638 66 TGAtvvPVAVFDVDAILEAIERERITVLPGPPTLFQSLLDH-PGR---KKFDLSSLRAAVTGAATVPVELVRRMRSELGF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 335 -PVLDHWWQTETGspiTASCIGLGNSKTPPPGQAGKSVPGYNVMILDDnmqklkarclGNIVVKlplPPGAFSGLWKNQE 413
Cdd:cd17638 142 eTVLTAYGLTEAG---VATMCRPGDDAETVATTCGRACPGFEVRIADD----------GEVLVR---GYNVMQGYLDDPE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 414 AFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLAL 493
Cdd:cd17638 206 ATAEAIDAD--GWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAF 283
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1191882763 494 CVLRKDINITEgqvlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKI 542
Cdd:cd17638 284 VVARPGVTLTE----EDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
329-547 |
4.96e-16 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 81.08 E-value: 4.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 329 KKVFRVPVLDHWWQTETgSPitASCIglgNSKTPPP--GQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFS 406
Cdd:PRK08751 350 KQVTGLTLVEAYGLTET-SP--AACI---NPLTLKEynGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIK---GPQVMK 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 407 GLWKNQEAFKHLYfeKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLK 486
Cdd:PRK08751 421 GYWKRPEETAKVM--DADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKS 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191882763 487 GHVpLALCVLRKDINITEgqvlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:PRK08751 499 GEI-VKVVIVKKDPALTA----EDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
341-547 |
1.33e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 79.81 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 341 WQTETGSPItasCIGLGNSKTPP-----------PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLW 409
Cdd:PRK05677 346 WKEVTGCAI---CEGYGMTETSPvvsvnpsqaiqVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVK---GPQVMKGYW 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 410 KNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHV 489
Cdd:PRK05677 420 QRPEATDEILDSD--GWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEA 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1191882763 490 PLALCVLRKDINITEGQVLEeivqHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:PRK05677 498 IKVFVVVKPGETLTKEQVME----HMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
187-548 |
1.56e-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: 75.90 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 187 YILYTSGTTGLPKGVVRPTGGyAVMLNWTMSSIYGLKPGEVWWAASDLGWVVGHSY--ICYGpLIHGNTTVLYEGKPVGT 264
Cdd:cd17648 98 YAIYTSGTTGKPKGVLVEHGS-VVNLRTSLSERYFGRDNGDEAVLFFSNYVFDFFVeqMTLA-LLNGQKLVVPPDEMRFD 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 265 PDagAYFRVLAEHGVAALFTAPTAIRAIRqqdpgaaLGKQYSLTRfktLFVAGERCDVETLEWSKKVFRVPVLDHWWQTE 344
Cdd:cd17648 176 PD--RFYAYINREKVTYLSGTPSVLQQYD-------LARLPHLKR---VDAAGEEFTAPVFEKLRSRFAGLIINAYGPTE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 345 TGspITasciglgNSKTPPPGQA------GKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGL---------- 408
Cdd:cd17648 244 TT--VT-------NHKRFFPGDQrfdkslGRPVRNTKCYVLNDAMK--------------RVPVGAVGELylggdgvarg 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 409 WKNQEAfkhLYFEKF----------------PGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGT 472
Cdd:cd17648 301 YLNRPE---LTAERFlpnpfqteqerargrnARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPG 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 473 VADCAVVGKEDPLKGHVPlalcvLRKDI---NITEGQVLEE--IVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:cd17648 378 VRECAVVAKEDASQAQSR-----IQKYLvgyYLPEPGHVPEsdLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
.
gi 1191882763 548 S 548
Cdd:cd17648 453 P 453
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
143-547 |
3.30e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 76.35 E-value: 3.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 143 KVLIYNRPNMETVPLASGR---DLDWDEEMAKAQSQDCVPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWtMSSI 219
Cdd:PRK12467 3194 KLLLTQAHLLEQLPAPAGDtalTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCW-IAEA 3272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 220 YGLKPGEVWWAASDLGWVVGHSYIcYGPLIHGNTTVLYEGKpVGTPDagAYFRVLAEHGVAALFTAPTAIRAIrqqdpgA 299
Cdd:PRK12467 3273 YELDANDRVLLFMSFSFDGAQERF-LWTLICGGCLVVRDND-LWDPE--ELWQAIHAHRISIACFPPAYLQQF------A 3342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 300 ALGKQYSLTRFKTLFVAGERCDVETLEWSKKVF-RVPVLDHWWQTETGSPITASCIGLGNSKTPPPGQAGKSVPGYNVMI 378
Cdd:PRK12467 3343 EDAGGADCASLDIYVFGGEAVPPAAFEQVKRKLkPRGLTNGYGPTEAVVTVTLWKCGGDAVCEAPYAPIGRPVAGRSIYV 3422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 379 LDDNMQklkarclgnivvklPLPPGAFSGLWKNQEAFKHLYFEK------------FPG----YYDTMDAGYMDEEGYVY 442
Cdd:PRK12467 3423 LDGQLN--------------PVPVGVAGELYIGGVGLARGYHQRpsltaerfvadpFSGsggrLYRTGDLARYRADGVIE 3488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 443 VMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKeDPLKGHVPLALCVLrkdiNITEGQVLEEIVQHVRQSIGPV 522
Cdd:PRK12467 3489 YLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVP----ADPQGDWRETLRDHLAASLPDY 3563
|
410 420
....*....|....*....|....*
gi 1191882763 523 AAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:PRK12467 3564 MVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
424-550 |
6.85e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 73.16 E-value: 6.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 424 PGYYDTMDAGYMDEeGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVlrkdINIT 503
Cdd:PRK07824 233 PGWFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVV----GDGG 307
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1191882763 504 EGQVLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAALSAL 550
Cdd:PRK07824 308 PAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRR 354
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
19-519 |
9.00e-14 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 74.16 E-value: 9.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIIY----DSPVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIympMIPQA--MYT-MLACARIGAIHSLIF 91
Cdd:PRK09274 21 DQLAVAVpggrGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVL---MVTPSleFFAlTFALFKAGAVPVLVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 92 GGFASKELSSRIDHAKPKVVVtasfGIepgrkveymPILEEAMRI-GQHKPD-KVLIynrpNMETVPLASGRDLDWDEEM 169
Cdd:PRK09274 98 PGMGIKNLKQCLAEAQPDAFI----GI---------PKAHLARRLfGWGKPSvRRLV----TVGGRLLWGGTTLATLLRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 170 AKAQSQDCVPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNwTMSSIYGLKPGEVwwaasDLgwvvgHSYicygPLI 249
Cdd:PRK09274 161 GAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIE-ALREDYGIEPGEI-----DL-----PTF----PLF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 250 H------GNTTVLYE---GKPvGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQqdpgAALGKQYSLTRFKTLFVAGERC 320
Cdd:PRK09274 226 AlfgpalGMTSVIPDmdpTRP-ATVDPAKLFAAIERYGVTNLFGSPALLERLGR----YGEANGIKLPSLRRVISAGAPV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 321 DVETLEWSKKVFR--VPVL---------------------DHWWQTETGSPItasCIglgnsktpppgqaGKSVPGYNVM 377
Cdd:PRK09274 301 PIAVIERFRAMLPpdAEILtpygatealpissiesreilfATRAATDNGAGI---CV-------------GRPVDGVEVR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 378 ILD---------DNMQKLKARCLGNIVVKLPL-------PPGA--FSGLWKNQEAFKHlyfekfpgyyDTMDAGYMDEEG 439
Cdd:PRK09274 365 IIAisdapipewDDALRLATGEIGEIVVAGPMvtrsyynRPEAtrLAKIPDGQGDVWH----------RMGDLGYLDAQG 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 440 YVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKedPLKGHVPLALCV-LRKDINITEGQVLEEIVQHVRQS 518
Cdd:PRK09274 435 RLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGV--GVPGAQRPVLCVeLEPGVACSKSALYQELRALAAAH 512
|
.
gi 1191882763 519 I 519
Cdd:PRK09274 513 P 513
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
183-547 |
1.42e-13 |
|
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: 73.24 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 183 EHPLYILYTSGTTGLPKGVVrPTGGYAVMLNWTMSSIYGL-KPGEVWWAASdLGWVVGHSYIcYGPLIHGNTTVLYEGKP 261
Cdd:cd17644 106 ENLAYVIYTSGSTGKPKGVM-IEHQSLVNLSHGLIKEYGItSSDRVLQFAS-IAFDVAAEEI-YVTLLSGATLVLRPEEM 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 262 VGTPDA----------------GAYFRVLAEHGVAALFTAPTAIRAIrqqdpgaalgkqysltrfktlFVAGERCDVETL 325
Cdd:cd17644 183 RSSLEDfvqyiqqwqltvlslpPAYWHLLVLELLLSTIDLPSSLRLV---------------------IVGGEAVQPELV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 326 E-WSKKVF-RVPVLDHWWQTEtgSPITASC-----IGLGNSKTPPpgqAGKSVPGYNVMILDDNMQKLKARCLGNIVV-K 397
Cdd:cd17644 242 RqWQKNVGnFIQLINVYGPTE--ATIAATVcrltqLTERNITSVP---IGRPIANTQVYILDENLQPVPVGVPGELHIgG 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 398 LPLPPGAFSGLWKNQEAFKHLYFEKFPG--YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVAD 475
Cdd:cd17644 317 VGLARGYLNRPELTAEKFISHPFNSSESerLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKT 396
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191882763 476 CAVVGKEDPLKGHVPLALCVLRKDINITegqvLEEIVQHVRQSIgPV----AAFrkaVFVQQLPKTRSGKIPRAAL 547
Cdd:cd17644 397 AVVIVREDQPGNKRLVAYIVPHYEESPS----TVELRQFLKAKL-PDymipSAF---VVLEELPLTPNGKIDRRAL 464
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
28-547 |
1.48e-13 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 73.25 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 28 PVTDTkatiTYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAI-HSLIFGGFAsKELSSRIDHA 106
Cdd:PRK06018 36 PIVRT----TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAIcHTVNPRLFP-EQIAWIINHA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 107 KPKVVVTasfgiepgrKVEYMPILEeamRIGQHKP--DKVLIYNrpNMETVPLASGRDLDWDEEMAKAQSQDCV-PVLSE 183
Cdd:PRK06018 111 EDRVVIT---------DLTFVPILE---KIADKLPsvERYVVLT--DAAHMPQTTLKNAVAYEEWIAEADGDFAwKTFDE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 184 HPLYIL-YTSGTTGLPKGVV---RPTGGYAVMLNwtMSSIYGLKpgevwwAASDLGWVVghsyicygPLIHGNT-TVLYE 258
Cdd:PRK06018 177 NTAAGMcYTSGTTGDPKGVLyshRSNVLHALMAN--NGDALGTS------AADTMLPVV--------PLFHANSwGIAFS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 259 GKPVGTP--------DAGAYFRVLAEHGVAalFTA--PTAIRAIRQQDPGAALgkqySLTRFKTLFVAGERCDVETLews 328
Cdd:PRK06018 241 APSMGTKlvmpgaklDGASVYELLDTEKVT--FTAgvPTVWLMLLQYMEKEGL----KLPHLKMVVCGGSAMPRSMI--- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 329 kKVFR---VPVLDHWWQTETgSPI-TASCIGLGNSKTPPPGQ------AGKSVPGYNVMILDDNMQKL--KARCLGNIVV 396
Cdd:PRK06018 312 -KAFEdmgVEVRHAWGMTEM-SPLgTLAALKPPFSKLPGDARldvlqkQGYPPFGVEMKITDDAGKELpwDGKTFGRLKV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 397 KLPLPPGAFSGLWKNQeafkhlyFEKfPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADC 476
Cdd:PRK06018 390 RGPAVAAAYYRVDGEI-------LDD-DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEA 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191882763 477 AVVGKEDPLKGHVPLALCVLRKDINITEgqvlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:PRK06018 462 AVIGVYHPKWDERPLLIVQLKPGETATR----EEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
35-547 |
1.69e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 73.32 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 35 TITYKEVLEQVSRLAGVLVKH-GVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVT 113
Cdd:PRK12492 49 TLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVY 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 114 AS-FG-----IEPGRKVEYmpiLEEAmRIGQHKP-----------DK----VLIYNRPnmETVP----LASGRDLdwdEE 168
Cdd:PRK12492 129 LNmFGklvqeVLPDTGIEY---LIEA-KMGDLLPaakgwlvntvvDKvkkmVPAYHLP--QAVPfkqaLRQGRGL---SL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 169 MAKAQSQDCVPVLSehplyilYTSGTTGLPKGVVRPTGG--------YAVMLNWTMSSIYGLKPG-EVWWAASDLGWVVG 239
Cdd:PRK12492 200 KPVPVGLDDIAVLQ-------YTGGTTGLAKGAMLTHGNlvanmlqvRACLSQLGPDGQPLMKEGqEVMIAPLPLYHIYA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 240 HSYICYGPLIHGNTTVLyegkpVGTP-DAGAYFRVLAEHGVAALFTAPTAIRAIRQQdPGAalgKQYSLTRFKTLFVAGE 318
Cdd:PRK12492 273 FTANCMCMMVSGNHNVL-----ITNPrDIPGFIKELGKWRFSALLGLNTLFVALMDH-PGF---KDLDFSALKLTNSGGT 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 319 RCDVETLEWSKKVFRVPVLDHWWQTETgSPItASCIGLGNSKTPppGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKl 398
Cdd:PRK12492 344 ALVKATAERWEQLTGCTIVEGYGLTET-SPV-ASTNPYGELARL--GTVGIPVPGTALKVIDDDGNELPLGERGELCIK- 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 399 plPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAV 478
Cdd:PRK12492 419 --GPQVMKGYWQQPEATAEALDAE--GWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAA 494
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191882763 479 VGKEDPLKGHVpLALCVLRKDINITegqvLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:PRK12492 495 IGVPDERSGEA-VKLFVVARDPGLS----VEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
19-547 |
1.88e-13 |
|
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: 72.89 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIIYDSpvtdtkATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 98
Cdd:cd17656 3 DAVAVVFEN------QKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 99 LSSRIDHAKPKVVVTASfgiepgrkveympileeamrigqHKPDKVliynRPNMETVPLasgrdlDWDEEMAKAQSQDCV 178
Cdd:cd17656 77 RIYIMLDSGVRVVLTQR-----------------------HLKSKL----SFNKSTILL------EDPSISQEDTSNIDY 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 179 PVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASdlgwvvgHSY-ICY----GPLIHGNT 253
Cdd:cd17656 124 INNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLQFAT-------CSFdVCYqeifSTLLSGGT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 254 tvLYEGKPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpgaalgKQYS---LTRFKTLFVAGERCDVETLewSKK 330
Cdd:cd17656 197 --LYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSE-------REFInrfPTCVKHIITAGEQLVITNE--FKE 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 331 VFR---VPVLDHWWQTETgSPITASCIGLGNS--KTPPpgqAGKSVPGYNVMILDDNMQKLKARCLGNIVVK-LPLPPGA 404
Cdd:cd17656 266 MLHehnVHLHNHYGPSET-HVVTTYTINPEAEipELPP---IGKPISNTWIYILDQEQQLQPQGIVGELYISgASVARGY 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 405 FSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDP 484
Cdd:cd17656 342 LNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADD 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191882763 485 LKGHVPLALCVLRKDINITegQVLEEIVQHVRQSIGPvAAFrkaVFVQQLPKTRSGKIPRAAL 547
Cdd:cd17656 422 KGEKYLCAYFVMEQELNIS--QLREYLAKQLPEYMIP-SFF---VPLDQLPLTPNGKVDRKAL 478
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
185-540 |
5.08e-13 |
|
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: 70.41 E-value: 5.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 185 PLYILYTSGTTGLPKGVVRPTGGYAVMlNWTMSSIYGLKPGEVwwaasdlgwvvghsYICYGPLIH------GNTTVLYE 258
Cdd:cd17636 2 PVLAIYTAAFSGRPNGALLSHQALLAQ-ALVLAVLQAIDEGTV--------------FLNSGPLFHigtlmfTLATFHAG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 259 GKPVGTP--DAGAYFRVLAEHGVAALFTAPTAIRAIRQqdpgAALGKQYSLTRFKTLFVAGERCD---VETLEWSKKVFr 333
Cdd:cd17636 67 GTNVFVRrvDAEEVLELIEAERCTHAFLLPPTIDQIVE----LNADGLYDLSSLRSSPAAPEWNDmatVDTSPWGRKPG- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 334 vpvldHWWQTETGSPITASciGLGNSKTpppGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLppgAFSGLWK--- 410
Cdd:cd17636 142 -----GYGQTEVMGLATFA--ALGGGAI---GGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPT---VMAGYWNrpe 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 411 -NQEAFKHlyfekfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHV 489
Cdd:cd17636 209 vNARRTRG-------GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQS 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1191882763 490 PLALCVLRKDINITEgqvlEEIVQHVRQSIgpvAAFRK---AVFVQQLPKTRSG 540
Cdd:cd17636 282 VKAIVVLKPGASVTE----AELIEHCRARI---ASYKKpksVEFADALPRTAGG 328
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
34-517 |
7.01e-13 |
|
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: 70.95 E-value: 7.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 34 ATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVvt 113
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAF-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 114 asfgiepgrkveympileeamrIGqhkpdkvliynrpnmetVPLAsgrdldwDEEMAkaqsqdcvpvlsehplyILYTSG 193
Cdd:cd05910 79 ----------------------IG-----------------IPKA-------DEPAA-----------------ILFTSG 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 194 TTGLPKGVVRPTGGYAVMLNwTMSSIYGLKPGEVWWAASDLgwvvghsYICYGPLIhGNTTVLYEGKPV--GTPDAGAYF 271
Cdd:cd05910 96 STGTPKGVVYRHGTFAAQID-ALRQLYGIRPGEVDLATFPL-------FALFGPAL-GLTSVIPDMDPTrpARADPQKLV 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 272 RVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQysLTRFKTLFVAGERCDVETLEWSKKVF--RVPVLDHWWQTETgSPI 349
Cdd:cd05910 167 GAIRQYGVSIVFGSPALLERVARY--CAQHGIT--LPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEA-LPV 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 350 TAscIG---LGNSKTPPPGQA-----GKSVPGYNVMILD---------DNMQKLKARCLGNIVVKLPL---------PPG 403
Cdd:cd05910 242 SS--IGsreLLATTTAATSGGagtcvGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVTGPTvtptyvnrpVAT 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 404 AFSGLWKNQEAFKHlyfekfpgyyDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKED 483
Cdd:cd05910 320 ALAKIDDNSEGFWH----------RMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGK 389
|
490 500 510
....*....|....*....|....*....|....*
gi 1191882763 484 PLKGHvPLaLCVLRKDINITE-GQVLEEIVQHVRQ 517
Cdd:cd05910 390 PGCQL-PV-LCVEPLPGTITPrARLEQELRALAKD 422
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
188-542 |
4.26e-12 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 69.18 E-value: 4.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 188 ILYTSGTTGLPKGVVrpTGGYAVMLNW-TMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVlYEGKPVgtpD 266
Cdd:PRK08633 787 IIFSSGSEGEPKGVM--LSHHNILSNIeQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVV-YHPDPT---D 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 267 AGAYFRVLAEHGVAALFTAPTAIRA-IRQQ--DPgaalgkqyslTRFKTL--FVAG-ERCDVETLEWSKKVFRVPVLDHW 340
Cdd:PRK08633 861 ALGIAKLVAKHRATILLGTPTFLRLyLRNKklHP----------LMFASLrlVVAGaEKLKPEVADAFEEKFGIRILEGY 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 341 WQTETGSPITASC-----------IGlgnSKtppPGQAGKSVPGYNVMILD-DNMQKLKARCLGNIVVKlplPPGAFSGL 408
Cdd:PRK08633 931 GATETSPVASVNLpdvlaadfkrqTG---SK---EGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIG---GPQVMKGY 1001
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 409 WKNQ----EAFKHLyfeKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESL--LSHGTVADCAVVGKE 482
Cdd:PRK08633 1002 LGDPektaEVIKDI---DGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELakALGGEEVVFAVTAVP 1078
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191882763 483 DPLKGHvplALCVLrkdINITEGQVlEEIVQHVRQS-IGPVAAFRKAVFVQQLPKTRSGKI 542
Cdd:PRK08633 1079 DEKKGE---KLVVL---HTCGAEDV-EELKRAIKESgLPNLWKPSRYFKVEALPLLGSGKL 1132
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
429-544 |
9.98e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 66.98 E-value: 9.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 429 TMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINitegqvL 508
Cdd:PRK08308 295 TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEID------P 368
|
90 100 110
....*....|....*....|....*....|....*.
gi 1191882763 509 EEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPR 544
Cdd:PRK08308 369 VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSR 404
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
368-546 |
1.03e-11 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 67.72 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 368 GKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLyfeKFPGYYDTMDAGYMdEEGYVYVMSRV 447
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHICVR---GPSLMSGYFRDEESQDVL---AADGWLDTGDLGYL-LDGYLYITGRA 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 448 DDVINVAGHRISAGAIEESLLSHGTV--ADCAVVGKEDPlKGHVPLALCVLRKDINITEGQVLEEIVQHVRQSIGpVAAF 525
Cdd:PRK09192 461 KDLIIINGRNIWPQDIEWIAEQEPELrsGDAAAFSIAQE-NGEKIVLLVQCRISDEERRGQLIHALAALVRSEFG-VEAA 538
|
170 180
....*....|....*....|.
gi 1191882763 526 RKAVFVQQLPKTRSGKIPRAA 546
Cdd:PRK09192 539 VELVPPHSLPRTSSGKLSRAK 559
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
7-552 |
1.37e-11 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 66.94 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 7 NAIDRHIESgkgDKVAIIydspvtDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAI 86
Cdd:PRK10946 29 DILTRHAAS---DAIAVI------CGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 87 HSLIFGGFASKELSSRIDHAKPKVVVTASfgiepgrkveympileeamrigQHK--PDKV----LIYNRPNMETVPLasg 160
Cdd:PRK10946 100 PVNALFSHQRSELNAYASQIEPALLIADR----------------------QHAlfSDDDflntLVAEHSSLRVVLL--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 161 RDLDWDEEMAKAQSQDCV-----PVLSEHPLYILYTSGTTGLPKGVVRPTGGYavmlnwtmssIYGLKpgevwwAASDLG 235
Cdd:PRK10946 155 LNDDGEHSLDDAINHPAEdftatPSPADEVAFFQLSGGSTGTPKLIPRTHNDY----------YYSVR------RSVEIC 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 236 WVVGHS-YICYGPLIH-------GNTTVLYEGKPV---GTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQ 304
Cdd:PRK10946 219 GFTPQTrYLCALPAAHnypmsspGALGVFLAGGTVvlaPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQA--IAEGGSR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 305 YSLTRFKTLFVAGERCDvETLewskkVFRVPVL-------------------------DHWWQTEtGSPITasciglgns 359
Cdd:PRK10946 297 AQLASLKLLQVGGARLS-ETL-----ARRIPAElgcqlqqvfgmaeglvnytrlddsdERIFTTQ-GRPMS--------- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 360 ktpppgqagksvPGYNVMILDDNmqklkarclGNivvklPLPPG-----------AFSGLWK----NQEAFKHlyfekfP 424
Cdd:PRK10946 361 ------------PDDEVWVADAD---------GN-----PLPQGevgrlmtrgpyTFRGYYKspqhNASAFDA------N 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 425 GYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITe 504
Cdd:PRK10946 409 GFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKAV- 487
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1191882763 505 gqvleEIVQHVRQSigPVAAFR---KAVFVQQLPKTRSGKIPRAALSALVN 552
Cdd:PRK10946 488 -----QLRRFLREQ--GIAEFKlpdRVECVDSLPLTAVGKVDKKQLRQWLA 531
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
167-547 |
3.68e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 65.88 E-value: 3.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 167 EEMAKAQSQDCV-PVLSEHPL-YILYTSGTTGLPKGVV---RPT--GGYAVMLNWTM--SSIYGLKPgevwwaasdlgwV 237
Cdd:PRK07008 158 ETLVGAQDGDYDwPRFDENQAsSLCYTSGTTGNPKGALyshRSTvlHAYGAALPDAMglSARDAVLP------------V 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 238 VghsyicygPLIHGNTTVL-YEGKPVGTP--------DAGAYFRVLAEHGVAalFTA--PTAIRAIRQQDPGAALgkqyS 306
Cdd:PRK07008 226 V--------PMFHVNAWGLpYSAPLTGAKlvlpgpdlDGKSLYELIEAERVT--FSAgvPTVWLGLLNHMREAGL----R 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 307 LTRFKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQTETgSPITASCiGLGNSKTPPPGQA--------GKSVPGYNVMI 378
Cdd:PRK07008 292 FSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEM-SPLGTLC-KLKWKHSQLPLDEqrkllekqGRVIYGVDMKI 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 379 LDDNMQKL--KARCLGNIVVKLPlppgafsglWKNQEAFKHlyfEKFP---GYYDTMDAGYMDEEGYVYVMSRVDDVINV 453
Cdd:PRK07008 370 VGDDGRELpwDGKAFGDLQVRGP---------WVIDRYFRG---DASPlvdGWFPTGDVATIDADGFMQITDRSKDVIKS 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 454 AGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINITEgqvlEEIVQHVRqsiGPVAAFR---KAVF 530
Cdd:PRK07008 438 GGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTR----EELLAFYE---GKVAKWWipdDVVF 510
|
410
....*....|....*..
gi 1191882763 531 VQQLPKTRSGKIPRAAL 547
Cdd:PRK07008 511 VDAIPHTATGKLQKLKL 527
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
26-553 |
5.78e-11 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 64.92 E-value: 5.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 26 DSPVTDTK-ATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIG------AIHSlifggfASKE 98
Cdd:PRK04813 17 DFPAYDYLgEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGhayipvDVSS------PAER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 99 LSSRIDHAKPKVVVTasfgiepgrkVEYMPILEEAMRIgqHKPDKVliynrpnmetvplasgrdldwdEEMAKAQsqdcV 178
Cdd:PRK04813 91 IEMIIEVAKPSLIIA----------TEELPLEILGIPV--ITLDEL----------------------KDIFATG----N 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 179 PVLSEHPL------YILYTSGTTGLPKGVvrpTGGYAVML---NWtMSSIYGLKPGEVWWAAS----DLGwvVGHSYICy 245
Cdd:PRK04813 133 PYDFDHAVkgddnyYIIFTSGTTGKPKGV---QISHDNLVsftNW-MLEDFALPEGPQFLNQApysfDLS--VMDLYPT- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 246 gpLIHGNTTVLYEgKPVgTPDAGAYFRVLAEHGVAALFTAPTAIRaIRQQDPGAAlGKQY-SLTRFktLFvAGERCDVET 324
Cdd:PRK04813 206 --LASGGTLVALP-KDM-TANFKQLFETLPQLPINVWVSTPSFAD-MCLLDPSFN-EEHLpNLTHF--LF-CGEELPHKT 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 325 LEwsKKVFRVP---VLDHWWQTE-----TGSPITASCIglgNSKTPPPgqAGKSVPGYNVMILDDNMQKLKARCLGNIVV 396
Cdd:PRK04813 277 AK--KLLERFPsatIYNTYGPTEatvavTSIEITDEML---DQYKRLP--IGYAKPDSPLLIIDEEGTKLPDGEQGEIVI 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 397 KLP-LPPGAFSGLWKNQEAFKHlyFEKFPGYYdTMDAGYMDEeGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVAD 475
Cdd:PRK04813 350 SGPsVSKGYLNNPEKTAEAFFT--FDGQPAYH-TGDAGYLED-GLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVES 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 476 CAVV-----GKEDPLKGHVPLALCVLRKDINITEgQVLEEIVQHVRQSIGPvaafRKAVFVQQLPKTRSGKIPRAALSAL 550
Cdd:PRK04813 426 AVVVpynkdHKVQYLIAYVVPKEEDFEREFELTK-AIKKELKERLMEYMIP----RKFIYRDSLPLTPNGKIDRKALIEE 500
|
...
gi 1191882763 551 VNG 553
Cdd:PRK04813 501 VNK 503
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
34-535 |
1.83e-10 |
|
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: 63.14 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 34 ATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVt 113
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 114 asfgiepgrkveympileeamrigqhkpdkvliynrpnmetVPLAsgrdldwdeemakaqsqdcvpvlsehpLYIlYTSG 193
Cdd:cd05940 81 -----------------------------------------VDAA---------------------------LYI-YTSG 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 194 TTGLPKGVVRPTGGYAVMLNWTMSSiYGLKPGEVWW--------AASDLGWVVGhsyicygpLIHGNTTVLyeGKPVgtp 265
Cdd:cd05940 92 TTGLPKAAIISHRRAWRGGAFFAGS-GGALPSDVLYtclplyhsTALIVGWSAC--------LASGATLVI--RKKF--- 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 266 DAGAYFRVLAEHGVAALFTAPTAIRAIRQQdPGAALGKQYSLTRfktLFVAGERCDVetleWS--KKVFRVP-VLDHWWQ 342
Cdd:cd05940 158 SASNFWDDIRKYQATIFQYIGELCRYLLNQ-PPKPTERKHKVRM---IFGNGLRPDI----WEefKERFGVPrIAEFYAA 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 343 TETGspitascIGLGN--SKtppPGQAGKS------VPGYNVMILD-DNMQKL---KARCL-------GNIVVKL-PLPP 402
Cdd:cd05940 230 TEGN-------SGFINffGK---PGAIGRNpsllrkVAPLALVKYDlESGEPIrdaEGRCIkvprgepGLLISRInPLEP 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 403 gaFSGLWKNQEAFKHLY---FEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVV 479
Cdd:cd05940 300 --FDGYTDPAATEKKILrdvFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVY 377
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1191882763 480 GKEDP-LKGHVPLALCVLRKDINITegqvLEEIVQHVRQSIgpvAAFRKAVFVQQLP 535
Cdd:cd05940 378 GVQVPgTDGRAGMAAIVLQPNEEFD----LSALAAHLEKNL---PGYARPLFLRLQP 427
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
424-552 |
2.15e-10 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 63.09 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 424 PGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHVPLALCVLrKDINIT 503
Cdd:PRK07445 323 QGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVP-KDPSIS 401
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1191882763 504 egqvLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAALSALVN 552
Cdd:PRK07445 402 ----LEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAV 446
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
188-544 |
2.87e-10 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 62.89 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 188 ILYTSGTTGLPKGVvrpTGGYAVMLNWTMSSIYglkpgevwwaasdlgwVVGHS----YICYGPLIH------GNTTVLY 257
Cdd:PLN02860 177 ICFTSGTTGRPKGV---TISHSALIVQSLAKIA----------------IVGYGeddvYLHTAPLCHigglssALAMLMV 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 258 EGKPVGTP--DAGAYFRVLAEHGVAALFTAPTAIRAIRQqdPGAALGKQYSLTRFKTLFVAGERCDVETLEWSKKVF-RV 334
Cdd:PLN02860 238 GACHVLLPkfDAKAALQAIKQHNVTSMITVPAMMADLIS--LTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFpNA 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 335 PVLDHWWQTETGSPIT----------------ASCIGLGNSKTPPPGQA--GKSVPGYNVMILDDNMQKLkarclGNIVV 396
Cdd:PLN02860 316 KLFSAYGMTEACSSLTfmtlhdptlespkqtlQTVNQTKSSSVHQPQGVcvGKPAPHVELKIGLDESSRV-----GRILT 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 397 KlplPPGAFSGLW-KNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVAD 475
Cdd:PLN02860 391 R---GPHVMLGYWgQNSETASVLSND---GWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVAS 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 476 CAVVGKEDPLKGHVPLAlCVLRKD-----INITEG-----QVLEEIVQHVRQSIGpVAAFR-KAVFVQ---QLPKTRSGK 541
Cdd:PLN02860 465 VVVVGVPDSRLTEMVVA-CVRLRDgwiwsDNEKENakknlTLSSETLRHHCREKN-LSRFKiPKLFVQwrkPFPLTTTGK 542
|
...
gi 1191882763 542 IPR 544
Cdd:PLN02860 543 IRR 545
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
35-480 |
3.11e-10 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 62.45 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 35 TITYKEVLEQVSRLAGVLVK-HGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKEL--SSRIDHAKpKVV 111
Cdd:cd05937 5 TWTYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLihCLKLSGSR-FVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 112 VTasfgiepgrkveympileeamrigqhkPDKVLIynrpnmetvplasgrdldwdeemakaqsqdcvpvlsehplyILYT 191
Cdd:cd05937 84 VD---------------------------PDDPAI-----------------------------------------LIYT 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 192 SGTTGLPKGVVRPTGGYAVMlNWTMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLYEGKPVGT-----PD 266
Cdd:cd05937 96 SGTTGLPKAAAISWRRTLVT-SNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQfwkdvRD 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 267 AGAYFRVLAEHGVAALFTAPTAIRAiRQQDPGAALGKqysltrfktlfvaGERCDVetleWSK--KVFRVPVLDHWWQTE 344
Cdd:cd05937 175 SGATIIQYVGELCRYLLSTPPSPYD-RDHKVRVAWGN-------------GLRPDI----WERfrERFNVPEIGEFYAAT 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 345 TG---------SPITASCIG---------LGNSKTP----PPGQagksvpgynvMILDDNMQKLKARCL----GNIVVKL 398
Cdd:cd05937 237 EGvfaltnhnvGDFGAGAIGhhglirrwkFENQVVLvkmdPETD----------DPIRDPKTGFCVRAPvgepGEMLGRV 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 399 PLPP-GAFSGLWKNQEAFKHLY----FEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTV 473
Cdd:cd05937 307 PFKNrEAFQGYLHNEDATESKLvrdvFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDI 386
|
....*..
gi 1191882763 474 ADCAVVG 480
Cdd:cd05937 387 AEANVYG 393
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
368-551 |
1.24e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 60.78 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 368 GKSVPGYNVMILDDNMQKLKARCLGNIVVKLP-LPPG--AFSGLWKNQEAfkhlyfekfPGYYDTMDAGYMDEEGYVYVM 444
Cdd:PRK07768 363 GPPLPGLEVRVVDEDGQVLPPRGVGVIELRGEsVTPGylTMDGFIPAQDA---------DGWLDTGDLGYLTEEGEVVVC 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 445 SRVDDVINVAGHRISAGAIEESLLS-HGTVADCAVVGKEDPLKGHVPLALCVLRKDI-NITEGQVLE-EIVQHVRQSIGp 521
Cdd:PRK07768 434 GRVKDVIIMAGRNIYPTDIERAAARvEGVRPGNAVAVRLDAGHSREGFAVAVESNAFeDPAEVRRIRhQVAHEVVAEVG- 512
|
170 180 190
....*....|....*....|....*....|..
gi 1191882763 522 vAAFRKAVFVQ--QLPKTRSGKIPRAALSALV 551
Cdd:PRK07768 513 -VRPRNVVVLGpgSIPKTPSGKLRRANAAELV 543
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
163-549 |
4.71e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 59.80 E-value: 4.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 163 LDWDEEMAKAQSQDCVPVLS--EHPLYILYTSGTTGLPKGVVRPTGGYAvMLNWTMSSIYGLKPGEV--------WWAAS 232
Cdd:PRK05691 2311 LEDDAAALAAYSDAPLPFLSlpQHQAYLIYTSGSTGKPKGVVVSHGEIA-MHCQAVIERFGMRADDCelhfysinFDAAS 2389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 233 DLGWVvghsyicygPLIHGNTTVLyegKPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpgaaLGKQYSLTRFKT 312
Cdd:PRK05691 2390 ERLLV---------PLLCGARVVL---RAQGQWGAEEICQLIREQQVSILGFTPSYGSQLAQW-----LAGQGEQLPVRM 2452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 313 LFVAGERCDVETLEWSKKVFRVPVL-DHWWQTETGSPITASCIGlgnsKTPPPGQA----GKSVPGYNVMILDDNMqklk 387
Cdd:PRK05691 2453 CITGGEALTGEHLQRIRQAFAPQLFfNAYGPTETVVMPLACLAP----EQLEEGAAsvpiGRVVGARVAYILDADL---- 2524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 388 arclgnivvkLPLPPGAFSGLWKNQEAFKHLYFEKfPG-----------------YYDTMDAGYMDEEGYVYVMSRVDDV 450
Cdd:PRK05691 2525 ----------ALVPQGATGELYVGGAGLAQGYHDR-PGltaerfvadpfaadggrLYRTGDLVRLRADGLVEYVGRIDHQ 2593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 451 INVAGHRISAGAIEESLLSHGTVADCAVVGKEDPlkGHVPLA---LCVLRKDINITEGQVLEEIVQHVRQSIGPVAAFRK 527
Cdd:PRK05691 2594 VKIRGFRIELGEIESRLLEHPAVREAVVLALDTP--SGKQLAgylVSAVAGQDDEAQAALREALKAHLKQQLPDYMVPAH 2671
|
410 420
....*....|....*....|..
gi 1191882763 528 AVFVQQLPKTRSGKIPRAALSA 549
Cdd:PRK05691 2672 LILLDSLPLTANGKLDRRALPA 2693
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
35-433 |
9.21e-09 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 58.21 E-value: 9.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 35 TITYKEVLEQVSRLAGVLVKHGVSKGDTVVI-------YMPMIPQAMYTMLACARIGAIHSLIFGGFAskELSSRIDHAK 107
Cdd:cd05921 25 RVTYAEALRQVRAIAQGLLDLGLSAERPLLIlsgnsieHALMALAAMYAGVPAAPVSPAYSLMSQDLA--KLKHLFELLK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 108 PKVVVTASFGIEPGRKVEYMPILEEAMRIGQHKPDKVLIYNRPNMETVPLAsgrdlDWDEEMAKAQSqDCVPVLsehply 187
Cdd:cd05921 103 PGLVFAQDAAPFARALAAIFPLGTPLVVSRNAVAGRGAISFAELAATPPTA-----AVDAAFAAVGP-DTVAKF------ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 188 iLYTSGTTGLPKGVV---RPTGGYAVMLNWTMSSIYGLKPGEVWWAAsdlgWvvGHSY---ICYGPLIH-GNTTVLYEGK 260
Cdd:cd05921 171 -LFTSGSTGLPKAVIntqRMLCANQAMLEQTYPFFGEEPPVLVDWLP----W--NHTFggnHNFNLVLYnGGTLYIDDGK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 261 PvgTPDA-GAYFRVLAEHGVAALFTAPTA----IRAIRQQDpgaALGKQYsLTRFKTLFVAGERCD------VETLEWSK 329
Cdd:cd05921 244 P--MPGGfEETLRNLREISPTVYFNVPAGwemlVAALEKDE---ALRRRF-FKRLKLMFYAGAGLSqdvwdrLQALAVAT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 330 KVFRVPVLDHWWQTETGsPITASCIGL----GNSKTPPPGQAGKSVPgynvmilddNMQKLKARCLGnivvklplpPGAF 405
Cdd:cd05921 318 VGERIPMMAGLGATETA-PTATFTHWPtersGLIGLPAPGTELKLVP---------SGGKYEVRVKG---------PNVT 378
|
410 420
....*....|....*....|....*...
gi 1191882763 406 SGLWKNQEAFKHLYFEKfpGYYDTMDAG 433
Cdd:cd05921 379 PGYWRQPELTAQAFDEE--GFYCLGDAA 404
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
19-546 |
3.16e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 57.10 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIIYDSPVTDTKATITYKEVLEQVSRLAGVLVKHGVSkGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 98
Cdd:PRK05691 24 DRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARASF-GDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESARR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 99 -----LSSRIDHAKPKVVVTASfgiepgrkveympileeAMRIGQHKPDKVLIYNRPNMETV-PLASGRDLDWDEEMAKA 172
Cdd:PRK05691 103 hhqerLLSIIADAEPRLLLTVA-----------------DLRDSLLQMEELAAANAPELLCVdTLDPALAEAWQEPALQP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 173 qsqdcvpvlsEHPLYILYTSGTTGLPKGVvRPTGGYAVMLNWTMSSIYGLKPGE----VWWAA--SDLGWVVGhsyiCYG 246
Cdd:PRK05691 166 ----------DDIAFLQYTSGSTALPKGV-QVSHGNLVANEQLIRHGFGIDLNPddviVSWLPlyHDMGLIGG----LLQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 247 PLIHGNTTVL-----YEGKPV----------GTPDAGAYF-------RVlAEHGVAAL--------FTAPTAIRairqQD 296
Cdd:PRK05691 231 PIFSGVPCVLmspayFLERPLrwleaiseygGTISGGPDFayrlcseRV-SESALERLdlsrwrvaYSGSEPIR----QD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 297 PGAALGKQYSLTRFK-------------TLFVAGER--CDVETLEWSKKVFRVPVLdhwwQTETGSPITaSCiglgnskt 361
Cdd:PRK05691 306 SLERFAEKFAACGFDpdsffasyglaeaTLFVSGGRrgQGIPALELDAEALARNRA----EPGTGSVLM-SC-------- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 362 pppgqaGKSVPGYNVMILDDN-MQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfPG--YYDTMDAGYMdEE 438
Cdd:PRK05691 373 ------GRSQPGHAVLIVDPQsLEVLGDNRVGEIWAS---GPSIAHGYWRNPEASAKTFVEH-DGrtWLRTGDLGFL-RD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 439 GYVYVMSRVDDVINVAGHRISAGAIEESL------LSHGTVADCAVvgKEDPLKGhVPLALCVLRKDINITEGQVLeeiV 512
Cdd:PRK05691 442 GELFVTGRLKDMLIVRGHNLYPQDIEKTVerevevVRKGRVAAFAV--NHQGEEG-IGIAAEISRSVQKILPPQAL---I 515
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1191882763 513 QHVRQSIGpvAAFRKAVFV------QQLPKTRSGKIPRAA 546
Cdd:PRK05691 516 KSIRQAVA--EACQEAPSVvlllnpGALPKTSSGKLQRSA 553
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
19-547 |
3.84e-08 |
|
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: 56.02 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIIYDSP-VTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFask 97
Cdd:cd17645 6 EQVERTPDHVaVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDY--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 98 elssridhakpkvvvtasfgiePGRKVEYMPILEEAmrigqhkpdKVLIYNRPNMetvplasgrdldwdeemakaqsqdc 177
Cdd:cd17645 83 ----------------------PGERIAYMLADSSA---------KILLTNPDDL------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 178 vpvlsehpLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSiYGLKPGEVWWAASDLG-----WVVgHSYICYGPLIHgn 252
Cdd:cd17645 107 --------AYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPY-FGVTPADKSLVYASFSfdasaWEI-FPHLTAGAALH-- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 253 ttVLYEGKPVGTPDAGAYFRvlaEHGVAALFTaPTairairqqdPGAALGKQYSLTRFKTLFVAGERCdvetlewsKKVF 332
Cdd:cd17645 175 --VVPSERRLDLDALNDYFN---QEGITISFL-PT---------GAAEQFMQLDNQSLRVLLTGGDKL--------KKIE 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 333 RVP--VLDHWWQTETGSPITASCIGLGNSKTPppgqAGKSVPGYNVMILDDNMQKLKARCLGNIVVklplppgAFSGLWK 410
Cdd:cd17645 232 RKGykLVNNYGPTENTVVATSFEIDKPYANIP----IGKPIDNTRVYILDEALQLQPIGVAGELCI-------AGEGLAR 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 411 NQEAFKHLYFEKF------PG--YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKE 482
Cdd:cd17645 301 GYLNRPELTAEKFivhpfvPGerMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKE 380
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191882763 483 DplKGHVPlALC---VLRKDINItegqvlEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAAL 547
Cdd:cd17645 381 D--ADGRK-YLVayvTAPEEIPH------EELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
35-551 |
4.93e-08 |
|
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: 55.63 E-value: 4.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 35 TITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGaihslifGGFASkelssrIDHAKPkvvvta 114
Cdd:cd05918 24 SLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAG-------GAFVP------LDPSHP------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 115 sfgiePGRKVEympILEEAmrigqhkpdkvliynrpnmetvplasgrdldwdeemakaqsqDCVPVLSEHP---LYILYT 191
Cdd:cd05918 85 -----LQRLQE---ILQDT------------------------------------------GAKVVLTSSPsdaAYVIFT 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 192 SGTTGLPKGVVRPTGGYAVMLNwTMSSIYGLKPGEVWWAASdlgwvvghSY---IC----YGPLIHGNTTVLyegkpvgT 264
Cdd:cd05918 115 SGSTGKPKGVVIEHRALSTSAL-AHGRALGLTSESRVLQFA--------SYtfdVSileiFTTLAAGGCLCI-------P 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 265 PDA---GAYFRVLAEHGVAALFTAPTAIRAIRQQDpgaalgkqysLTRFKTLFVAGE---RCDVETleWSKKVFrvpVLD 338
Cdd:cd05918 179 SEEdrlNDLAGFINRLRVTWAFLTPSVARLLDPED----------VPSLRTLVLGGEaltQSDVDT--WADRVR---LIN 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 339 HWWQTETgspitasCIGLGNSKTPPPGQA---GKSVPGyNVMILD-DNMQKLkarclgnivvklpLPPGAFSGLW----- 409
Cdd:cd05918 244 AYGPAEC-------TIAATVSPVVPSTDPrniGRPLGA-TCWVVDpDNHDRL-------------VPIGAVGELLiegpi 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 410 ----------KNQEAF-KHLYFEKFPGY------YDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGT 472
Cdd:cd05918 303 largylndpeKTAAAFiEDPAWLKQEGSgrgrrlYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLP 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 473 VADCAVVGKEDPLKGHVPLAL-CVLRKDINITEGQVLEEIVQHVRQSIGPVAAFRKA---------------VFVQQLPK 536
Cdd:cd05918 383 GAKEVVVEVVKPKDGSSSPQLvAFVVLDGSSSGSGDGDSLFLEPSDEFRALVAELRSklrqrlpsymvpsvfLPLSHLPL 462
|
570
....*....|....*
gi 1191882763 537 TRSGKIPRAALSALV 551
Cdd:cd05918 463 TASGKIDRRALRELA 477
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
35-483 |
1.18e-07 |
|
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: 54.53 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 35 TITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAihslifggfaskelssridhakpkVVVTA 114
Cdd:cd17639 5 YMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNI------------------------PIVTV 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 115 sfgiepgrkveYMPILEEAMRIGQHKPDKVLIYNRPNMETVPLasgrdldwdeemakaqsqdcvpvlsehplyILYTSGT 194
Cdd:cd17639 61 -----------YATLGEDALIHSLNETECSAIFTDGKPDDLAC------------------------------IMYTSGS 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 195 TGLPKGVvrptggyaVMLNWTM-SSIYGLKPGEVWWAASDlgwvvgHSYICYGPLIH-----GNTTVLYEGKPVG--TP- 265
Cdd:cd17639 100 TGNPKGV--------MLTHGNLvAGIAGLGDRVPELLGPD------DRYLAYLPLAHifelaAENVCLYRGGTIGygSPr 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 266 ------------DAGAyFR--VLAehGVAALF-TAPTAIRAirQQDPGAALGKQYsltrFKTLFVAGE---RCDVETLEW 327
Cdd:cd17639 166 tltdkskrgckgDLTE-FKptLMV--GVPAIWdTIRKGVLA--KLNPMGGLKRTL----FWTAYQSKLkalKEGPGTPLL 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 328 SKKVFR--------------------------------VPVLDHWWQTET--GSPI------TASCIGLgnsktPPPGQA 367
Cdd:cd17639 237 DELVFKkvraalggrlrymlsggaplsadtqeflnivlCPVIQGYGLTETcaGGTVqdpgdlETGRVGP-----PLPCCE 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 368 GK--SVPGYNVMILDDNMQklkarclGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMS 445
Cdd:cd17639 312 IKlvDWEEGGYSTDKPPPR-------GEILIR---GPNVFKGYYKNPEKTKEAFDGD--GWFHTGDIGEFHPDGTLKIID 379
|
490 500 510
....*....|....*....|....*....|....*....
gi 1191882763 446 RVDD-VINVAGHRISAGAIEESLLSHGTVADCAVVGKED 483
Cdd:cd17639 380 RKKDlVKLQNGEYIALEKLESIYRSNPLVNNICVYADPD 418
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
183-549 |
2.19e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.40 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 183 EHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVVGhSYICYGPLIHGNTTVLyeGKPV 262
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNTHAALAERLQW-MQATYALDDSDVLMQKAPISFDVS-VWECFWPLITGCRLVL--AGPG 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 263 GTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdPGAAlgkqySLTRFKTLFVAGERCDVEtlewskkvFRVPVLDHWWQ 342
Cdd:PRK05691 1349 EHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDE-PLAA-----ACTSLRRLFSGGEALPAE--------LRNRVLQRLPQ 1414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 343 tetgspitascIGLGNSKTPPpgQAGKSVPGYNVMIlDDNMQKLKARCLGNIVVKL------PLPPGAF-------SGLW 409
Cdd:PRK05691 1415 -----------VQLHNRYGPT--ETAINVTHWQCQA-EDGERSPIGRPLGNVLCRVldaelnLLPPGVAgelciggAGLA 1480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 410 KNQEAFKHLYFEKF-------PG--YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVG 480
Cdd:PRK05691 1481 RGYLGRPALTAERFvpdplgeDGarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLV 1560
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191882763 481 KEDpLKGHVPLALCVLRKDINITEGQVLEEIVQHVRQSIGPVAAFRkavfVQQLPKTRSGKIPRAALSA 549
Cdd:PRK05691 1561 REG-AAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIR----LDQMPLGPSGKLDRRALPE 1624
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
34-202 |
3.36e-07 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 53.23 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 34 ATITYKEVLEQVSRLAGVL-VKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVv 112
Cdd:cd17632 66 ETITYAELWERVGAVAAAHdPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLL- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 113 TASfgiepgrkVEYMPILEEAMRIGQHKPDKVLIYNRPNMET--VPLASGR-------------DLDWDEEMAKAQSQDC 177
Cdd:cd17632 145 AVS--------AEHLDLAVEAVLEGGTPPRLVVFDHRPEVDAhrAALESARerlaavgipvttlTLIAVRGRDLPPAPLF 216
|
170 180
....*....|....*....|....*.
gi 1191882763 178 VPVLSEHPLYIL-YTSGTTGLPKGVV 202
Cdd:cd17632 217 RPEPDDDPLALLiYTSGSTGTPKGAM 242
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
37-547 |
3.39e-07 |
|
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: 52.81 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 37 TYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTAsf 116
Cdd:cd05939 5 TFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIFN-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 117 giepgrkveympileeamrigQHKPDKVLIYNRPNmetvplasgrdldwdeemakaqSQDCVPVLSEhpLYILYTSGTTG 196
Cdd:cd05939 83 ---------------------LLDPLLTQSSTEPP----------------------SQDDVNFRDK--LFYIYTSGTTG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 197 LPKGvvrptggyAVMLNWTMSSI-------YGLKPGEVWW--------AASDLGwvVGHSyicygpLIHGNTTVLYEgkp 261
Cdd:cd05939 118 LPKA--------AVIVHSRYYRIaagayyaFGMRPEDVVYdclplyhsAGGIMG--VGQA------LLHGSTVVIRK--- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 262 vgTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALGKQysltRFKTLFVAGERCDVetleWSKKV--FRVP-VLD 338
Cdd:cd05939 179 --KFSASNFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKH----NVRLAVGNGLRPQI----WEQFVrrFGIPqIGE 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 339 HWWQTETGSPI-----TASCIGLgNSKTPPpgqagKSVPGYNVMILDDNMQKLKAR---CL-----------GNIVVKLP 399
Cdd:cd05939 249 FYGATEGNSSLvnidnHVGACGF-NSRILP-----SVYPIRLIKVDEDTGELIRDSdglCIpcqpgepgllvGKIIQNDP 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 400 LPpgAFSGLWKNQEAFKHLY---FEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADC 476
Cdd:cd05939 323 LR--RFDGYVNEGATNKKIArdvFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDV 400
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1191882763 477 AVVGKEDP-LKGHVPLALCVlrkdiNITEGQVLEEIVQHVRQSIGPVAafrKAVFV---QQLPKTRSGKIPRAAL 547
Cdd:cd05939 401 VVYGVEVPgVEGRAGMAAIV-----DPERKVDLDRFSAVLAKSLPPYA---RPQFIrllPEVDKTGTFKLQKTDL 467
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
36-250 |
4.98e-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: 52.60 E-value: 4.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 36 ITYKEVLEQVSRLAGVLVKHGV--SKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVt 113
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVF- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 114 asfgIEPGRKVEympILEEAMRIGqhkpdkvliynRPNMETVPLASGRDLdwdeemakaqsqdCVpvlsehplyILYTSG 193
Cdd:cd05927 85 ----CDAGVKVY---SLEEFEKLG-----------KKNKVPPPPPKPEDL-------------AT---------ICYTSG 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 194 TTGLPKGVVRPTGGYA---VMLNWTMSSIYGLKPGEVwwaasdlgwvvghsYICYGPLIH 250
Cdd:cd05927 125 TTGNPKGVMLTHGNIVsnvAGVFKILEILNKINPTDV--------------YISYLPLAH 170
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
424-551 |
2.47e-06 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 50.48 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 424 PGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHvplALCVLRKDINIT 503
Cdd:PRK08043 590 RGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGE---ALVLFTTDSELT 666
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1191882763 504 EgqvlEEIVQHVRQSIGP-VAAFRKAVFVQQLPKTRSGKIPRAALSALV 551
Cdd:PRK08043 667 R----EKLQQYAREHGVPeLAVPRDIRYLKQLPLLGSGKPDFVTLKSMV 711
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
36-263 |
6.16e-06 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 49.34 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 36 ITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACAR-------IGA-------IHSLifggfASKELSS 101
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRqnitvvtIYAslgeealCHSL-----NETEVTT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 102 RI-DHAKPKVVVTASFGIEPGRKVEYMPilEEAMRIGQhkpdkvliyNRPNMETVPLASGRDLdwdEEMAKAQSQDCVPV 180
Cdd:PLN02387 182 VIcDSKQLKKLIDISSQLETVKRVIYMD--DEGVDSDS---------SLSGSSNWTVSSFSEV---EKLGKENPVDPDLP 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 181 LSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVwwaasdlgwvvghsYICYGPLIH-----GNTTV 255
Cdd:PLN02387 248 SPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDV--------------YLAYLPLAHilelaAESVM 313
|
....*...
gi 1191882763 256 LYEGKPVG 263
Cdd:PLN02387 314 AAVGAAIG 321
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
427-550 |
6.43e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 49.40 E-value: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 427 YDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEESLLSHGTVADCAVVGKEDPLKGHvpLALCVLRKDINITEGQ 506
Cdd:PRK05691 4104 YRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNGKH--LVGYLVPHQTVLAQGA 4181
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1191882763 507 VLEEIVQHVRQSIGPVAAFRKAVFVQQLPKTRSGKIPRAALSAL 550
Cdd:PRK05691 4182 LLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPAL 4225
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
35-250 |
1.39e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 48.05 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 35 TITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTA 114
Cdd:PTZ00216 121 YITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCN 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 115 sfgiepGRKVeymPILEEAMRIGQhKPDKVLIYNRPNMETVPLASGRDLDWDEEMAKAQSqdcvpVLSEHPL-------- 186
Cdd:PTZ00216 201 ------GKNV---PNLLRLMKSGG-MPNTTIIYLDSLPASVDTEGCRLVAWTDVVAKGHS-----AGSHHPLnipenndd 265
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 187 --YILYTSGTTGLPKGVVRPTG----GYAVMLNWTMSSIYGLKPGEVwwaasdlgwvvghsYICYGPLIH 250
Cdd:PTZ00216 266 laLIMYTSGTTGDPKGVMHTHGsltaGILALEDRLNDLIGPPEEDET--------------YCSYLPLAH 321
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
36-438 |
1.61e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 47.73 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 36 ITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAI-------HSLIFGGFAskELSSRIDHAKP 108
Cdd:PRK12582 81 VTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPaapvspaYSLMSHDHA--KLKHLFDLVKP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 109 KVVVtasfgiepgrkVEYMPILEEAMRI-GQHKPDKVLIYNRPNME-TVPLAsgrdlDW-----DEEMAKAQSQ---DCV 178
Cdd:PRK12582 159 RVVF-----------AQSGAPFARALAAlDLLDVTVVHVTGPGEGIaSIAFA-----DLaatppTAAVAAAIAAitpDTV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 179 PvlsehplYILYTSGTTGLPKGVVRPTGGYAVMLNWTMssiyGLKPGEVWWAASD-LGW-----VVGHSYICYGPLIHGN 252
Cdd:PRK12582 223 A-------KYLFTSGSTGMPKAVINTQRMMCANIAMQE----QLRPREPDPPPPVsLDWmpwnhTMGGNANFNGLLWGGG 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 253 TTVLYEGKPVgtpdAGAY---FRVLAEHGVAALFTAPTAIRAI---RQQDPgaALGKQYsLTRFKTLFVAGERCDVETLE 326
Cdd:PRK12582 292 TLYIDDGKPL----PGMFeetIRNLREISPTVYGNVPAGYAMLaeaMEKDD--ALRRSF-FKNLRLMAYGGATLSDDLYE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 327 WSKKV------FRVPVLDHWWQTETgSPITASC---------IGLgnsktPPPGQAGKSVPgynvmilddNMQKLKARCL 391
Cdd:PRK12582 365 RMQALavrttgHRIPFYTGYGATET-APTTTGThwdtervglIGL-----PLPGVELKLAP---------VGDKYEVRVK 429
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1191882763 392 GNIVVKlplppgafsGLWKNQEAFKHLYFEKfpGYYDTMDAG-YMDEE 438
Cdd:PRK12582 430 GPNVTP---------GYHKDPELTAAAFDEE--GFYRLGDAArFVDPD 466
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
425-560 |
3.02e-05 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 47.27 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 425 GYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE--SLLSHGtvADCAVVGKEDPLKGHvPLALCVLRKDINi 502
Cdd:PRK06814 1010 GWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEElaAELWPD--ALHAAVSIPDARKGE-RIILLTTASDAT- 1085
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1191882763 503 tegqvLEEIVQHVR-QSIGPVAAFRKAVFVQQLPKTRSGKIPRAALSALVNGKPYKVTP 560
Cdd:PRK06814 1086 -----RAAFLAHAKaAGASELMVPAEIITIDEIPLLGTGKIDYVAVTKLAEEAAAKPEA 1139
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
19-226 |
2.71e-04 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 43.66 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 19 DKVAIIYDSPVTDTKA-TITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLifggfask 97
Cdd:cd17647 3 ERTCVVETPSLNSSKTrSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSV-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 98 elssrIDHAKPkvvvtasfgiePGRKVEYMPILEEAMRIGQHKPDKVLiynrpnmetvplasgrdldwdeemakaqSQDC 177
Cdd:cd17647 75 -----IDPAYP-----------PARQNIYLGVAKPRGLIVIRAAGVVV----------------------------GPDS 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1191882763 178 VPVLSehplyilYTSGTTGLPKGVVRPTGGYAVMLNWtMSSIYGLKPGE 226
Cdd:cd17647 111 NPTLS-------FTSGSEGIPKGVLGRHFSLAYYFPW-MAKRFNLSEND 151
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
37-202 |
3.89e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 43.47 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 37 TYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVV----- 111
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVfveek 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 112 -VTASFGIEPGrKVEYMpilEEAMRIGQHKPDKvliynRPNMETVPLASgrdLDWDE--EMAKAQSQDcVPVLSEHPL-Y 187
Cdd:PLN02614 161 kISELFKTCPN-STEYM---KTVVSFGGVSREQ-----KEEAETFGLVI---YAWDEflKLGEGKQYD-LPIKKKSDIcT 227
|
170
....*....|....*
gi 1191882763 188 ILYTSGTTGLPKGVV 202
Cdd:PLN02614 228 IMYTSGTTGDPKGVM 242
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
368-548 |
5.41e-04 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 42.86 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 368 GKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMdEEGYVYVMSRV 447
Cdd:cd05908 317 GKPIDETDIRICDEDNKILPDGYIGHIQIR---GKNVTPGYYNNPEATAKVFTDD--GWLKTGDLGFI-RNGRLVITGRE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882763 448 DDVI-----NVAGHRISAGAIEESLLSHGTVADCAVVGKEDplKGHVPLALCVLRKDIN--ITEGQvleEIVQHVRQSIG 520
Cdd:cd05908 391 KDIIfvngqNVYPHDIERIAEELEGVELGRVVACGVNNSNT--RNEEIFCFIEHRKSEDdfYPLGK---KIKKHLNKRGG 465
|
170 180
....*....|....*....|....*...
gi 1191882763 521 pvAAFRKAVFVQQLPKTRSGKIPRAALS 548
Cdd:cd05908 466 --WQINEVLPIRRIPKTTSGKVKRYELA 491
|
|
| |
