|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
7-547 |
0e+00 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 1107.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 7 LPSYASGISEVPLLGDTIGDNFDRTVAAFGDRDALVDRAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAE 86
Cdd:PRK08315 1 GLSYVRGPTDVPLLEQTIGQLLDRTAARYPDREALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 87 WTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVASDKFKTSDYPAMVEEVREKCAR-------------LEHV 153
Cdd:PRK08315 81 WVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAADGFKDSDYVAMLYELAPELATcepgqlqsarlpeLRRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 154 VVLGGE------SWQELMDAGRRGDPAQLAHLRAGLSADDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEE 227
Cdd:PRK08315 161 IFLGDEkhpgmlNFDELLALGRAVDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 228 DKVCIPVPFYHCFGMVMGNLACTSHGACMVIPAPAFDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTG 307
Cdd:PRK08315 241 DRLCIPVPLYHCFGMVLGNLACVTHGATMVYPGEGFDPLATLAAVEEERCTALYGVPTMFIAELDHPDFARFDLSSLRTG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 308 IMAGSPCPVEVMKQVIDRMGMAEVSICYGMTETSPVSTQTRADDSIERRVSTVGRVGPHLEVKVVDPESGLTVPRGEPGE 387
Cdd:PRK08315 321 IMAGSPCPIEVMKRVIDKMHMSEVTIAYGMTETSPVSTQTRTDDPLEKRVTTVGRALPHLEVKIVDPETGETVPRGEQGE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 388 LCTRGYSVMLGYWEQPDKTAEAIDAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQV 467
Cdd:PRK08315 401 LCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 468 IGVPDEKYGEELMAWVRMREGASpLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMREKSITLLGLETAA 547
Cdd:PRK08315 481 VGVPDEKYGEEVCAWIILRPGAT-LTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMIEELGLQAAK 559
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
8-543 |
0e+00 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 851.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 8 PSYASGISEVPLLGDTIGDNFDRTVAAFGDRDALVDRAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEW 87
Cdd:PRK12583 4 PSYYQGGGDKPLLTQTIGDAFDATVARFPDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 88 TFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVASDKFKTSDYPAMVEEV-------------REKCARLEHVV 154
Cdd:PRK12583 84 LLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADAFKTSDYHAMLQELlpglaegqpgalaCERLPELRGVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 155 VLGGE------SWQELMDAGRRGDPAQLAHLRAGLSADDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEED 228
Cdd:PRK12583 164 SLAPApppgflAWHELQARGETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 229 KVCIPVPFYHCFGMVMGNLACTSHGACMVIPAPAFDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGI 308
Cdd:PRK12583 244 RLCVPVPLYHCFGMVLANLGCMTVGACLVYPNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 309 MAGSPCPVEVMKQVIDRMGMAEVSICYGMTETSPVSTQTRADDSIERRVSTVGRVGPHLEVKVVDPEsGLTVPRGEPGEL 388
Cdd:PRK12583 324 MAGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSPVSLQTTAADDLERRVETVGRTQPHLEVKVVDPD-GATVPRGEIGEL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 389 CTRGYSVMLGYWEQPDKTAEAIDAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVI 468
Cdd:PRK12583 403 CTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVF 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522130465 469 GVPDEKYGEELMAWVRMREGASpLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMREKSITLLGL 543
Cdd:PRK12583 483 GVPDEKYGEEIVAWVRLHPGHA-ASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREISIEELAL 556
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
186-534 |
0e+00 |
|
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: 682.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 186 DDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGACMVIPAPAFDP 265
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSPSFDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 266 RATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSICYGMTETSPVST 345
Cdd:cd05917 82 LAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETSPVST 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 346 QTRADDSIERRVSTVGRVGPHLEVKVVDPESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAARWMHTGDLAVMD 425
Cdd:cd05917 162 QTRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 426 GDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASPlTAEKVREFCSGKL 505
Cdd:cd05917 242 EDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAEL-TEEDIKAYCKGKI 320
|
330 340
....*....|....*....|....*....
gi 522130465 506 AHYKIPRYVHVVDEFPMTVTGKVRKVEMR 534
Cdd:cd05917 321 AHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
24-535 |
0e+00 |
|
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: 558.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 24 IGDNFDRTVAAFGDRDALVDraAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVN 103
Cdd:COG0318 1 LADLLRRAAARHPDRPALVF--GGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 104 INPAYRSHELEYVLDQAGIRLLVAsdkfktsdypamveevrekcarlehvvvlggeswqelmdagrrgdpaqlahlragl 183
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVT-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 184 saddpINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGACMVIPaPAF 263
Cdd:COG0318 103 -----ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLL-PRF 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 264 DPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGmAEVSICYGMTETSPV 343
Cdd:COG0318 177 DPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFG-VRIVEGYGLTETSPV 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 344 STqTRADDSIERRVSTVGRVGPHLEVKVVDPEsGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIdAARWMHTGDLAV 423
Cdd:COG0318 256 VT-VNPEDPGERRPGSVGRPLPGVEVRIVDED-GRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGR 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 424 MDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASpLTAEKVREFCSG 503
Cdd:COG0318 333 LDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAE-LDAEELRAFLRE 411
|
490 500 510
....*....|....*....|....*....|..
gi 522130465 504 KLAHYKIPRYVHVVDEFPMTVTGKVRKVEMRE 535
Cdd:COG0318 412 RLARYKVPRRVEFVDELPRTASGKIDRRALRE 443
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
23-536 |
5.41e-170 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 491.34 E-value: 5.41e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 23 TIGDNFDRTVAAFGDRDALVDraAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILV 102
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVF--GDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 103 NINPAYRSHELEYVLDQAGIRLLVASDKFKTSDYPAMveevrEKCARLEHVVVLGGE----------SWQELMdagRRGD 172
Cdd:PRK07656 84 PLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSAT-----TRLPALEHVVICETEeddphtekmkTFTDFL---AAGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 173 PAQLAhlrAGLSADDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSH 252
Cdd:PRK07656 156 PAERA---PEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 253 GACMvIPAPAFDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVS 332
Cdd:PRK07656 233 GATI-LPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 333 ICYGMTETSPVSTQTRADDSIERRVSTVGRVGPHLEVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDA 412
Cdd:PRK07656 312 TGYGLSEASGVTTFNRLDDDRKTVAGTIGTAIAGVENKIVN-ELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 413 ARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGAsPL 492
Cdd:PRK07656 391 DGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGA-EL 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 522130465 493 TAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMREK 536
Cdd:PRK07656 470 TEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
24-534 |
1.48e-157 |
|
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: 457.80 E-value: 1.48e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 24 IGDNFDRTVAAFGDRDALVDRaaGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVN 103
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFM--GRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 104 INPAYRSHELEYVLDQAGIRLLVAsdkfktsdypamveevrekcarlehvvvlgGESWQELMDAGRRGDPaqlahlRAGL 183
Cdd:cd05936 79 LNPLYTPRELEHILNDSGAKALIV------------------------------AVSFTDLLAAGAPLGE------RVAL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 184 SADDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCN--YTEEDKVCIPVPFYHCFGMVMGNLACTSHGACMVIpAP 261
Cdd:cd05936 123 TPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEdlLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVL-IP 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 262 AFDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGmAEVSICYGMTETS 341
Cdd:cd05936 202 RFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTG-VPIVEGYGLTETS 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 342 PVSTQTRADDsiERRVSTVGRVGPHLEVKVVDPEsGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAArWMHTGDL 421
Cdd:cd05936 281 PVVAVNPLDG--PRKPGSIGIPLPGTEVKIVDDD-GEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDG-WLRTGDI 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 422 AVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASpLTAEKVREFC 501
Cdd:cd05936 357 GYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGAS-LTEEEIIAFC 435
|
490 500 510
....*....|....*....|....*....|...
gi 522130465 502 SGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMR 534
Cdd:cd05936 436 REQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
28-530 |
1.22e-149 |
|
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: 436.66 E-value: 1.22e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 28 FDRTVAAFGDRDALVDRaaGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPA 107
Cdd:cd17631 1 LRRRARRHPDRTALVFG--GRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 108 YRSHELEYVLDQAGIRLLVasdkfktsdypamveevrekcarlehvvvlggeswqelmdagrrgdpaqlahlraglsaDD 187
Cdd:cd17631 79 LTPPEVAYILADSGAKVLF-----------------------------------------------------------DD 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 188 PINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGACMVIPaPAFDPRA 267
Cdd:cd17631 100 LALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVIL-RKFDPET 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 268 TLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMgmAEVSICYGMTETSPVSTQT 347
Cdd:cd17631 179 VLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQARG--VKFVQGYGMTETSPGVTFL 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 348 RADDSIERRVStVGRVGPHLEVKVVDPEsGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAArWMHTGDLAVMDGD 427
Cdd:cd17631 257 SPEDHRRKLGS-AGRPVFFVEVRIVDPD-GREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDG-WFHTGDLGRLDED 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 428 GYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGAsPLTAEKVREFCSGKLAH 507
Cdd:cd17631 334 GYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGA-ELDEDELIAHCRERLAR 412
|
490 500
....*....|....*....|...
gi 522130465 508 YKIPRYVHVVDEFPMTVTGKVRK 530
Cdd:cd17631 413 YKIPKSVEFVDALPRNATGKILK 435
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
28-443 |
1.63e-145 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 425.19 E-value: 1.63e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 28 FDRTVAAFGDRDALVDrAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPA 107
Cdd:pfam00501 1 LERQAARTPDKTALEV-GEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 108 YRSHELEYVLDQAGIRLLVASDKFKtsdyPAMVEEVREKCARLEHVVVLGGESWQELMDAGRRGDPAQLAHLR-AGLSAD 186
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDALK----LEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPpPPPDPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 187 DPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELC----NYTEEDKVCIPVPFYHCFGMVMGNLACTSHGACMVI--PA 260
Cdd:pfam00501 156 DLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLppGF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 261 PAFDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAeVSICYGMTET 340
Cdd:pfam00501 236 PALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTET 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 341 SPVSTQTRADDSIERRVSTVGRVGPHLEVKVVDPESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAARWMHTGD 420
Cdd:pfam00501 315 TGVVTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGD 394
|
410 420
....*....|....*....|...
gi 522130465 421 LAVMDGDGYVNITGRIKDMVIRG 443
Cdd:pfam00501 395 LGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
23-536 |
2.08e-144 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 426.14 E-value: 2.08e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 23 TIGDNFDRTVAAFGDRDALVDRaaGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILV 102
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYFD--GRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 103 NINPAYRSHELEYVLDQAGIRLLVASDKFKtsdypAMVEEVREKCARLEHVVVLGGE----------SWQELMDAGRRGD 172
Cdd:PRK06187 85 PINIRLKPEEIAYILNDAEDRVVLVDSEFV-----PLLAAILPQLPTVRTVIVEGDGpaaplapevgEYEELLAAASDTF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 173 PAQlahlraGLSADDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLAcTSH 252
Cdd:PRK06187 160 DFP------DIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLA-LMA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 253 GACMVIPApAFDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVS 332
Cdd:PRK06187 233 GAKQVIPR-RFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 333 IcYGMTETSPVSTQTRADDSIERRVS---TVGRVGPHLEVKVVDPEsGLTVPR--GEPGELCTRGYSVMLGYWEQPDKTA 407
Cdd:PRK06187 312 G-YGMTETSPVVSVLPPEDQLPGQWTkrrSAGRPLPGVEARIVDDD-GDELPPdgGEVGEIIVRGPWLMQGYWNRPEATA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 408 EAIDAArWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMRE 487
Cdd:PRK06187 390 ETIDGG-WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKP 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 522130465 488 GAsPLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMREK 536
Cdd:PRK06187 469 GA-TLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQ 516
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
22-535 |
4.05e-134 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 400.08 E-value: 4.05e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 22 DTIGDNFDRTVAAFGDRDALVDRAAggRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAIL 101
Cdd:PRK08316 11 QTIGDILRRSARRYPDKTALVFGDR--SWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 102 VNINPAYRSHELEYVLDQAGIRLLVASdkfktsdyPAMVEEVREKCARLEHVVVL---------GGESWQELMDAGRRGD 172
Cdd:PRK08316 89 VPVNFMLTGEELAYILDHSGARAFLVD--------PALAPTAEAALALLPVDTLIlslvlggreAPGGWLDFADWAEAGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 173 PAQLAhlrAGLSADDPINIQYTSGTTGFPKGATLSHHNILNNgyFVGEL--CNYTEEDKVCIPVPFYHCFGM---VMGNL 247
Cdd:PRK08316 161 VAEPD---VELADDDLAQILYTSGTESLPKGAMLTHRALIAE--YVSCIvaGDMSADDIPLHALPLYHCAQLdvfLGPYL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 248 ACtshGACMVI-PAPafDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRM 326
Cdd:PRK08316 236 YV---GATNVIlDAP--DPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 327 GMAEVSICYGMTETSPVSTQTRADDsIERRVSTVGRVGPHLEVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKT 406
Cdd:PRK08316 311 PGLRFYNCYGQTEIAPLATVLGPEE-HLRRPGSAGRPVLNVETRVVD-DDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 407 AEAIdAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMR 486
Cdd:PRK08316 389 AEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPK 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 522130465 487 EGASpLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMRE 535
Cdd:PRK08316 468 AGAT-VTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRE 515
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
187-529 |
5.16e-128 |
|
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: 377.78 E-value: 5.16e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 187 DPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMvMGNLACTSHGACMVIPaPAFDPR 266
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGL-FGLLGALLAGGTVVLL-PKFDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 267 ATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGmAEVSICYGMTETSPVSTQ 346
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPG-IKLVNGYGLTETGGTVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 347 TRADDsIERRVSTVGRVGPHLEVKVVDPEsGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAiDAARWMHTGDLAVMDG 426
Cdd:cd04433 158 GPPDD-DARKPGSVGRPVPGVEVRIVDPD-GGELPPGEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 427 DGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGAsPLTAEKVREFCSGKLA 506
Cdd:cd04433 235 DGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGA-DLDAEELRAHVRERLA 313
|
330 340
....*....|....*....|...
gi 522130465 507 HYKIPRYVHVVDEFPMTVTGKVR 529
Cdd:cd04433 314 PYKVPRRVVFVDALPRTASGKID 336
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
21-535 |
6.80e-126 |
|
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: 379.10 E-value: 6.80e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 21 GDTIGDNFDRTVAAFGDRDALVDRaaGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAI 100
Cdd:COG1021 24 GETLGDLLRRRAERHPDRIAVVDG--ERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 101 LVNINPAYRSHELEYVLDQAGIRLLVASDKFKTSDYPAMVEEVREKCARLEHVVVLG----GESWQELMDAGRRGDPaql 176
Cdd:COG1021 102 PVFALPAHRRAEISHFAEQSEAVAYIIPDRHRGFDYRALARELQAEVPSLRHVLVVGdageFTSLDALLAAPADLSE--- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 177 ahlrAGLSADDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDK--VCIPVPfyHCFGM-VMGNLACTSHG 253
Cdd:COG1021 179 ----PRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVylAALPAA--HNFPLsSPGVLGVLYAG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 254 ACMVIpAPAFDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRM------- 326
Cdd:COG1021 253 GTVVL-APDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALgctlqqv 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 327 -GMAEVSICYgmtetspvstqTRADDSIERRVSTVGR-VGPHLEVKVVDPEsGLTVPRGEPGELCTRGYSVMLGYWEQPD 404
Cdd:COG1021 332 fGMAEGLVNY-----------TRLDDPEEVILTTQGRpISPDDEVRIVDED-GNPVPPGEVGELLTRGPYTIRGYYRAPE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 405 KTAEAIDAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVR 484
Cdd:COG1021 400 HNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVV 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 522130465 485 MREgaSPLTAEKVREFCSGK-LAHYKIPRYVHVVDEFPMTVTGKVRKVEMRE 535
Cdd:COG1021 480 PRG--EPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRA 529
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
40-528 |
5.75e-117 |
|
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: 354.60 E-value: 5.75e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 40 ALVDRAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQ 119
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 120 AGIRLLVASdkfktsdyPAMVEEVREKCARL---EHVVVLGGES----WQELMDAGRRGDPAQLAHLRAGLSADDPINIQ 192
Cdd:cd05911 81 SKPKVIFTD--------PDGLEKVKEAAKELgpkDKIIVLDDKPdgvlSIEDLLSPTLGEEDEDLPPPLKDGKDDTAAIL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 193 YTSGTTGFPKGATLSHHNILNNGYFVG--ELCNYTEEDKVCIPVPFYHCFGMVMGnLACTSHGACMVIpAPAFDPRATLE 270
Cdd:cd05911 153 YSSGTTGLPKGVCLSHRNLIANLSQVQtfLYGNDGSNDVILGFLPLYHIYGLFTT-LASLLNGATVII-MPKFDSELFLD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 271 AVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSICYGMTETSPVSTQTRAD 350
Cdd:cd05911 231 LIEKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVNPDG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 351 DSierRVSTVGRVGPHLEVKVVDPESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAARWMHTGDLAVMDGDGYV 430
Cdd:cd05911 311 DD---KPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 431 NITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASpLTAEKVREFCSGKLAHYKI 510
Cdd:cd05911 388 YIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEK-LTEKEVKDYVAKKVASYKQ 466
|
490
....*....|....*....
gi 522130465 511 PRY-VHVVDEFPMTVTGKV 528
Cdd:cd05911 467 LRGgVVFVDEIPKSASGKI 485
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
28-535 |
1.58e-115 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 353.65 E-value: 1.58e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 28 FDRTVAAFGDRDALVDRAAGG---RWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNI 104
Cdd:COG0365 15 LDRHAEGRGDKVALIWEGEDGeerTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 105 NPAYRSHELEYVLDQAGIRLLVASD----KFKTSDYPAMVEEVREKCARLEHVVVLGGE----------SWQELMD-AGR 169
Cdd:COG0365 95 FPGFGAEALADRIEDAEAKVLITADgglrGGKVIDLKEKVDEALEELPSLEHVIVVGRTgadvpmegdlDWDELLAaASA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 170 RGDPAQLAhlraglsADDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGEL-CNYTEEDKV-CIPVPF--YHCFGMVMG 245
Cdd:COG0365 175 EFEPEPTD-------ADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYvLDLKPGDVFwCTADIGwaTGHSYIVYG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 246 NLActsHGACMVI--PAPAF-DPRATLEAVAAERCTSLYGVPT---MFIAELNHPdFGEFDLSSLRTGIMAGSPCPVEVM 319
Cdd:COG0365 248 PLL---NGATVVLyeGRPDFpDPGRLWELIEKYGVTVFFTAPTairALMKAGDEP-LKKYDLSSLRLLGSAGEPLNPEVW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 320 KQVIDRMGMAEVSIcYGMTET-SPVSTQTRADDSierRVSTVGRVGPHLEVKVVDPEsGLTVPRGEPGELCTRGY--SVM 396
Cdd:COG0365 324 EWWYEAVGVPIVDG-WGQTETgGIFISNLPGLPV---KPGSMGKPVPGYDVAVVDED-GNPVPPGEEGELVIKGPwpGMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 397 LGYWEQPDKTAEAI--DAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEK 474
Cdd:COG0365 399 RGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEI 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522130465 475 YGEELMAWVRMREG--ASPLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMRE 535
Cdd:COG0365 479 RGQVVKAFVVLKPGvePSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRK 541
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
23-535 |
5.85e-114 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 348.97 E-value: 5.85e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 23 TIGDNFDRTVAAFGDRDALVDRAAGG----RWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIG 98
Cdd:PRK13295 25 TINDDLDACVASCPDKTAVTAVRLGTgaprRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 99 AILVNINPAYRSHELEYVLDQAGIRLLVASDKFKTSDYPAMVEEVREKCARLEHVVVLGGE---SWQELMDAGR----RG 171
Cdd:PRK13295 105 AVLNPLMPIFRERELSFMLKHAESKVLVVPKTFRGFDHAAMARRLRPELPALRHVVVVGGDgadSFEALLITPAweqePD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 172 DPAQLAHLRAGlsADDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTS 251
Cdd:PRK13295 185 APAILARLRPG--PDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVM 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 252 HGACMVIpAPAFDPRATLEAVAAERCTSLYGvPTMFIAEL-NHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAE 330
Cdd:PRK13295 263 LGATAVL-QDIWDPARAAELIRTEGVTFTMA-STPFLTDLtRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 331 VSiCYGMTETSPVSTqTRADDSIERRVSTVGRVGPHLEVKVVDPEsGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEai 410
Cdd:PRK13295 341 VS-AWGMTENGAVTL-TKLDDPDERASTTDGCPLPGVEVRVVDAD-GAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGT-- 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 411 DAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGAS 490
Cdd:PRK13295 416 DADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQS 495
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 522130465 491 pLTAEKVREFC-SGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMRE 535
Cdd:PRK13295 496 -LDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKIQKFRLRE 540
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
3-542 |
3.18e-110 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 340.44 E-value: 3.18e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 3 DAPALPSYASGIS-EVPLLGDTIGDNFDRTVAAFGDRDALvdRAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWS 81
Cdd:PRK05605 12 DKPWLQSYAPWTPhDLDYGDTTLVDLYDNAVARFGDRPAL--DFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 82 PNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVASDKFKtsdypAMVEEVREKcARLEHVV------- 154
Cdd:PRK05605 90 PNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVA-----PTVERLRRT-TPLETIVsvnmiaa 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 155 --------------------------VLGGESWQELMDAGRRGDPAQLAHLRAglSADDPINIQYTSGTTGFPKGATLSH 208
Cdd:PRK05605 164 mpllqrlalrlpipalrkaraaltgpAPGTVPWETLVDAAIGGDGSDVSHPRP--TPDDVALILYTSGTTGKPKGAQLTH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 209 HNILNNG----YFVGELCNYTEedKVCIPVPFYHCFGMVMGNLACTSHGACMVIpAPAFDPRATLEAVAAERCTSLYGVP 284
Cdd:PRK05605 242 RNLFANAaqgkAWVPGLGDGPE--RVLAALPMFHAYGLTLCLTLAVSIGGELVL-LPAPDIDLILDAMKKHPPTWLPGVP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 285 TMF--IAELNHPDfgEFDLSSLRTGIMAGSPCPVEVMKQVIDRMG--MAEvsiCYGMTETSPVSTQTRADDSieRRVSTV 360
Cdd:PRK05605 319 PLYekIAEAAEER--GVDLSGVRNAFSGAMALPVSTVELWEKLTGglLVE---GYGLTETSPIIVGNPMSDD--RRPGYV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 361 GRVGPHLEVKVVDPES-GLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIdAARWMHTGDLAVMDGDGYVNITGRIKDM 439
Cdd:PRK05605 392 GVPFPDTEVRIVDPEDpDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKEL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 440 VIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASpLTAEKVREFCSGKLAHYKIPRYVHVVDE 519
Cdd:PRK05605 471 IITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAA-LDPEGLRAYCREHLTRYKVPRRFYHVDE 549
|
570 580
....*....|....*....|...
gi 522130465 520 FPMTVTGKVRKVEMREKSITLLG 542
Cdd:PRK05605 550 LPRDQLGKVRRREVREELLEKLG 572
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
49-535 |
3.12e-108 |
|
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: 330.50 E-value: 3.12e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 49 RWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVAS 128
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 129 DKFKTSDYPAMveevrekcarlehvvvlggeswqelmdagrRGDPAQLAhlraglsaddpiniqYTSGTTGFPKGATLSH 208
Cdd:cd05903 81 ERFRQFDPAAM------------------------------PDAVALLL---------------FTSGTTGEPKGVMHSH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 209 HNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGACMVIpAPAFDPRATLEAVAAERCTSLYGvPTMFI 288
Cdd:cd05903 116 NTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVL-QDIWDPDKALALMREHGVTFMMG-ATPFL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 289 AEL-NHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGmAEVSICYGMTETSPVSTQTRADDSiERRVSTVGRVGPHL 367
Cdd:cd05903 194 TDLlNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLG-AKVCSAYGSTECPGAVTSITPAPE-DRRLYTDGRPLPGV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 368 EVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAArWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENL 447
Cdd:cd05903 272 EIKVVD-DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAPEG-WFRTGDLARLDEDGYLRITGRSKDIIIRGGENI 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 448 YPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASPlTAEKVREFCSGK-LAHYKIPRYVHVVDEFPMTVTG 526
Cdd:cd05903 350 PVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALL-TFDELVAYLDRQgVAKQYWPERLVHVDDLPRTPSG 428
|
....*....
gi 522130465 527 KVRKVEMRE 535
Cdd:cd05903 429 KVQKFRLRE 437
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
22-550 |
4.99e-108 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 333.64 E-value: 4.99e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 22 DTIGDNFDRTVAAFGDRDALVDRAaGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAIL 101
Cdd:PRK06087 23 ASLADYWQQTARAMPDKIAVVDNH-GASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 102 VNINPAYRSHELEYVLDQAGIRLLVASDKFKTSDYPAMVEEVREKCARLEHVVvlggeswqeLMDAGRRGDPA-QLAHLR 180
Cdd:PRK06087 102 VPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVDLILPLQNQLPQLQQIV---------GVDKLAPATSSlSLSQII 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 181 AG---------LSADDPINIQYTSGTTGFPKGATLSHHNIL-NNGYFVGELcNYTEEDKVCIPVPFYHCFGMVMGNLACT 250
Cdd:PRK06087 173 ADyeplttaitTHGDELAAVLFTSGTEGLPKGVMLTHNNILaSERAYCARL-NLTWQDVFMMPAPLGHATGFLHGVTAPF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 251 SHGACMVIpAPAFDPRATLEAVAAERCTSLYGVpTMFIAE-LNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRmGMA 329
Cdd:PRK06087 252 LIGARSVL-LDIFTPDACLALLEQQRCTCMLGA-TPFIYDlLNLLEKQPADLSALRFFLCGGTTIPKKVARECQQR-GIK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 330 EVSiCYGMTETSPvSTQTRADDSIERRVSTVGRVGPHLEVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEA 409
Cdd:PRK06087 329 LLS-VYGSTESSP-HAVVNLDDPLSRFMHTDGYAAAGVEIKVVD-EARKTLPPGCEGEEASRGPNVFMGYLDEPELTARA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 410 IDAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGA 489
Cdd:PRK06087 406 LDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPH 485
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522130465 490 SPLTAEKVREF-CSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMREKSITLLGLETAAATK 550
Cdd:PRK06087 486 HSLTLEEVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDIMRRLTQDVCEEIE 547
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
37-535 |
6.65e-108 |
|
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: 331.58 E-value: 6.65e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 37 DRDALVDRAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYV 116
Cdd:cd05926 2 DAPALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 117 LDQAGIRLLVASdkfKTSDYPAMVEEVREKCARLEhvvvLGGESwqelMDAGRRGDPAQLAHLRAGLSA---------DD 187
Cdd:cd05926 82 LADLGSKLVLTP---KGELGPASRAASKLGLAILE----LALDV----GVLIRAPSAESLSNLLADKKNaksegvplpDD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 188 PINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGACMVIPaPAFDPRA 267
Cdd:cd05926 151 LALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLP-PRFSAST 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 268 TLEAVAAERCTSLYGVPTMFIAELNHPD-FGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGmAEVSICYGMTETSPVSTQ 346
Cdd:cd05926 230 FWPDVRDYNATWYTAVPTIHQILLNRPEpNPESPPPKLRFIRSCSASLPPAVLEALEATFG-APVLEAYGMTEAAHQMTS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 347 TRADdSIERRVSTVGR-VGPhlEVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAARWMHTGDLAVMD 425
Cdd:cd05926 309 NPLP-PGPRKPGSVGKpVGV--EVRILD-EDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 426 GDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASPlTAEKVREFCSGKL 505
Cdd:cd05926 385 ADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASV-TEEELRAFCRKHL 463
|
490 500 510
....*....|....*....|....*....|
gi 522130465 506 AHYKIPRYVHVVDEFPMTVTGKVRKVEMRE 535
Cdd:cd05926 464 AAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
32-530 |
1.27e-107 |
|
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: 331.51 E-value: 1.27e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 32 VAAFGDRDALVDRAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSH 111
Cdd:cd05904 15 ASAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 112 ELEYVLDQAGIRLLVAsdkfktsdypamVEEVREKCARLEHVVVLGGESWQELMDAGRRGDPA-QLAHLRAGLSADDPIN 190
Cdd:cd05904 95 EIAKQVKDSGAKLAFT------------TAELAEKLASLALPVVLLDSAEFDSLSFSDLLFEAdEAEPPVVVIKQDDVAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 191 IQYTSGTTGFPKGATLSHHNILNN--GYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGACMVIpAPAFDPRAT 268
Cdd:cd05904 163 LLYSSGTTGRSKGVMLTHRNLIAMvaQFVAGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVV-MPRFDLEEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 269 LEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSICYGMTETSPVSTQTR 348
Cdd:cd05904 242 LAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTGVVAMCF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 349 ADDSIERRVSTVGRVGPHLEVKVVDPESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAARWMHTGDLAVMDGDG 428
Cdd:cd05904 322 APEKDRAKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 429 YVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVrMREGASPLTAEKVREFCSGKLAHY 508
Cdd:cd05904 402 YLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFV-VRKPGSSLTEDEIMDFVAKQVAPY 480
|
490 500
....*....|....*....|...
gi 522130465 509 KIPRYVHVVDEFPMTVTGKV-RK 530
Cdd:cd05904 481 KKVRKVAFVDAIPKSPSGKIlRK 503
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
37-535 |
1.02e-104 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 323.74 E-value: 1.02e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 37 DRDALVdrAAGGRWTYRELAGEVTALALGLVAR-GIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEY 115
Cdd:PRK06839 17 DRIAII--TEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 116 VLDQAGIRLLVASdkfktSDYPAMVEEVREKcARLEHVVVLggESWQELMDAGRRG-DPAqlahlraglSADDPINIQYT 194
Cdd:PRK06839 95 QLKDSGTTVLFVE-----KTFQNMALSMQKV-SYVQRVISI--TSLKEIEDRKIDNfVEK---------NESASFIICYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 195 SGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGACMVIPApAFDPRATLEAVAA 274
Cdd:PRK06839 158 SGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPR-KFEPTKALSMIEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 275 ERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDR---MGMAevsicYGMTETSPVSTQTRADD 351
Cdd:PRK06839 237 HKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDRgflFGQG-----FGMTETSPTVFMLSEED 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 352 SiERRVSTVGRVGPHLEVKVVDPESGlTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAArWMHTGDLAVMDGDGYVN 431
Cdd:PRK06839 312 A-RRKVGSIGKPVLFCDYELIDENKN-KVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDG-WLCTGDLARVDEDGFVY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 432 ITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASpLTAEKVREFCSGKLAHYKIP 511
Cdd:PRK06839 389 IVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSV-LIEKDVIEHCRLFLAKYKIP 467
|
490 500
....*....|....*....|....
gi 522130465 512 RYVHVVDEFPMTVTGKVRKVEMRE 535
Cdd:PRK06839 468 KEIVFLKELPKNATGKIQKAQLVN 491
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
37-535 |
1.78e-104 |
|
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: 321.16 E-value: 1.78e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 37 DRDALVDraAGGRWTYRELAGEVTALALGLVARG-IGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEY 115
Cdd:cd05941 1 DRIAIVD--DGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 116 VLDQAGIRLLVAsdkfktsdyPAMveevrekcarlehvvvlggeswqelmdagrrgdpaqlahlraglsaddpinIQYTS 195
Cdd:cd05941 79 VITDSEPSLVLD---------PAL---------------------------------------------------ILYTS 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 196 GTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGnLACT--SHGACMVIPApaFDPRATLEAVA 273
Cdd:cd05941 99 GTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNA-LLCPlfAGASVEFLPK--FDPKEVAISRL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 274 AERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAG--------SPCPVEVMKQVIDRMGMAEVSIcYGMTETSpVST 345
Cdd:cd05941 176 MPSITVFMGVPTIYTRLLQYYEAHFTDPQFARAAAAERlrlmvsgsAALPVPTLEEWEAITGHTLLER-YGMTEIG-MAL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 346 QTRADDsiERRVSTVGRVGPHLEVKVVDPESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAARWMHTGDLAVMD 425
Cdd:cd05941 254 SNPLDG--ERRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVD 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 426 GDGYVNITGRIKDMVI-RGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASPLTAEKVREFCSGK 504
Cdd:cd05941 332 EDGYYWILGRSSVDIIkSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLEELKEWAKQR 411
|
490 500 510
....*....|....*....|....*....|.
gi 522130465 505 LAHYKIPRYVHVVDEFPMTVTGKVRKVEMRE 535
Cdd:cd05941 412 LAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
47-534 |
5.96e-104 |
|
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: 319.24 E-value: 5.96e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 47 GGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLV 126
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 127 AsdkfktsdypamveevrekcarlehvvvlggeswqelmdagrrgdpaqlahlraglsadDPINIQYTSGTTGFPKGATL 206
Cdd:cd05934 81 V-----------------------------------------------------------DPASILYTSGTTGPPKGVVI 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 207 SHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGACMVIpAPAFDPRATLEAVAAERCTSLYGVPTM 286
Cdd:cd05934 102 THANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVL-LPRFSASRFWSDVRRYGATVTNYLGAM 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 287 FIAELNHPDFGEFDLSSLRTGimAGSPCPVEVMKQVIDRMGMAEVSIcYGMTETSPVSTQTRADDsieRRVSTVGRVGPH 366
Cdd:cd05934 181 LSYLLAQPPSPDDRAHRLRAA--YGAPNPPELHEEFEERFGVRLLEG-YGMTETIVGVIGPRDEP---RRPGSIGRPAPG 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 367 LEVKVVDPEsGLTVPRGEPGELCTR---GYSVMLGYWEQPDKTAEAIdAARWMHTGDLAVMDGDGYVNITGRIKDMVIRG 443
Cdd:cd05934 255 YEVRIVDDD-GQELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRR 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 444 GENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGAsPLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMT 523
Cdd:cd05934 333 GENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGE-TLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKT 411
|
490
....*....|.
gi 522130465 524 VTGKVRKVEMR 534
Cdd:cd05934 412 PTEKVAKAQLR 422
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
21-536 |
1.45e-98 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 308.45 E-value: 1.45e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 21 GDTIGDNFDRTVAAFGDRDALVDraAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAI 100
Cdd:PRK06188 11 GATYGHLLVSALKRYPDRPALVL--GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 101 LVNINP--AYRSHelEYVLDQAGIRLLVASDkfktSDYPAMVEEVREKCARLEHVVVLG-GESWQELMDAGRRGDPaqlA 177
Cdd:PRK06188 89 RTALHPlgSLDDH--AYVLEDAGISTLIVDP----APFVERALALLARVPSLKHVLTLGpVPDGVDLLAAAAKFGP---A 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 178 HLRAGLSADDPINIQYTSGTTGFPKGATLSHHNILnnGYFVGELCNYT--EEDKVCIPVPFYHCFG-MVMGNLActsHGA 254
Cdd:PRK06188 160 PLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIA--TMAQIQLAEWEwpADPRFLMCTPLSHAGGaFFLPTLL---RGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 255 CMVIpAPAFDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMG--MAEVs 332
Cdd:PRK06188 235 TVIV-LAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGpiFAQY- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 333 icYGMTET-SPVSTQTRAD--DSIERRVSTVGRVGPHLEVKVVDPEsGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEA 409
Cdd:PRK06188 313 --YGQTEApMVITYLRKRDhdPDDPKRLTSCGRPTPGLRVALLDED-GREVAQGEVGEICVRGPLVMDGYWNRPEETAEA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 410 IdAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGA 489
Cdd:PRK06188 390 F-RDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGA 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 522130465 490 SPLTAEKVREFCSGKLAHYKiPRYVHVVDEFPMTVTGKVRKVEMREK 536
Cdd:PRK06188 469 AVDAAELQAHVKERKGSVHA-PKQVDFVDSLPLTALGKPDKKALRAR 514
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
27-536 |
4.17e-98 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 307.35 E-value: 4.17e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 27 NFDRTVAA-FGDRDALVDRAagGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNIN 105
Cdd:PRK07470 11 HFLRQAARrFPDRIALVWGD--RSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 106 PAYRSHELEYVLDQAGIRLLVASdkfktSDYPAMVEEVREKCARLEHVVVLG----GESWQELM--DAGRRGDPAQLAHl 179
Cdd:PRK07470 89 FRQTPDEVAYLAEASGARAMICH-----ADFPEHAAAVRAASPDLTHVVAIGgaraGLDYEALVarHLGARVANAAVDH- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 180 raglsaDDPINIQYTSGTTGFPKGATLSHHN---ILNNgyfvgELCNY----TEEDKVCIPVPFYHcfGMVMGNLACTSH 252
Cdd:PRK07470 163 ------DDPCWFFFTSGTTGRPKAAVLTHGQmafVITN-----HLADLmpgtTEQDASLVVAPLSH--GAGIHQLCQVAR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 253 GACMVI-PAPAFDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMG---- 327
Cdd:PRK07470 230 GAATVLlPSERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGkvlv 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 328 ----MAEVSICygMTETSPVSTQtrADDSIERRVSTVGRVGPHLEVKVVDPEsGLTVPRGEPGELCTRGYSVMLGYWEQP 403
Cdd:PRK07470 310 qyfgLGEVTGN--ITVLPPALHD--AEDGPDARIGTCGFERTGMEVQIQDDE-GRELPPGETGEICVIGPAVFAGYYNNP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 404 DKTAEAIDAArWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWV 483
Cdd:PRK07470 385 EANAKAFRDG-WFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVC 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 522130465 484 RMREGAsPLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMREK 536
Cdd:PRK07470 464 VARDGA-PVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREE 515
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
28-536 |
3.37e-97 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 304.49 E-value: 3.37e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 28 FDRTVAAFGDRDALVDRAAGG-RWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINP 106
Cdd:PRK07514 6 FDALRAAFADRDAPFIETPDGlRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 107 AYRSHELEYVLDQAGIRLLVASdkfktsdyPAMVEEVREKCARL--EHVVVLGGESWQELMDAGRRGDPAQLAHLRAgls 184
Cdd:PRK07514 86 AYTLAELDYFIGDAEPALVVCD--------PANFAWLSKIAAAAgaPHVETLDADGTGSLLEAAAAAPDDFETVPRG--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 185 ADDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGM-VMGNLACTShGACMvIPAPAF 263
Cdd:PRK07514 155 ADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLfVATNVALLA-GASM-IFLPKF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 264 DPRATLEAVAaeRCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAevsIC--YGMTETS 341
Cdd:PRK07514 233 DPDAVLALMP--RATVMMGVPTFYTRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHA---ILerYGMTETN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 342 pVSTQTRADDsiERRVSTVGRVGPHLEVKVVDPESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAARWMHTGDL 421
Cdd:PRK07514 308 -MNTSNPYDG--ERRAGTVGFPLPGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 422 AVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASpLTAEKVREFC 501
Cdd:PRK07514 385 GKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAA-LDEAAILAAL 463
|
490 500 510
....*....|....*....|....*....|....*
gi 522130465 502 SGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMREK 536
Cdd:PRK07514 464 KGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
22-529 |
1.14e-96 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 305.87 E-value: 1.14e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 22 DTIGDNFDRTVAAFGDRDALVDRAAGG--RWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGA 99
Cdd:COG1022 11 DTLPDLLRRRAARFPDRVALREKEDGIwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 100 ILVNINPAYRSHELEYVLDQAGIRLLVASDKFKTsdypAMVEEVREKCARLEHVVVLGGE---------SWQELMDAGR- 169
Cdd:COG1022 91 VTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQL----DKLLEVRDELPSLRHIVVLDPRglrddprllSLDELLALGRe 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 170 RGDPAQLAHLRAGLSADDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGnLAC 249
Cdd:COG1022 167 VADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVS-YYA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 250 TSHGACMVIPApafDPRATLEAVAAERCTSLYGVP---------------------------------TMFIAELNHPDF 296
Cdd:COG1022 246 LAAGATVAFAE---SPDTLAEDLREVKPTFMLAVPrvwekvyagiqakaeeagglkrklfrwalavgrRYARARLAGKSP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 297 GEFDL-------------------SSLRTGIMAGSPCPVEVMKqVIDRMGmaeVSIC--YGMTETSPVSTQTRADDsieR 355
Cdd:COG1022 323 SLLLRlkhaladklvfsklrealgGRLRFAVSGGAALGPELAR-FFRALG---IPVLegYGLTETSPVITVNRPGD---N 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 356 RVSTVGRVGPHLEVKVvdpesgltvprGEPGELCTRGYSVMLGYWEQPDKTAEAIDAARWMHTGDLAVMDGDGYVNITGR 435
Cdd:COG1022 396 RIGTVGPPLPGVEVKI-----------AEDGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGR 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 436 IKDMVI-RGGENLYPREIEEFLYTHPDVLDAQVIG----------VPDEkygEELMAWVRMR--EGASP---LTAEKVRE 499
Cdd:COG1022 465 KKDLIVtSGGKNVAPQPIENALKASPLIEQAVVVGdgrpflaaliVPDF---EALGEWAEENglPYTSYaelAQDPEVRA 541
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 522130465 500 F-------CSGKLAHYKIPRYVHVVDEFP------MTVTGKVR 529
Cdd:COG1022 542 LiqeevdrANAGLSRAEQIKRFRLLPKEFtiengeLTPTLKLK 584
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
187-530 |
2.33e-95 |
|
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: 293.64 E-value: 2.33e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 187 DPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGAcMVIPAPAFDPR 266
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGA-TVVPVAVFDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 267 ATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSICYGMTETSpVSTQ 346
Cdd:cd17638 80 AILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAG-VATM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 347 TRADDSIERRVSTVGRVGPHLEVKVVDPesgltvprgepGELCTRGYSVMLGYWEQPDKTAEAIDAARWMHTGDLAVMDG 426
Cdd:cd17638 159 CRPGDDAETVATTCGRACPGFEVRIADD-----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 427 DGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASpLTAEKVREFCSGKLA 506
Cdd:cd17638 228 RGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVT-LTEEDVIAWCRERLA 306
|
330 340
....*....|....*....|....
gi 522130465 507 HYKIPRYVHVVDEFPMTVTGKVRK 530
Cdd:cd17638 307 NYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
34-536 |
3.11e-94 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 297.84 E-value: 3.11e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 34 AFGDRDALVDRAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHEL 113
Cdd:PRK07786 27 ALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 114 EYVLDQAGIRLLVASDKFKtsdypAMVEEVREKCARLEHVVVLGGESWQELMDAGRRGDPAQLAHLRAGLSADDPINIQY 193
Cdd:PRK07786 107 AFLVSDCGAHVVVTEAALA-----PVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 194 TSGTTGFPKGATLSHHN--------ILNNGYFVGELCNYteedkvcIPVPFYHCFGMvmGNLACTSH-GACMVI-PAPAF 263
Cdd:PRK07786 182 TSGTTGRPKGAVLTHANltgqamtcLRTNGADINSDVGF-------VGVPLFHIAGI--GSMLPGLLlGAPTVIyPLGAF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 264 DPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSsLRTGIMAGSPCPVEVMKQVIDRMGMAEVSICYGMTETSPV 343
Cdd:PRK07786 253 DPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLA-LRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSPV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 344 STQTRADDSIeRRVSTVGRVGPHLEVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAArWMHTGDLAV 423
Cdd:PRK07786 332 TCMLLGEDAI-RKLGSVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGG-WFHSGDLVR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 424 MDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASPLTAEKVREFCSG 503
Cdd:PRK07786 409 QDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTLEDLAEFLTD 488
|
490 500 510
....*....|....*....|....*....|...
gi 522130465 504 KLAHYKIPRYVHVVDEFPMTVTGKVRKVEMREK 536
Cdd:PRK07786 489 RLARYKHPKALEIVDALPRNPAGKVLKTELRER 521
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
28-535 |
5.64e-94 |
|
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: 296.46 E-value: 5.64e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 28 FDRTVAAFGDRDALVDRAAGG--RWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNIN 105
Cdd:cd12119 2 LEHAARLHGDREIVSRTHEGEvhRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 106 PAYRSHELEYVLDQAGIRLLVASDKFKtsdypAMVEEVREKCARLEHVVVLGGESWQELMDAGRRGDPAQLAHLRAG--- 182
Cdd:cd12119 82 PRLFPEQIAYIINHAEDRVVFVDRDFL-----PLLEAIAPRLPTVEHVVVMTDDAAMPEPAGVGVLAYEELLAAESPeyd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 183 ---LSADDPINIQYTSGTTGFPKGATLSH-----HN--ILNNGYFvgelcNYTEEDKVCIPVPFYH--CFGMvmgNLACT 250
Cdd:cd12119 157 wpdFDENTAAAICYTSGTTGNPKGVVYSHrslvlHAmaALLTDGL-----GLSESDVVLPVVPMFHvnAWGL---PYAAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 251 SHGACMVIPAPAFDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQvIDRMGMaE 330
Cdd:cd12119 229 MVGAKLVLPGPYLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEA-FEERGV-R 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 331 VSICYGMTETSPVSTQTR---------ADDSIERRVSTvGRVGPHLEVKVVDPEsGLTVPR--GEPGELCTRGYSVMLGY 399
Cdd:cd12119 307 VIHAWGMTETSPLGTVARppsehsnlsEDEQLALRAKQ-GRPVPGVELRIVDDD-GRELPWdgKAVGELQVRGPWVTKSY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 400 WeQPDKTAEAIDAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEEL 479
Cdd:cd12119 385 Y-KNDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERP 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 522130465 480 MAWVRMREGASPlTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMRE 535
Cdd:cd12119 464 LAVVVLKEGATV-TAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
2-534 |
1.94e-92 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 293.85 E-value: 1.94e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 2 PDAPALPSYASGI-SEVPLLG-DTIGDNFDRTVAAFGDRDALVdrAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGI 79
Cdd:PRK07059 1 MEKIWLKSYPPGVpAEIDASQyPSLADLLEESFRQYADRPAFI--CMGKAITYGELDELSRALAAWLQSRGLAKGARVAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 80 WSPNraewtFLQY--ATAKI---GAILVNINPAYRSHELEYVLDQAGIRLLVASDKFKTSdypamVEEVREKCArLEHVV 154
Cdd:PRK07059 79 MMPN-----VLQYpvAIAAVlraGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLENFATT-----VQQVLAKTA-VKHVV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 155 V------LGGE----------------SWQ--------ELMDAGRRgdpaqLAHLRAGLSADDPINIQYTSGTTGFPKGA 204
Cdd:PRK07059 148 VasmgdlLGFKghivnfvvrrvkkmvpAWSlpghvrfnDALAEGAR-----QTFKPVKLGPDDVAFLQYTGGTTGVSKGA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 205 TLSHHNILNN-----GYFVGELCNYTEEDK---VCiPVPFYHCFGM-VMGNLACTSHGACMVIPAPAfDPRATLEAVAAE 275
Cdd:PRK07059 223 TLLHRNIVANvlqmeAWLQPAFEKKPRPDQlnfVC-ALPLYHIFALtVCGLLGMRTGGRNILIPNPR-DIPGFIKELKKY 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 276 RCTSLYGVPTMFIAELNHPDFGEFDLSSLRT---GIMAgspcpveVMKQVIDRMgmAEVSIC-----YGMTETSPVSTQT 347
Cdd:PRK07059 301 QVHIFPAVNTLYNALLNNPDFDKLDFSKLIVangGGMA-------VQRPVAERW--LEMTGCpitegYGLSETSPVATCN 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 348 RADDSieRRVSTVGRVGPHLEVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAARWMHTGDLAVMDGD 427
Cdd:PRK07059 372 PVDAT--EFSGTIGLPLPSTEVSIRD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDER 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 428 GYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGAspLTAEKVREFCSGKLAH 507
Cdd:PRK07059 449 GYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKDPA--LTEEDVKAFCKERLTN 526
|
570 580
....*....|....*....|....*..
gi 522130465 508 YKIPRYVHVVDEFPMTVTGKVRKVEMR 534
Cdd:PRK07059 527 YKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
26-536 |
5.89e-92 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 292.25 E-value: 5.89e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 26 DNFDRTVAAFGDRDALVdrAAGGRWTYRELAGEVTALALGLVAR-GIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNI 104
Cdd:PRK08314 14 HNLEVSARRYPDKTAIV--FYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 105 NPAYRSHELEYVLDQAGIRLLVAsdkfkTSDYPAMVEEVREKcARLEHVVV----------------------------- 155
Cdd:PRK08314 92 NPMNREEELAHYVTDSGARVAIV-----GSELAPKVAPAVGN-LRLRHVIVaqysdylpaepeiavpawlraepplqala 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 156 -LGGESWQELMDAGRRGDPAQlahlrAGlsADDPINIQYTSGTTGFPKGATLSH----HNILNNGYFVgelcNYTEEDKV 230
Cdd:PRK08314 166 pGGVVAWKEALAAGLAPPPHT-----AG--PDDLAVLPYTSGTTGVPKGCMHTHrtvmANAVGSVLWS----NSTPESVV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 231 CIPVPFYHCFGMVMGNLACTSHGACMVIpAPAFDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMA 310
Cdd:PRK08314 235 LAVLPLFHVTGMVHSMNAPIYAGATVVL-MPRWDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 311 GSPCPVEVMKQVIDRMGMAEVSiCYGMTETSpvsTQTRADDSIERRVSTVGRvgPHLEV--KVVDPESGLTVPRGEPGEL 388
Cdd:PRK08314 314 GAAMPEAVAERLKELTGLDYVE-GYGLTETM---AQTHSNPPDRPKLQCLGI--PTFGVdaRVIDPETLEELPPGEVGEI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 389 CTRGYSVMLGYWEQPDKTAEA---IDAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDA 465
Cdd:PRK08314 388 VVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEA 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522130465 466 QVIGVPDEKYGEELMAWVRMREGA-SPLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKV--RKVEMREK 536
Cdd:PRK08314 468 CVIATPDPRRGETVKAVVVLRPEArGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKIlwRQLQEQEK 541
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
37-535 |
2.28e-88 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 280.93 E-value: 2.28e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 37 DRDALVDRAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYV 116
Cdd:PRK09088 10 QRLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 117 LDQAGIRLLVASDKFKTsdypamveevrekcARLEhvvvlgGESWQELMDAGRRGDPAqlahLRAGLSADDPINIQYTSG 196
Cdd:PRK09088 90 LQDAEPRLLLGDDAVAA--------------GRTD------VEDLAAFIASADALEPA----DTPSIPPERVSLILFTSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 197 TTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGACMVIpAPAFDPRATLEAVA--A 274
Cdd:PRK09088 146 TSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILV-SNGFEPKRTLGRLGdpA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 275 ERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMK-------QVIDRMGMAEVSICYGMtetsPVSTqt 347
Cdd:PRK09088 225 LGITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEDILgwlddgiPMVDGFGMSEAGTVFGM----SVDC-- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 348 radDSIERRVSTVGRVGPHLEVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAARWMHTGDLAVMDGD 427
Cdd:PRK09088 299 ---DVIRAKAGAAGIPTPTVQTRVVD-DQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDAD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 428 GYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGAsPLTAEKVREFCSGKLAH 507
Cdd:PRK09088 375 GFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGA-PLDLERIRSHLSTRLAK 453
|
490 500
....*....|....*....|....*...
gi 522130465 508 YKIPRYVHVVDEFPMTVTGKVRKVEMRE 535
Cdd:PRK09088 454 YKVPKHLRLVDALPRTASGKLQKARLRD 481
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
29-535 |
2.43e-88 |
|
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: 280.72 E-value: 2.43e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 29 DRTVAAFGDRDALVDRAAggRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAY 108
Cdd:cd12118 11 ERAAAVYPDRTSIVYGDR--RYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 109 RSHELEYVLDQAGIRLLVASDKFKTSDypamveevrekcarlehvVVLGGESWQELMdagrrgdPAQlahlraglSADDP 188
Cdd:cd12118 89 DAEEIAFILRHSEAKVLFVDREFEYED------------------LLAEGDPDFEWI-------PPA--------DEWDP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 189 INIQYTSGTTGFPKGATLSHHnilnnGYFVGELCN--YTEEDKVCI---PVPFYHC----FGMVMGNLACTShgACMvip 259
Cdd:cd12118 136 IALNYTSGTTGRPKGVVYHHR-----GAYLNALANilEWEMKQHPVylwTLPMFHCngwcFPWTVAAVGGTN--VCL--- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 260 aPAFDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQViDRMGMaEVSICYGMTE 339
Cdd:cd12118 206 -RKVDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKM-EELGF-DVTHVYGLTE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 340 TSPVST----QTRADD-SIERRVSTVGRVG-PHL---EVKVVDPESGLTVPR-GEP-GELCTRGYSVMLGYWEQPDKTAE 408
Cdd:cd12118 283 TYGPATvcawKPEWDElPTEERARLKARQGvRYVgleEVDVLDPETMKPVPRdGKTiGEIVFRGNIVMKGYLKNPEATAE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 409 AIdAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREG 488
Cdd:cd12118 363 AF-RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEG 441
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 522130465 489 ASpLTAEKVREFCSGKLAHYKIPRYVhVVDEFPMTVTGKVRKVEMRE 535
Cdd:cd12118 442 AK-VTEEEIIAFCREHLAGFMVPKTV-VFGELPKTSTGKIQKFVLRD 486
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
51-536 |
3.99e-88 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 282.69 E-value: 3.99e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 51 TYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVASDK 130
Cdd:PRK06710 51 TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 131 FktsdYPAMVEEvrEKCARLEHVVVLGGESW-------------QELMDAGRRGDPAQLAHLRAGLSAD---------DP 188
Cdd:PRK06710 131 V----FPRVTNV--QSATKIEHVIVTRIADFlpfpknllypfvqKKQSNLVVKVSESETIHLWNSVEKEvntgvevpcDP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 189 IN----IQYTSGTTGFPKGATLSHHNILNNGYF-VGELCNYTEEDKVCIPV-PFYHCFGMVMGNLACTSHGACMVIpAPA 262
Cdd:PRK06710 205 ENdlalLQYTGGTTGFPKGVMLTHKNLVSNTLMgVQWLYNCKEGEEVVLGVlPFFHVYGMTAVMNLSIMQGYKMVL-IPK 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 263 FDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQvIDRMGMAEVSICYGMTETSP 342
Cdd:PRK06710 284 FDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEK-FETVTGGKLVEGYGLTESSP 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 343 VstqTRADDSIERRV-STVGRVGPHLEVKVVDPESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAArWMHTGDL 421
Cdd:PRK06710 363 V---THSNFLWEKRVpGSIGVPWPDTEAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVLQDG-WLHTGDV 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 422 AVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGaSPLTAEKVREFC 501
Cdd:PRK06710 439 GYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEG-TECSEEELNQFA 517
|
490 500 510
....*....|....*....|....*....|....*.
gi 522130465 502 SGKLAHYKIPRYVHVVDEFPMTVTGKV-RKVEMREK 536
Cdd:PRK06710 518 RKYLAAYKVPKVYEFRDELPKTTVGKIlRRVLIEEE 553
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
22-538 |
2.01e-87 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 280.79 E-value: 2.01e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 22 DTIGDNFDRTVAAFGDRDALVDraAGGRWTYRELAGEVTALA------LGLVargigKGDRVGIWSPNraewtFLQYATA 95
Cdd:PRK08974 23 QSLVDMFEQAVARYADQPAFIN--MGEVMTFRKLEERSRAFAaylqngLGLK-----KGDRVALMMPN-----LLQYPIA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 96 -----KIGAILVNINPAYRSHELEYVLDQAGIRLLVAsdkfkTSDYPAMVEEVREKcARLEHVVV--LGGE--------- 159
Cdd:PRK08974 91 lfgilRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVI-----VSNFAHTLEKVVFK-TPVKHVILtrMGDQlstakgtlv 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 160 --------------------SWQELMDAGRRgdpaqLAHLRAGLSADDPINIQYTSGTTGFPKGATLSHHNILNN----G 215
Cdd:PRK08974 165 nfvvkyikrlvpkyhlpdaiSFRSALHKGRR-----MQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANleqaK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 216 YFVGELCNYTEEdKVCIPVPFYHCFGMVMGNLACTSHGACMVIPAPAFDPRATLEAVAAERCTSLYGVPTMFIAELNHPD 295
Cdd:PRK08974 240 AAYGPLLHPGKE-LVVTALPLYHIFALTVNCLLFIELGGQNLLITNPRDIPGFVKELKKYPFTAITGVNTLFNALLNNEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 296 FGEFDLSSLRTGIMAGSPcpveVMKQVIDRMgmAEVSIC-----YGMTETSPVSTQTRADdsIERRVSTVGRVGPHLEVK 370
Cdd:PRK08974 319 FQELDFSSLKLSVGGGMA----VQQAVAERW--VKLTGQyllegYGLTECSPLVSVNPYD--LDYYSGSIGLPVPSTEIK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 371 VVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAArWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPR 450
Cdd:PRK08974 391 LVD-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVIKDG-WLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPN 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 451 EIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREgaSPLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRK 530
Cdd:PRK08974 469 EIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKD--PSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILR 546
|
....*...
gi 522130465 531 VEMREKSI 538
Cdd:PRK08974 547 RELRDEAR 554
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
8-539 |
1.18e-86 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 280.69 E-value: 1.18e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 8 PSYASG-----ISEVPL----LGDTIGDNFDRTVAAFGDRDAL-----VDRAAGG-RWTYRELAGEVTALALGLVARGIG 72
Cdd:PRK07529 2 PAFATLadieaIEAVPLaardLPASTYELLSRAAARHPDAPALsflldADPLDRPeTWTYAELLADVTRTANLLHSLGVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 73 KGDRVGIWSPNRAE--WTFLQYATAKIgailVN-INPAYRSHELEYVLDQAGIRLLVASDKFKTSDYPAMVEEVREKCAR 149
Cdd:PRK07529 82 PGDVVAFLLPNLPEthFALWGGEAAGI----ANpINPLLEPEQIAELLRAAGAKVLVTLGPFPGTDIWQKVAEVLAALPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 150 LEHVVVLGG----ESWQELMDAGRRGDP--------AQLAHLRA-GLSADDPINIQ------YTSGTTGFPKGATLSHHN 210
Cdd:PRK07529 158 LRTVVEVDLarylPGPKRLAVPLIRRKAharildfdAELARQPGdRLFSGRPIGPDdvaayfHTGGTTGMPKLAQHTHGN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 211 ILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGACMVIPAPA--FDPRAT---LEAVAAERCTSLYGVPT 285
Cdd:PRK07529 238 EVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLATPQgyRGPGVIanfWKIVERYRINFLSGVPT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 286 MFIAELNHPdFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGmaeVSIC--YGMTETSPVSTQTRADDsiERRVSTVGRV 363
Cdd:PRK07529 318 VYAALLQVP-VDGHDISSLRYALCGAAPLPVEVFRRFEAATG---VRIVegYGLTEATCVSSVNPPDG--ERRIGSVGLR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 364 GPHLEVKVV--DPESGLTV--PRGEPGELCTRGYSVMLGYWEqPDKTAEAIDAARWMHTGDLAVMDGDGYVNITGRIKDM 439
Cdd:PRK07529 392 LPYQRVRVVilDDAGRYLRdcAVDEVGVLCIAGPNVFSGYLE-AAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 440 VIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASpLTAEKVREFCSGKLAH-YKIPRYVHVVD 518
Cdd:PRK07529 471 IIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGAS-ATEAELLAFARDHIAErAAVPKHVRILD 549
|
570 580
....*....|....*....|.
gi 522130465 519 EFPMTVTGKVRKVEMREKSIT 539
Cdd:PRK07529 550 ALPKTAVGKIFKPALRRDAIR 570
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
23-527 |
1.25e-86 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 277.92 E-value: 1.25e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 23 TIGDNFDRTVAAFGDRDALV--DRaaggRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAI 100
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALVcgDR----RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 101 LVNINPAYRSHELEYVLDQAGIRLLVASDKFKtsdypAMVEEVREKCARLEHVVVLGGESWQELMDAGRR-------GDP 173
Cdd:PRK07798 80 PVNVNYRYVEDELRYLLDDSDAVALVYEREFA-----PRVAEVLPRLPKLRTLVVVEDGSGNDLLPGAVDyedalaaGSP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 174 AQLAHLRaglSADDpINIQYTSGTTGFPKGATLSHHNI----LNNGYFVGELCNYTEEDKV------------CIPvPFY 237
Cdd:PRK07798 155 ERDFGER---SPDD-LYLLYTGGTTGMPKGVMWRQEDIfrvlLGGRDFATGEPIEDEEELAkraaagpgmrrfPAP-PLM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 238 HCFGMVMGNLACTSHGACMVIPAPAFDPRATLEAVAAERCTSL------YGVPtmFIAELNHPdfGEFDLSSLRTGIMAG 311
Cdd:PRK07798 230 HGAGQWAAFAALFSGQTVVLLPDVRFDADEVWRTIEREKVNVItivgdaMARP--LLDALEAR--GPYDLSSLFAIASGG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 312 SPCPVEVMKQVIDRMGMAEVSICYGMTETSPVSTQTRADDSierrVSTVG-RVGPHLEVKVVDPESGLTVP-RGEPGELC 389
Cdd:PRK07798 306 ALFSPSVKEALLELLPNVVLTDSIGSSETGFGGSGTVAKGA----VHTGGpRFTIGPRTVVLDEDGNPVEPgSGEIGWIA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 390 TRGYsVMLGYWEQPDKTAEA---IDAARWMHTGDLAVMDGDGYVNITGRiKDMVIR-GGENLYPREIEEFLYTHPDVLDA 465
Cdd:PRK07798 382 RRGH-IPLGYYKDPEKTAETfptIDGVRYAIPGDRARVEADGTITLLGR-GSVCINtGGEKVFPEEVEEALKAHPDVADA 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522130465 466 QVIGVPDEKYGEELMAWVRMREGASPlTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGK 527
Cdd:PRK07798 460 LVVGVPDERWGQEVVAVVQLREGARP-DLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
43-535 |
3.94e-86 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 277.31 E-value: 3.94e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 43 DRAA----GGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLD 118
Cdd:PRK06178 48 QRPAiifyGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELN 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 119 QAGIRLLVASDKFktsdYPaMVEEVREKCArLEHVVV-----------------------LGGESWQELMDAgRRGDPAQ 175
Cdd:PRK06178 128 DAGAEVLLALDQL----AP-VVEQVRAETS-LRHVIVtsladvlpaeptlplpdslraprLAAAGAIDLLPA-LRACTAP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 176 LAHLRAGLsaDDPINIQYTSGTTGFPKGATLSHHNILnngYFVGELCNYT---EEDKVCIP-VPFYHCFGMVMGNLACTS 251
Cdd:PRK06178 201 VPLPPPAL--DALAALNYTGGTTGMPKGCEHTQRDMV---YTAAAAYAVAvvgGEDSVFLSfLPEFWIAGENFGLLFPLF 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 252 HGACMVIPApAFDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTgIMAGS---PCPVEVMKQVIDRMG- 327
Cdd:PRK06178 276 SGATLVLLA-RWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQ-VRVVSfvkKLNPDYRQRWRALTGs 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 328 -MAEVSicYGMTETSPVSTQTRA--DDSIERRVST--VGRVGPHLEVKVVDPESGLTVPRGEPGELCTRGYSVMLGYWEQ 402
Cdd:PRK06178 354 vLAEAA--WGMTETHTCDTFTAGfqDDDFDLLSQPvfVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNK 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 403 PDKTAEAIDAArWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAW 482
Cdd:PRK06178 432 PEATAEALRDG-WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAF 510
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 522130465 483 VRMREGAsPLTAEKVREFCSGKLAHYKIPRyVHVVDEFPMTVTGKVRKVEMRE 535
Cdd:PRK06178 511 VQLKPGA-DLTAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKVRKQDLQA 561
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
24-543 |
1.89e-85 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 275.49 E-value: 1.89e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 24 IGDNFDRTVAAFGDRDALVdrAAGGRWTYRELAGEVTALALGLVAR-GIGKGDRVGIWSPNraewtFLQYATAKIGA--- 99
Cdd:PRK05677 26 IQAVLKQSCQRFADKPAFS--NLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPN-----VLQYPVAVFGAmra 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 100 --ILVNINPAYRSHELEYVLDQAGIRLLVAsdkfkTSDYPAMVEEVREKCArLEHVVV-----LGGESWQELMDAG---- 168
Cdd:PRK05677 99 glIVVNTNPLYTAREMEHQFNDSGAKALVC-----LANMAHLAEKVLPKTG-VKHVIVtevadMLPPLKRLLINAVvkhv 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 169 RRGDPA----QLAHLRAGLS-------------ADDPINIQYTSGTTGFPKGATLSHHNILNN--------GYFVGELCn 223
Cdd:PRK05677 173 KKMVPAyhlpQAVKFNDALAkgagqpvteanpqADDVAVLQYTGGTTGVAKGAMLTHRNLVANmlqcralmGSNLNEGC- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 224 yteeDKVCIPVPFYHCFG--------MVMGNlactsHGacMVIPAPAfDPRATLEAVAAERCTSLYGVPTMFIAELNHPD 295
Cdd:PRK05677 252 ----EILIAPLPLYHIYAftfhcmamMLIGN-----HN--ILISNPR-DLPAMVKELGKWKFSGFVGLNTLFVALCNNEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 296 FGEFDLSSLR---TGIMAGSPCPVEVMKQVIDrmgmAEVSICYGMTETSPVSTQTRADDSierRVSTVGRVGPHLEVKVV 372
Cdd:PRK05677 320 FRKLDFSALKltlSGGMALQLATAERWKEVTG----CAICEGYGMTETSPVVSVNPSQAI---QVGTIGIPVPSTLCKVI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 373 DPEsGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREI 452
Cdd:PRK05677 393 DDD-GNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNEL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 453 EEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASpLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVE 532
Cdd:PRK05677 472 EDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGET-LTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRE 550
|
570
....*....|.
gi 522130465 533 MREKSITLLGL 543
Cdd:PRK05677 551 LRDEELKKAGL 561
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
6-539 |
4.10e-85 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 273.94 E-value: 4.10e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 6 ALPSYASGISEVPLLGDTIGDNFDRTVAAFGDRDALvdRAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRA 85
Cdd:PRK06155 5 GAGLAARAVDPLPPSERTLPAMLARQAERYPDRPLL--VFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 86 EWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVASdkfktSDYPAMVEEVREKCARLEHVVVLGGESWQELM 165
Cdd:PRK06155 83 EFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVE-----AALLAALEAADPGDLPLPAVWLLDAPASVSVP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 166 DAGRRGDPAQLAHL--RAGLSADDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMV 243
Cdd:PRK06155 158 AGWSTAPLPPLDAPapAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 244 MGNLACTsHGACMVIpAPAFDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPcpVEVMKQVI 323
Cdd:PRK06155 238 AFFQALL-AGATYVL-EPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVP--AALHAAFR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 324 DRMGMAEVSiCYGMTETSPVSTQTRAddsiERRVSTVGRVGPHLEVKVVDpESGLTVPRGEPGELCTRG---YSVMLGYW 400
Cdd:PRK06155 314 ERFGVDLLD-GYGSTETNFVIAVTHG----SQRPGSMGRLAPGFEARVVD-EHDQELPDGEPGELLLRAdepFAFATGYF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 401 EQPDKTAEAIDAArWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELM 480
Cdd:PRK06155 388 GMPEKTVEAWRNL-WFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVM 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 522130465 481 AWVRMREGASpLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMREKSIT 539
Cdd:PRK06155 467 AAVVLRDGTA-LEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVT 524
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
21-530 |
2.22e-84 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 271.56 E-value: 2.22e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 21 GDTIGDNFDRTVAAFGDRDALVDRAAGG---RWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKI 97
Cdd:PRK08008 6 GQHLRQMWDDLADVYGHKTALIFESSGGvvrRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 98 GAILVNINPAYRSHELEYVLDQAGIRLLVASDKFktsdYPAMVEEVREKCARLEHVVVLGGESWQE--LMDAGRRGD--P 173
Cdd:PRK08008 86 GAIMVPINARLLREESAWILQNSQASLLVTSAQF----YPMYRQIQQEDATPLRHICLTRVALPADdgVSSFTQLKAqqP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 174 AQLAHLRAgLSADDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHG 253
Cdd:PRK08008 162 ATLCYAPP-LSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 254 ACMVIpAPAFDPRATLEAVAAERCTSLYGVPTMfiaelnhpdfgefdlssLRTgIMAGSPCPVE---VMKQVIDRMGMAE 330
Cdd:PRK08008 241 ATFVL-LEKYSARAFWGQVCKYRATITECIPMM-----------------IRT-LMVQPPSANDrqhCLREVMFYLNLSD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 331 -----------VSI--CYGMTET-SPVSTQTRADdsiERRVSTVGRVGPHLEVKVVDpESGLTVPRGEPGELCTRGY--- 393
Cdd:PRK08008 302 qekdafeerfgVRLltSYGMTETiVGIIGDRPGD---KRRWPSIGRPGFCYEAEIRD-DHNRPLPAGEIGEICIKGVpgk 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 394 SVMLGYWEQPDKTAEAIDAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDE 473
Cdd:PRK08008 378 TIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDS 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 522130465 474 KYGEELMAWVRMREGASpLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRK 530
Cdd:PRK08008 458 IRDEAIKAFVVLNEGET-LSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIK 513
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
51-528 |
2.52e-84 |
|
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: 268.58 E-value: 2.52e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 51 TYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVAsdk 130
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 131 fktsdypamveevrekcarlehvvvlggeswqelmdagrrgdpaqlahlraGLSADDPINIQYTSGTTGFPKGATLSHHN 210
Cdd:cd05935 80 ---------------------------------------------------GSELDDLALIPYTSGTTGLPKGCMHTHFS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 211 ILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGACMVIPApAFDPRATLEAVAAERCTSLYGVPTMFIAE 290
Cdd:cd05935 109 AAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMA-RWDRETALELIEKYKVTFWTNIPTMLVDL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 291 LNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSIcYGMTETSPvstQTRADDSIERRVSTVGRVGPHLEVK 370
Cdd:cd05935 188 LATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEG-YGLTETMS---QTHTNPPLRPKLQCLGIP*FGVDAR 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 371 VVDPESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEA---IDAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENL 447
Cdd:cd05935 264 VIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESfieIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 448 YPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREG-ASPLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTG 526
Cdd:cd05935 344 WPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEyRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASG 423
|
..
gi 522130465 527 KV 528
Cdd:cd05935 424 KI 425
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
47-536 |
1.19e-83 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 269.08 E-value: 1.19e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 47 GGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLV 126
Cdd:PRK08276 9 GEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 127 ASdkfktsdyPAMVEEVREKCARLEHVVVLggeswqELMDAGRRGDPAQLAHLRAGLSADDPIN------IQYTSGTTGF 200
Cdd:PRK08276 89 VS--------AALADTAAELAAELPAGVPL------LLVVAGPVPGFRSYEEALAAQPDTPIADetagadMLYSSGTTGR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 201 PKG--ATLSHHNI---LNNGYFVGELCNYTEEDKVCI-PVPFYHC----FGMVMGNLACTshgacmVIPAPAFDPRATLE 270
Cdd:PRK08276 155 PKGikRPLPGLDPdeaPGMMLALLGFGMYGGPDSVYLsPAPLYHTaplrFGMSALALGGT------VVVMEKFDAEEALA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 271 AVAAERCTSLYGVPTMFIAELNHPDF--GEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAeVSICYGMTETSPVSTQTr 348
Cdd:PRK08276 229 LIERYRVTHSQLVPTMFVRMLKLPEEvrARYDVSSLRVAIHAAAPCPVEVKRAMIDWWGPI-IHEYYASSEGGGVTVIT- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 349 ADDSIERRvSTVGR--VGphlEVKVVDpESGLTVPRGEPGELctrgYSVMLG----YWEQPDKTAEAIDAARWMHTGDLA 422
Cdd:PRK08276 307 SEDWLAHP-GSVGKavLG---EVRILD-EDGNELPPGEIGTV----YFEMDGypfeYHNDPEKTAAARNPHGWVTVGDVG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 423 VMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREG--ASPLTAEKVREF 500
Cdd:PRK08276 378 YLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGadAGDALAAELIAW 457
|
490 500 510
....*....|....*....|....*....|....*.
gi 522130465 501 CSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMREK 536
Cdd:PRK08276 458 LRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDR 493
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
26-535 |
1.81e-83 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 270.54 E-value: 1.81e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 26 DNFDRTVAAFGDRDALVDraAGGRWTYRELAGEVTALALGLVAR-GIGKGDRVGIWSPNraewtFLQYATAKIGA----- 99
Cdd:PRK12492 28 EVFERSCKKFADRPAFSN--LGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPN-----VLQYPIAVFGAlragl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 100 ILVNINPAYRSHELEYVLDQAGIRLLVASDKFKTsdypaMVEEVREKCArLEHVV---------VLGGESWQELMDAGRR 170
Cdd:PRK12492 101 IVVNTNPLYTAREMRHQFKDSGARALVYLNMFGK-----LVQEVLPDTG-IEYLIeakmgdllpAAKGWLVNTVVDKVKK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 171 GDPA-----------------QLAHLRAGLSADDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEED----- 228
Cdd:PRK12492 175 MVPAyhlpqavpfkqalrqgrGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDgqplm 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 229 ----KVCI-PVPFYHCFgmvmgnlACTSHGACMVIPAP----AFDPR---ATLEAVAAERCTSLYGVPTMFIAELNHPDF 296
Cdd:PRK12492 255 kegqEVMIaPLPLYHIY-------AFTANCMCMMVSGNhnvlITNPRdipGFIKELGKWRFSALLGLNTLFVALMDHPGF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 297 GEFDLSSLRTGIMAGSPcpveVMKQVIDRMgmAEVSIC-----YGMTETSPV-STQTRADDSierRVSTVGRVGPHLEVK 370
Cdd:PRK12492 328 KDLDFSALKLTNSGGTA----LVKATAERW--EQLTGCtivegYGLTETSPVaSTNPYGELA---RLGTVGIPVPGTALK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 371 VVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPR 450
Cdd:PRK12492 399 VID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPN 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 451 EIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGAspLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRK 530
Cdd:PRK12492 478 EIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPG--LSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILR 555
|
....*
gi 522130465 531 VEMRE 535
Cdd:PRK12492 556 RELRD 560
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
21-531 |
2.69e-83 |
|
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: 267.66 E-value: 2.69e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 21 GDTIGDNFDRTVAAFGDRDALVDraAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAI 100
Cdd:cd05920 14 DEPLGDLLARSAARHPDRIAVVD--GDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 101 LVNINPAYRSHELEYVLDQAGIRLLVASDKFKTSDYPAMVEEVREKCArlehvvvlggeswqelmdagrrgDPAQLahlr 180
Cdd:cd05920 92 PVLALPSHRRSELSAFCAHAEAVAYIVPDRHAGFDHRALARELAESIP-----------------------EVALF---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 181 aglsaddpiniQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGM----VMGNLACtshGACM 256
Cdd:cd05920 145 -----------LLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLacpgVLGTLLA---GGRV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 257 VIPAPAfDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGmAEVSICYG 336
Cdd:cd05920 211 VLAPDP-SPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLG-CTLQQVFG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 337 MTETspVSTQTRADDSIERRVSTVGR-VGPHLEVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAARW 415
Cdd:cd05920 289 MAEG--LLNYTRLDDPDEVIIHTQGRpMSPDDEIRVVD-EEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 416 MHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREgaSPLTAE 495
Cdd:cd05920 366 YRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRD--PPPSAA 443
|
490 500 510
....*....|....*....|....*....|....*..
gi 522130465 496 KVREFCSGK-LAHYKIPRYVHVVDEFPMTVTGKVRKV 531
Cdd:cd05920 444 QLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKK 480
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
37-536 |
2.39e-82 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 265.60 E-value: 2.39e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 37 DRDALVDRaaGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYV 116
Cdd:PRK06145 17 DRAALVYR--DQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 117 LDQAGIRLLvasdkfktsdypaMVEEVREKCARLEH-VVVLGGESWQELMDAGRRGDPAQLAHLRAglsADDPINIQYTS 195
Cdd:PRK06145 95 LGDAGAKLL-------------LVDEEFDAIVALETpKIVIDAAAQADSRRLAQGGLEIPPQAAVA---PTDLVRLMYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 196 GTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGACMVIpAPAFDPRATLEAVAAE 275
Cdd:PRK06145 159 GTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRI-HREFDPEAVLAAIERH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 276 RCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSICYGMTETSPVSTQTRADDSIER 355
Cdd:PRK06145 238 RLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREIEK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 356 RVSTvGRVGPHLEVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIdAARWMHTGDLAVMDGDGYVNITGR 435
Cdd:PRK06145 318 IGST-GRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 436 IKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASpLTAEKVREFCSGKLAHYKIPRYVH 515
Cdd:PRK06145 395 KKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGAT-LTLEALDRHCRQRLASFKVPRQLK 473
|
490 500
....*....|....*....|.
gi 522130465 516 VVDEFPMTVTGKVRKVEMREK 536
Cdd:PRK06145 474 VRDELPRNPSGKVLKRVLRDE 494
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
3-535 |
1.04e-80 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 263.28 E-value: 1.04e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 3 DAPALPSYASGIS-EVPLLG-DTIGDNFDRTVAAFGDRDALvdRAAGGRWTYRE---LAGEVTALALGLVArgIGKGDRV 77
Cdd:PRK08751 4 ARPWLQSYPAGVAaEIDLEQfRTVAEVFATSVAKFADRPAY--HSFGKTITYREadqLVEQFAAYLLGELQ--LKKGDRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 78 GIWSPNraewtFLQYATAKIGAIL-----VNINPAYRSHELEYVLDQAGIRLLVASDKFKTS------DYPamVEEV--- 143
Cdd:PRK08751 80 ALMMPN-----CLQYPIATFGVLRagltvVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTvqqviaDTP--VKQVitt 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 144 -------REKCARLEHVV-----------VLGGESWQELMDAGRRGD--PAQLAHlraglsaDDPINIQYTSGTTGFPKG 203
Cdd:PRK08751 153 glgdmlgFPKAALVNFVVkyvkklvpeyrINGAIRFREALALGRKHSmpTLQIEP-------DDIAFLQYTGGTTGVAKG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 204 ATLSHHNILNNGYFVGELCNYT---EEDK--VCIPVPFYHCFGMVMGNLACTSHGACMVIPAPAFDPRATLEAVAAERCT 278
Cdd:PRK08751 226 AMLTHRNLVANMQQAHQWLAGTgklEEGCevVITALPLYHIFALTANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 279 SLYGVPTMFIAELNHPDFGEFDLSSLRT---GIMAGSPCPVEVMKQVidrMGMAEVSiCYGMTETSPVSTQTRADdsIER 355
Cdd:PRK08751 306 AFTGVNTLFNGLLNTPGFDQIDFSSLKMtlgGGMAVQRSVAERWKQV---TGLTLVE-AYGLTETSPAACINPLT--LKE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 356 RVSTVGRVGPHLEVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAARWMHTGDLAVMDGDGYVNITGR 435
Cdd:PRK08751 380 YNGSIGLPIPSTDACIKD-DAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDR 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 436 IKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGAspLTAEKVREFCSGKLAHYKIPRYVH 515
Cdd:PRK08751 459 KKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKDPA--LTAEDVKAHARANLTGYKQPRIIE 536
|
570 580
....*....|....*....|
gi 522130465 516 VVDEFPMTVTGKVRKVEMRE 535
Cdd:PRK08751 537 FRKELPKTNVGKILRRELRD 556
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
37-536 |
1.43e-79 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 257.97 E-value: 1.43e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 37 DRDALVDraAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYV 116
Cdd:PRK03640 17 DRTAIEF--EEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 117 LDQAGIRLLVASDKFK---TSDYPAMVEEVREKcaRLEHVvvlggeSWQELMDAgrrgdpaqlahlraglsaDDPINIQY 193
Cdd:PRK03640 95 LDDAEVKCLITDDDFEaklIPGISVKFAELMNG--PKEEA------EIQEEFDL------------------DEVATIMY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 194 TSGTTGFPKGATLSHHN--------ILNNGYfvgelcnyTEEDKVCIPVPFYHCFGM--VMGNLActsHGACMVIpAPAF 263
Cdd:PRK03640 149 TSGTTGKPKGVIQTYGNhwwsavgsALNLGL--------TEDDCWLAAVPIFHISGLsiLMRSVI---YGMRVVL-VEKF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 264 DPRATLEAVAAERCTSLYGVPTM---FIAEL---NHPdfgefdlSSLRTGIMAGSPCPVEVMKQVIDRmGMAeVSICYGM 337
Cdd:PRK03640 217 DAEKINKLLQTGGVTIISVVSTMlqrLLERLgegTYP-------SSFRCMLLGGGPAPKPLLEQCKEK-GIP-VYQSYGM 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 338 TET-SPVSTQTrADDSIERrvstVGRVGPHL---EVKVVDpeSGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAA 413
Cdd:PRK03640 288 TETaSQIVTLS-PEDALTK----LGSAGKPLfpcELKIEK--DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 414 rWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMregASPLT 493
Cdd:PRK03640 361 -WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK---SGEVT 436
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 522130465 494 AEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMREK 536
Cdd:PRK03640 437 EEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
37-535 |
4.29e-79 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 258.32 E-value: 4.29e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 37 DRDALVDRAagGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYV 116
Cdd:PRK07788 64 DRAALIDER--GTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 117 LDQAGIRLLVASDKFKT--SDYPAMVEEVR--EKCARLEHVVVLGGESWQELMDAGRRGdPAQLAHLRAGLsaddpinIQ 192
Cdd:PRK07788 142 AAREGVKALVYDDEFTDllSALPPDLGRLRawGGNPDDDEPSGSTDETLDDLIAGSSTA-PLPKPPKPGGI-------VI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 193 YTSGTTGFPKGATLSHHNILN-NGYFVGELCNYTEEdKVCIPVPFYHCFGMVMGNLAcTSHGACMVIPApAFDPRATLEA 271
Cdd:PRK07788 214 LTSGTTGTPKGAPRPEPSPLApLAGLLSRVPFRAGE-TTLLPAPMFHATGWAHLTLA-MALGSTVVLRR-RFDPEATLED 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 272 VAAERCTSLYGVPTMFIAELNHPD--FGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGmaEVsIC--YGMTETSPVSTQT 347
Cdd:PRK07788 291 IAKHKATALVVVPVMLSRILDLGPevLAKYDTSSLKIIFVSGSALSPELATRALEAFG--PV-LYnlYGSTEVAFATIAT 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 348 RADdsIERRVSTVGRVGPHLEVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKtaEAIDAarWMHTGDLAVMDGD 427
Cdd:PRK07788 368 PED--LAEAPGTVGRPPKGVTVKILD-ENGNEVPRGVVGRIFVGNGFPFEGYTDGRDK--QIIDG--LLSSGDVGYFDED 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 428 GYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASpLTAEKVREFCSGKLAH 507
Cdd:PRK07788 441 GLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAA-LDEDAIKDYVRDNLAR 519
|
490 500
....*....|....*....|....*...
gi 522130465 508 YKIPRYVHVVDEFPMTVTGKVRKVEMRE 535
Cdd:PRK07788 520 YKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
22-547 |
4.32e-79 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 258.13 E-value: 4.32e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 22 DTIGDNFDRTVAAFGDRDALVDRaaGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAIL 101
Cdd:PRK06164 10 DTLASLLDAHARARPDAVALIDE--DRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 102 VNINPAYRSHELEYVLDQAGIRLLVASDKFKTSDYPAMVEEV-REKCARLEHVVVLGGESWQELMDAGRRG-------DP 173
Cdd:PRK06164 88 IAVNTRYRSHEVAHILGRGRARWLVVWPGFKGIDFAAILAAVpPDALPPLRAIAVVDDAADATPAPAPGARvqlfalpDP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 174 AQLAHLRAGLSADDPINIQY-TSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMgnLACTSH 252
Cdd:PRK06164 168 APPAAAGERAADPDAGALLFtTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFST--LLGALA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 253 GACMVIPAPAFDPRATLEAVAAERCTSLYGVPTMFIAELNHPDfGEFDLSSLRT-GIMAGSPCPVEVMKQVIDRmGMAEV 331
Cdd:PRK06164 246 GGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAG-ERADFPSARLfGFASFAPALGELAALARAR-GVPLT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 332 SIcYGMTET-SPVSTQTRADDSIERRVSTVGRVGPHLEVKVVDPESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAI 410
Cdd:PRK06164 324 GL-YGSSEVqALVALQPATDPVSVRIEGGGRPASPEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARAL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 411 DAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYgEELMAWVRMREGAS 490
Cdd:PRK06164 403 TDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGK-TVPVAFVIPTDGAS 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 491 PlTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTG---KVRKVEMREKSITLLGLETAA 547
Cdd:PRK06164 482 P-DEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMAQARLAAERAA 540
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
23-539 |
3.15e-78 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 256.06 E-value: 3.15e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 23 TIGDNFDRTVAAFGDRDALVDRAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILV 102
Cdd:PLN02330 29 TLPDFVLQDAELYADKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 103 NINPAYRSHELEYVLDQAGIRLLVASD----KFKTSDYPAMVeevrekcarLEHVVVLGGESWQELMDAGRR-GDpaQLA 177
Cdd:PLN02330 109 GANPTALESEIKKQAEAAGAKLIVTNDtnygKVKGLGLPVIV---------LGEEKIEGAVNWKELLEAADRaGD--TSD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 178 H---LRAGLSAddpinIQYTSGTTGFPKGATLSHHNILNN---------GYFVGELCNYTEedkvcipVPFYHCFGMVmG 245
Cdd:PLN02330 178 NeeiLQTDLCA-----LPFSSGTTGISKGVMLTHRNLVANlcsslfsvgPEMIGQVVTLGL-------IPFFHIYGIT-G 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 246 NLACTSHGACMVIPAPAFDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLR-TGIM-AGSPCPVEVMKQVI 323
Cdd:PLN02330 245 ICCATLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKlQAIMtAAAPLAPELLTAFE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 324 DRMGMAEVSICYGMTETSPVsTQTRADDS----IERRvSTVGRVGPHLEVKVVDPESGLTVPRGEPGELCTRGYSVMLGY 399
Cdd:PLN02330 325 AKFPGVQVQEAYGLTEHSCI-TLTHGDPEkghgIAKK-NSVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGY 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 400 WEQPDKTAEAIDAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEEL 479
Cdd:PLN02330 403 YNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIP 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 480 MAWVRMREGASPlTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMREKSIT 539
Cdd:PLN02330 483 AACVVINPKAKE-SEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLS 541
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
37-536 |
4.34e-78 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 255.00 E-value: 4.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 37 DRDALVDRAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYV 116
Cdd:PRK13391 12 DKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 117 LDQAGIRLLVASdkfktSDYPAMVEEVREKCARLEHVVVLGG----ESWQELMDAgrrgdpaqLAHLRAGLSADDPI--N 190
Cdd:PRK13391 92 VDDSGARALITS-----AAKLDVARALLKQCPGVRHRLVLDGdgelEGFVGYAEA--------VAGLPATPIADESLgtD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 191 IQYTSGTTGFPKG--ATLSHHNI---LNNGYFVGELCNYTEEDKVCIPVPFYHC----FGMVMGNLACTshgacmVIPAP 261
Cdd:PRK13391 159 MLYSSGTTGRPKGikRPLPEQPPdtpLPLTAFLQRLWGFRSDMVYLSPAPLYHSapqrAVMLVIRLGGT------VIVME 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 262 AFDPRATLEAVAAERCTSLYGVPTMFIAELNHPD--FGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAeVSICYGMTE 339
Cdd:PRK13391 233 HFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEevRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPI-IHEYYAATE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 340 TSPVsTQTRADDSIERRvSTVGRV--GphlEVKVVDpESGLTVPRGEPGELCTRGYSvMLGYWEQPDKTAEAIDA-ARWM 416
Cdd:PRK13391 312 GLGF-TACDSEEWLAHP-GTVGRAmfG---DLHILD-DDGAELPPGEPGTIWFEGGR-PFEYLNDPAKTAEARHPdGTWS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 417 HTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREG--ASPLTA 494
Cdd:PRK13391 385 TVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGvdPGPALA 464
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 522130465 495 EKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMREK 536
Cdd:PRK13391 465 AELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDR 506
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
30-536 |
2.39e-77 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 253.72 E-value: 2.39e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 30 RTVAAFGDRDALV--DRaaggRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPA 107
Cdd:PRK08162 26 RAAEVYPDRPAVIhgDR----RRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 108 YRSHELEYVLDQAGIRLLVASdkfktSDYPAMVEEVREKCARLEHVVV------------LGGESWQELMDAGrrgDPAQ 175
Cdd:PRK08162 102 LDAASIAFMLRHGEAKVLIVD-----TEFAEVAREALALLPGPKPLVIdvddpeypggrfIGALDYEAFLASG---DPDF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 176 LAHLraglSAD--DPINIQYTSGTTGFPKGaTLSHHNilnnGYFVGELCNYTEEDKVCIPV-----PFYHCFG------- 241
Cdd:PRK08162 174 AWTL----PADewDAIALNYTSGTTGNPKG-VVYHHR----GAYLNALSNILAWGMPKHPVylwtlPMFHCNGwcfpwtv 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 242 -MVMGNLACTShgacmvipapAFDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMK 320
Cdd:PRK08162 245 aARAGTNVCLR----------KVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAGAAPPAAVIA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 321 QViDRMGMaEVSICYGMTET-SPVST---QTRADD-SIERRVSTVGRVG---PHLE-VKVVDPESGLTVPR-GEP-GELC 389
Cdd:PRK08162 315 KM-EEIGF-DLTHVYGLTETyGPATVcawQPEWDAlPLDERAQLKARQGvryPLQEgVTVLDPDTMQPVPAdGETiGEIM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 390 TRGYSVMLGYWEQPDKTAEAIdAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIG 469
Cdd:PRK08162 393 FRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVA 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522130465 470 VPDEKYGEELMAWVRMREGASpLTAEKVREFCSGKLAHYKIPRYVhVVDEFPMTVTGKVRKVEMREK 536
Cdd:PRK08162 472 KPDPKWGEVPCAFVELKDGAS-ATEEEIIAHCREHLAGFKVPKAV-VFGELPKTSTGKIQKFVLREQ 536
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
23-528 |
3.59e-77 |
|
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: 252.04 E-value: 3.59e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 23 TIGDNFDRTVAAFGDRDALVDRAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILV 102
Cdd:cd05923 2 TVFEMLRRAASRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 103 NINPAYRSHELEYVLDQAGIRLLVASDkfktsDYPAMvEEVREKCARLEHVVVLGGeswqeLMDAGRRGDPAQLAHLRAG 182
Cdd:cd05923 82 LINPRLKAAELAELIERGEMTAAVIAV-----DAQVM-DAIFQSGVRVLALSDLVG-----LGEPESAGPLIEDPPREPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 183 lsadDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCN--YTEEDKVCIPVPFYHCFGmVMGNLACTSHGACMVIPA 260
Cdd:cd05923 151 ----QPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGlrHGRHNVVLGLMPLYHVIG-FFAVLVAALALDGTYVVV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 261 PAFDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSIcYGMTET 340
Cdd:cd05923 226 EEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNI-YGTTEA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 341 SpvsTQTRADDSierRVSTVGRVGPHLEVKVVD--PESGLTVPRGEPGELCTR--GYSVMLGYWEQPDKTAEAIdAARWM 416
Cdd:cd05923 305 M---NSLYMRDA---RTGTEMRPGFFSEVRIVRigGSPDEALANGEEGELIVAaaADAAFTGYLNQPEATAKKL-QDGWY 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 417 HTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGasPLTAEK 496
Cdd:cd05923 378 RTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG--TLSADE 455
|
490 500 510
....*....|....*....|....*....|...
gi 522130465 497 VREFC-SGKLAHYKIPRYVHVVDEFPMTVTGKV 528
Cdd:cd05923 456 LDQFCrASELADFKRPRRYFFLDELPKNAMNKV 488
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
28-534 |
6.06e-77 |
|
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: 251.90 E-value: 6.06e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 28 FDRTVAAFGDRDALVDRAagGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPA 107
Cdd:cd05959 10 DLNLNEGRGDKTAFIDDA--GSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 108 YRSHELEYVLDQAGIRLLVASDKFktsdYPAMVEEVREKCARLEHVVVLGGESWQELMDagrrgdpaQLAHLRAGLS--- 184
Cdd:cd05959 88 LTPDDYAYYLEDSRARVVVVSGEL----APVLAAALTKSEHTLVVLIVSGGAGPEAGAL--------LLAELVAAEAeql 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 185 ------ADDPINIQYTSGTTGFPKGATLSHHNIlnngYFVGELCN----YTEEDKVCIPVP-FYHCFGMvmGNlACT--- 250
Cdd:cd05959 156 kpaathADDPAFWLYSSGSTGRPKGVVHLHADI----YWTAELYArnvlGIREDDVCFSAAkLFFAYGL--GN-SLTfpl 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 251 SHGACMVIPAPAFDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMaE 330
Cdd:cd05959 229 SVGATTVLMPERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGL-D 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 331 VSICYGMTETSPVSTQTRADDSierRVSTVGRVGPHLEVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAI 410
Cdd:cd05959 308 ILDGIGSTEMLHIFLSNRPGRV---RYGTTGKPVPGYEVELRD-EDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 411 DAArWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGAS 490
Cdd:cd05959 384 QGE-WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYE 462
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 522130465 491 PLTA--EKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMR 534
Cdd:cd05959 463 DSEAleEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
37-528 |
9.22e-77 |
|
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: 249.37 E-value: 9.22e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 37 DRDALVDraAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYV 116
Cdd:cd05930 2 DAVAVVD--GDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 117 LDQAGIRLLVAsdkfktsdypamveevrekcarlehvvvlggeswqelmdagrrgDPAQLAHlraglsaddpinIQYTSG 196
Cdd:cd05930 80 LEDSGAKLVLT--------------------------------------------DPDDLAY------------VIYTSG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 197 TTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFyhCF-GMVMGNLACTSHGACMVIPAP--AFDPRATLEAVA 273
Cdd:cd05930 104 STGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSF--SFdVSVWEIFGALLAGATLVVLPEevRKDPEALADLLA 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 274 AERCTSLYGVPTMFIAELNHPDFGefDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSICYGMTETSPVSTQTR-ADDS 352
Cdd:cd05930 182 EEGITVLHLTPSLLRLLLQELELA--ALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRvPPDD 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 353 IERRVSTVGRVGPHLEVKVVDPESGLtVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAARWMH------TGDLAVMDG 426
Cdd:cd05930 260 EEDGRVPIGRPIPNTRVYVLDENLRP-VPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPgermyrTGDLVRWLP 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 427 DGyvNIT--GRIKDMV-IRGgenlY---PREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGAsPLTAEKVREF 500
Cdd:cd05930 339 DG--NLEflGRIDDQVkIRG----YrieLGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGG-ELDEEELRAH 411
|
490 500
....*....|....*....|....*...
gi 522130465 501 CSGKLAHYKIPRYVHVVDEFPMTVTGKV 528
Cdd:cd05930 412 LAERLPDYMVPSAFVVLDALPLTPNGKV 439
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
50-535 |
1.14e-76 |
|
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: 248.03 E-value: 1.14e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 50 WTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLlvasd 129
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 130 kfktsdypamveevrekcarlehvvvlggeswqelmdagrrgdpaqlahlraglsaDDPINIQYTSGTTGFPKGATLSHH 209
Cdd:cd05912 77 --------------------------------------------------------DDIATIMYTSGTTGKPKGVQQTFG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 210 NILNNGYFVGELCNYTEEDKVCIPVPFYHCFGM--VMGNLACtshgACMVIPAPAFDPRATLEAVAAERCTSLYGVPTMF 287
Cdd:cd05912 101 NHWWSAIGSALNLGLTEDDNWLCALPLFHISGLsiLMRSVIY----GMTVYLVDKFDAEQVLHLINSGKVTIISVVPTML 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 288 IAELNhpDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRmGMAeVSICYGMTETSPVSTQTRADDSIERrVSTVGRVGPHL 367
Cdd:cd05912 177 QRLLE--ILGEGYPNNLRCILLGGGPAPKPLLEQCKEK-GIP-VYQSYGMTETCSQIVTLSPEDALNK-IGSAGKPLFPV 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 368 EVKVVDPEsgltVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAArWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENL 447
Cdd:cd05912 252 ELKIEDDG----QPPYEVGEILLKGPNVTKGYLNRPDATEESFENG-WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENI 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 448 YPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRmreGASPLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGK 527
Cdd:cd05912 327 YPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVV---SERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGK 403
|
....*...
gi 522130465 528 VRKVEMRE 535
Cdd:cd05912 404 LLRHELKQ 411
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
50-529 |
1.70e-76 |
|
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: 248.66 E-value: 1.70e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 50 WTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVninPAYRSH---ELEYVLDQAGIRLLV 126
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPV---PIYPTSsaeQIAYILNDSEAKALF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 127 ASDkfktsdypamveevrekcarlehvvvlggeswqelmdagrrgdpaqlahlraglsADDPINIQYTSGTTGFPKGATL 206
Cdd:cd05907 83 VED-------------------------------------------------------PDDLATIIYTSGTTGRPKGVML 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 207 SHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGACMVIPAPAFDPRATLEAVaaeRCTSLYGVPTM 286
Cdd:cd05907 108 SHRNILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLLDDLSEV---RPTVFLAVPRV 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 287 F---IAELNHPDFGEFD--------LSSLRTGIMAGSPCPVEVMKQViDRMGMaEVSICYGMTETSPVSTQTRADDsieR 355
Cdd:cd05907 185 WekvYAAIKVKAVPGLKrklfdlavGGRLRFAASGGAPLPAELLHFF-RALGI-PVYEGYGLTETSAVVTLNPPGD---N 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 356 RVSTVGRVGPHLEVKVvdpesgltvprGEPGELCTRGYSVMLGYWEQPDKTAEAIDAARWMHTGDLAVMDGDGYVNITGR 435
Cdd:cd05907 260 RIGTVGKPLPGVEVRI-----------ADDGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGR 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 436 IKDMVI-RGGENLYPREIEEFLYTHPDVLDAQVIG----------VPDEkygEELMAWVRMREGASPLTAEKVREFC--- 501
Cdd:cd05907 329 KKDLIItSGGKNISPEPIENALKASPLISQAVVIGdgrpflvaliVPDP---EALEAWAEEHGIAYTDVAELAANPAvra 405
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 522130465 502 ---------SGKLAHY-KIPRYVHVVDEFP-----MTVTGKVR 529
Cdd:cd05907 406 eieaaveaaNARLSRYeQIKKFLLLPEPFTiengeLTPTLKLK 448
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
51-528 |
1.53e-75 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 245.82 E-value: 1.53e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 51 TYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVASDK 130
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 131 FKTSDYPAMveevrekcarlehvvvlggeSWQELMDAGRRGdpaqlAHLRAGLSADDPINIQYTSGTTGFPKGATLSHHN 210
Cdd:TIGR01923 81 LEEKDFQAD--------------------SLDRIEAAGRYE-----TSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 211 ILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMgNLACTSHGACMVIPAPAFDpraTLEAVAAERCTSLYGVPTM---F 287
Cdd:TIGR01923 136 HYASAVGSKENLGFTEDDNWLLSLPLYHISGLSI-LFRWLIEGATLRIVDKFNQ---LLEMIANERVTHISLVPTQlnrL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 288 IAELNHPDfgefdlsSLRTGIMAGSPCPVEVMKQVIDRmGMaEVSICYGMTETSPVSTQTRADDSIERrvSTVGRVGPHL 367
Cdd:TIGR01923 212 LDEGGHNE-------NLRKILLGGSAIPAPLIEEAQQY-GL-PIYLSYGMTETCSQVTTATPEMLHAR--PDVGRPLAGR 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 368 EVKVVDPEsgltvpRGEPGELCTRGYSVMLGYWEQPDKTaEAIDAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENL 447
Cdd:TIGR01923 281 EIKIKVDN------KEGHGEIMVKGANLMKGYLYQGELT-PAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENI 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 448 YPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMRegaSPLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGK 527
Cdd:TIGR01923 354 YPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSE---SDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGK 430
|
.
gi 522130465 528 V 528
Cdd:TIGR01923 431 I 431
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
49-535 |
9.17e-75 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 246.15 E-value: 9.17e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 49 RWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVAS 128
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 129 DKfktsdypaMVEEVREkcARLEHVVVLGGESWQEL-----MDAGRRGDPAQLAHLRAGLSADDPI---------NIQYT 194
Cdd:PRK12406 91 AD--------LLHGLAS--ALPAGVTVLSVPTPPEIaaayrISPALLTPPAGAIDWEGWLAQQEPYdgppvpqpqSMIYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 195 SGTTGFPKG---ATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYH----CFGMVMGNLACTshgacmVIPAPAFDPRA 267
Cdd:PRK12406 161 SGTTGHPKGvrrAAPTPEQAAAAEQMRALIYGLKPGIRALLTGPLYHsapnAYGLRAGRLGGV------LVLQPRFDPEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 268 TLEAVAAERCTSLYGVPTMFIAELNHPDF--GEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAevsIC--YGMTETSPV 343
Cdd:PRK12406 235 LLQLIERHRITHMHMVPTMFIRLLKLPEEvrAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGPV---IYeyYGSTESGAV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 344 STQTrADDSIeRRVSTVGRVGPHLEVKVVDpESGLTVPRGEPGELCTRGYSVML-GYWEQPDKTAEaIDAARWMHTGDLA 422
Cdd:PRK12406 312 TFAT-SEDAL-SHPGTVGKAAPGAELRFVD-EDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAE-IDRGGFITSGDVG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 423 VMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASpLTAEKVREFCS 502
Cdd:PRK12406 388 YLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGAT-LDEADIRAQLK 466
|
490 500 510
....*....|....*....|....*....|...
gi 522130465 503 GKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMRE 535
Cdd:PRK12406 467 ARLAGYKVPKHIEIMAELPREDSGKIFKRRLRD 499
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
28-536 |
6.62e-72 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 239.11 E-value: 6.62e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 28 FDRtVAAFGDRDALVDRAAGGRWTYRELagEVTA--LALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNIN 105
Cdd:PLN02246 30 FER-LSEFSDRPCLIDGATGRVYTYADV--ELLSrrVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTAN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 106 PAYRSHELEYVLDQAGIRLLVASdkfktsdyPAMVEEVREkCARLEHVVVL-------GGESWQELMDAgrrgDPAQLAh 178
Cdd:PLN02246 107 PFYTPAEIAKQAKASGAKLIITQ--------SCYVDKLKG-LAEDDGVTVVtiddppeGCLHFSELTQA----DENELP- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 179 lRAGLSADDPINIQYTSGTTGFPKGATLSHHNILN-----------NGYFvgelcnyTEEDKVCIPVPFYHCFGM--VMg 245
Cdd:PLN02246 173 -EVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTsvaqqvdgenpNLYF-------HSDDVILCVLPMFHIYSLnsVL- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 246 nLACTSHGACMVIpAPAFDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDR 325
Cdd:PLN02246 244 -LCGLRVGAAILI-MPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 326 MGMAEVSICYGMTETSPVSTQTR--ADDSIERRVSTVGRVGPHLEVKVVDPESGLTVPRGEPGELCTRGYSVMLGYWEQP 403
Cdd:PLN02246 322 LPNAVLGQGYGMTEAGPVLAMCLafAKEPFPVKSGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYLNDP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 404 DKTAEAIDAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWV 483
Cdd:PLN02246 402 EATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFV 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 522130465 484 rMREGASPLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMREK 536
Cdd:PLN02246 482 -VRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAK 533
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
51-534 |
2.75e-71 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 234.66 E-value: 2.75e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 51 TYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVASdk 130
Cdd:cd05919 12 TYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTS-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 131 fktsdypamveevrekcarlehvvvlggeswqelmdagrrgdpaqlahlraglsADDPINIQYTSGTTGFPKGATLSHHN 210
Cdd:cd05919 90 ------------------------------------------------------ADDIAYLLYSSGTTGPPKGVMHAHRD 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 211 -ILNNGYFVGELCNYTEEDKV-CIPVPFYhCFGM---VMGNLACtshGACMVIPAPAFDPRATLEAVAAERCTSLYGVPT 285
Cdd:cd05919 116 pLLFADAMAREALGLTPGDRVfSSAKMFF-GYGLgnsLWFPLAV---GASAVLNPGWPTAERVLATLARFRPTVLYGVPT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 286 MFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGmaeVSICYGM--TETSPVSTQTRADDSierRVSTVGRV 363
Cdd:cd05919 192 FYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFG---GPILDGIgaTEVGHIFLSNRPGAW---RLGSTGRP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 364 GPHLEVKVVDPEsGLTVPRGEPGELCTRGYSVMLGYWEQPDKTaEAIDAARWMHTGDLAVMDGDGYVNITGRIKDMVIRG 443
Cdd:cd05919 266 VPGYEIRLVDEE-GHTIPPGEEGDLLVRGPSAAVGYWNNPEKS-RATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 444 GENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASP--LTAEKVREFCSGKLAHYKIPRYVHVVDEFP 521
Cdd:cd05919 344 GQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPqeSLARDIHRHLLERLSAHKVPRRIAFVDELP 423
|
490
....*....|...
gi 522130465 522 MTVTGKVRKVEMR 534
Cdd:cd05919 424 RTATGKLQRFKLR 436
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
187-528 |
4.28e-70 |
|
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: 228.31 E-value: 4.28e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 187 DPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGnLACTSHGACMVIpAPAFDPR 266
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLA-LATFHAGGANVV-MEKFDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 267 ATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRtgIMAGSPCPvevmkQVIDR---MGMAEVSICYGMTETSPV 343
Cdd:cd17637 79 EALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLR--HVLGLDAP-----ETIQRfeeTTGATFWSLYGQTETSGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 344 STQTRADDsierRVSTVGRVGPHLEVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAArWMHTGDLAV 423
Cdd:cd17637 152 VTLSPYRE----RPGSAGRPGPLVRVRIVD-DNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG-WHHTGDLGR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 424 MDGDGYVNITGRI--KDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASpLTAEKVREFC 501
Cdd:cd17637 226 FDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGAT-LTADELIEFV 304
|
330 340
....*....|....*....|....*..
gi 522130465 502 SGKLAHYKIPRYVHVVDEFPMTVTGKV 528
Cdd:cd17637 305 GSRIARYKKPRYVVFVEALPKTADGSI 331
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
37-536 |
4.10e-69 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 231.96 E-value: 4.10e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 37 DRDALVDRAagGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYV 116
Cdd:PRK13382 58 DRPGLIDEL--GTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 117 LDQAGIRLLVASDKF-KTSD-------YPAMVEEVREKCARLEHVVVLGGESWQELMDAGRRGDpaqlahlraglsaddp 188
Cdd:PRK13382 136 VTREGVDTVIYDEEFsATVDraladcpQATRIVAWTDEDHDLTVEVLIAAHAGQRPEPTGRKGR---------------- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 189 iNIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMvmGNLACTSHGACMVIPAPAFDPRAT 268
Cdd:PRK13382 200 -VILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWGF--SQLVLAASLACTIVTRRRFDPEAT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 269 LEAVAAERCTSLYGVPTMF--IAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSIcYGMTETSPVSTQ 346
Cdd:PRK13382 277 LDLIDRHRATGLAVVPVMFdrIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNN-YNATEAGMIATA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 347 TRADdsIERRVSTVGRVGPHLEVKVVDPEsGLTVPRGEPGELCTRGYSVMLGYweQPDKTAEAIDAarWMHTGDLAVMDG 426
Cdd:PRK13382 356 TPAD--LRAAPDTAGRPAEGTEIRILDQD-FREVPTGEVGTIFVRNDTQFDGY--TSGSTKDFHDG--FMASGDVGYLDE 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 427 DGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASpLTAEKVREFCSGKLA 506
Cdd:PRK13382 429 NGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGAS-ATPETLKQHVRDNLA 507
|
490 500 510
....*....|....*....|....*....|
gi 522130465 507 HYKIPRYVHVVDEFPMTVTGKVRKVEMREK 536
Cdd:PRK13382 508 NYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
19-531 |
2.17e-68 |
|
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: 229.28 E-value: 2.17e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 19 LLGDTIGDNFDRTVAAfgdrDALVDRaaGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIG 98
Cdd:TIGR03098 1 LLHHLLEDAAARLPDA----TALVHH--DRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 99 AILVNINPAYRSHELEYVLDQAGIRLLVASdkfktSDYPAMVEEVREKCARLEHVVVLGGE-------------SWQELM 165
Cdd:TIGR03098 75 GVFVPINPLLKAEQVAHILADCNVRLLVTS-----SERLDLLHPALPGCHDLRTLIIVGDPahaseghpgeepaSWPKLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 166 DAGrrgdPAQLAHLRAglsADDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMG 245
Cdd:TIGR03098 150 ALG----DADPPHPVI---DSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 246 NLAcTSHGAcMVIPAPAFDPRATLEAVAAERCTSLYGVPTMFiAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDR 325
Cdd:TIGR03098 223 TTA-FYVGA-TVVLHDYLLPRDVLKALEKHGITGLAAVPPLW-AQLAQLDWPESAAPSLRYLTNSGGAMPRATLSRLRSF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 326 MGMAEVSICYGMTETspVSTQTRADDSIERRVSTVGRVGPHLEVKVVDPESGLTVPrGEPGELCTRGYSVMLGYWEQPDK 405
Cdd:TIGR03098 300 LPNARLFLMYGLTEA--FRSTYLPPEEVDRRPDSIGKAIPNAEVLVLREDGSECAP-GEEGELVHRGALVAMGYWNDPEK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 406 TAEAI-------------DAARWmhTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPD 472
Cdd:TIGR03098 377 TAERFrplppfpgelhlpELAVW--SGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPD 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 522130465 473 EKYGEELMAWVRMREGAsPLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKV 531
Cdd:TIGR03098 455 PTLGQAIVLVVTPPGGE-ELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRK 512
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
59-528 |
2.96e-67 |
|
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: 224.63 E-value: 2.96e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 59 VTALALGLVARGIGKGDRVGIWSPNRAE--WTFLQ--YATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVASDKFKTS 134
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTyiELSFAvaYAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 135 DYPAMVeevrekcARLEHVVVLGGESWqelmDAGRRGDPAQLahlragLSADDPINIQYTSGTTGFPKGATLSHHNILNN 214
Cdd:cd05922 83 LRDALP-------ASPDPGTVLDADGI----RAARASAPAHE------VSHEDLALLLYTSGSTGSPKLVRLSHQNLLAN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 215 GYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLAcTSHGACMVIPAPAFDPRATLEAVAAERCTSLYGVPTMFiAELNHP 294
Cdd:cd05922 146 ARSIAEYLGITADDRALTVLPLSYDYGLSVLNTH-LLRGATLVLTNDGVLDDAFWEDLREHGATGLAGVPSTY-AMLTRL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 295 DFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSICYGMTETSPVSTqTRADDSIERRVSTVGRVGPHLEVKVVDP 374
Cdd:cd05922 224 GFDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMT-YLPPERILEKPGSIGLAIPGGEFEILDD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 375 ESGLTVPrGEPGELCTRGYSVMLGYWEQPDKTAEAIDAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEE 454
Cdd:cd05922 303 DGTPTPP-GEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEA 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522130465 455 FLYTHPDVLDAQVIGVPDEKyGEELMAWVrmrEGASPLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKV 528
Cdd:cd05922 382 AARSIGLIIEAAAVGLPDPL-GEKLALFV---TAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKV 451
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
44-534 |
5.11e-67 |
|
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: 223.51 E-value: 5.11e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 44 RAAGGRWTYRELAGEVTALALGLVAR-GIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGI 122
Cdd:cd05958 5 RSPEREWTYRDLLALANRIANVLVGElGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 123 RLLVASDKFKTSDypamveevrekcarlehvvvlggeswqelmdagrrgdpaqlahlraglsadDPINIQYTSGTTGFPK 202
Cdd:cd05958 85 TVALCAHALTASD---------------------------------------------------DICILAFTSGTTGAPK 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 203 GATLSHHNILN--NGYFVGELcNYTEEDKVCIPVPFYHCFGMvMGNLACTSHGACMVIPAPAFDPRATLEAVAAERCTSL 280
Cdd:cd05958 114 ATMHFHRDPLAsaDRYAVNVL-RLREDDRFVGSPPLAFTFGL-GGVLLFPFGVGASGVLLEEATPDLLLSAIARYKPTVL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 281 YGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMaEVSICYGMTETSPVSTQTRADDSierRVSTV 360
Cdd:cd05958 192 FTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGI-PIIDGIGSTEMFHIFISARPGDA---RPGAT 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 361 GRVGPHLEVKVVDpESGLTVPRGEPGELCTRGYSvmlGYWEQPDKTAEAIDAARWMHTGDLAVMDGDGYVNITGRIKDMV 440
Cdd:cd05958 268 GKPVPGYEAKVVD-DEGNPVPDGTIGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMI 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 441 IRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREG--ASPLTAEKVREFCSGKLAHYKIPRYVHVVD 518
Cdd:cd05958 344 VSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGviPGPVLARELQDHAKAHIAPYKYPRAIEFVT 423
|
490
....*....|....*.
gi 522130465 519 EFPMTVTGKVRKVEMR 534
Cdd:cd05958 424 ELPRTATGKLQRFALR 439
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
33-535 |
1.54e-66 |
|
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: 225.10 E-value: 1.54e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 33 AAFGDRDALVDRAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHE 112
Cdd:cd17642 28 ASVPGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 113 LEYVLDQAGIRLLVASDKfkTSDypaMVEEVREKCARLEHVVVLGG-ESWQELMDAgrrgDPAQLAHLRAGLSADDPIN- 190
Cdd:cd17642 108 LDHSLNISKPTIVFCSKK--GLQ---KVLNVQKKLKIIKTIIILDSkEDYKGYQCL----YTFITQNLPPGFNEYDFKPp 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 191 ----------IQYTSGTTGFPKGATLSHHNIL------NNGYFVGELcnyTEEDKVCIPVPFYHCFGM--VMGNLACtsh 252
Cdd:cd17642 179 sfdrdeqvalIMNSSGSTGLPKGVQLTHKNIVarfshaRDPIFGNQI---IPDTAILTVIPFHHGFGMftTLGYLIC--- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 253 GACMVIpAPAFDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVS 332
Cdd:cd17642 253 GFRVVL-MYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIR 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 333 ICYGMTE-TSPVSTQTRADDsierRVSTVGRVGPHLEVKVVDPESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAID 411
Cdd:cd17642 332 QGYGLTEtTSAILITPEGDD----KPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALID 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 412 AARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASp 491
Cdd:cd17642 408 KDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKT- 486
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 522130465 492 LTAEKVREFCSGKLAHYKIPR-YVHVVDEFPMTVTGKVRKVEMRE 535
Cdd:cd17642 487 MTEKEVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
38-534 |
2.41e-65 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 222.37 E-value: 2.41e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 38 RDALVDRAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNrAEWtFLQY--ATAKIGAILVNINPAYRSHELEY 115
Cdd:PLN02860 21 GNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALN-SDL-YLEWllAVACAGGIVAPLNYRWSFEEAKS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 116 VLDQAGIRLLVAS-------DKFKTSDYPAMVEEV--REKCARLEHV---VVLGGESWQelmdagRRGDPAQLAHLRAgl 183
Cdd:PLN02860 99 AMLLVRPVMLVTDetcsswyEELQNDRLPSLMWQVflESPSSSVFIFlnsFLTTEMLKQ------RALGTTELDYAWA-- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 184 sADDPINIQYTSGTTGFPKGATLSHHNI----LNNGYFVGelcnYTEEDKVCIPVPFYH------CFGMVMGnlactshG 253
Cdd:PLN02860 171 -PDDAVLICFTSGTTGRPKGVTISHSALivqsLAKIAIVG----YGEDDVYLHTAPLCHigglssALAMLMV-------G 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 254 ACMVIpAPAFDPRATLEAVAAERCTSLYGVPTMF--IAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEV 331
Cdd:PLN02860 239 ACHVL-LPKFDAKAALQAIKQHNVTSMITVPAMMadLISLTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 332 SICYGMTET-SPVSTQTRADDSIERRVST-------------------VGRVGPHLEVKVVDPESGLTvprgepGELCTR 391
Cdd:PLN02860 318 FSAYGMTEAcSSLTFMTLHDPTLESPKQTlqtvnqtksssvhqpqgvcVGKPAPHVELKIGLDESSRV------GRILTR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 392 GYSVMLGYWEQPDKTAEAIDAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVP 471
Cdd:PLN02860 392 GPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVP 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522130465 472 DEKYGEELMAWVRMREG-----ASPLTAEKVREFCSGKLAH---------YKIPR-YVHVVDEFPMTVTGKVRKVEMR 534
Cdd:PLN02860 472 DSRLTEMVVACVRLRDGwiwsdNEKENAKKNLTLSSETLRHhcreknlsrFKIPKlFVQWRKPFPLTTTGKIRRDEVR 549
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
68-535 |
1.63e-64 |
|
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: 218.02 E-value: 1.63e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 68 ARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAIlvninPAYRSHELEYVLDQAGIRLLvasdkfktsdypamveevreKC 147
Cdd:cd05929 36 AEGVWIADGVYIYLINSILTVFAAAAAWKCGAC-----PAYKSSRAPRAEACAIIEIK--------------------AA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 148 ARLEHVVVLGGESWqelmdaGRRGDPAQLAHLRAGLSADD--PINIQYTSGTTGFPKGATLSH-HNILNNGYFVGE--LC 222
Cdd:cd05929 91 ALVCGLFTGGGALD------GLEDYEAAEGGSPETPIEDEaaGWKMLYSGGTTGRPKGIKRGLpGGPPDNDTLMAAalGF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 223 NYTEEDKVCIPVPFYHC--FGMVMGNLACTSHgacmVIPAPAFDPRATLEAVAAERCTSLYGVPTMFIAELNHPD--FGE 298
Cdd:cd05929 165 GPGADSVYLSPAPLYHAapFRWSMTALFMGGT----LVLMEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEavRNA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 299 FDLSSLRTGIMAGSPCPVEVMKQVIDRMGmaEVSI-CYGMTETSPvSTQTRADDSIERRVStVGRVGPHlEVKVVDpESG 377
Cdd:cd05929 241 YDLSSLKRVIHAAAPCPPWVKEQWIDWGG--PIIWeYYGGTEGQG-LTIINGEEWLTHPGS-VGRAVLG-KVHILD-EDG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 378 LTVPRGEPGELCTRGYSVMLgYWEQPDKTAEAIDAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLY 457
Cdd:cd05929 315 NEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 458 THPDVLDAQVIGVPDEKYGEELMAWVRMREGASPLT--AEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMRE 535
Cdd:cd05929 394 AHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTalAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
47-534 |
2.39e-64 |
|
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: 217.97 E-value: 2.39e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 47 GGRWTYRELAGEVTALALgLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLV 126
Cdd:cd05909 5 GTSLTYRKLLTGAIALAR-KLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 127 ASDKF---------KTSDYPAMV---EEVREKCARLEHVVV-LGGESWQELMDagrrgdpaqLAHLRAGLSADDPINIQY 193
Cdd:cd05909 84 TSKQFieklklhhlFDVEYDARIvylEDLRAKISKADKCKAfLAGKFPPKWLL---------RIFGVAPVQPDDPAVILF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 194 TSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGACMVIPAPAFDPRATLEAVA 273
Cdd:cd05909 155 TSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNPLDYKKIPELIY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 274 AERCTSLYGVPTMFIAELN--HPDfgefDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSiCYGMTETSPVSTQTRADd 351
Cdd:cd05909 235 DKKATILLGTPTFLRGYARaaHPE----DFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILE-GYGTTECSPVISVNTPQ- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 352 sIERRVSTVGRVGPHLEVKVVDPESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIdAARWMHTGDLAVMDGDGYVN 431
Cdd:cd05909 309 -SPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 432 ITGRIKDMVIRGGENLYPREIEEFLYTH--PDVLDAqVIGVPDEKYGEELMAWVRMREgaspLTAEKVREFC-SGKLAHY 508
Cdd:cd05909 387 ITGRLSRFAKIAGEMVSLEAIEDILSEIlpEDNEVA-VVSVPDGRKGEKIVLLTTTTD----TDPSSLNDILkNAGISNL 461
|
490 500
....*....|....*....|....*.
gi 522130465 509 KIPRYVHVVDEFPMTVTGKVRKVEMR 534
Cdd:cd05909 462 AKPSYIHQVEEIPLLGTGKPDYVTLK 487
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
26-536 |
1.77e-63 |
|
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: 216.98 E-value: 1.77e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 26 DNFDRTVAAFGDRDALV---DRAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILV 102
Cdd:cd05970 21 DVVDAMAKEYPDKLALVwcdDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 103 NINPAYRSHELEYVLDQAGIRLLVASDKfktSDYPAMVEEVREKCARLEHVVVLGG---ESW----QELMDAGRRGDPAQ 175
Cdd:cd05970 101 PATHQLTAKDIVYRIESADIKMIVAIAE---DNIPEEIEKAAPECPSKPKLVWVGDpvpEGWidfrKLIKNASPDFERPT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 176 LAHLRAGlsaDDPINIQYTSGTTGFPKgaTLSHHNILNNGYFV-GELCNYTEEDKVCIPVP---FYHC-FGMVMGNLACT 250
Cdd:cd05970 178 ANSYPCG---EDILLVYFSSGTTGMPK--MVEHDFTYPLGHIVtAKYWQNVREGGLHLTVAdtgWGKAvWGKIYGQWIAG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 251 ShgACMVIPAPAFDPRATLEAVAAERCTSLYGVPTMFiAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMaE 330
Cdd:cd05970 253 A--AVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIY-RFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGI-K 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 331 VSICYGMTETSpVSTQTRAddSIERRVSTVGRVGPHLEVKVVDPEsGLTVPRGEPGELCTR---GYSVML--GYWEQPDK 405
Cdd:cd05970 329 LMEGFGQTETT-LTIATFP--WMEPKPGSMGKPAPGYEIDLIDRE-GRSCEAGEEGEIVIRtskGKPVGLfgGYYKDAEK 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 406 TAEAIDAARWmHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRM 485
Cdd:cd05970 405 TAEVWHDGYY-HTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVL 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 522130465 486 REGASP---LTAEkVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMREK 536
Cdd:cd05970 484 AKGYEPseeLKKE-LQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRER 536
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
37-534 |
1.88e-63 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 216.03 E-value: 1.88e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 37 DRDALVDRAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYV 116
Cdd:PRK13390 12 DRPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 117 LDQAGIRLLVASdkfktsdyPAMVEEVREKCARLEHVVVLGGEswqelMDAgrrgdpaqLAHLRAGLSADDP-------- 188
Cdd:PRK13390 92 VGDSGARVLVAS--------AALDGLAAKVGADLPLRLSFGGE-----IDG--------FGSFEAALAGAGPrlteqpcg 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 189 INIQYTSGTTGFPKG--ATLSHHNILNNG----YFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGAcmVIPAPA 262
Cdd:PRK13390 151 AVMLYSSGTTGFPKGiqPDLPGRDVDAPGdpivAIARAFYDISESDIYYSSAPIYHAAPLRWCSMVHALGGT--VVLAKR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 263 FDPRATLEAVAAERCTSLYGVPTMFIA--ELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGmaevSICYGMTET 340
Cdd:PRK13390 229 FDAQATLGHVERYRITVTQMVPTMFVRllKLDADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLG----PIVYEYYSS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 341 SPVSTQTRADDSieRRVSTVGRVGPHL--EVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAAR--WM 416
Cdd:PRK13390 305 TEAHGMTFIDSP--DWLAHPGSVGRSVlgDLHICD-DDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 417 HTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASPlTAEK 496
Cdd:PRK13390 382 TVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRG-SDEL 460
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 522130465 497 VRE---FCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMR 534
Cdd:PRK13390 461 ARElidYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
28-528 |
9.68e-63 |
|
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: 213.60 E-value: 9.68e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 28 FDRTVAAFGDRDALVDRaaGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPA 107
Cdd:cd12117 3 FEEQAARTPDAVAVVYG--DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 108 YRSHELEYVLDQAGIRLLVASDKFKTSdypamveevrekcARLEHVVVLGGESWqelmdagrrgDPAQLAHLRAGLSADD 187
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRSLAGR-------------AGGLEVAVVIDEAL----------DAGPAGNPAVPVSPDD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 188 PINIQYTSGTTGFPKGATLSHHNILN---NGYFVGElcnyTEEDKV--CIPVPF----YHCFGmvmgnlaCTSHGACMVI 258
Cdd:cd12117 138 LAYVMYTSGSTGRPKGVAVTHRGVVRlvkNTNYVTL----GPDDRVlqTSPLAFdastFEIWG-------ALLNGARLVL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 259 --PAPAFDPRATLEAVAAERCTSLYGVPTMF--IAELNhPDFgefdLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSIC 334
Cdd:cd12117 207 apKGTLLDPDALGALIAEEGVTVLWLTAALFnqLADED-PEC----FAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 335 YGMTETSPVSTQ--TRADDSIERRVStVGRVGPHLEVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAE---- 408
Cdd:cd12117 282 YGPTENTTFTTShvVTELDEVAGSIP-IGRPIANTRVYVLD-EDGRPVPPGVPGELYVGGDGLALGYLNRPALTAErfva 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 409 --AIDAARWMHTGDLAVMDGDGYVNITGRIKDMV-IRGgenlY---PREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAW 482
Cdd:cd12117 360 dpFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVkIRG----FrieLGEIEAALRAHPGVREAVVVVREDAGGDKRLVAY 435
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 522130465 483 VRMREgasPLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKV 528
Cdd:cd12117 436 VVAEG---ALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKV 478
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
37-534 |
2.83e-62 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 213.70 E-value: 2.83e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 37 DRDALVDraaGGR-WTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEY 115
Cdd:PRK10946 38 DAIAVIC---GERqFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVAPVNALFSHQRSELNA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 116 VLDQAGIRLLVASDKFKTSDYPAMVEEVREKCARLEHVVVLGGESWQELMDAGRRGDPAQLAHLRAglsADDPINIQYTS 195
Cdd:PRK10946 115 YASQIEPALLIADRQHALFSDDDFLNTLVAEHSSLRVVLLLNDDGEHSLDDAINHPAEDFTATPSP---ADEVAFFQLSG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 196 GTTGFPKGATLSHhnilnNGYFVG-----ELCNYTEEDKVCIPVPFYHCFGMVM-GNLACTSHGACMVIpapAFDPRATL 269
Cdd:PRK10946 192 GSTGTPKLIPRTH-----NDYYYSvrrsvEICGFTPQTRYLCALPAAHNYPMSSpGALGVFLAGGTVVL---APDPSATL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 270 --EAVAAERCTSLYGVP---TMFIAELNHPDFGEfDLSSLRTGIMAGSPCPVEVMKQVIDRM--------GMAEVSICYg 336
Cdd:PRK10946 264 cfPLIEKHQVNVTALVPpavSLWLQAIAEGGSRA-QLASLKLLQVGGARLSETLARRIPAELgcqlqqvfGMAEGLVNY- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 337 mtetspvstqTRADDSIERRVSTVGR-VGPHLEVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAARW 415
Cdd:PRK10946 342 ----------TRLDDSDERIFTTQGRpMSPDDEVWVAD-ADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 416 MHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREgasPLTAE 495
Cdd:PRK10946 411 YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKE---PLKAV 487
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 522130465 496 KVREFCSGK-LAHYKIPRYVHVVDEFPMTVTGKVRKVEMR 534
Cdd:PRK10946 488 QLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLR 527
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
193-538 |
5.23e-62 |
|
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: 208.10 E-value: 5.23e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 193 YTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGACMVIPAPA--FDPRATLE 270
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAgyRNPGLFDN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 271 ---AVAAERCTSLYGVPTMFIAELNHPDfgEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGmaeVSIC--YGMTETSPVST 345
Cdd:cd05944 89 fwkLVERYRITSLSTVPTVYAALLQVPV--NADISSLRFAMSGAAPLPVELRARFEDATG---LPVVegYGLTEATCLVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 346 qtRADDSIERRVSTVGRVGPHLEVKVV--DPESGLTVPRG--EPGELCTRGYSVMLGYWEQPDKTAEAIDAaRWMHTGDL 421
Cdd:cd05944 164 --VNPPDGPKRPGSVGLRLPYARVRIKvlDGVGRLLRDCApdEVGEICVAGPGVFGGYLYTEGNKNAFVAD-GWLNTGDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 422 AVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASpLTAEKVREFC 501
Cdd:cd05944 241 GRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAV-VEEEELLAWA 319
|
330 340 350
....*....|....*....|....*....|....*...
gi 522130465 502 SGKLAHY-KIPRYVHVVDEFPMTVTGKVRKVEMREKSI 538
Cdd:cd05944 320 RDHVPERaAVPKHIEVLEELPVTAVGKVFKPALRADAI 357
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
50-534 |
9.81e-62 |
|
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: 209.12 E-value: 9.81e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 50 WTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVASd 129
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 130 kfktsdypamveevrekcarlehvvvlggeswqelmdagrrgdpaqlahlraglsADDPINIQYTSGTTGFPKGATLSHH 209
Cdd:cd05972 80 -------------------------------------------------------AEDPALIYFTSGTTGLPKGVLHTHS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 210 NILNNGYFVGELCNYTEEDKV-CIPVP--FYHCFGMVMGNLActsHGAC-MVIPAPAFDPRATLEAVAAERCTSLYGVPT 285
Cdd:cd05972 105 YPLGHIPTAAYWLGLRPDDIHwNIADPgwAKGAWSSFFGPWL---LGATvFVYEGPRFDAERILELLERYGVTSFCGPPT 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 286 ---MFIAELNHpdfgEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMaEVSICYGMTETSPVSTQTRAddsIERRVSTVGR 362
Cdd:cd05972 182 ayrMLIKQDLS----SYKFSHLRLVVSAGEPLNPEVIEWWRAATGL-PIRDGYGQTETGLTVGNFPD---MPVKPGSMGR 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 363 VGPHLEVKVVDpESGLTVPRGEPGELCTR--GYSVMLGYWEQPDKTAEAIDAArWMHTGDLAVMDGDGYVNITGRIKDMV 440
Cdd:cd05972 254 PTPGYDVAIID-DDGRELPPGEEGDIAIKlpPPGLFLGYVGDPEKTEASIRGD-YYLTGDRAYRDEDGYFWFVGRADDII 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 441 IRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASPL--TAEKVREFCSGKLAHYKIPRYVHVVD 518
Cdd:cd05972 332 KSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSeeLAEELQGHVKKVLAPYKYPREIEFVE 411
|
490
....*....|....*.
gi 522130465 519 EFPMTVTGKVRKVEMR 534
Cdd:cd05972 412 ELPKTISGKIRRVELR 427
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
51-530 |
4.16e-61 |
|
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: 208.45 E-value: 4.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 51 TYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVASDK 130
Cdd:cd05914 9 TYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 131 fktsdypamveevrekcarlehvvvlggeswqelmdagrrgdpaqlahlraglsaDDPINIQYTSGTTGFPKGATLSHHN 210
Cdd:cd05914 89 -------------------------------------------------------DDVALINYTSGTTGNSKGVMLTYRN 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 211 ILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGACMV----IPAPafdpraTLEAVAAERCTSLYGVPTM 286
Cdd:cd05914 114 IVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVfldkIPSA------KIIALAFAQVTPTLGVPVP 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 287 FI-------AELN----------------------------HPDFGefdlSSLRTGIMAGSPCPVEVmKQVIDRMGMAeV 331
Cdd:cd05914 188 LViekifkmDIIPkltlkkfkfklakkinnrkirklafkkvHEAFG----GNIKEFVIGGAKINPDV-EEFLRTIGFP-Y 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 332 SICYGMTETSPVSTQTRADdsiERRVSTVGRVGPHLEVKVVDPEsgltvPRGEPGELCTRGYSVMLGYWEQPDKTAEAID 411
Cdd:cd05914 262 TIGYGMTETAPIISYSPPN---RIRLGSAGKVIDGVEVRIDSPD-----PATGEGEIIVRGPNVMKGYYKNPEATAEAFD 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 412 AARWMHTGDLAVMDGDGYVNITGRIKDMVIRG-GENLYPREIEEFLYTHPDVLDAQVIgvpDEKYGEELMAWV-----RM 485
Cdd:cd05914 334 KDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVLESLVV---VQEKKLVALAYIdpdflDV 410
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 522130465 486 REGASPLTAEKVREFCSGKLaHYKIPRYVHVVD------EFPMTVTGKVRK 530
Cdd:cd05914 411 KALKQRNIIDAIKWEVRDKV-NQKVPNYKKISKvkivkeEFEKTPKGKIKR 460
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
30-535 |
4.52e-61 |
|
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: 210.56 E-value: 4.52e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 30 RTVAAFGDRDALV----DRAAGGRWTYRELAGEVTALALGLVARGiGKGDRVGIWSPNRAEW--TFL--QYAtakiGAIL 101
Cdd:cd05931 1 RRAAARPDRPAYTflddEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFvaAFLgcLYA----GAIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 102 VninPAY-----RSHE-LEYVLDQAGIRLLVASDKFKtsdypamvEEVREKCARLEHVVVLGGESWQELMDAGRRGDPAq 175
Cdd:cd05931 76 V---PLPpptpgRHAErLAAILADAGPRVVLTTAAAL--------AAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPP- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 176 lahlrAGLSADDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGAC 255
Cdd:cd05931 144 -----PSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 256 MVIPAP-AF--DPRATLEAVAAERCTSLYGvptmfiaelnhPDFG--------------EFDLSSLRTGIMAGSPCPVEV 318
Cdd:cd05931 219 SVLMSPaAFlrRPLRWLRLISRYRATISAA-----------PNFAydlcvrrvrdedleGLDLSSWRVALNGAEPVRPAT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 319 MKQVIDRM---GMAEVSI--CYGMTE------TSPVSTQTR-----------------ADDSIERRVSTVGRVGPHLEVK 370
Cdd:cd05931 288 LRRFAEAFapfGFRPEAFrpSYGLAEatlfvsGGPPGTGPVvlrvdrdalagravavaADDPAARELVSCGRPLPDQEVR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 371 VVDPESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAE------AIDAARWMHTGDLAVMdGDGYVNITGRIKDMVIRGG 444
Cdd:cd05931 368 IVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaATDEGGWLRTGDLGFL-HDGELYITGRLKDLIIVRG 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 445 ENLYPREIEEFLYTHPDVLDAQ---VIGVPDEKyGEELMAWVRMREGASPLTAEKVREFCSGKLA--HYKIPRYVHVV-- 517
Cdd:cd05931 447 RNHYPQDIEATAEEAHPALRPGcvaAFSVPDDG-EERLVVVAEVERGADPADLAAIAAAIRAAVAreHGVAPADVVLVrp 525
|
570
....*....|....*...
gi 522130465 518 DEFPMTVTGKVRKVEMRE 535
Cdd:cd05931 526 GSIPRTSSGKIQRRACRA 543
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
16-535 |
1.46e-60 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 209.18 E-value: 1.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 16 EVPLLGDTIGDNFDRTvaaFGDRDALVDRAAGG--RWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYA 93
Cdd:PRK07008 7 DMPLLISSLIAHAARH---AGDTEIVSRRVEGDihRYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 94 TAKIGAILVNINPAYRSHELEYVLDQAGIRLLVasdkFKTSDYPaMVEEVREKCARLEHvvvlggesWQELMDAgrrgdp 173
Cdd:PRK07008 84 VSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVL----FDLTFLP-LVDALAPQCPNVKG--------WVAMTDA------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 174 aqlAHLRAG----LSADDPINIQ------------------YTSGTTGFPKGATLSHHNILNNGYFVG--ELCNYTEEDK 229
Cdd:PRK07008 145 ---AHLPAGstplLCYETLVGAQdgdydwprfdenqasslcYTSGTTGNPKGALYSHRSTVLHAYGAAlpDAMGLSARDA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 230 VCIPVPFYH--CFGMvmgNLACTSHGACMVIPAPAFDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTG 307
Cdd:PRK07008 222 VLPVVPMFHvnAWGL---PYSAPLTGAKLVLPGPDLDGKSLYELIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 308 IMAGSPCPVEVMKQVIDRMGMaEVSICYGMTETSPVST--------QTRADDSIERRVSTVGRVGPHLEVKVVDPEsGLT 379
Cdd:PRK07008 299 VIGGSACPPAMIRTFEDEYGV-EVIHAWGMTEMSPLGTlcklkwkhSQLPLDEQRKLLEKQGRVIYGVDMKIVGDD-GRE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 380 VP-RGEP-GELCTRGYSVMLGYWEQpdKTAEAIDaaRWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLY 457
Cdd:PRK07008 377 LPwDGKAfGDLQVRGPWVIDRYFRG--DASPLVD--GWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAV 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522130465 458 THPDVLDAQVIGVPDEKYGEELMAWVRMREGASpLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMRE 535
Cdd:PRK07008 453 AHPAVAEAACIACAHPKWDERPLLVVVKRPGAE-VTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLRE 529
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
28-528 |
1.63e-60 |
|
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: 207.58 E-value: 1.63e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 28 FDRTVAAFGDRDALVDRaaGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPA 107
Cdd:cd17651 1 FERQAARTPDAPALVAE--GRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 108 YRSHELEYVLDQAGIRLLVASDKFKtsdypamveevrekcARLEHVVVLGGESWQELMDAGRRGDPaqlahlRAGLSADD 187
Cdd:cd17651 79 YPAERLAFMLADAGPVLVLTHPALA---------------GELAVELVAVTLLDQPGAAAGADAEP------DPALDADD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 188 PINIQYTSGTTGFPKGATLSHHNILNngyFVGELCNYTE---EDKVC--IPVPFYHCFGMVMGNLACtshGACMVIPAPA 262
Cdd:cd17651 138 LAYVIYTSGSTGRPKGVVMPHRSLAN---LVAWQARASSlgpGARTLqfAGLGFDVSVQEIFSTLCA---GATLVLPPEE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 263 --FDPRATLEAVAAERCTSLYgVPTMFIAEL-NHPDFGEFDLSSLRTGIMAGSPCPV-EVMKQVIDRMGMAEVSICYGMT 338
Cdd:cd17651 212 vrTDPPALAAWLDEQRISRVF-LPTVALRALaEHGRPLGVRLAALRYLLTGGEQLVLtEDLREFCAGLPGLRLHNHYGPT 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 339 ETSPVSTQT-RADDSIERRVSTVGRVGPHLEVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDA----- 412
Cdd:cd17651 291 ETHVVTALSlPGDPAAWPAPPPIGRPIDNTRVYVLD-AALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPdpfvp 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 413 -ARWMHTGDLAVMDGDGYVNITGRIKDMV-IRgGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGAS 490
Cdd:cd17651 370 gARMYRTGDLARWLPDGELEFLGRADDQVkIR-GFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAP 448
|
490 500 510
....*....|....*....|....*....|....*...
gi 522130465 491 PLTAEkVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKV 528
Cdd:cd17651 449 VDAAE-LRAALATHLPEYMVPSAFVLLDALPLTPNGKL 485
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
33-534 |
2.03e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 207.15 E-value: 2.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 33 AAFGDRDALvdRAAGGRWTYRELAGEVTAlalglVARGIGKGDRVGIWspnrAEWTfLQYATAKIGAIL-----VNINPA 107
Cdd:PRK07787 11 AAADIADAV--RIGGRVLSRSDLAGAATA-----VAERVAGARRVAVL----ATPT-LATVLAVVGALIagvpvVPVPPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 108 YRSHELEYVLDQAGIRLLVAsdkfktsdypamveEVREKCARLEHV-VVLGGESWqelmdagrrgdpaqlaHLRAGLSAD 186
Cdd:PRK07787 79 SGVAERRHILADSGAQAWLG--------------PAPDDPAGLPHVpVRLHARSW----------------HRYPEPDPD 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 187 DPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGACMVIPApafdpR 266
Cdd:PRK07787 129 APALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTG-----R 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 267 ATLEAVAAE---RCTSLYGVPTMF--IAElnHPDFGEfDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSIcYGMTETS 341
Cdd:PRK07787 204 PTPEAYAQAlseGGTLYFGVPTVWsrIAA--DPEAAR-ALRGARLLVSGSAALPVPVFDRLAALTGHRPVER-YGMTETL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 342 pVSTQTRADDsiERRVSTVGRVGPHLEVKVVDpESGLTVPR-GEP-GELCTRGYSVMLGYWEQPDKTAEAIDAARWMHTG 419
Cdd:PRK07787 280 -ITLSTRADG--ERRPGWVGLPLAGVETRLVD-EDGGPVPHdGETvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 420 DLAVMDGDGYVNITGRIK-DMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVrmrEGASPLTAEKVR 498
Cdd:PRK07787 356 DVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYV---VGADDVAADELI 432
|
490 500 510
....*....|....*....|....*....|....*.
gi 522130465 499 EFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMR 534
Cdd:PRK07787 433 DFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
28-528 |
3.63e-60 |
|
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: 206.74 E-value: 3.63e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 28 FDRTVAAFGDRDALVDraAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPA 107
Cdd:cd17646 4 VAEQAARTPDAPAVVD--EGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 108 YRSHELEYVLDQAGIRLLVASdkfktsdypamvEEVREKCARLEHVVVLGGESWQELMDAG--RRGDPAQLAHLraglsa 185
Cdd:cd17646 82 YPADRLAYMLADAGPAVVLTT------------ADLAARLPAGGDVALLGDEALAAPPATPplVPPRPDNLAYV------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 186 ddpiniQYTSGTTGFPKGATLSHHNILNngYFVGELCNY--TEEDKVCIPVPF------YHCFGMVMgnlactsHGACMV 257
Cdd:cd17646 144 ------IYTSGSTGRPKGVMVTHAGIVN--RLLWMQDEYplGPGDRVLQKTPLsfdvsvWELFWPLV-------AGARLV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 258 IPAPAF--DPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGefDLSSLRTGIMAGSPCPVEVMKQVIDRMGmAEVSICY 335
Cdd:cd17646 209 VARPGGhrDPAYLAALIREHGVTTCHFVPSMLRVFLAEPAAG--SCASLRRVFCSGEALPPELAARFLALPG-AELHNLY 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 336 GMTETSPVSTQTRADDSIERRVSTVGRVGPHLEVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDA--- 412
Cdd:cd17646 286 GPTEAAIDVTHWPVRGPAETPSVPIGRPVPNTRLYVLD-DALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPdpf 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 413 ---ARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGA 489
Cdd:cd17646 365 gpgSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGA 444
|
490 500 510
....*....|....*....|....*....|....*....
gi 522130465 490 SPLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKV 528
Cdd:cd17646 445 AGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKL 483
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
187-529 |
3.50e-58 |
|
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: 196.75 E-value: 3.50e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 187 DPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHcFGMVMGNLAcTSH--GACMVIPApaFD 264
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFH-IGTLMFTLA-TFHagGTNVFVRR--VD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 265 PRATLEAVAAERCTSLYGVPTMF--IAELNhpDFGEFDLSSLRtgimAGSPCPVEVMKQVIDRMGMAEVSICYGMTETSP 342
Cdd:cd17636 77 AEEVLELIEAERCTHAFLLPPTIdqIVELN--ADGLYDLSSLR----SSPAAPEWNDMATVDTSPWGRKPGGYGQTEVMG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 343 VSTQTRADDSierRVSTVGRVGPHLEVKVVDPEsGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIdAARWMHTGDLA 422
Cdd:cd17636 151 LATFAALGGG---AIGGAGRPSPLVQVRILDED-GREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT-RGGWHHTNDLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 423 VMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASpLTAEKVREFCS 502
Cdd:cd17636 226 RREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGAS-VTEAELIEHCR 304
|
330 340
....*....|....*....|....*..
gi 522130465 503 GKLAHYKIPRYVHVVDEFPMTVTGKVR 529
Cdd:cd17636 305 ARIASYKKPKSVEFADALPRTAGGADD 331
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
23-528 |
1.07e-57 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 208.24 E-value: 1.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 23 TIGDNFDRTVAAFGDRDALVDrAAGGRWTYRE-LAGevtALAL-GLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAI 100
Cdd:PRK08633 616 PLAEAWIDTAKRNWSRLAVAD-STGGELSYGKaLTG---ALALaRLLKRELKDEENVGILLPPSVAGALANLALLLAGKV 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 101 LVNINpaYRSHE--LEYVLDQAGIRLLVASDKFktsdypamVEEVREKCARLE-----HVVVLggeswQELMDAGRRGD- 172
Cdd:PRK08633 692 PVNLN--YTASEaaLKSAIEQAQIKTVITSRKF--------LEKLKNKGFDLElpenvKVIYL-----EDLKAKISKVDk 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 173 ----------PAQL--AHLRAGLSADDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCF 240
Cdd:PRK08633 757 ltallaarllPARLlkRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSF 836
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 241 GMVMGNLACTSHGACMVIPAPAFDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTgIMAGS-PCPVEVM 319
Cdd:PRK08633 837 GLTVTLWLPLLEGIKVVYHPDPTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRL-VVAGAeKLKPEVA 915
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 320 KQVIDRMGMaEVSICYGMTETSPVST----QTRADDSIERRVSTVGRVG---PHLEVKVVDPESGLTVPRGEPGELCTRG 392
Cdd:PRK08633 916 DAFEEKFGI-RILEGYGATETSPVASvnlpDVLAADFKRQTGSKEGSVGmplPGVAVRIVDPETFEELPPGEDGLILIGG 994
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 393 YSVMLGYWEQPDKTAEAI---DAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYThpdVLDAQ--- 466
Cdd:PRK08633 995 PQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAK---ALGGEevv 1071
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522130465 467 --VIGVPDEKYGEELMAWVRMregaSPLTAEKVREFCS-GKLAHYKIPRYVHVVDEFPMTVTGKV 528
Cdd:PRK08633 1072 faVTAVPDEKKGEKLVVLHTC----GAEDVEELKRAIKeSGLPNLWKPSRYFKVEALPLLGSGKL 1132
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
26-535 |
1.09e-57 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 200.45 E-value: 1.09e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 26 DNFDRTVAA-FGDRDALVDRAagGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNI 104
Cdd:TIGR02262 8 DLLDRNVVEgRGGKTAFIDDI--SSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 105 NPAYRSHELEYVLDQAGIRLLVASDKFktsdYPaMVEEVREKCARLEHVVVLGGESWQELMDAGRRGDPAQLAHlRAGLS 184
Cdd:TIGR02262 86 NTLLTADDYAYMLEDSRARVVFVSGAL----LP-VIKAALGKSPHLEHRVVVGRPEAGEVQLAELLATESEQFK-PAATQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 185 ADDPINIQYTSGTTGFPKGATLSHHN-ILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGACMVIPAPAF 263
Cdd:TIGR02262 160 ADDPAFWLYSSGSTGMPKGVVHTHSNpYWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGERP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 264 DPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSiCYGMTETSPV 343
Cdd:TIGR02262 240 TPDAVFDRLRRHQPTIFYGVPTLYAAMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVD-GIGSTEMLHI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 344 STQTRADDSierRVSTVGRVGPHLEVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAArWMHTGDLAV 423
Cdd:TIGR02262 319 FLSNLPGDV---RYGTSGKPVPGYRLRLVG-DGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTFQGE-WTRSGDKYV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 424 MDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASPLTAEkVREFCSG 503
Cdd:TIGR02262 394 RNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTALETE-LKEHVKD 472
|
490 500 510
....*....|....*....|....*....|..
gi 522130465 504 KLAHYKIPRYVHVVDEFPMTVTGKVRKVEMRE 535
Cdd:TIGR02262 473 RLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
18-548 |
4.11e-57 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 199.98 E-value: 4.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 18 PLLGDTIGDNFDRTvaaFGDRDaLVDRAAGG---RWTYRELAGEVTALALGLVARGIGKGDRVGI--WSPNR--AEWtfl 90
Cdd:PRK06018 9 PLLCHRIIDHAARI---HGNRE-VVTRSVEGpivRTTYAQIHDRALKVSQALDRDGIKLGDRVATiaWNTWRhlEAW--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 91 qYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVASDKFktsdYPaMVEEVREKCARLEHVVVLGG------------ 158
Cdd:PRK06018 82 -YGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLTF----VP-ILEKIADKLPSVERYVVLTDaahmpqttlkna 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 159 ---ESWQElmdaGRRGDPAQlahlrAGLSADDPINIQYTSGTTGFPKGATLSHH-NIL-----NNGYFVGELCnyteEDK 229
Cdd:PRK06018 156 vayEEWIA----EADGDFAW-----KTFDENTAAGMCYTSGTTGDPKGVLYSHRsNVLhalmaNNGDALGTSA----ADT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 230 VCIPVPFYHC--FGMVMgnlACTSHGACMVIPAPAFDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTG 307
Cdd:PRK06018 223 MLPVVPLFHAnsWGIAF---SAPSMGTKLVMPGAKLDGASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 308 IMAGSPCPvEVMKQVIDRMGmAEVSICYGMTETSPVST--------QTRADDSIERRVSTVGRVGPHLEVKVVDPEsGLT 379
Cdd:PRK06018 300 VCGGSAMP-RSMIKAFEDMG-VEVRHAWGMTEMSPLGTlaalkppfSKLPGDARLDVLQKQGYPPFGVEMKITDDA-GKE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 380 VPRG--EPGELCTRGYSVMLGYWEQPDktaEAIDAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLY 457
Cdd:PRK06018 377 LPWDgkTFGRLKVRGPAVAAAYYRVDG---EILDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAV 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 458 THPDVLDAQVIGVPDEKYGEELMAWVRMREGASPlTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMREKS 537
Cdd:PRK06018 454 GHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETA-TREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQF 532
|
570
....*....|.
gi 522130465 538 ITlLGLETAAA 548
Cdd:PRK06018 533 KD-YKLPTAAA 542
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
37-530 |
3.03e-56 |
|
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: 195.16 E-value: 3.03e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 37 DRDALVDRaaGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYV 116
Cdd:cd05945 6 DRPAVVEG--GRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 117 LDQAGIRLLVAsdkfktsdypamveevrekcarlehvvvlggeswqelmdagrrgDPaqlahlraglsaDDPINIQYTSG 196
Cdd:cd05945 84 LDAAKPALLIA--------------------------------------------DG------------DDNAYIIFTSG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 197 TTGFPKGATLSHHNILNngyFVGELCNYT--EEDKVCIPVPFYHcFGMVMGNLACT-SHGACMVIPAPA--FDPRATLEA 271
Cdd:cd05945 108 STGRPKGVQISHDNLVS---FTNWMLSDFplGPGDVFLNQAPFS-FDLSVMDLYPAlASGATLVPVPRDatADPKQLFRF 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 272 VAAERCTSLYGVPTmFIAE-LNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSICYGMTETSPVSTQTRAD 350
Cdd:cd05945 184 LAEHGITVWVSTPS-FAAMcLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIEVT 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 351 DSIERRVSTV--GRVGPHLEVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEA---IDAARWMHTGDLAVMD 425
Cdd:cd05945 263 PEVLDGYDRLpiGYAKPGAKLVILD-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAffpDEGQRAYRTGDLVRLE 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 426 GDGYVNITGRIKDMV-IRGgenlYpR----EIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASPLTAEKVREF 500
Cdd:cd05945 342 ADGLLFYRGRLDFQVkLNG----Y-RieleEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGLTKAIKAE 416
|
490 500 510
....*....|....*....|....*....|.
gi 522130465 501 CSGKLAHYKIPRYVHVVDEFPMTVTGKV-RK 530
Cdd:cd05945 417 LAERLPPYMIPRRFVYLDELPLNANGKIdRK 447
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
194-536 |
5.67e-56 |
|
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: 191.01 E-value: 5.67e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 194 TSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGnLACTSHGACMVIPAPAFDPRATLEAVA 273
Cdd:cd17630 8 TSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAIL-VRSLLAGAELVLLERNQALAEDLAPPG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 274 AeRCTSLygVPTMfIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMgmAEVSICYGMTETSPVSTQTRADDSI 353
Cdd:cd17630 87 V-THVSL--VPTQ-LQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADRG--IPLYTTYGMTETASQVATKRPDGFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 354 ErrvSTVGRVGPHLEVKVVDPesgltvprgepGELCTRGYSVMLGYWEQPdkTAEAIDAARWMHTGDLAVMDGDGYVNIT 433
Cdd:cd17630 161 R---GGVGVLLPGRELRIVED-----------GEIWVGGASLAMGYLRGQ--LVPEFNEDGWFTTKDLGELHADGRLTVL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 434 GRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASPltaEKVREFCSGKLAHYKIPRY 513
Cdd:cd17630 225 GRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADP---AELRAWLKDKLARFKLPKR 301
|
330 340
....*....|....*....|...
gi 522130465 514 VHVVDEFPMTVTGKVRKVEMREK 536
Cdd:cd17630 302 IYPVPELPRTGGGKVDRRALRAW 324
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
23-530 |
6.87e-56 |
|
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: 203.16 E-value: 6.87e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 23 TIGDNFDRTVAAFGDRDALVDraAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILV 102
Cdd:COG1020 477 TLHELFEAQAARTPDAVAVVF--GDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYV 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 103 NINPAYRSHELEYVLDQAGIRLLVASdkfktsdypamvEEVREKCARLEHVVVLggeswqeLMDAGRRGDPAQLahLRAG 182
Cdd:COG1020 555 PLDPAYPAERLAYMLEDAGARLVLTQ------------SALAARLPELGVPVLA-------LDALALAAEPATN--PPVP 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 183 LSADDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVcipvpfyhcfgmvmgnLACTS----------- 251
Cdd:COG1020 614 VTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRV----------------LQFASlsfdasvweif 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 252 ----HGACMVIPAP--AFDPRATLEAVAAERCTSLYGVPTMFiAELnhPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDR 325
Cdd:COG1020 678 gallSGATLVLAPPeaRRDPAALAELLARHRVTVLNLTPSLL-RAL--LDAAPEALPSLRLVLVGGEALPPELVRRWRAR 754
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 326 MGMAEVSICYGMTETSPVSTQTR-ADDSIERRVSTVGRVGPHLEVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPD 404
Cdd:COG1020 755 LPGARLVNLYGPTETTVDSTYYEvTPPDADGGSVPIGRPIANTRVYVLD-AHLQPVPVGVPGELYIGGAGLARGYLNRPE 833
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 405 KTAEA-------IDAARWMHTGDLAVMDGDG---YVnitGRIKDMV-IRGgenlY---PREIEEFLYTHPDVLDAQVIGV 470
Cdd:COG1020 834 LTAERfvadpfgFPGARLYRTGDLARWLPDGnleFL---GRADDQVkIRG----FrieLGEIEAALLQHPGVREAVVVAR 906
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 471 PDEKyGEELMAWVRMREGASPLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRK 530
Cdd:COG1020 907 EDAP-GDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDR 965
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
23-535 |
1.60e-55 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 196.63 E-value: 1.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 23 TIGDNFDRTVAAFGDRDALVDRaaGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILV 102
Cdd:PRK08279 38 SLGDVFEEAAARHPDRPALLFE--DQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 103 NINPAYRSHELEYVLDQAGIRLLVASDKFKtsdypAMVEEVREKCARLEHVVVLGGES------WQELMDAGRrGDPAQL 176
Cdd:PRK08279 116 LLNTQQRGAVLAHSLNLVDAKHLIVGEELV-----EAFEEARADLARPPRLWVAGGDTlddpegYEDLAAAAA-GAPTTN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 177 AHLRAGLSADDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYH------CFGMVMGNlact 250
Cdd:PRK08279 190 PASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHntggtvAWSSVLAA---- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 251 shGACMVIpAPAFDPRATLEAVAAERCTSLygvptMFIAEL-----NHPDfGEFDLS-SLRTGIMAG-SPcpvEVMKQVI 323
Cdd:PRK08279 266 --GATLAL-RRKFSASRFWDDVRRYRATAF-----QYIGELcryllNQPP-KPTDRDhRLRLMIGNGlRP---DIWDEFQ 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 324 DRMGMAEVSICYGMTEtSPVSTQtraddSIERRVSTVGRV-----GPHLEVKvVDPESG----------LTVPRGEPGEL 388
Cdd:PRK08279 334 QRFGIPRILEFYAASE-GNVGFI-----NVFNFDGTVGRVplwlaHPYAIVK-YDVDTGepvrdadgrcIKVKPGEVGLL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 389 CTR--------GYSvmlgyweQPDKTAEAI--------DAarWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREI 452
Cdd:PRK08279 407 IGRitdrgpfdGYT-------DPEASEKKIlrdvfkkgDA--WFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 453 EEFLYTHPDVLDAQVIGVP----DEKYGeelMAWVRMREGAsPLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKV 528
Cdd:PRK08279 478 ENALSGFPGVEEAVVYGVEvpgtDGRAG---MAAIVLADGA-EFDLAALAAHLYERLPAYAVPLFVRLVPELETTGTFKY 553
|
....*..
gi 522130465 529 RKVEMRE 535
Cdd:PRK08279 554 RKVDLRK 560
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
184-527 |
1.74e-55 |
|
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: 190.67 E-value: 1.74e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 184 SADDpINIQYTSGTTGFPKGATLSHHNI---LNNGYFVGELCNYTEEDK----------VCIPV-PFYHCFGMVMGNLAC 249
Cdd:cd05924 2 SADD-LYILYTGGTTGMPKGVMWRQEDIfrmLMGGADFGTGEFTPSEDAhkaaaaaagtVMFPApPLMHGTGSWTAFGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 250 TShGACMVIPAPAFDPRATLEAVAAERCTSLYGVPTMF----IAELNhpDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDR 325
Cdd:cd05924 81 LG-GQTVVLPDDRFDPEEVWRTIEKHKVTSMTIVGDAMarplIDALR--DAGPYDLSSLFAISSGGALLSPEVKQGLLEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 326 MGMAEVSICYGMTETSPVSTQTRADDSIERRVSTvgRVGPhlEVKVVDPESG-LTVPRGEPGELCTRGYsVMLGYWEQPD 404
Cdd:cd05924 158 VPNITLVDAFGSSETGFTGSGHSAGSGPETGPFT--RANP--DTVVLDDDGRvVPPGSGGVGWIARRGH-IPLGYYGDEA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 405 KTAEA---IDAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMA 481
Cdd:cd05924 233 KTAETfpeVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVA 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 522130465 482 WVRMREGASPlTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGK 527
Cdd:cd05924 313 VVQLREGAGV-DLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
36-530 |
4.42e-55 |
|
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: 192.51 E-value: 4.42e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 36 GDRDALVDRaaGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEY 115
Cdd:cd12116 1 PDATAVRDD--DRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 116 VLDQAGIRLLVASDkfktsdypAMVEEVREKCARLEHVVvlggeswqelmdagrRGDPAQLAHLRAGLSADDPINIQYTS 195
Cdd:cd12116 79 ILEDAEPALVLTDD--------ALPDRLPAGLPVLLLAL---------------AAAAAAPAAPRTPVSPDDLAYVIYTS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 196 GTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFyhCFGM-VMGNLACTSHGACMVIpAPA---FDPRATLEA 271
Cdd:cd12116 136 GSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTY--AFDIsLLELLLPLLAGARVVI-APRetqRDPEALARL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 272 VAAERCTSLYGVPTMFIAELnhpDFGEFDLSSLrTGIMAGSPCPVEVMKQVIDRMGmaEVSICYGMTETSPVSTQTRADD 351
Cdd:cd12116 213 IEAHSITVMQATPATWRMLL---DAGWQGRAGL-TALCGGEALPPDLAARLLSRVG--SLWNLYGPTETTIWSTAARVTA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 352 siERRVSTVGRVGPHLEVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAI-------DAARWMHTGDLAVM 424
Cdd:cd12116 287 --AAGPIPIGRPLANTQVYVLD-AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFvpdpfagPGSRLYRTGDLVRR 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 425 DGDGYVNITGRIKDMV-IRgGENLYPREIEEFLYTHPDVLDAQVIGVPDEKyGEELMAWVRMREGASPlTAEKVREFCSG 503
Cdd:cd12116 364 RADGRLEYLGRADGQVkIR-GHRIELGEIEAALAAHPGVAQAAVVVREDGG-DRRLVAYVVLKAGAAP-DAAALRAHLRA 440
|
490 500
....*....|....*....|....*...
gi 522130465 504 KLAHYKIPRYVHVVDEFPMTVTGKV-RK 530
Cdd:cd12116 441 TLPAYMVPSAFVRLDALPLTANGKLdRK 468
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
20-526 |
8.02e-55 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 193.56 E-value: 8.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 20 LGDTIGDNFDRTVAAFGDRDALVDRAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGA 99
Cdd:PRK05852 14 FGPRIADLVEVAATRLPEAPALVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 100 ILVNINPAYRSHELEYVLDQAGIR-LLVASDKfktsdypamVEEVREKCARLEHVVV-LGGESWQE----LMDAGRRGDP 173
Cdd:PRK05852 94 VVVPLDPALPIAEQRVRSQAAGARvVLIDADG---------PHDRAEPTTRWWPLTVnVGGDSGPSggtlSVHLDAATEP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 174 AQLAHLRAGLSADDPInIQYTSGTTGFPKGATLSHHNILNN------GYFVGElcnyteEDKVCIPVPFYHCFGMVMGNL 247
Cdd:PRK05852 165 TPATSTPEGLRPDDAM-IMFTGGTTGLPKMVPWTHANIASSvraiitGYRLSP------RDATVAVMPLYHGHGLIAALL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 248 ACTSHGACMVIPAPA-FDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDL--SSLRTGIMAGSPCPVEVMKQVID 324
Cdd:PRK05852 238 ATLASGGAVLLPARGrFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRkpAALRFIRSCSAPLTAETAQALQT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 325 RMGmAEVSICYGMTETSPVSTQTRAD--DSIERRVSTVGRVGPH--LEVKVVDPEsGLTVPRGEPGELCTRGYSVMLGYW 400
Cdd:PRK05852 318 EFA-APVVCAFGMTEATHQVTTTQIEgiGQTENPVVSTGLVGRStgAQIRIVGSD-GLPLPAGAVGEVWLRGTTVVRGYL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 401 EQPDKTAEAIDAArWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELM 480
Cdd:PRK05852 396 GDPTITAANFTDG-WLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVA 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 522130465 481 AWVRMREGASPlTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTG 526
Cdd:PRK05852 475 AVIVPRESAPP-TAEELVQFCRERLAAFEIPASFQEASGLPHTAKG 519
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
51-467 |
1.35e-54 |
|
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: 189.78 E-value: 1.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 51 TYRELAGEVTALALGLVAR-GIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVASd 129
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 130 kfktsdypamvEEVREKCARLEHVVVLGGESWQELMDAGRRGDPAQlahlrAGLSADDPINIQYTSGTTGFPKGATLSHH 209
Cdd:TIGR01733 80 -----------SALASRLAGLVLPVILLDPLELAALDDAPAPPPPD-----APSGPDDLAYVIYTSGSTGRPKGVVVTHR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 210 NILNngyFVGELCNYTE--EDKVCIPVPFYHCFGMVMGNLACTSHGACMVIPAPA---FDPRATLEAVAAERCTSLYGVP 284
Cdd:TIGR01733 144 SLVN---LLAWLARRYGldPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDeerDDAALLAALIAEHPVTVLNLTP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 285 TMF--IAELNHPDfgefdLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSICYGMTETSPVSTQTRADDSIERRVSTV-- 360
Cdd:TIGR01733 221 SLLalLAAALPPA-----LASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRESPVpi 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 361 GRVGPHLEVKVVDPEsGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAI--------DAARWMHTGDLAVMDGDGYVNI 432
Cdd:TIGR01733 296 GRPLANTRLYVLDDD-LRPVPVGVVGELYIGGPGVARGYLNRPELTAERFvpdpfaggDGARLYRTGDLVRYLPDGNLEF 374
|
410 420 430
....*....|....*....|....*....|....*....
gi 522130465 433 TGRIKDMV-IRGgenlY---PREIEEFLYTHPDVLDAQV 467
Cdd:TIGR01733 375 LGRIDDQVkIRG----YrieLGEIEAALLRHPGVREAVV 409
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
49-534 |
7.37e-54 |
|
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: 188.41 E-value: 7.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 49 RWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVAS 128
Cdd:cd05971 6 KVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 129 dkfktsdypamveevrekcarlehvvvlggeswqelmdagrrgdpaqlahlraglSADDPINIQYTSGTTGFPKGATLSH 208
Cdd:cd05971 86 -------------------------------------------------------GSDDPALIIYTSGTTGPPKGALHAH 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 209 HNILNNG---YFVGEL------CNYTEEDKVCIP------VPFYHcFGMVMgnLACTSHGacmvipapaFDPRATLEAVA 273
Cdd:cd05971 111 RVLLGHLpgvQFPFNLfprdgdLYWTPADWAWIGglldvlLPSLY-FGVPV--LAHRMTK---------FDPKAALDLMS 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 274 AERCTSLYGVPT---MFIAELNHPDFGEFDLSSLRTGimaGSPCPVEVMKQVIDRMGmAEVSICYGMTETSPVSTQTRAD 350
Cdd:cd05971 179 RYGVTTAFLPPTalkMMRQQGEQLKHAQVKLRAIATG---GESLGEELLGWAREQFG-VEVNEFYGQTECNLVIGNCSAL 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 351 DSIerRVSTVGRVGPHLEVKVVDpESGLTVPRGEPGELCTR--GYSVMLGYWEQPDKTAEAIdAARWMHTGDLAVMDGDG 428
Cdd:cd05971 255 FPI--KPGSMGKPIPGHRVAIVD-DNGTPLPPGEVGEIAVElpDPVAFLGYWNNPSATEKKM-AGDWLLTGDLGRKDSDG 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 429 YVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASPLT--AEKVREFCSGKLA 506
Cdd:cd05971 331 YFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDalAREIQELVKTRLA 410
|
490 500
....*....|....*....|....*...
gi 522130465 507 HYKIPRYVHVVDEFPMTVTGKVRKVEMR 534
Cdd:cd05971 411 AHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
37-530 |
1.93e-50 |
|
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: 180.16 E-value: 1.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 37 DRDALVDraAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYV 116
Cdd:cd12114 2 DATAVIC--GDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 117 LDQAGIRLLVasdkfktSDYPAmvEEVREKCARLEHVVVLGGESWQELMDAGRrgDPAQLAHlraglsaddpinIQYTSG 196
Cdd:cd12114 80 LADAGARLVL-------TDGPD--AQLDVAVFDVLILDLDALAAPAPPPPVDV--APDDLAY------------VIFTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 197 TTGFPKGATLSHHNILNNGYFVGELCNYTEEDKV------CIPVPFYHCFGMvmgnlacTSHGACMVIPAPA--FDPRAT 268
Cdd:cd12114 137 STGTPKGVMISHRAALNTILDINRRFAVGPDDRVlalsslSFDLSVYDIFGA-------LSAGATLVLPDEArrRDPAHW 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 269 LEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSICYGMTETSPVSTQTR 348
Cdd:cd12114 210 AELIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 349 ADDSIERRVST-VGRVGPHLEVKVVDPeSGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEA----IDAARWMHTGDLAV 423
Cdd:cd12114 290 IDEVPPDWRSIpYGRPLANQRYRVLDP-RGRDCPDWVPGELWIGGRGVALGYLGDPELTAARfvthPDGERLYRTGDLGR 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 424 MDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVpDEKYGEELMAWVRMREGASPLTAEKVREFCSG 503
Cdd:cd12114 369 YRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDNDGTPIAPDALRAFLAQ 447
|
490 500
....*....|....*....|....*..
gi 522130465 504 KLAHYKIPRYVHVVDEFPMTVTGKVRK 530
Cdd:cd12114 448 TLPAYMIPSRVIALEALPLTANGKVDR 474
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
37-528 |
5.94e-50 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 178.27 E-value: 5.94e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 37 DRDALVDraAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYV 116
Cdd:cd17643 2 EAVAVVD--EDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 117 LDQAGIRLLVasdkfktsdypamveevrekcarlehvvvlggeswqelmdagrrGDPAQLAHlraglsaddpinIQYTSG 196
Cdd:cd17643 80 LADSGPSLLL--------------------------------------------TDPDDLAY------------VIYTSG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 197 TTGFPKGATLSHHNILnnGYFV--GELCNYTEEDKVcipVPFYHC---FGM--VMGNLactSHGACMVIPAP--AFDPRA 267
Cdd:cd17643 104 STGRPKGVVVSHANVL--ALFAatQRWFGFNEDDVW---TLFHSYafdFSVweIWGAL---LHGGRLVVVPYevARSPED 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 268 TLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGM--AEVSICYGMTETSPVST 345
Cdd:cd17643 176 FARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLdrPQLVNMYGITETTVHVT 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 346 QTR--ADDSIERRVSTVGRVGPHLEVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAE-------AIDAARWM 416
Cdd:cd17643 256 FRPldAADLPAAAASPIGRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMY 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 417 HTGDLAVMDGDGYVNITGRIKDMV-IRgGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASPLTAE 495
Cdd:cd17643 335 RTGDLARRLPDGELEYLGRADEQVkIR-GFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAE 413
|
490 500 510
....*....|....*....|....*....|...
gi 522130465 496 kVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKV 528
Cdd:cd17643 414 -LRALLKELLPDYMVPARYVPLDALPLTVNGKL 445
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
51-534 |
1.11e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 178.43 E-value: 1.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 51 TYRELAGEVTALALGLVARGiGKGDRVGIWSPNRAEwtFLQY--ATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVAs 128
Cdd:PRK07638 28 TYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIE--FLQLfaGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVT- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 129 DKFKTSDYPAmveevrEKCArlehvvVLGGESWQELMDAgRRGDPAQLAHLRaglsaDDPINIQYTSGTTGFPKGATLSH 208
Cdd:PRK07638 104 ERYKLNDLPD------EEGR------VIEIDEWKRMIEK-YLPTYAPIENVQ-----NAPFYMGFTSGSTGKPKAFLRAQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 209 HNILNNgyFVgelCNYTE-----EDKVCIPVPFYHC---FGMVmgnlaCTSHGACMVIPAPAFDPRATLEAVAAERCTSL 280
Cdd:PRK07638 166 QSWLHS--FD---CNVHDfhmkrEDSVLIAGTLVHSlflYGAI-----STLYVGQTVHLMRKFIPNQVLDKLETENISVM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 281 YGVPTMFIAELNHPDFGEFDLsslrTGIMAGSPCPVEVMKQVIDRMGMAEVSICYGMTETSPVSTQTRADDsiERRVSTV 360
Cdd:PRK07638 236 YTVPTMLESLYKENRVIENKM----KIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSFVTALVDEES--ERRPNSV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 361 GRvgPHLEVKV-VDPESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEaIDAARWMHTGDLAVMDGDGYVNITGRIKDM 439
Cdd:PRK07638 310 GR--PFHNVQVrICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVGYEDEEGFIYIVGREKNM 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 440 VIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREgasplTAEKVREFCSGKLAHYKIPRYVHVVDE 519
Cdd:PRK07638 387 ILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSA-----TKQQLKSFCLQRLSSFKIPKEWHFVDE 461
|
490
....*....|....*
gi 522130465 520 FPMTVTGKVRKVEMR 534
Cdd:PRK07638 462 IPYTNSGKIARMEAK 476
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
50-531 |
1.54e-49 |
|
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: 176.92 E-value: 1.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 50 WTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVASd 129
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 130 kfktsdypamveevrekcarlehvvvlggeswQELMDagrRGDPaqlahlraglsaDDPINIQYTSGTTGFPKGATLSHh 209
Cdd:cd05969 80 --------------------------------EELYE---RTDP------------EDPTLLHYTSGTTGTPKGVLHVH- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 210 NILNNGYFVGE-LCNYTEEDKV-CIPVPFYhCFGMVMGNLACTSHGACMVIPAPAFDPRATLEAVAAERCTSLYGVPTMF 287
Cdd:cd05969 112 DAMIFYYFTGKyVLDLHPDDIYwCTADPGW-VTGTVYGIWAPWLNGVTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAI 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 288 IAELNHPDF--GEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAeVSICYGMTETSpvsTQTRAD-DSIERRVSTVGRVG 364
Cdd:cd05969 191 RMLMKEGDElaRKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVP-IHDTWWQTETG---SIMIANyPCMPIKPGSMGKPL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 365 PHLEVKVVDpESGLTVPRGEPGELCTR-GYSVML-GYWEQPDKTAEA-IDAarWMHTGDLAVMDGDGYVNITGRIKDMVI 441
Cdd:cd05969 267 PGVKAAVVD-ENGNELPPGTKGILALKpGWPSMFrGIWNDEERYKNSfIDG--WYLTGDLAYRDEDGYFWFVGRADDIIK 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 442 RGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASPLTA--EKVREFCSGKLAHYKIPRYVHVVDE 519
Cdd:cd05969 344 TSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDElkEEIINFVRQKLGAHVAPREIEFVDN 423
|
490
....*....|...
gi 522130465 520 FPMTVTGKV-RKV 531
Cdd:cd05969 424 LPKTRSGKImRRV 436
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
29-537 |
1.75e-49 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 179.66 E-value: 1.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 29 DRTVAAFGDRDALVDRAAggRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAY 108
Cdd:PLN02479 27 ERAAVVHPTRKSVVHGSV--RYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 109 RSHELEYVLDQAGIRLLVASDKFKT--SDYPAMVEEVREKCARLEHVVVLGGESWqelmdagrrgDPAQLAH-LRAG--- 182
Cdd:PLN02479 105 NAPTIAFLLEHSKSEVVMVDQEFFTlaEEALKILAEKKKSSFKPPLLIVIGDPTC----------DPKSLQYaLGKGaie 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 183 ----LSADDP-------------INIQYTSGTTGFPKGATLSHHnilnnGYFVGELCNY----TEEDKVCI-PVPFYHC- 239
Cdd:PLN02479 175 yekfLETGDPefawkppadewqsIALGYTSGTTASPKGVVLHHR-----GAYLMALSNAliwgMNEGAVYLwTLPMFHCn 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 240 ---FGMVMGNLACTShgacmvIPAPAFDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPV 316
Cdd:PLN02479 250 gwcFTWTLAALCGTN------ICLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETILPLPRVVHVMTAGAAPP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 317 EVMKQVIDRMGMaEVSICYGMTETSPVST-------------QTRADDSIERRVSTVGRVGphleVKVVDPESGLTVPR- 382
Cdd:PLN02479 324 PSVLFAMSEKGF-RVTHTYGLSETYGPSTvcawkpewdslppEEQARLNARQGVRYIGLEG----LDVVDTKTMKPVPAd 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 383 -GEPGELCTRGYSVMLGYWEQPDKTAEAIdAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPD 461
Cdd:PLN02479 399 gKTMGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 462 VLDAQVIGVPDEKYGEELMAWVRMREGA----SPLTAEKVREFCSGKLAHYKIPRYVhVVDEFPMTVTGKVRKVEMREKS 537
Cdd:PLN02479 478 VLEASVVARPDERWGESPCAFVTLKPGVdksdEAALAEDIMKFCRERLPAYWVPKSV-VFGPLPKTATGKIQKHVLRAKA 556
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
36-534 |
2.03e-48 |
|
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: 177.51 E-value: 2.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 36 GDRDALV-DRAAGG---RWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSH 111
Cdd:cd05967 65 GDQIALIyDSPVTGterTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 112 ELEYVLDQAGIRLLVASD----KFKTSDYPAMVEE-VREKCARLEHVVVLGGES-------------WQELMDAGRRGDP 173
Cdd:cd05967 145 ELASRIDDAKPKLIVTAScgiePGKVVPYKPLLDKaLELSGHKPHHVLVLNRPQvpadltkpgrdldWSELLAKAEPVDC 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 174 AQLAhlraglsADDPINIQYTSGTTGFPKGATLShhnilNNGYFVGelCNYTeedkvcipvpFYHCFGMVMGNLA-CTS- 251
Cdd:cd05967 225 VPVA-------ATDPLYILYTSGTTGKPKGVVRD-----NGGHAVA--LNWS----------MRNIYGIKPGDVWwAASd 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 252 ----------------HGACMVI----PAPAFDPRATLEAVAAERCTSLYGVPTMFIA---ELNHPDFGE-FDLSSLRTG 307
Cdd:cd05967 281 vgwvvghsyivygpllHGATTVLyegkPVGTPDPGAFWRVIEKYQVNALFTAPTAIRAirkEDPDGKYIKkYDLSSLRTL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 308 IMAGSPCPVEVM--------KQVIDRmgmaevsicYGMTET-SPVSTQTRADDSIERRVSTVGRVGPHLEVKVVDPEsGL 378
Cdd:cd05967 361 FLAGERLDPPTLewaentlgVPVIDH---------WWQTETgWPITANPVGLEPLPIKAGSPGKPVPGYQVQVLDED-GE 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 379 TVPRGEPGELCTRGY---SVMLGYWEQPD--KTAEAIDAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIE 453
Cdd:cd05967 431 PVGPNELGNIVIKLPlppGCLLTLWKNDErfKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEME 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 454 EFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASPlTAEKVREFCSgKLAHYKI-----PRYVHVVDEFPMTVTGKV 528
Cdd:cd05967 511 ESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKI-TAEELEKELV-ALVREQIgpvaaFRLVIFVKRLPKTRSGKI 588
|
....*.
gi 522130465 529 RKVEMR 534
Cdd:cd05967 589 LRRTLR 594
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
4-534 |
5.95e-48 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 175.42 E-value: 5.95e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 4 APALPSYASGISEVPLLGDTIGD--NFDRTVAAFGDRDALVDRAAGGRWTYRELAGEVTALALGLVAR-GIGKGDRVGIW 80
Cdd:PLN02574 19 SPETGIYSSKHPPVPLPSDPNLDavSFIFSHHNHNGDTALIDSSTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 81 SPNRAEWTFLQYATAKIGAILVNINPAyrSHELEyvldqagirllVASDKFKTSDYPAMVE-EVREKCARLEHVVVLGGE 159
Cdd:PLN02574 99 LPNSVYFPVIFLAVLSLGGIVTTMNPS--SSLGE-----------IKKRVVDCSVGLAFTSpENVEKLSPLGVPVIGVPE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 160 SWQelMDAGRRGDPAQLAHL--------RAGLSADDPINIQYTSGTTGFPKGATLSHHNILNNG----YFVGELCNYTEE 227
Cdd:PLN02574 166 NYD--FDSKRIEFPKFYELIkedfdfvpKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVelfvRFEASQYEYPGS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 228 DKVCIPV-PFYHCFGMVMGNLACTSHGACMVIpAPAFDPRATLEAVAAERCTSLYGVPTMFIAeLNH---PDFGEfDLSS 303
Cdd:PLN02574 244 DNVYLAAlPMFHIYGLSLFVVGLLSLGSTIVV-MRRFDASDMVKVIDRFKVTHFPVVPPILMA-LTKkakGVCGE-VLKS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 304 LRTGIMAGSPCPVEVMKQVIDRMGMAEVSICYGMTETSPVSTQTRADDSIeRRVSTVGRVGPHLEVKVVDPESGLTVPRG 383
Cdd:PLN02574 321 LKQVSCGAAPLSGKFIQDFVQTLPHVDFIQGYGMTESTAVGTRGFNTEKL-SKYSSVGLLAPNMQAKVVDWSTGCLLPPG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 384 EPGELCTRGYSVMLGYWEQPDKTAEAIDAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVL 463
Cdd:PLN02574 400 NCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEII 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522130465 464 DAQVIGVPDEKYGEELMAWVRMREGaSPLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMR 534
Cdd:PLN02574 480 DAAVTAVPDKECGEIPVAFVVRRQG-STLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELK 549
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
49-535 |
7.84e-48 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 175.21 E-value: 7.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 49 RWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLvas 128
Cdd:PLN03102 39 RFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKIL--- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 129 dkFKTSDYPAMVEEVRE----KCARLEHVVVLGGE-------SWQELMDAG--RRGDPAQLAHLRAGLSAD--DPINIQY 193
Cdd:PLN03102 116 --FVDRSFEPLAREVLHllssEDSNLNLPVIFIHEidfpkrpSSEELDYECliQRGEPTPSLVARMFRIQDehDPISLNY 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 194 TSGTTGFPKGATLSHHnilnnGYFVGELCNYTEEDKVCIPV-----PFYHCFGMVM--------GNLACTSHgacmvIPA 260
Cdd:PLN03102 194 TSGTTADPKGVVISHR-----GAYLSTLSAIIGWEMGTCPVylwtlPMFHCNGWTFtwgtaargGTSVCMRH-----VTA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 261 PAFDPRATLEAVAAERCtslygVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQViDRMGMaEVSICYGMTE- 339
Cdd:PLN03102 264 PEIYKNIEMHNVTHMCC-----VPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKV-QRLGF-QVMHAYGLTEa 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 340 TSPVSTQTRADD--------SIERRVSTVGRVGPHLEVKVVDPESGLTVPR-GEP-GELCTRGYSVMLGYWEQPDKTAEA 409
Cdd:PLN03102 337 TGPVLFCEWQDEwnrlpenqQMELKARQGVSILGLADVDVKNKETQESVPRdGKTmGEIVIKGSSIMKGYLKNPKATSEA 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 410 IDAArWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGA 489
Cdd:PLN03102 417 FKHG-WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGE 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 522130465 490 SPLTAEKVR---------EFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMRE 535
Cdd:PLN03102 496 TTKEDRVDKlvtrerdliEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRD 550
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
51-535 |
1.33e-47 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 174.59 E-value: 1.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 51 TYRELAGEVTALALGLVAR-GIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVASd 129
Cdd:PRK05620 40 TFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVAD- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 130 kfktsdyPAMVE---EVREKCARLEHVVVLGGESwqelMDAGRRGDPAQLA-----HLRAGLSA---------DDPINIQ 192
Cdd:PRK05620 119 -------PRLAEqlgEILKECPCVRAVVFIGPSD----ADSAAAHMPEGIKvysyeALLDGRSTvydwpeldeTTAAAIC 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 193 YTSGTTGFPKGATLSHHNILNNGYfvgelcNYTEEDKVCIP--------VPFYHCFGMVMgNLACTSHGACMVIPAPAFD 264
Cdd:PRK05620 188 YSTGTTGAPKGVVYSHRSLYLQSL------SLRTTDSLAVThgesflccVPIYHVLSWGV-PLAAFMSGTPLVFPGPDLS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 265 PRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMaEVSICYGMTETSPVS 344
Cdd:PRK05620 261 APTLAKIIATAMPRVAHGVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGV-DVVHVWGMTETSPVG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 345 TQTR--ADDSIERRVS---TVGRVGPHLEVKVVDPESGLTVPRGEPGELCTRGYSVMLGYWEQPDKT---------AEAI 410
Cdd:PRK05620 340 TVARppSGVSGEARWAyrvSQGRFPASLEYRIVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPTEEgggaastfrGEDV 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 411 DAAR-------WMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWV 483
Cdd:PRK05620 420 EDANdrftadgWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVT 499
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 522130465 484 RMREGASPL--TAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMRE 535
Cdd:PRK05620 500 VLAPGIEPTreTAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
29-531 |
1.60e-47 |
|
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: 174.99 E-value: 1.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 29 DRTVAAFGDRDALV---DRAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNIN 105
Cdd:cd05968 68 DKWLADTRTRPALRwegEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 106 PAYRSHELEYVLDQAGIRLLVASDKF----KTSDYPAMVEEVREKCARLEHVVVLGGESWQELMDAGRRGDP-----AQL 176
Cdd:cd05968 148 SGFGKEAAATRLQDAEAKALITADGFtrrgREVNLKEEADKACAQCPTVEKVVVVRHLGNDFTPAKGRDLSYdeekeTAG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 177 AHLrAGLSADDPINIQYTSGTTGFPKGATLSHHNI-LNNGYFVGELCNYTEEDKVCipvpFYHCFGMVMGN---LACTSH 252
Cdd:cd05968 228 DGA-ERTESEDPLMIIYTSGTTGKPKGTVHVHAGFpLKAAQDMYFQFDLKPGDLLT----WFTDLGWMMGPwliFGGLIL 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 253 GACMVI--PAPAFDPRATL-EAVAAERCTSLYGVPTMFIAELNHPD--FGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMG 327
Cdd:cd05968 303 GATMVLydGAPDHPKADRLwRMVEDHEITHLGLSPTLIRALKPRGDapVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVG 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 328 MAEVSIC--YGMTEtspVSTQTRADDSIER-RVSTVGRVGPHLEVKVVDpESGLTVpRGEPGELCTRGYSVML--GYWEQ 402
Cdd:cd05968 383 KGRNPIInySGGTE---ISGGILGNVLIKPiKPSSFNGPVPGMKADVLD-ESGKPA-RPEVGELVLLAPWPGMtrGFWRD 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 403 PDKTAEA----IDAArWMHtGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEE 478
Cdd:cd05968 458 EDRYLETywsrFDNV-WVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEA 535
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 522130465 479 LMAWVRMREGASP--LTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKV-RKV 531
Cdd:cd05968 536 IVCFVVLKPGVTPteALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVmRRV 591
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
49-536 |
1.97e-47 |
|
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: 173.42 E-value: 1.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 49 RWTYRELaGEVTALALGLV--ARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLV 126
Cdd:cd05928 41 KWSFREL-GSLSRKAANVLsgACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 127 ASDKFKtsdypAMVEEVREKCARLEHVVVLGGESW------QELMDAgrrgdpAQLAHLRAGLSADDPINIQYTSGTTGF 200
Cdd:cd05928 120 TSDELA-----PEVDSVASECPSLKTKLLVSEKSRdgwlnfKELLNE------ASTEHHCVETGSQEPMAIYFTSGTTGS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 201 PKGATLSHHNiLNNGYFVG--ELCNYTEEDkvcipvpfyhcfgmVMGNLACTS--------------HGACMVI-PAPAF 263
Cdd:cd05928 189 PKMAEHSHSS-LGLGLKVNgrYWLDLTASD--------------IMWNTSDTGwiksawsslfepwiQGACVFVhHLPRF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 264 DPRATLEAVAAERCTSLYGVPTMFiAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMaEVSICYGMTETSPV 343
Cdd:cd05928 254 DPLVILKTLSSYPITTFCGAPTVY-RMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGL-DIYEGYGQTETGLI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 344 STQTRAddsIERRVSTVGRVGPHLEVKVVDpESGLTVPRGEPGELC-----TRGYSVMLGYWEQPDKTAEAIDAARWMhT 418
Cdd:cd05928 332 CANFKG---MKIKPGSMGKASPPYDVQIID-DNGNVLPPGTEGDIGirvkpIRPFGLFSGYVDNPEKTAATIRGDFYL-T 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 419 GDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMregASP------- 491
Cdd:cd05928 407 GDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVL---APQflshdpe 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 522130465 492 -LTAEkVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMREK 536
Cdd:cd05928 484 qLTKE-LQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
28-528 |
6.68e-47 |
|
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: 169.81 E-value: 6.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 28 FDRTVAAFGDRDALVdrAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPA 107
Cdd:cd12115 5 VEAQAARTPDAIALV--CGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 108 YRSHELEYVLDQAGIRLLVAsdkfktsdypamveevrekcarlehvvvlggeswqelmdagrrgDPAQLAHlraglsadd 187
Cdd:cd12115 83 YPPERLRFILEDAQARLVLT--------------------------------------------DPDDLAY--------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 188 pinIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFyhCFGMVMGNLACT-SHGACMVIPAPAFDPr 266
Cdd:cd12115 110 ---VIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEELAGVLASTSI--CFDLSVFELFGPlATGGKVVLADNVLAL- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 267 atLEAVAAERCTSLYGVPTMFIAELNHPDFGEfdlsSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSICYGMTETSPVSTQ 346
Cdd:cd12115 184 --PDLPAAAEVTLINTVPSAAAELLRHDALPA----SVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTV 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 347 TRADDSIERRVStVGRVGPHLEVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAI------DAARWMHTGD 420
Cdd:cd12115 258 APVPPGASGEVS-IGRPLANTQAYVLD-RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFlpdpfgPGARLYRTGD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 421 LAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVrMREGASPLTAEKVREF 500
Cdd:cd12115 336 LVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYI-VAEPGAAGLVEDLRRH 414
|
490 500
....*....|....*....|....*...
gi 522130465 501 CSGKLAHYKIPRYVHVVDEFPMTVTGKV 528
Cdd:cd12115 415 LGTRLPAYMVPSRFVRLDALPLTPNGKI 442
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
29-528 |
6.89e-47 |
|
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: 172.76 E-value: 6.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 29 DRTVAAFGDRDALV----DRAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNI 104
Cdd:cd17634 60 DRHLRENGDRTAIIyegdDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 105 NPAYRSHELEYVLDQAGIRLLVASDKF----KTSDYPAMVEEVREKCA-RLEHVVVLGGES------------WQELMDA 167
Cdd:cd17634 140 FGGFAPEAVAGRIIDSSSRLLITADGGvragRSVPLKKNVDDALNPNVtSVEHVIVLKRTGsdidwqegrdlwWRDLIAK 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 168 grrgdpAQLAHLRAGLSADDPINIQYTSGTTGFPKGAtlshhnILNNGyfvGELCNYTEEDKVCI---PVPFYHCF---G 241
Cdd:cd17634 220 ------ASPEHQPEAMNAEDPLFILYTSGTTGKPKGV------LHTTG---GYLVYAATTMKYVFdygPGDIYWCTadvG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 242 MVMGN-------LACtshGACMVI--PAPAF-DPRATLEAVAAERCTSLYGVPTMFIAELNH-PDFGE-FDLSSLRTGIM 309
Cdd:cd17634 285 WVTGHsyllygpLAC---GATTLLyeGVPNWpTPARMWQVVDKHGVNILYTAPTAIRALMAAgDDAIEgTDRSSLRILGS 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 310 AGSPCPVEVMKQVIDRMGMAEVSIC--YGMTETS-PVSTQTRADDSIERRVSTVGRVGphLEVKVVDPEsGLTVPRGEPG 386
Cdd:cd17634 362 VGEPINPEAYEWYWKKIGKEKCPVVdtWWQTETGgFMITPLPGAIELKAGSATRPVFG--VQPAVVDNE-GHPQPGGTEG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 387 ELC-TRGYSVM-LGYWEQPDKTAEAIDA---ARWMHtGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPD 461
Cdd:cd17634 439 NLViTDPWPGQtRTLFGDHERFEQTYFStfkGMYFS-GDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPK 517
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522130465 462 VLDAQVIGVPDEKYGEELMAWVRMREGA--SPLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKV 528
Cdd:cd17634 518 VAEAAVVGIPHAIKGQAPYAYVVLNHGVepSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
29-530 |
1.25e-46 |
|
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: 170.20 E-value: 1.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 29 DRTVAAFGDRdalvdraaggRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAY 108
Cdd:cd17655 12 DHTAVVFEDQ----------TLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 109 RSHELEYVLDQAGIRLLVASdkfktsdypamvEEVREKCARLEHVVVLGGESWQElmdagrrGDPAQLAHLRaglSADDP 188
Cdd:cd17655 82 PEERIQYILEDSGADILLTQ------------SHLQPPIAFIGLIDLLDEDTIYH-------EESENLEPVS---KSDDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 189 INIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYhcF----GMVMGNLACtSHGACMVIPAPAFD 264
Cdd:cd17655 140 AYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASIS--FdasvTEIFASLLS-GNTLYIVRKETVLD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 265 PRATLEAVAAERCTSLYGVPTmFIAELNHPDFGEFdlSSLRTGIMAGSPCPVEVMKQVIDRMGMA-EVSICYGMTETSPV 343
Cdd:cd17655 217 GQALTQYIRQNRITIIDLTPA-HLKLLDAADDSEG--LSLKHLIVGGEALSTELAKKIIELFGTNpTITNAYGPTETTVD 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 344 STQTRADDSIERRVST-VGRVGPHLEVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEA------IDAARWM 416
Cdd:cd17655 294 ASIYQYEPETDQQVSVpIGKPLGNTRIYILD-QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKfvddpfVPGERMY 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 417 HTGDLAVMDGDGYVNITGRIKDMV-IRG-----GEnlypreIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREgas 490
Cdd:cd17655 373 RTGDLARWLPDGNIEFLGRIDHQVkIRGyrielGE------IEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEK--- 443
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 522130465 491 PLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKV-RK 530
Cdd:cd17655 444 ELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVdRK 484
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
49-535 |
3.45e-46 |
|
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: 170.09 E-value: 3.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 49 RW-TYRELAGEVTALALGLVARGI--GKGDRVGIWSPNRAEWTFLQYATAKIGAILVninPAYRS--HE-LEYVLDQAGI 122
Cdd:cd05927 4 EWiSYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTV---PLYDTlgPEaIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 123 RLLVASDKFKTsdypamveevrekcarlehvvvlggESWQELMDAGRRgdpAQLAHLRAglSADDPINIQYTSGTTGFPK 202
Cdd:cd05927 81 SIVFCDAGVKV-------------------------YSLEEFEKLGKK---NKVPPPPP--KPEDLATICYTSGTTGNPK 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 203 GATLSHHNILNNgyfVGELCNYTEEDKVCIPV-------PFYHCFGMVMGNLACtSHGACMvipapAF---DPRATLEAV 272
Cdd:cd05927 131 GVMLTHGNIVSN---VAGVFKILEILNKINPTdvyisylPLAHIFERVVEALFL-YHGAKI-----GFysgDIRLLLDDI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 273 AAERCTSLYGVPTMF-----------------------------IAELNHPD-----------FGEFDLS---SLRTGIM 309
Cdd:cd05927 202 KALKPTVFPGVPRVLnriydkifnkvqakgplkrklfnfalnykLAELRSGVvraspfwdklvFNKIKQAlggNVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 310 AGSPCPVEVMK--QVIdrMGmAEVSICYGMTETSPVSTQTRADDsieRRVSTVGRVGPHLEVKVVD-PESGLTVPRGEP- 385
Cdd:cd05927 282 GSAPLSPEVLEflRVA--LG-CPVLEGYGQTECTAGATLTLPGD---TSVGHVGGPLPCAEVKLVDvPEMNYDAKDPNPr 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 386 GELCTRGYSVMLGYWEQPDKTAEAIDAARWMHTGDLAVMDGDGYVNITGRIKDMV-IRGGENLYPREIE------EFL-- 456
Cdd:cd05927 356 GEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIEniyarsPFVaq 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 457 -YTHPDVLDAQVIG--VPDEkygEELMAWVRMREGASP-----LTAEKVREF---------CSGKLAHYKIPRYVHVVDE 519
Cdd:cd05927 436 iFVYGDSLKSFLVAivVPDP---DVLKEWAASKGGGTGsfeelCKNPEVKKAiledlvrlgKENGLKGFEQVKAIHLEPE 512
|
570 580
....*....|....*....|..
gi 522130465 520 -FP-----MTVTGKVRKVEMRE 535
Cdd:cd05927 513 pFSvenglLTPTFKLKRPQLKK 534
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
187-528 |
9.86e-46 |
|
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: 163.35 E-value: 9.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 187 DPINIQYTSGTTGFPKGATLSHHNILNNgYFVGE-LCNYTEEDKVCIPVPFYHCfGMVMGNLACTSHGACMVIPApAFDP 265
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIES-FVCNEdLFNISGEDAILAPGPLSHS-LFLYGAISALYLGGTFIGQR-KFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 266 RATLEAVAAERCTSLYGVPTMFIAELNHpdfgEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSICYGMTETSPVST 345
Cdd:cd17633 78 KSWIRKINQYNATVIYLVPTMLQALART----LEPESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFITY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 346 qtRADDSiERRVSTVGRVGPHLEVKVVDPESGltvprgEPGELCTRGYSVMLGYweqpdKTAEAIDAARWMHTGDLAVMD 425
Cdd:cd17633 154 --NFNQE-SRPPNSVGRPFPNVEIEIRNADGG------EIGKIFVKSEMVFSGY-----VRGGFSNPDGWMSVGDIGYVD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 426 GDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVrmrEGASpLTAEKVREFCSGKL 505
Cdd:cd17633 220 EEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALY---SGDK-LTYKQLKRFLKQKL 295
|
330 340
....*....|....*....|...
gi 522130465 506 AHYKIPRYVHVVDEFPMTVTGKV 528
Cdd:cd17633 296 SRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
49-497 |
3.15e-44 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 162.91 E-value: 3.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 49 RWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAilVNINPAYRS--HELEYVLDQAGIRLLV 126
Cdd:cd17640 5 RITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGA--VDVVRGSDSsvEELLYILNHSESVALV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 127 asdkfktsdypamVEEvrekcarlehvvvlggeswqelmdagrrgdpaqlahlraglSADDPINIQYTSGTTGFPKGATL 206
Cdd:cd17640 83 -------------VEN-----------------------------------------DSDDLATIIYTSGTTGNPKGVML 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 207 SHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCF-----------GMVMgnlACTShgacmvipapafdPRATLEAVAAE 275
Cdd:cd17640 109 THANLLHQIRSLSDIVPPQPGDRFLSILPIWHSYersaeyfifacGCSQ---AYTS-------------IRTLKDDLKRV 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 276 RCTSLYGVPTMFIAELNHPD-------------FGEFDL-SSLRTGIMAGSPCPvevmkQVIDRMGMA---EVSICYGMT 338
Cdd:cd17640 173 KPHYIVSVPRLWESLYSGIQkqvsksspikqflFLFFLSgGIFKFGISGGGALP-----PHVDTFFEAigiEVLNGYGLT 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 339 ETSPVSTQTRADDSIerrVSTVGRVGPHLEVKVVDPESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAARWMHT 418
Cdd:cd17640 248 ETSPVVSARRLKCNV---RGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNT 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 419 GDLAVMDGDGYVNITGRIKD-MVIRGGENLYPREIEEFLYTHPDVLDAQVIG----------VPDEkygEELMAW----- 482
Cdd:cd17640 325 GDLGWLTCGGELVLTGRAKDtIVLSNGENVEPQPIEEALMRSPFIEQIMVVGqdqkrlgaliVPNF---EELEKWakesg 401
|
490
....*....|....*
gi 522130465 483 VRMREGASPLTAEKV 497
Cdd:cd17640 402 VKLANDRSQLLASKK 416
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
31-533 |
5.10e-44 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 163.63 E-value: 5.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 31 TVAAFGDRDALVDRaaGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRS 110
Cdd:PRK13383 44 TAARWPGRTAIIDD--DGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 111 HELEYVLDQAGIRLLVASDKFKtsdypamveevrEKCARLEHVVVLGGESWQELMDAGRRgdPAQLAHLRAGLsaddpin 190
Cdd:PRK13383 122 DALAAALRAHHISTVVADNEFA------------ERIAGADDAVAVIDPATAGAEESGGR--PAVAAPGRIVL------- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 191 iqYTSGTTGFPKGATLSHHNILNNGYFVG--ELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGAcmVIPAPAFDPRAT 268
Cdd:PRK13383 181 --LTSGTTGKPKGVPRAPQLRSAVGVWVTilDRTRLRTGSRISVAMPMFHGLGLGMLMLTIALGGT--VLTHRHFDAEAA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 269 LEAVAAERCTSLYGVPTMFIAELNHPD--FGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSIcYGMTETSPVSTQ 346
Cdd:PRK13383 257 LAQASLHRADAFTAVPVVLARILELPPrvRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNG-YGSTEVGIGALA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 347 TRADdsIERRVSTVGRVGPHLEVKVVDPESGLTVPRGEP-----GELCTRGYSvmlgyweqpDKTAEA-IDAArwMHTGD 420
Cdd:PRK13383 336 TPAD--LRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGrifvgGELAGTRYT---------DGGGKAvVDGM--TSTGD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 421 LAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGaSPLTAEKVREF 500
Cdd:PRK13383 403 MGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPG-SGVDAAQLRDY 481
|
490 500 510
....*....|....*....|....*....|...
gi 522130465 501 CSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEM 533
Cdd:PRK13383 482 LKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
49-535 |
1.91e-43 |
|
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: 160.60 E-value: 1.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 49 RWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDqagirllvas 128
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLN---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 129 dkfktsdypamveevrekCARLEHVVVlggeswqelmdagrrgDPAQLAhlraglsaddpiniqYTSGTTGFPKGATLSH 208
Cdd:cd05940 73 ------------------VSSAKHLVV----------------DAALYI---------------YTSGTTGLPKAAIISH 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 209 HNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGACMVIpAPAFDPRATLEAVAAERCTSLygvptMFI 288
Cdd:cd05940 104 RRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVI-RKKFSASNFWDDIRKYQATIF-----QYI 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 289 AE-----LNHPDFGEFDLSSLRtgIMAGSPCPVEVMKQVIDRMGMAEVSICYGMTETSPVSTqtraddSIERRVSTVGRV 363
Cdd:cd05940 178 GElcrylLNQPPKPTERKHKVR--MIFGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFI------NFFGKPGAIGRN 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 364 GPHLE-------VKvVDPESG----------LTVPRGEPGELCTR--GYSVMLGYWEqPDKTAEAI------DAARWMHT 418
Cdd:cd05940 250 PSLLRkvaplalVK-YDLESGepirdaegrcIKVPRGEPGLLISRinPLEPFDGYTD-PAATEKKIlrdvfkKGDAWFNT 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 419 GDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVP----DEKYGeelMAWVRMREGAsPLTA 494
Cdd:cd05940 328 GDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvpgtDGRAG---MAAIVLQPNE-EFDL 403
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 522130465 495 EKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMRE 535
Cdd:cd05940 404 SALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
37-528 |
9.14e-43 |
|
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: 158.18 E-value: 9.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 37 DRDALVDRaaGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYV 116
Cdd:cd17652 2 DAPAVVFG--DETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 117 LDQAGIRLLVASdkfktsdypamveevrekcarlehvvvlggeswqelmdagrrgdpaqlahlraglsADDPINIQYTSG 196
Cdd:cd17652 80 LADARPALLLTT--------------------------------------------------------PDNLAYVIYTSG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 197 TTGFPKGATLSHHNILNNGYFVGELCNYTEEDKV--CIPVPFYHCFGMVMGNLACtshGACMVI-PAPAFDPRATLEAVA 273
Cdd:cd17652 104 STGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVlqFASPSFDASVWELLMALLA---GATLVLaPAEELLPGEPLADLL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 274 AERCTSLYGVPTMFIAELNhPDfgefDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEvsiCYGMTETSPVSTQTRADDSi 353
Cdd:cd17652 181 REHRITHVTLPPAALAALP-PD----DLPDLRTLVVAGEACPAELVDRWAPGRRMIN---AYGPTETTVCATMAGPLPG- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 354 eRRVSTVGRVGPHLEVKVVDPESGLtVPRGEPGELCTRGYSVMLGYWEQPDKTAE-------AIDAARWMHTGDLAVMDG 426
Cdd:cd17652 252 -GGVPPIGRPVPGTRVYVLDARLRP-VPPGVPGELYIAGAGLARGYLNRPGLTAErfvadpfGAPGSRMYRTGDLARWRA 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 427 DGYVNITGRIKDMV-IRGgenlY---PREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASPlTAEKVREFCS 502
Cdd:cd17652 330 DGQLEFLGRADDQVkIRG----FrieLGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAP-TAAELRAHLA 404
|
490 500
....*....|....*....|....*.
gi 522130465 503 GKLAHYKIPRYVHVVDEFPMTVTGKV 528
Cdd:cd17652 405 ERLPGYMVPAAFVVLDALPLTPNGKL 430
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
51-534 |
1.84e-42 |
|
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: 157.68 E-value: 1.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 51 TYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVAsdk 130
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 131 fktsdypamveevrekcarlehvvvlggeswqelmdagrrgDPAQLAHLraglsADDPINIQYTSGTTGFPKGATLSHHN 210
Cdd:cd05973 79 -----------------------------------------DAANRHKL-----DSDPFVMMFTSGTTGLPKGVPVPLRA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 211 ILNNGYFVGELCNYTEEDKV-CIPVP--FYHCFGMVMGNLACtshGACMVIPAPAFDPRATLEAVAAERCTSLYGVPTMF 287
Cdd:cd05973 113 LAAFGAYLRDAVDLRPEDSFwNAADPgwAYGLYYAITGPLAL---GHPTILLEGGFSVESTWRVIERLGVTNLAGSPTAY 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 288 IAELNHPDFGEFDLS-SLRTGIMAGSPCPVEVMKQVIDRMGMAeVSICYGMTETSPVSTQTRADDSiERRVSTVGRVGPH 366
Cdd:cd05973 190 RLLMAAGAEVPARPKgRLRRVSSAGEPLTPEVIRWFDAALGVP-IHDHYGQTELGMVLANHHALEH-PVHAGSAGRAMPG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 367 LEVKVVDpESGLTVPRGEPGELCT-RGYSVML---GYWEQPDKTAeaidAARWMHTGDLAVMDGDGYVNITGRIKDMVIR 442
Cdd:cd05973 268 WRVAVLD-DDGDELGPGEPGRLAIdIANSPLMwfrGYQLPDTPAI----DGGYYLTGDTVEFDPDGSFSFIGRADDVITM 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 443 GGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREG--ASPLTAEKVREFCSGKLAHYKIPRYVHVVDEF 520
Cdd:cd05973 343 SGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGheGTPALADELQLHVKKRLSAHAYPRTIHFVDEL 422
|
490
....*....|....
gi 522130465 521 PMTVTGKVRKVEMR 534
Cdd:cd05973 423 PKTPSGKIQRFLLR 436
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
34-535 |
6.47e-42 |
|
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: 157.59 E-value: 6.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 34 AFGDRDALV--DRAAGG-RWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRS 110
Cdd:cd05915 6 ALFGRKEVVsrLHTGEVhRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 111 HELEYVLDQAGIRLLvasdkFKTSDYPAMVEEvreKCARLEHVVVLGGES--WQELMDAGRRGDPaQLAHLRAgLSADDP 188
Cdd:cd05915 86 KEIAYILNHAEDKVL-----LFDPNLLPLVEA---IRGELKTVQHFVVMDekAPEGYLAYEEALG-EEADPVR-VPERAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 189 INIQYTSGTTGFPKGATLSHHNILNNGYFVG---ELCNYTEEDKVCIpVPFYHCFGMVMgNLACTSHGACMVIPAPAFDP 265
Cdd:cd05915 156 CGMAYTTGTTGLPKGVVYSHRALVLHSLAASlvdGTALSEKDVVLPV-VPMFHVNAWCL-PYAATLVGAKQVLPGPRLDP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 266 RATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSsLRTGIMAGSPCPVEVMKQvIDRMGMAEVSICYGMTETSPVST 345
Cdd:cd05915 234 ASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLK-TLRRLVVGGSAAPRSLIA-RFERMGVEVRQGYGLTETSPVVV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 346 --------QTRADDSIERRVSTVGRVGPHLEVKVVDPESgLTVPRGEPG--ELCTRGYSVMLGYWEQPDKTAEAIDAARW 415
Cdd:cd05915 312 qnfvkshlESLSEEEKLTLKAKTGLPIPLVRLRVADEEG-RPVPKDGKAlgEVQLKGPWITGGYYGNEEATRSALTPDGF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 416 MHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASplTAE 495
Cdd:cd05915 391 FRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKP--TPE 468
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 522130465 496 KVREFCSGKLAHYK-IPRYVHVVDEFPMTVTGKVRKVEMRE 535
Cdd:cd05915 469 ELNEHLLKAGFAKWqLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
49-462 |
1.34e-41 |
|
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: 157.06 E-value: 1.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 49 RWTYRELAGEVTALALGLVARGIGKGDRVgIWSPNRAEwtflQYATAKIGAIL-------VNINPAYR--SHELEYVldq 119
Cdd:cd05906 39 FQSYQDLLEDARRLAAGLRQLGLRPGDSV-ILQFDDNE----DFIPAFWACVLagfvpapLTVPPTYDepNARLRKL--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 120 AGIRLLVASDKFKTSdyPAMVEEVR--EKCARLEHVVVLggeSWQELMDAGRrgdpaqLAHLRAGlSADDPINIQYTSGT 197
Cdd:cd05906 111 RHIWQLLGSPVVLTD--AELVAEFAglETLSGLPGIRVL---SIEELLDTAA------DHDLPQS-RPDDLALLMLTSGS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 198 TGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGACMV-IPAPAF--DPRATLEAVAA 274
Cdd:cd05906 179 TGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVhVPTEEIlaDPLRWLDLIDR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 275 ERCTSLYGvPTMFIAELNH----PDFGEFDLSSLRTGIMAGspcpvevmKQVIDRMGMAEVSI-------------CYGM 337
Cdd:cd05906 259 YRVTITWA-PNFAFALLNDlleeIEDGTWDLSSLRYLVNAG--------EAVVAKTIRRLLRLlepyglppdairpAFGM 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 338 TETSP---VSTQTRADDSIER-RVSTVGRVGPHLEVKVVDPESGLtVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAA 413
Cdd:cd05906 330 TETCSgviYSRSFPTYDHSQAlEFVSLGRPIPGVSMRIVDDEGQL-LPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTED 408
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 522130465 414 RWMHTGDLAVMDgDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDV 462
Cdd:cd05906 409 GWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGV 456
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
187-530 |
1.40e-41 |
|
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: 152.80 E-value: 1.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 187 DPINIQYTSGTTGFPKGATLSHHN-ILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGnLACTSHGACMVIPAPAFDP 265
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTfFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWI-LTCLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 266 RATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTgIMAGSPCPVEVMKQVIDRMGMAEVSICYGMTETSPVST 345
Cdd:cd17635 81 KSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRL-IGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 346 QTRADDSIErrVSTVGRVGPHLEVKVVDPEsGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIdAARWMHTGDLAVMD 425
Cdd:cd17635 160 LPTDDDSIE--INAVGRPYPGVDVYLAATD-GIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 426 GDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASPLTAEKVREFCSGKL 505
Cdd:cd17635 236 EDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENAIRALKHTIRREL 315
|
330 340
....*....|....*....|....*
gi 522130465 506 AHYKIPRYVHVVDEFPMTVTGKVRK 530
Cdd:cd17635 316 EPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
26-528 |
6.14e-41 |
|
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: 153.23 E-value: 6.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 26 DNFDRTVAAFGDRDALVDraAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNIN 105
Cdd:cd17653 1 DAFERIAAAHPDAVAVES--LGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 106 PAYRSHELEYVLDQAGIRLLVASDkfktsdypamveevrekcarlehvvvlggeswqelmdagrrgdpaqlahlraglSA 185
Cdd:cd17653 79 AKLPSARIQAILRTSGATLLLTTD------------------------------------------------------SP 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 186 DDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVC--IPVPFYHCFGMVmgnLACTSHGACMVIPapaf 263
Cdd:cd17653 105 DDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAqvLSIAFDACIGEI---FSTLCNGGTLVLA---- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 264 DPRATLEAVAAErCTSLYGVPTmFIAELNhPDfgefDLSSLRTGIMAGSPCPvevmKQVIDRMGmAEVSI--CYGMTETS 341
Cdd:cd17653 178 DPSDPFAHVART-VDALMSTPS-ILSTLS-PQ----DFPNLKTIFLGGEAVP----PSLLDRWS-PGRRLynAYGPTECT 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 342 PVSTQTRAddSIERRVsTVGRVGPHLEVKVVDPEsGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAARWMH---- 417
Cdd:cd17653 246 ISSTMTEL--LPGQPV-TIGKPIPNSTCYILDAD-LQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPgsrm 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 418 --TGDLAVMDGDGYVNITGRIKDMV-IRGGE-NLYprEIEEFLYT-HPDVLDAQVIGVpdekyGEELMAWVrmregaSPL 492
Cdd:cd17653 322 yrTGDYGRWTEDGGLEFLGREDNQVkVRGFRiNLE--EIEEVVLQsQPEVTQAAAIVV-----NGRLVAFV------TPE 388
|
490 500 510
....*....|....*....|....*....|....*...
gi 522130465 493 TA--EKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKV 528
Cdd:cd17653 389 TVdvDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKV 426
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
28-530 |
3.19e-40 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 156.86 E-value: 3.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 28 FDRTVAAFGDRDALVdrAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPA 107
Cdd:PRK12467 1580 IEDQAAATPEAVALV--FGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPE 1657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 108 YRSHELEYVLDQAGIRLLVASdkfktsdypamveevREKCARL------EHVVVLGGESWQE---LMDAGRRGDPAQLAH 178
Cdd:PRK12467 1658 YPRERLAYMIEDSGIELLLTQ---------------SHLQARLplpdglRSLVLDQEDDWLEgysDSNPAVNLAPQNLAY 1722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 179 lraglsaddpinIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGM--VMGNLActsHGACM 256
Cdd:PRK12467 1723 ------------VIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVweLFWPLI---NGARL 1787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 257 VIPAPAF--DPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLsSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSIC 334
Cdd:PRK12467 1788 VIAPPGAhrDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPL-SLRRVVCGGEALEVEALRPWLERLPDTGLFNL 1866
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 335 YGMTETSPVSTQ---TRADDSiERRVSTVGRVGPHLEVKVVDPESGLtVPRGEPGELCTRGYSVMLGYWEQPDKTAE--- 408
Cdd:PRK12467 1867 YGPTETAVDVTHwtcRRKDLE-GRDSVPIGQPIANLSTYILDASLNP-VPIGVAGELYLGGVGLARGYLNRPALTAErfv 1944
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 409 ----AIDAARWMHTGDLAVMDGDGYVNITGRIKDMV-IRG-----GenlyprEIEEFLYTHPDVLDAQVIGVpDEKYGEE 478
Cdd:PRK12467 1945 adpfGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVkIRGfrielG------EIEARLREQGGVREAVVIAQ-DGANGKQ 2017
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 479 LMAWV-----RMREGASPLTA--EKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKV-RK 530
Cdd:PRK12467 2018 LVAYVvptdpGLVDDDEAQVAlrAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLdRK 2077
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
19-535 |
4.52e-40 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 152.87 E-value: 4.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 19 LLGDTIGDnfDRTVAAFGDRDalvdraaggrWTYRELAGEvtALALGLVARGIGKGDR---VGIWSPNRAEWTFLQYATA 95
Cdd:PRK13388 8 LLRDRAGD--DTIAVRYGDRT----------WTWREVLAE--AAARAAALIALADPDRplhVGVLLGNTPEMLFWLAAAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 96 KIGAILVNINPAYRSHELEYVLDQAGIRLLVASDkfktsdypamveEVREKCARLE----HVVVLGGESWQELMDAGRRG 171
Cdd:PRK13388 74 LGGYVLVGLNTTRRGAALAADIRRADCQLLVTDA------------EHRPLLDGLDlpgvRVLDVDTPAYAELVAAAGAL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 172 DPAqlahlrAGLSADDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDkVC-IPVPFYHCFGMVMGNLACT 250
Cdd:PRK13388 142 TPH------REVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDD-VCyVSMPLFHSNAVMAGWAPAV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 251 SHGACMVIPaPAFDPRATLEAVAAERCTSL-Y-GVPTMFI-AELNHPDFGEfdlSSLRTGImaGSPCPVEVMKQVIDRMG 327
Cdd:PRK13388 215 ASGAAVALP-AKFSASGFLDDVRRYGATYFnYvGKPLAYIlATPERPDDAD---NPLRVAF--GNEASPRDIAEFSRRFG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 328 mAEVSICYGMTETspVSTQTRADDSIErrvSTVGRvgPHLEVKVVDPESGLTVPRGE-------------PGELC-TRGY 393
Cdd:PRK13388 289 -CQVEDGYGSSEG--AVIVVREPGTPP---GSIGR--GAPGVAIYNPETLTECAVARfdahgallnadeaIGELVnTAGA 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 394 SVMLGYWEQPDKTAEAIdAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDE 473
Cdd:PRK13388 361 GFFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDE 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522130465 474 KYGEELMAWVRMREGASpLTAEKVREFCSGK--LAHYKIPRYVHVVDEFPMTVTGKVRKVEMRE 535
Cdd:PRK13388 440 RVGDQVMAALVLRDGAT-FDPDAFAAFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
29-539 |
2.67e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 150.60 E-value: 2.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 29 DRTVAAFGDRDALVDR----AAGGRWTYRELAGEVTALALGLVAR-GIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVN 103
Cdd:PRK07867 4 APTVAELLLPLAEDDDrglyFEDSFTSWREHIRGSAARAAALRARlDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 104 INPAYRSHELEYVLDQAGIRLLVASDKfktsdYPAMVEEVREKCArlehVVVLGGESWQELMDAGRRGDPAqlahlRAGL 183
Cdd:PRK07867 84 LNPTRRGAALARDIAHADCQLVLTESA-----HAELLDGLDPGVR----VINVDSPAWADELAAHRDAEPP-----FRVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 184 SADDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGACMVIPApAF 263
Cdd:PRK07867 150 DPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRR-KF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 264 DPRATLEAVAAERCTSL-Y-GVPTMFI-AELNHPDFGEfdlSSLRtgIMAG---SPCPVEVMKQvidRMGMAEVSiCYGM 337
Cdd:PRK07867 229 SASGFLPDVRRYGATYAnYvGKPLSYVlATPERPDDAD---NPLR--IVYGnegAPGDIARFAR---RFGCVVVD-GFGS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 338 TETSPvstqtraddSIERRVST----VGRVGPhlEVKVVDPESGLTVPRGEP------------GELC-TRGYSVMLGYW 400
Cdd:PRK07867 300 TEGGV---------AITRTPDTppgaLGPLPP--GVAIVDPDTGTECPPAEDadgrllnadeaiGELVnTAGPGGFEGYY 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 401 EQPDKTAEAIdAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELM 480
Cdd:PRK07867 369 NDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVM 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522130465 481 AWVRMREGAsPLTAEKVREFCSGK--LAHYKIPRYVHVVDEFPMTVTGKVRKVEMREKSIT 539
Cdd:PRK07867 448 AALVLAPGA-KFDPDAFAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEGVD 507
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
29-545 |
3.13e-39 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 150.82 E-value: 3.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 29 DRTVA-AFGDRDAL--VDRAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNIN 105
Cdd:PRK04319 50 DRHADgGRKDKVALryLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 106 PAYRSHELEYVLDQAGIRLLVASdkfktsdyPAMVEE-VREKCARLEHVVVLGGE--------SWQELMDAGrrGDPAQL 176
Cdd:PRK04319 130 EAFMEEAVRDRLEDSEAKVLITT--------PALLERkPADDLPSLKHVLLVGEDveegpgtlDFNALMEQA--SDEFDI 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 177 AHLRAglsaDDPINIQYTSGTTGFPKGATLSHHNILNN---GYFVGELcnytEEDKVcipvpfYHCF-------GMVMGN 246
Cdd:PRK04319 200 EWTDR----EDGAILHYTSGSTGKPKGVLHVHNAMLQHyqtGKYVLDL----HEDDV------YWCTadpgwvtGTSYGI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 247 LACTSHGACMVIPAPAFDPRATLEAVAAERCTSLYGVPT---MFI---AELnhpdFGEFDLSSLRTGIMAGSPCPVEVMK 320
Cdd:PRK04319 266 FAPWLNGATNVIDGGRFSPERWYRILEDYKVTVWYTAPTairMLMgagDDL----VKKYDLSSLRHILSVGEPLNPEVVR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 321 QVIDRMGMaEVSICYGMTETS-------PvstqtraddSIERRVSTVGRVGPHLEVKVVDPEsGLTVPRGEPGELCTR-G 392
Cdd:PRK04319 342 WGMKVFGL-PIHDNWWMTETGgimianyP---------AMDIKPGSMGKPLPGIEAAIVDDQ-GNELPPNRMGNLAIKkG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 393 Y-SVMLGYWEQPDKTAEAIdAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVP 471
Cdd:PRK04319 411 WpSMMRGIWNNPEKYESYF-AGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKP 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522130465 472 DEKYGEELMAWVRMREGASPLTA--EKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKV--RKVEMREksitlLGLET 545
Cdd:PRK04319 490 DPVRGEIIKAFVALRPGYEPSEElkEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKImrRVLKAWE-----LGLPE 562
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
29-528 |
1.51e-38 |
|
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: 147.13 E-value: 1.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 29 DRTVAAFGDRdalvdraaggRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAY 108
Cdd:cd17649 2 DAVALVFGDQ----------SLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 109 RSHELEYVLDQAGIRLLVASDkfktsdypamveevrekcarlehvvvlggeswqelmdagrrgdPAQLAHlraglsaddp 188
Cdd:cd17649 72 PAERLRYMLEDSGAGLLLTHH-------------------------------------------PRQLAY---------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 189 inIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVC--IPVPFYHCFGMVMGNLACtshGACMVIPAP--AFD 264
Cdd:cd17649 99 --VIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELqfASFNFDGAHEQLLPPLIC---GACVVLRPDelWAS 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 265 PRATLEAVAAERCTSLyGVPT----MFIAELNHPDFGefDLSSLRTGIMAGSPCPVEVMKqvidRMGMAEVSIC--YGMT 338
Cdd:cd17649 174 ADELAEMVRELGVTVL-DLPPaylqQLAEEADRTGDG--RPPSLRLYIFGGEALSPELLR----RWLKAPVRLFnaYGPT 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 339 ET--SPVSTQTRADDSIERRVSTVGRVGPHLEVKVVDPESGLtVPRGEPGELCTRGYSVMLGYWEQPDKTAEAI------ 410
Cdd:cd17649 247 EAtvTPLVWKCEAGAARAGASMPIGRPLGGRSAYILDADLNP-VPVGVTGELYIGGEGLARGYLGRPELTAERFvpdpfg 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 411 -DAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKyGEELMAWVRMREGA 489
Cdd:cd17649 326 aPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG-GKQLVAYVVLRAAA 404
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 522130465 490 S-PLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKV 528
Cdd:cd17649 405 AqPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKL 444
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
23-501 |
1.74e-38 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 149.86 E-value: 1.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 23 TIGDNFDRTVAAFGDRDAL-----VDRAAGG-RW-TYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATA 95
Cdd:PLN02736 45 TLHDNFVYAVETFRDYKYLgtrirVDGTVGEyKWmTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACS 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 96 KIGAILVninPAYRS---HELEYVLDQAGIR-LLVASDKFKT-----SDYPamveevrekCARLehVVVLGGE------- 159
Cdd:PLN02736 125 AYSYVSV---PLYDTlgpDAVKFIVNHAEVAaIFCVPQTLNTllsclSEIP---------SVRL--IVVVGGAdeplpsl 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 160 ---------SWQELMDAGRRgdpaqlaHLRAGLSA--DDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEED 228
Cdd:PLN02736 191 psgtgveivTYSKLLAQGRS-------SPQPFRPPkpEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 229 KVCIPVPFYHCFGMvMGNLACTSHGAcmvipAPAF---DPRATLEAVAAERCTSLYGVP--------------------- 284
Cdd:PLN02736 264 VHISYLPLAHIYER-VNQIVMLHYGV-----AVGFyqgDNLKLMDDLAALRPTIFCSVPrlynriydgitnavkesgglk 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 285 -TMFIAELNHPdfgefdlsslRTGIMAG-SPCPVE---VMKQVIDRMG-----------------MAEVSIC-------- 334
Cdd:PLN02736 338 eRLFNAAYNAK----------KQALENGkNPSPMWdrlVFNKIKAKLGgrvrfmssgasplspdvMEFLRICfggrvleg 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 335 YGMTETSPVSTQTRADDsierrvSTVGRVG---PHLEVKVVD-PESGLT-----VPRgepGELCTRGYSVMLGYWEQPDK 405
Cdd:PLN02736 408 YGMTETSCVISGMDEGD------NLSGHVGspnPACEVKLVDvPEMNYTsedqpYPR---GEICVRGPIIFKGYYKDEVQ 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 406 TAEAIDAARWMHTGDLAVMDGDGYVNITGRIKDMV-IRGGENLYPREIE------EFL---YTHPDVLDAQVIGV--PDE 473
Cdd:PLN02736 479 TREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIEnvyakcKFVaqcFVYGDSLNSSLVAVvvVDP 558
|
570 580
....*....|....*....|....*...
gi 522130465 474 kygEELMAWVRmREGaspLTAEKVREFC 501
Cdd:PLN02736 559 ---EVLKAWAA-SEG---IKYEDLKQLC 579
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
29-534 |
7.16e-38 |
|
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: 147.32 E-value: 7.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 29 DRTVAAFGDRDALV----DRAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNI 104
Cdd:cd05966 60 DRHLKERGDKVAIIwegdEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 105 NPAYRSHEL-EYVLDqAGIRLLVASDKF----KTSDYPAMVEEVREKCARLEHVVVL---GGES---------WQELMDA 167
Cdd:cd05966 140 FAGFSAESLaDRIND-AQCKLVITADGGyrggKVIPLKEIVDEALEKCPSVEKVLVVkrtGGEVpmtegrdlwWHDLMAK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 168 GRRGDPAQLahlragLSADDPINIQYTSGTTGFPKGATLSHhnilnNGYFVGELC------NYTEEDkvcipvpFYHCFG 241
Cdd:cd05966 219 QSPECEPEW------MDSEDPLFILYTSGSTGKPKGVVHTT-----GGYLLYAATtfkyvfDYHPDD-------IYWCTA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 242 ----------MVMGNLACtshGACMVI--PAPAF-DPRATLEAVAAERCTSLYGVPT---MFIAELNHPdFGEFDLSSLR 305
Cdd:cd05966 281 digwitghsyIVYGPLAN---GATTVMfeGTPTYpDPGRYWDIVEKHKVTIFYTAPTairALMKFGDEW-VKKHDLSSLR 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 306 TGIMAGSPCPVEVMKQVIDRMGMAEVSIC--YGMTETS-------PVSTQTRAddsierrvSTVGRVGPHLEVKVVDPEs 376
Cdd:cd05966 357 VLGSVGEPINPEAWMWYYEVIGKERCPIVdtWWQTETGgimitplPGATPLKP--------GSATRPFFGIEPAILDEE- 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 377 GLTVPRGEPGELC-TRGY-SVMLGYWEQPDktaeaidaaRWMHT-----------GDLAVMDGDGYVNITGRIKDMVIRG 443
Cdd:cd05966 428 GNEVEGEVEGYLViKRPWpGMARTIYGDHE---------RYEDTyfskfpgyyftGDGARRDEDGYYWITGRVDDVINVS 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 444 GENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREG--ASPLTAEKVREFCSGKLAHYKIPRYVHVVDEFP 521
Cdd:cd05966 499 GHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGeePSDELRKELRKHVRKEIGPIATPDKIQFVPGLP 578
|
570
....*....|...
gi 522130465 522 MTVTGKVrkveMR 534
Cdd:cd05966 579 KTRSGKI----MR 587
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
28-530 |
9.23e-38 |
|
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: 144.62 E-value: 9.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 28 FDRTVAAFGDRDALVDRaaGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPA 107
Cdd:cd17645 4 FEEQVERTPDHVAVVDR--GQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 108 YRSHELEYVLDQAGIRLLVAsdkfktsdypamveevrekcarlehvvvlggeswqelmdagrrgDPAQLAHlraglsadd 187
Cdd:cd17645 82 YPGERIAYMLADSSAKILLT--------------------------------------------NPDDLAY--------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 188 pinIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIpvpfYHCFGMVMGNLACTSH---GACMVIpapaFD 264
Cdd:cd17645 109 ---VIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLV----YASFSFDASAWEIFPHltaGAALHV----VP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 265 PRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGspcpvEVMKqVIDRMGMAEVSiCYGMTETSPVS 344
Cdd:cd17645 178 SERRLDLDALNDYFNQEGITISFLPTGAAEQFMQLDNQSLRVLLTGG-----DKLK-KIERKGYKLVN-NYGPTENTVVA 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 345 TQTRADDSiERRVStVGRvgPHLEVKVVDPESGLTV-PRGEPGELCTRGYSVMLGYWEQPDKTAEA------IDAARWMH 417
Cdd:cd17645 251 TSFEIDKP-YANIP-IGK--PIDNTRVYILDEALQLqPIGVAGELCIAGEGLARGYLNRPELTAEKfivhpfVPGERMYR 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 418 TGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASPltaEKV 497
Cdd:cd17645 327 TGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPH---EEL 403
|
490 500 510
....*....|....*....|....*....|...
gi 522130465 498 REFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRK 530
Cdd:cd17645 404 REWLKNDLPDYMIPTYFVHLKALPLTANGKVDR 436
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
29-539 |
1.07e-37 |
|
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: 147.01 E-value: 1.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 29 DRTVAAFGDRDALV---DRAAGGR-WTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNI 104
Cdd:TIGR02188 64 DRHLEARPDKVAIIwegDEPGEVRkITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 105 NPAYRSHELEYVLDQAGIRLLVASDKF----KTSDYPAMVEEVREKC-ARLEHVVVL---GGES----------WQELM- 165
Cdd:TIGR02188 144 FGGFSAEALADRINDAGAKLVITADEGlrggKVIPLKAIVDEALEKCpVSVEHVLVVrrtGNPVvpwvegrdvwWHDLMa 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 166 DAGRRGDPAQLahlraglSADDPINIQYTSGTTGFPKGATlshHNIlnNGYFVGE------LCNYTEEDKvcipvpfYHC 239
Cdd:TIGR02188 224 KASAYCEPEPM-------DSEDPLFILYTSGSTGKPKGVL---HTT--GGYLLYAamtmkyVFDIKDGDI-------FWC 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 240 FG----------MVMGNLACtshGACMVI--PAPAF-DPRATLEAVAAERCTSLYGVPT---MFIAE-LNHPDfgEFDLS 302
Cdd:TIGR02188 285 TAdvgwitghsyIVYGPLAN---GATTVMfeGVPTYpDPGRFWEIIEKHKVTIFYTAPTairALMRLgDEWVK--KHDLS 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 303 SLRTGIMAGSPCPVEVMKQVIDRMGMAEVSIC--YGMTETS-------PVSTQTRAddsierrvSTVGRVGPHLEVKVVD 373
Cdd:TIGR02188 360 SLRLLGSVGEPINPEAWMWYYKVVGKERCPIVdtWWQTETGgimitplPGATPTKP--------GSATLPFFGIEPAVVD 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 374 pESGLTVPR-GEPGELCTRGY--SVMLGYWEQPDKTAEA-IDAARWMH-TGDLAVMDGDGYVNITGRIKDMVIRGGENLY 448
Cdd:TIGR02188 432 -EEGNPVEGpGEGGYLVIKQPwpGMLRTIYGDHERFVDTyFSPFPGYYfTGDGARRDKDGYIWITGRVDDVINVSGHRLG 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 449 PREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASP--LTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTG 526
Cdd:TIGR02188 511 TAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPddELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSG 590
|
570
....*....|....*...
gi 522130465 527 KV-----RKVEMREKSIT 539
Cdd:TIGR02188 591 KImrrllRKIAAGEAEIL 608
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
50-469 |
1.65e-37 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) 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. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It 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: 341256 [Multi-domain] Cd Length: 596 Bit Score: 146.35 E-value: 1.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 50 WTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVASD 129
Cdd:cd05933 9 LTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVEN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 130 KFKTsdypAMVEEVREKCARLEHVVVLGGE---------SWQELMDAGRRGDPAQLAHLRAGLSADDPINIQYTSGTTGF 200
Cdd:cd05933 89 QKQL----QKILQIQDKLPHLKAIIQYKEPlkekepnlySWDEFMELGRSIPDEQLDAIISSQKPNQCCTLIYTSGTTGM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 201 PKGATLSHHNIL-NNGYFVGELCNYTEEDKVCIPV---PFYHCFGMVMGNLACTSHGACMVIPAPafDP-RATLEAVAAE 275
Cdd:cd05933 165 PKGVMLSHDNITwTAKAASQHMDLRPATVGQESVVsylPLSHIAAQILDIWLPIKVGGQVYFAQP--DAlKGTLVKTLRE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 276 -RCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGI---------------MAG-SPCPVE-------VMKQVIDRMGMAEV 331
Cdd:cd05933 243 vRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIaswakgvgletnlklMGGeSPSPLFyrlakklVFKKVRKALGLDRC 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 332 SIC-------------------------YGMTETSPVSTQTRADDSierRVSTVGRVGPHLEVKVVDPES-GLtvprgep 385
Cdd:cd05933 323 QKFftgaapisretlefflslnipimelYGMSETSGPHTISNPQAY---RLLSCGKALPGCKTKIHNPDAdGI------- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 386 GELCTRGYSVMLGYWEQPDKTAEAIDAARWMHTGDLAVMDGDGYVNITGRIKDMVIR-GGENLYPREIEEFLYTH-PDVL 463
Cdd:cd05933 393 GEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITaGGENVPPVPIEDAVKKElPIIS 472
|
....*.
gi 522130465 464 DAQVIG 469
Cdd:cd05933 473 NAMLIG 478
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
49-530 |
2.00e-37 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 148.57 E-value: 2.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 49 RWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVaS 128
Cdd:PRK12316 536 TLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLL-S 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 129 DKFKTSDYPAmveevrekCARLEHVVVLGGESWqelMDAGRRGDPAQLAHlraglsADDPINIQYTSGTTGFPKGATLSH 208
Cdd:PRK12316 615 QSHLGRKLPL--------AAGVQVLDLDRPAAW---LEGYSEENPGTELN------PENLAYVIYTSGSTGKPKGAGNRH 677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 209 HNILN------NGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGnlactshGACMVIPAP--AFDPRATLEAVAAERCTSL 280
Cdd:PRK12316 678 RALSNrlcwmqQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMS-------GARLVVAAPgdHRDPAKLVELINREGVDTL 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 281 YGVPTMFIAELnhPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSICYGMTETSPVSTQTRADDSIERRVStV 360
Cdd:PRK12316 751 HFVPSMLQAFL--QDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGGDSVP-I 827
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 361 GRVGPHLEVKVVDPESGlTVPRGEPGELCTRGYSVMLGYWEQPDKTAEA------IDAARWMHTGDLAVMDGDGYVNITG 434
Cdd:PRK12316 828 GRPIANLACYILDANLE-PVPVGVLGELYLAGRGLARGYHGRPGLTAERfvpspfVAGERMYRTGDLARYRADGVIEYAG 906
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 435 RIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPdekyGEELMAWVrMREGASPLTAEKVREFCSGKLAHYKIPRYV 514
Cdd:PRK12316 907 RIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYV-VLESEGGDWREALKAHLAASLPEYMVPAQW 981
|
490
....*....|....*..
gi 522130465 515 HVVDEFPMTVTGKV-RK 530
Cdd:PRK12316 982 LALERLPLTPNGKLdRK 998
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
28-530 |
4.40e-37 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 147.41 E-value: 4.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 28 FDRTVAAFGDRDALVdrAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPA 107
Cdd:PRK12316 4557 VAERARMTPDAVAVV--FDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPE 4634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 108 YRSHELEYVLDQAGIRLLVaSDKFKTSDYPAmveevrekCARLEHVVVLGGESWQELMDAG--RRGDPAQLAHlraglsa 185
Cdd:PRK12316 4635 YPRERLAYMMEDSGAALLL-TQSHLLQRLPI--------PDGLASLALDRDEDWEGFPAHDpaVRLHPDNLAY------- 4698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 186 ddpinIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPF-YHCFGM-VMGNLACtshGACMVIPAP-A 262
Cdd:PRK12316 4699 -----VIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFsFDGSHEgLYHPLIN---GASVVIRDDsL 4770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 263 FDPRATLEAVAAERCTSLYGVPTMFIAELNHPDfGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSICYGMTETSP 342
Cdd:PRK12316 4771 WDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAE-RDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTV 4849
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 343 VST--QTRADDSIERRVSTVGRVGPHLEVKVVDPESGLtVPRGEPGELCTRGYSVMLGYWEQPDKTAE-----AIDA--A 413
Cdd:PRK12316 4850 TVLlwKARDGDACGAAYMPIGTPLGNRSGYVLDGQLNP-LPVGVAGELYLGGEGVARGYLERPALTAErfvpdPFGApgG 4928
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 414 RWMHTGDLAVMDGDGYVNITGRIKDMV-IRG-----GenlyprEIEEFLYTHPDVLDAQVIGVPDeKYGEELMAWV---- 483
Cdd:PRK12316 4929 RLYRTGDLARYRADGVIDYLGRVDHQVkIRGfrielG------EIEARLREHPAVREAVVIAQEG-AVGKQLVGYVvpqd 5001
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 522130465 484 -RMREGASPLTA--EKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKV-RK 530
Cdd:PRK12316 5002 pALADADEAQAElrDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLdRK 5052
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
48-530 |
8.54e-37 |
|
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: 142.68 E-value: 8.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 48 GRWTYRELAGEVTALALGLVARGIGKGDRVGIwSPNRAEWTFL-QYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLV 126
Cdd:cd05918 23 GSLTYAELDRLSSRLAHHLRSLGVGPGVFVPL-CFEKSKWAVVaMLAVLKAGGAFVPLDPSHPLQRLQEILQDTGAKVVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 127 ASDkfktsdypamveevrekcarlehvvvlggeswqelmdagrrgdpaqlahlraglsADDPINIQYTSGTTGFPKGATL 206
Cdd:cd05918 102 TSS-------------------------------------------------------PSDAAYVIFTSGSTGKPKGVVI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 207 SHHNILNNGYFVGELCNYTEEDKVcipVPFY-HCFGMVMGNLACT-SHGACMVIPaPAFDPRATLEAVAAE-RCTSLYGV 283
Cdd:cd05918 127 EHRALSTSALAHGRALGLTSESRV---LQFAsYTFDVSILEIFTTlAAGGCLCIP-SEEDRLNDLAGFINRlRVTWAFLT 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 284 PTMfiAELNHPDfgefDLSSLRTGIMAGspcpvEVMKQ-VIDR-MGMAEVSICYGMTETSPVSTQTRADDSieRRVSTVG 361
Cdd:cd05918 203 PSV--ARLLDPE----DVPSLRTLVLGG-----EALTQsDVDTwADRVRLINAYGPAECTIAATVSPVVPS--TDPRNIG 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 362 R---VGPHlevkVVDPES-GLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEA-IDAARWMH------------TGDLAVM 424
Cdd:cd05918 270 RplgATCW----VVDPDNhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAfIEDPAWLKqegsgrgrrlyrTGDLVRY 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 425 DGDGYVNITGRIKDMV-IRG-----GenlyprEIEEFLYTHPDVLD---AQVIGVPDEKYGEELMAWVRMREGAS----- 490
Cdd:cd05918 346 NPDGSLEYVGRKDTQVkIRGqrvelG------EIEHHLRQSLPGAKevvVEVVKPKDGSSSPQLVAFVVLDGSSSgsgdg 419
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 522130465 491 -----------PLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKV-RK 530
Cdd:cd05918 420 dslflepsdefRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIdRR 471
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
47-535 |
8.76e-37 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 143.59 E-value: 8.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 47 GGRWTYRELAGEVTALALGLVA-RGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLL 125
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 126 VASdkfktsdyPAMVEEVREKCARLE----HVVVLGGES-------WQELMDAGrrGDPAQLAHLRAGLSADDPINIQYT 194
Cdd:cd05938 83 VVA--------PELQEAVEEVLPALRadgvSVWYLSHTSntegvisLLDKVDAA--SDEPVPASLRAHVTIKSPALYIYT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 195 SGTTGFPKGATLSHHNILnNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGACMVIpAPAFdpratleavAA 274
Cdd:cd05938 153 SGTTGLPKAARISHLRVL-QCSGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVL-KPKF---------SA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 275 ER----CTSlYGVPTM-FIAEL-----NHPDFGEFDLSSLRTGImaGSPCPVEVMKQVIDRMGMAEVSICYGMTETSpVS 344
Cdd:cd05938 222 SQfwddCRK-HNVTVIqYIGELlrylcNQPQSPNDRDHKVRLAI--GNGLRADVWREFLRRFGPIRIREFYGSTEGN-IG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 345 TQTRADdsierRVSTVGRVG-------PHLEVKvVDPESG----------LTVPRGEPGELCTR--GYSVMLGYWEQPDK 405
Cdd:cd05938 298 FFNYTG-----KIGAVGRVSylykllfPFELIK-FDVEKEepvrdaqgfcIPVAKGEPGLLVAKitQQSPFLGYAGDKEQ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 406 TAEAI--DAAR----WMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKY-GEE 478
Cdd:cd05938 372 TEKKLlrDVFKkgdvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHeGRI 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 522130465 479 LMAWVRMREGASpLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMRE 535
Cdd:cd05938 452 GMAAVKLKPGHE-FDGKKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQKVRLVE 507
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
28-530 |
1.34e-36 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 146.07 E-value: 1.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 28 FDRTVAAFGDRDALVdrAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPA 107
Cdd:PRK12467 518 IEAQARQHPERPALV--FGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPE 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 108 YRSHELEYVLDQAGIRLLVA-SDKFKTSDYPAMV------EEVREKCARLEHVVVLggeswqelmdagrRGDPAQLAHlr 180
Cdd:PRK12467 596 YPQDRLAYMLDDSGVRLLLTqSHLLAQLPVPAGLrslcldEPADLLCGYSGHNPEV-------------ALDPDNLAY-- 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 181 aglsaddpinIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFG--MVMGNLActsHGACMVI 258
Cdd:PRK12467 661 ----------VIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGvtELFGALA---SGATLHL 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 259 PAP--AFDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGEfdLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSICYG 336
Cdd:PRK12467 728 LPPdcARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVAL--PRPQRALVCGGEALQVDLLARVRALGPGARLINHYG 805
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 337 MTETSPVSTQTR-ADDSIERRVSTVGRVGPHLEVKVVDPESGLtVPRGEPGELCTRGYSVMLGYWEQPDKTAE------- 408
Cdd:PRK12467 806 PTETTVGVSTYElSDEERDFGNVPIGQPLANLGLYILDHYLNP-VPVGVVGELYIGGAGLARGYHRRPALTAErfvpdpf 884
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 409 AIDAARWMHTGDLAVMDGDGYVNITGRIKDMV-IRgGENLYPREIEEFLYTHPDVLDAQVIGVPDEKyGEELMAWV---R 484
Cdd:PRK12467 885 GADGGRLYRTGDLARYRADGVIEYLGRMDHQVkIR-GFRIELGEIEARLLAQPGVREAVVLAQPGDA-GLQLVAYLvpaA 962
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 522130465 485 MREGASP-LTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKV-RK 530
Cdd:PRK12467 963 VADGAEHqATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLdRK 1010
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
5-530 |
1.52e-36 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 146.07 E-value: 1.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 5 PALPSYASGISEVPLLGDTIGDNFDRTVAAFGDRdalvdraaggRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNR 84
Cdd:PRK12467 3086 ATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQ----------QLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERS 3155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 85 AEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVASdkfktsdypamvEEVREKCARLEHV--VVLGGESWQ 162
Cdd:PRK12467 3156 VEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQ------------AHLLEQLPAPAGDtaLTLDRLDLN 3223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 163 ELMDAG--RRGDPAQLAHlraglsaddpinIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFyhCF 240
Cdd:PRK12467 3224 GYSENNpsTRVMGENLAY------------VIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSF--SF 3289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 241 GM----VMGNLACtshGACMVI-PAPAFDPRATLEAVAAERCTSLYGVPTMFIAELNhpDFGEFDLSSLRTGIMAGSPCP 315
Cdd:PRK12467 3290 DGaqerFLWTLIC---GGCLVVrDNDLWDPEELWQAIHAHRISIACFPPAYLQQFAE--DAGGADCASLDIYVFGGEAVP 3364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 316 VEVMKQVIDRMGMAEVSICYGMTETSPVST--QTRADDSIERRVSTVGRVGPHLEVKVVDpESGLTVPRGEPGELCTRGY 393
Cdd:PRK12467 3365 PAAFEQVKRKLKPRGLTNGYGPTEAVVTVTlwKCGGDAVCEAPYAPIGRPVAGRSIYVLD-GQLNPVPVGVAGELYIGGV 3443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 394 SVMLGYWEQPDKTAEAIDA-------ARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQ 466
Cdd:PRK12467 3444 GLARGYHQRPSLTAERFVAdpfsgsgGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAV 3523
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522130465 467 VIGVPDEKyGEELMAWVRMREGASPLtAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKV-RK 530
Cdd:PRK12467 3524 VLARDGAG-GKQLVAYVVPADPQGDW-RETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVdRK 3586
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
35-511 |
2.31e-36 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 140.78 E-value: 2.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 35 FGDRDALvdRAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELE 114
Cdd:PRK09029 16 RPQAIAL--RLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 115 YVLDQAGIRLLVASDKFKTsdyPAMVEEVREKCARLEHVVvlggeSWQelmdagrrgdPAQLAHLraglsaddpiniQYT 194
Cdd:PRK09029 94 ELLPSLTLDFALVLEGENT---FSALTSLHLQLVEGAHAV-----AWQ----------PQRLATM------------TLT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 195 SGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGM--VMGNLACtshGACMVIPAPAfdpraTLEAv 272
Cdd:PRK09029 144 SGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQDSWLLSLPLFHVSGQgiVWRWLYA---GATLVVRDKQ-----PLEQ- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 273 AAERCT--SLygVPTMFIAELNHPdfgEFDLSsLRTGIMAGSPCPVEVMKQvidrmgMAEVSIC----YGMTETSpvSTQ 346
Cdd:PRK09029 215 ALAGCThaSL--VPTQLWRLLDNR---SEPLS-LKAVLLGGAAIPVELTEQ------AEQQGIRcwcgYGLTEMA--STV 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 347 T--RADDSierrvSTVGRVGPHLEVKVVDpesgltvprgepGELCTRGYSVMLGYWEQpDKTAEAIDAARWMHTGDLAVM 424
Cdd:PRK09029 281 CakRADGL-----AGVGSPLPGREVKLVD------------GEIWLRGASLALGYWRQ-GQLVPLVNDEGWFATRDRGEW 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 425 DGDGYVnITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVrmrEGASPLTAEKVREFCSGK 504
Cdd:PRK09029 343 QNGELT-ILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVV---ESDSEAAVVNLAEWLQDK 418
|
....*..
gi 522130465 505 LAHYKIP 511
Cdd:PRK09029 419 LARFQQP 425
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
27-535 |
1.06e-35 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 142.80 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 27 NFDRTV------AA--FGDRDALVDRAAGGRWTYRELAgeVTALALG-LVARGIGKGDRVGIWSPNRAEWTFLQYATAKI 97
Cdd:PRK06814 628 DYDRTLfealieAAkiHGFKKLAVEDPVNGPLTYRKLL--TGAFVLGrKLKKNTPPGENVGVMLPNANGAAVTFFALQSA 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 98 G---AIL------VNINPAYRSheleyvldqAGIRLLVASDKF-KTSDYPAMVEEVrEKCARLEHV--VVLGGESWQELM 165
Cdd:PRK06814 706 GrvpAMInfsagiANILSACKA---------AQVKTVLTSRAFiEKARLGPLIEAL-EFGIRIIYLedVRAQIGLADKIK 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 166 D--AGRRgdPAQLAHLRaglSADDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMV 243
Cdd:PRK06814 776 GllAGRF--PLVYFCNR---DPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLT 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 244 MGNLACTSHGACMVI-PAPaFDPRATLEAVAAERCTSLYGVPTmFI---AELNHPdfgeFDLSSLRTgIMAGSpcpvEVM 319
Cdd:PRK06814 851 GGLVLPLLSGVKVFLyPSP-LHYRIIPELIYDTNATILFGTDT-FLngyARYAHP----YDFRSLRY-VFAGA----EKV 919
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 320 KQVIDRMGMAEVSI----CYGMTETSPV-STQTRADDsierRVSTVGRVGPHLEVKvVDPESGLTvprgEPGELCTRGYS 394
Cdd:PRK06814 920 KEETRQTWMEKFGIrileGYGVTETAPViALNTPMHN----KAGTVGRLLPGIEYR-LEPVPGID----EGGRLFVRGPN 990
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 395 VMLGYW--EQPDKTAEAIDAarWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYT-HPDVLDAqVIGVP 471
Cdd:PRK06814 991 VMLGYLraENPGVLEPPADG--WYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAElWPDALHA-AVSIP 1067
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522130465 472 DEKYGEELMAWVRMREGASPLTAEKVREFCSGKLAhykIPRYVHVVDEFPMTVTGKVRKVEMRE 535
Cdd:PRK06814 1068 DARKGERIILLTTASDATRAAFLAHAKAAGASELM---VPAEIITIDEIPLLGTGKIDYVAVTK 1128
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
50-469 |
1.81e-35 |
|
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: 140.25 E-value: 1.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 50 WTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVASD 129
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAED 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 130 KFKTSDypamVEEVREKCARLEHVV--------------VLGGESWQELMDAGRRGDPAQLAHLRAGLSADDPINIQYTS 195
Cdd:cd17641 92 EEQVDK----LLEIADRIPSVRYVIycdprgmrkyddprLISFEDVVALGRALDRRDPGLYEREVAAGKGEDVAVLCTTS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 196 GTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVC--IPVPFYHCFGMVMGN-LACtshGACMVIP------------- 259
Cdd:cd17641 168 GTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVsvLPLPWIGEQMYSVGQaLVC---GFIVNFPeepetmmedlrei 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 260 APAF---DPRaTLEAVAAE---------------------------------RCTSLYGVPTMFIAE--LNHPDFGEFDL 301
Cdd:cd17641 245 GPTFvllPPR-VWEGIAADvrarmmdatpfkrfmfelgmklglraldrgkrgRPVSLWLRLASWLADalLFRPLRDRLGF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 302 SSLRTGIMAGSPCPVEV----------MKQVidrmgmaevsicYGMTETSPVSTQTRADDSierRVSTVGRVGPHLEVKV 371
Cdd:cd17641 324 SRLRSAATGGAALGPDTfrffhaigvpLKQL------------YGQTELAGAYTVHRDGDV---DPDTVGVPFPGTEVRI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 372 VdpesgltvprgEPGELCTRGYSVMLGYWEQPDKTAEAIDAARWMHTGDLAVMDGDGYVNITGRIKD-MVIRGGENLYPR 450
Cdd:cd17641 389 D-----------EVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDvGTTSDGTRFSPQ 457
|
490
....*....|....*....
gi 522130465 451 EIEEFLYTHPDVLDAQVIG 469
Cdd:cd17641 458 FIENKLKFSPYIAEAVVLG 476
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
49-528 |
2.01e-35 |
|
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: 137.98 E-value: 2.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 49 RWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVAs 128
Cdd:cd17650 12 QLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLT- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 129 dkfktsdypamveevrekcarlehvvvlggeswqelmdagrrgDPaqlahlraglsaDDPINIQYTSGTTGFPKGATLSH 208
Cdd:cd17650 91 -------------------------------------------QP------------EDLAYVIYTSGTTGKPKGVMVEH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 209 HNILNnGYFVGElcnyTEEDKVCIPVPFYH----CFGMVMGNLACT-SHGACMVI-PAPA-FDPRATLEAVAAERCTSLY 281
Cdd:cd17650 116 RNVAH-AAHAWR----REYELDSFPVRLLQmasfSFDVFAGDFARSlLNGGTLVIcPDEVkLDPAALYDLILKSRITLME 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 282 GVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSI-CYGMTETSPVST--QTRADDSIERRVS 358
Cdd:cd17650 191 STPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGMRIInSYGVTEATIDSTyyEEGRDPLGDSANV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 359 TVGRVGPHLEVKVVDPESGLtVPRGEPGELCTRGYSVMLGYWEQPDKTAEAI------DAARWMHTGDLAVMDGDGYVNI 432
Cdd:cd17650 271 PIGRPLPNTAMYVLDERLQP-QPVGVAGELYIGGAGVARGYLNRPELTAERFvenpfaPGERMYRTGDLARWRADGNVEL 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 433 TGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMRegASPLTAEkVREFCSGKLAHYKIPR 512
Cdd:cd17650 350 LGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAA--ATLNTAE-LRAFLAKELPSYMIPS 426
|
490
....*....|....*.
gi 522130465 513 YVHVVDEFPMTVTGKV 528
Cdd:cd17650 427 YYVQLDALPLTPNGKV 442
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
50-538 |
2.11e-35 |
|
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: 138.33 E-value: 2.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 50 WTYRELAGEVTALALGLV-ARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVAS 128
Cdd:cd05937 6 WTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVIVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 129 DkfktsDYPAMveevrekcarlehvvvlggeswqelmdagrrgdpaqlahlraglsaddpinIQYTSGTTGFPKGATLSH 208
Cdd:cd05937 86 P-----DDPAI---------------------------------------------------LIYTSGTTGLPKAAAISW 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 209 HNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGACMVIpAPAF----------DPRATLEAVAAERCT 278
Cdd:cd05937 110 RRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLAL-SRKFsasqfwkdvrDSGATIIQYVGELCR 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 279 SLYGVPTMfIAELNHpdfgefdlsslRTGIMAGSPCPVEVMKQVIDRMGMAEVSICYGMTETSPVSTQTRADD------- 351
Cdd:cd05937 189 YLLSTPPS-PYDRDH-----------KVRVAWGNGLRPDIWERFRERFNVPEIGEFYAATEGVFALTNHNVGDfgagaig 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 352 ---SIERR----VSTVGRVGPHLEVKVVDPESGLTV--PRGEPGELCTR----GYSVMLGYWEQPDKTAEAI--DAAR-- 414
Cdd:cd05937 257 hhgLIRRWkfenQVVLVKMDPETDDPIRDPKTGFCVraPVGEPGEMLGRvpfkNREAFQGYLHNEDATESKLvrDVFRkg 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 415 --WMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKY-GEELMAWVRMREGASP 491
Cdd:cd05937 337 diYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHdGRAGCAAITLEESSAV 416
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 522130465 492 LTAE---KVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMREKSI 538
Cdd:cd05937 417 PTEFtksLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGV 466
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
52-499 |
1.40e-34 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 137.44 E-value: 1.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 52 YRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILV--NINPAYRSHElEYVlDQagIRLLVASD 129
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVplPLPMGFGGRE-SYI-AQ--LRGMLASA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 130 KFKTSDYPA-MVEEVREKCARLEHVVVLGGEsWQELMDAGRRGDPAqlahlragLSADDPINIQYTSGTTGFPKGATLSH 208
Cdd:PRK09192 128 QPAAIITPDeLLPWVNEATHGNPLLHVLSHA-WFKALPEADVALPR--------PTPDDIAYLQYSSGSTRFPRGVIITH 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 209 HNILNNgyFVGELCN---YTEEDKvCIP-VPFYHCFGMV---MGNLACTSHGACMVIPAPAFDPRATLEAVAAERCTSLY 281
Cdd:PRK09192 199 RALMAN--LRAISHDglkVRPGDR-CVSwLPFYHDMGLVgflLTPVATQLSVDYLPTRDFARRPLQWLDLISRNRGTISY 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 282 GvPTmFIAEL-----NHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVS-----ICYGMTET------SPVST 345
Cdd:PRK09192 276 S-PP-FGYELcarrvNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEAFAPAGFDdkafmPSYGLAEAtlavsfSPLGS 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 346 QTRAD----------------DSIERRVSTVGRVGPHL---EVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDkT 406
Cdd:PRK09192 354 GIVVEevdrdrleyqgkavapGAETRRVRTFVNCGKALpghEIEIRN-EAGMPLPERVVGHICVRGPSLMSGYFRDEE-S 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 407 AEAIDAARWMHTGDLAVMdGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVL--DAQVIGVPDEKyGEELMAWVR 484
Cdd:PRK09192 432 QDVLAADGWLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQEN-GEKIVLLVQ 509
|
490
....*....|....*
gi 522130465 485 MReGASPLTAEKVRE 499
Cdd:PRK09192 510 CR-ISDEERRGQLIH 523
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
41-539 |
2.42e-34 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 137.86 E-value: 2.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 41 LVDRAAGGRWTYRE--LAGEVT--------ALALG--LVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAY 108
Cdd:PRK06060 10 LAEQASEAGWYDRPafYAADVVthgqihdgAARLGevLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 109 RSHELEYVLDQAGIRLLVAS----DKFKTSDypaMVEEVrekcarlehvvvlggeswqELMDAGRRGDPAQLAHLraglS 184
Cdd:PRK06060 90 HRDDHALAARNTEPALVVTSdalrDRFQPSR---VAEAA-------------------ELMSEAARVAPGGYEPM----G 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 185 ADDPINIQYTSGTTGFPKGATLSHHNILNngyFVGELC----NYTEEDKVCIPVPFYHCFGMvmGN---LACTSHGACMV 257
Cdd:PRK06060 144 GDALAYATYTSGTTGPPKAAIHRHADPLT---FVDAMCrkalRLTPEDTGLCSARMYFAYGL--GNsvwFPLATGGSAVI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 258 IPAPAFDPRATLEAVAAERcTSLYGVPTMF--IAELNHPDfgefDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSICY 335
Cdd:PRK06060 219 NSAPVTPEAAAILSARFGP-SVLYGVPNFFarVIDSCSPD----SFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 336 GMTETSpvstQTRADDSI-ERRVSTVGRVGPHLEVKVVDPESGLTVPRGEpGELCTRGYSVMLGYWEQPDKTAEAIDaar 414
Cdd:PRK06060 294 GSTEVG----QTFVSNRVdEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVE-GDLWVRGPAIAKGYWNRPDSPVANEG--- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 415 WMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWV--RMREGASPL 492
Cdd:PRK06060 366 WLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLvaTSGATIDGS 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 522130465 493 TAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMREKSIT 539
Cdd:PRK06060 446 VMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQSPT 492
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
50-469 |
3.09e-34 |
|
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: 135.67 E-value: 3.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 50 WTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVASd 129
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVG- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 130 kfKTSDYPAMVEEVREK---CARLEHVVVLGGESWQELMdagRRGDPAQLAHLRAglsADDPINIQYTSGTTGFPKGATL 206
Cdd:cd05932 86 --KLDDWKAMAPGVPEGlisISLPPPSAANCQYQWDDLI---AQHPPLEERPTRF---PEQLATLIYTSGTTGQPKGVML 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 207 SHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMV---MGNLactsHGACMVIPAPAFDprATLEAVAAERCTSLYGV 283
Cdd:cd05932 158 TFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVfveGGSL----YGGVLVAFAESLD--TFVEDVQRARPTLFFSV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 284 PTMFI------------AELN-------------HPDFGEFDLSSLRTGIMAGSPCPVEVMKQViDRMGMaEVSICYGMT 338
Cdd:cd05932 232 PRLWTkfqqgvqdkipqQKLNlllkipvvnslvkRKVLKGLGLDQCRLAGCGSAPVPPALLEWY-RSLGL-NILEAYGMT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 339 ETSPVSTQTRADDsieRRVSTVGRVGPHLEVKVvdpesgltvprGEPGELCTRGYSVMLGYWEQPDKTAEAIDAARWMHT 418
Cdd:cd05932 310 ENFAYSHLNYPGR---DKIGTVGNAGPGVEVRI-----------SEDGEILVRSPALMMGYYKDPEATAEAFTADGFLRT 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 522130465 419 GDLAVMDGDGYVNITGRIKDMV-IRGGENLYPREIEEFLYTHPDVLDAQVIG 469
Cdd:cd05932 376 GDKGELDADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
36-532 |
3.99e-34 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 136.85 E-value: 3.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 36 GDRDALVDRAAGG---RWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHE 112
Cdd:PRK03584 98 DDRPAIIFRGEDGprrELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 113 leyVLD---QAGIRLLVASDKF----KTSDYPAMVEEVREKCARLEHVVVL-------------GGESWQELMDAGRrgd 172
Cdd:PRK03584 178 ---VLDrfgQIEPKVLIAVDGYryggKAFDRRAKVAELRAALPSLEHVVVVpylgpaaaaaalpGALLWEDFLAPAE--- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 173 PAQLAHLRagLSADDPINIQYTSGTTGFPKGATLSHHNILNNgyFVGEL---CNYTEEDKVCipvpFYHCFGMVMGN--- 246
Cdd:PRK03584 252 AAELEFEP--VPFDHPLWILYSSGTTGLPKCIVHGHGGILLE--HLKELglhCDLGPGDRFF----WYTTCGWMMWNwlv 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 247 --LACtshGACMVI--PAPAF-DPRATLEAVAAERCTsLYGVPTMFIAELN----HPDFgEFDLSSLRTGIMAGSPCPVE 317
Cdd:PRK03584 324 sgLLV---GATLVLydGSPFYpDPNVLWDLAAEEGVT-VFGTSAKYLDACEkaglVPGE-THDLSALRTIGSTGSPLPPE 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 318 ----VMKQVIDRMGMAEVS----ICYGMTETSPVSTQTRaddsierrvstvGRV-GPHL--EVKVVDpESGLTVpRGEPG 386
Cdd:PRK03584 399 gfdwVYEHVKADVWLASISggtdICSCFVGGNPLLPVYR------------GEIqCRGLgmAVEAWD-EDGRPV-VGEVG 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 387 EL-CTRGYSVM-LGYWEQPDKtaeaidaAR------------WMHtGDLAVMDGDGYVNITGRiKDMVI-RGG------E 445
Cdd:PRK03584 465 ELvCTKPFPSMpLGFWNDPDG-------SRyrdayfdtfpgvWRH-GDWIEITEHGGVVIYGR-SDATLnRGGvrigtaE 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 446 nLYpREIEEFlythPDVLDAQVIGVPDEKYGEELMAWVRMREGAsPLTAE-------KVREFCSgklahykiPRYV---- 514
Cdd:PRK03584 536 -IY-RQVEAL----PEVLDSLVIGQEWPDGDVRMPLFVVLAEGV-TLDDAlrarirtTIRTNLS--------PRHVpdki 600
|
570
....*....|....*...
gi 522130465 515 HVVDEFPMTVTGKvrKVE 532
Cdd:PRK03584 601 IAVPDIPRTLSGK--KVE 616
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
52-528 |
9.96e-34 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 134.75 E-value: 9.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 52 YRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILV----NINPAYRSHELEyVLDQAGIrLLVA 127
Cdd:PRK05857 44 YRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVmadgNLPIAAIERFCQ-ITDPAAA-LVAP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 128 SDKFKTSDYPamveevrEKCARLEHVVVLGGESWQELMDAGRRGDPAQlahlRAGLSADDPINIQYTSGTTGFPKGATLS 207
Cdd:PRK05857 122 GSKMASSAVP-------EALHSIPVIAVDIAAVTRESEHSLDAASLAG----NADQGSEDPLAMIFTSGTTGEPKAVLLA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 208 HH------NILNN------GYFVGElCNYTeedkvciPVPFYHcFGMVMGNLACTSHGACMVIPAPafDPRATLEAVAAE 275
Cdd:PRK05857 191 NRtffavpDILQKeglnwvTWVVGE-TTYS-------PLPATH-IGGLWWILTCLMHGGLCVTGGE--NTTSLLEILTTN 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 276 RCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCpVEVMKQVIDRMGMAEVSIcYGMTETSPVSTQTRADD-SIE 354
Cdd:PRK05857 260 AVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGSRA-IAADVRFIEATGVRTAQV-YGLSETGCTALCLPTDDgSIV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 355 R-RVSTVGRVGPHLEVKVVDPE-SGLTVPRGEP----GELCTRGYSVMLGYWEQPDKTAEAIdAARWMHTGDLAVMDGDG 428
Cdd:PRK05857 338 KiEAGAVGRPYPGVDVYLAATDgIGPTAPGAGPsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 429 YVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEEL-MAWVrmreGASPLTAEKVREFCSGKLAH 507
Cdd:PRK05857 417 FFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVgLAVV----ASAELDESAARALKHTIAAR 492
|
490 500
....*....|....*....|....*...
gi 522130465 508 YK-------IPRYVHVVDEFPMTVTGKV 528
Cdd:PRK05857 493 FRresepmaRPSTIVIVTDIPRTQSGKV 520
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
35-454 |
1.34e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 134.35 E-value: 1.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 35 FGDRDALVdraaggRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNIN-PAYRSHEL 113
Cdd:PRK07768 21 TGEPDAPV------RHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHqPTPRTDLA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 114 EY------VLDQAGIRLLVASDKFKtsdypAMVEEVREKCARlehvVVLGGESWqelmdAGRRGDPAQLahlraglSADD 187
Cdd:PRK07768 95 VWaedtlrVIGMIGAKAVVVGEPFL-----AAAPVLEEKGIR----VLTVADLL-----AADPIDPVET-------GEDD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 188 PINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIP-VPFYHCFGMVmGNLA---CTSHGACMVIPAPAF 263
Cdd:PRK07768 154 LALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSwLPLFHDMGMV-GFLTvpmYFGAELVKVTPMDFL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 264 -DP----------RATLEA-------VAAERCTSLygvptmfiaelnhPDFGEFDLSSLRTGIMAGSPCPVEVMKQVID- 324
Cdd:PRK07768 233 rDPllwaeliskyRGTMTAapnfayaLLARRLRRQ-------------AKPGAFDLSSLRFALNGAEPIDPADVEDLLDa 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 325 --RMGMAEVSI--CYGMTET------SPVSTQTRAD----DSIE-------------RRVSTVGRVGPHLEVKVVDpESG 377
Cdd:PRK07768 300 gaRFGLRPEAIlpAYGMAEAtlavsfSPCGAGLVVDevdaDLLAalrravpatkgntRRLATLGPPLPGLEVRVVD-EDG 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522130465 378 LTVPRGEPGELCTRGYSVMLGYWEqPDKTAEAIDAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEE 454
Cdd:PRK07768 379 QVLPPRGVGVIELRGESVTPGYLT-MDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIER 454
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
37-528 |
5.06e-33 |
|
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: 131.83 E-value: 5.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 37 DRDALVDRAAggRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYV 116
Cdd:cd17656 3 DAVAVVFENQ--KLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 117 LDQAGIRLLVASdkfktSDYPAMVEEvrekcaRLEHVVVLGGESWQELMdagrrgdpaqlAHLRAGLSADDPINIQYTSG 196
Cdd:cd17656 81 MLDSGVRVVLTQ-----RHLKSKLSF------NKSTILLEDPSISQEDT-----------SNIDYINNSDDLLYIIYTSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 197 TTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVC--IPVPFYHCFGMVMGNLacTSHGACMVIPAPA-FDPRATLEAVA 273
Cdd:cd17656 139 TTGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLqfATCSFDVCYQEIFSTL--LSGGTLYIIREETkRDVEQLFDLVK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 274 AERCTSLYgVPTMF---IAELNH--PDFGEfdlsSLRTGIMAGSPCpveVMKQVIDRMGMAE-VSIC--YGMTETSPVST 345
Cdd:cd17656 217 RHNIEVVF-LPVAFlkfIFSEREfiNRFPT----CVKHIITAGEQL---VITNEFKEMLHEHnVHLHnhYGPSETHVVTT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 346 QTRADDSIERRVSTVGRVGPHLEVKVVDPESGLtVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDA------ARWMHTG 419
Cdd:cd17656 289 YTINPEAEIPELPPIGKPISNTWIYILDQEQQL-QPQGIVGELYISGASVARGYLNRQELTAEKFFPdpfdpnERMYRTG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 420 DLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREgasPLTAEKVRE 499
Cdd:cd17656 368 DLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQ---ELNISQLRE 444
|
490 500
....*....|....*....|....*....
gi 522130465 500 FCSGKLAHYKIPRYVHVVDEFPMTVTGKV 528
Cdd:cd17656 445 YLAKQLPEYMIPSFFVPLDQLPLTPNGKV 473
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
185-536 |
3.99e-32 |
|
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: 129.53 E-value: 3.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 185 ADDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGAC-MVIPAPAF 263
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNqYLMPTRLF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 264 DPRATL------EAVAAERCTSLYGVpTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRM---GMAEVSI- 333
Cdd:cd05908 185 IRRPILwlkkasEHKATIVSSPNFGY-KYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMskyGLKRNAIl 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 334 -CYGMTETSPVSTQTRAD----------------------DSIERRVSTVGRVGPHL---EVKVVDpESGLTVPRGEPGE 387
Cdd:cd05908 264 pVYGLAEASVGASLPKAQspfktitlgrrhvthgepepevDKKDSECLTFVEVGKPIdetDIRICD-EDNKILPDGYIGH 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 388 LCTRGYSVMLGYWEQPDKTAEAIDAARWMHTGDLAVMDgDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQV 467
Cdd:cd05908 343 IQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFIR-NGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRV 421
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522130465 468 --IGVPDEKY-GEELMAWVRMREGASPLT--AEKVREFCSgKLAHYKIPRyVHVVDEFPMTVTGKVRKVEMREK 536
Cdd:cd05908 422 vaCGVNNSNTrNEEIFCFIEHRKSEDDFYplGKKIKKHLN-KRGGWQINE-VLPIRRIPKTTSGKVKRYELAQR 493
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
28-530 |
4.75e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 132.39 E-value: 4.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 28 FDRTVAAFGDRDALVdrAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPA 107
Cdd:PRK12316 3063 FEEQVERTPDAVALA--FGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPE 3140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 108 YRSHELEYVLDQAGIRLLVASdkfktsdypamveevrekcarlEHVVVLGGESWQELMdAGRRGDPAQLAHLRAGLSADD 187
Cdd:PRK12316 3141 YPEERLAYMLEDSGAQLLLSQ----------------------SHLRLPLAQGVQVLD-LDRGDENYAEANPAIRTMPEN 3197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 188 PINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFyHCFGMVMGNLACTSHGACMVIPAP--AFDP 265
Cdd:PRK12316 3198 LAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTF-SFDVFVEELFWPLMSGARVVLAGPedWRDP 3276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 266 RATLEAVAAERCTSLYGVPTMFIAELNHPDfgEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVsicYGMTETSPVST 345
Cdd:PRK12316 3277 ALLVELINSEGVDVLHAYPSMLQAFLEEED--AHRCTSLKRIVCGGEALPADLQQQVFAGLPLYNL---YGPTEATITVT 3351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 346 QTRADDSIERRVStVGRVGPHLEVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDA------ARWMHTG 419
Cdd:PRK12316 3352 HWQCVEEGKDAVP-IGRPIANRACYILD-GSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPdpfvpgERLYRTG 3429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 420 DLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPdekyGEELMAWVRMREGASPLTaEKVRE 499
Cdd:PRK12316 3430 DLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVD----GRQLVAYVVPEDEAGDLR-EALKA 3504
|
490 500 510
....*....|....*....|....*....|..
gi 522130465 500 FCSGKLAHYKIPRYVHVVDEFPMTVTGKV-RK 530
Cdd:PRK12316 3505 HLKASLPEYMVPAHLLFLERMPLTPNGKLdRK 3536
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
17-530 |
1.96e-31 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 129.78 E-value: 1.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 17 VPLLGDTIGDNFDRTVAAFGDRDALVDraAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAK 96
Cdd:PRK10252 453 VEIPETTLSALVAQQAAKTPDAPALAD--ARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVE 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 97 IGAILVNINPAYRSHELEYVLDQAGIRLLVASDkfktsdypamveevrEKCARLEHVVVLGGESWQELmDAGRRGDPAQL 176
Cdd:PRK10252 531 AGAAWLPLDTGYPDDRLKMMLEDARPSLLITTA---------------DQLPRFADVPDLTSLCYNAP-LAPQGAAPLQL 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 177 AHlraglsADDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVP---------FYHCFgMVmgnl 247
Cdd:PRK10252 595 SQ------PHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPcsfdvsvweFFWPF-IA---- 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 248 actshGACMVIPAPAF--DPRATLEAVAAERCTSLYGVPTM---FIAELNhPDFGEFDLSSLRTGIMAGSPCPVEVMKQV 322
Cdd:PRK10252 664 -----GAKLVMAEPEAhrDPLAMQQFFAEYGVTTTHFVPSMlaaFVASLT-PEGARQSCASLRQVFCSGEALPADLCREW 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 323 IDRMGmAEVSICYGMTETS------PVStqtrADDSIERRVSTV--GRVGPHLEVKVVDpESGLTVPRGEPGELCTRGYS 394
Cdd:PRK10252 738 QQLTG-APLHNLYGPTEAAvdvswyPAF----GEELAAVRGSSVpiGYPVWNTGLRILD-ARMRPVPPGVAGDLYLTGIQ 811
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 395 VMLGYWEQPDKTAE------AIDAARWMHTGDLAVMDGDGYVNITGRIKDMV-IRgGENLYPREIEEFLYTHPDV----L 463
Cdd:PRK10252 812 LAQGYLGRPDLTASrfiadpFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLkIR-GQRIELGEIDRAMQALPDVeqavT 890
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 464 DAQVIGVPDEKYGEE--LMAWVRMREGAsPLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKV-RK 530
Cdd:PRK10252 891 HACVINQAAATGGDArqLVGYLVSQSGL-PLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLdRK 959
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
36-538 |
3.23e-31 |
|
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: 128.16 E-value: 3.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 36 GDRDALVDRAAGG---RWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHE 112
Cdd:cd05943 82 ADDPAAIYAAEDGertEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 113 leyVLD---QAGIRLLVASD----KFKTSDYPAMVEEVREKCARLEHVVVLGGESWQELMDAG------------RRGDP 173
Cdd:cd05943 162 ---VLDrfgQIEPKVLFAVDaytyNGKRHDVREKVAELVKGLPSLLAVVVVPYTVAAGQPDLSkiakaltledflATGAA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 174 AQLAHLRagLSADDPINIQYTSGTTGFPK------GATLSHH---NILNngyfvgelCNYTEEDKVCipvpFYHCFGMVM 244
Cdd:cd05943 239 GELEFEP--LPFDHPLYILYSSGTTGLPKcivhgaGGTLLQHlkeHILH--------CDLRPGDRLF----YYTTCGWMM 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 245 GN-----LACtshGACMVI--PAPAF-DPRATLEAVAAERCTsLYGVPTMFIAELNHPDFG---EFDLSSLRTGIMAGSP 313
Cdd:cd05943 305 WNwlvsgLAV---GATIVLydGSPFYpDTNALWDLADEEGIT-VFGTSAKYLDALEKAGLKpaeTHDLSSLRTILSTGSP 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 314 CPVE----VMKQVIDRMGMAEVS----ICYGMTETSPVSTQTRADDSierrvstvgrvGPHL--EVKVVDPEsGLTVpRG 383
Cdd:cd05943 381 LKPEsfdyVYDHIKPDVLLASISggtdIISCFVGGNPLLPVYRGEIQ-----------CRGLgmAVEAFDEE-GKPV-WG 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 384 EPGEL-CTRGYSVM-LGYWEQPdktaeaiDAAR------------WMHtGDLAVMDGDGYVNITGRiKDMVI-RGGENLY 448
Cdd:cd05943 448 EKGELvCTKPFPSMpVGFWNDP-------DGSRyraayfakypgvWAH-GDWIEITPRGGVVILGR-SDGTLnPGGVRIG 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 449 PREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASpLTAE-------KVREFCSgklahykiPRYV----HVV 517
Cdd:cd05943 519 TAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVE-LDDElrkrirsTIRSALS--------PRHVpakiIAV 589
|
570 580
....*....|....*....|.
gi 522130465 518 DEFPMTVTGKvrKVEMREKSI 538
Cdd:cd05943 590 PDIPRTLSGK--KVEVAVKKI 608
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
51-535 |
7.00e-31 |
|
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: 124.99 E-value: 7.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 51 TYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAE-W-TFLqyATAKIGAILVninPAyrsheleyvldqagIRLLVAS 128
Cdd:cd05974 2 SFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVElWeAML--AAMKLGAVVI---PA--------------TTLLTPD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 129 DkfktsdypamveeVREKCARLEHVVVLGGESwqelmdagrrgdpaqlahlragLSADDPINIQYTSGTTGFPKGATLSH 208
Cdd:cd05974 63 D-------------LRDRVDRGGAVYAAVDEN----------------------THADDPMLLYFTSGTTSKPKLVEHTH 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 209 HNI----LNNGYFVGeLCNYTEEDKVCIPVPFYH---CFgmvmgnLACTSHGACMVI-PAPAFDPRATLEAVAAERCTSL 280
Cdd:cd05974 108 RSYpvghLSTMYWIG-LKPGDVHWNISSPGWAKHawsCF------FAPWNAGATVFLfNYARFDAKRVLAALVRYGVTTL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 281 YGVPT---MFIAElnhpDFGEFDLSsLRTGIMAGSPCPVEVMKQVIDRMGMAeVSICYGMTETSPVSTQTRADDSierRV 357
Cdd:cd05974 181 CAPPTvwrMLIQQ----DLASFDVK-LREVVGAGEPLNPEVIEQVRRAWGLT-IRDGYGQTETTALVGNSPGQPV---KA 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 358 STVGRVGPHLEVKVVDPESGltvPRGEpGELC-----TRGYSVMLGYWEQPDKTAEAIDAARWmHTGDLAVMDGDGYVNI 432
Cdd:cd05974 252 GSMGRPLPGYRVALLDPDGA---PATE-GEVAldlgdTRPVGLMKGYAGDPDKTAHAMRGGYY-RTGDIAMRDEDGYLTY 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 433 TGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGA--SPLTAEKVREFCSGKLAHYKI 510
Cdd:cd05974 327 VGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYepSPETALEIFRFSRERLAPYKR 406
|
490 500
....*....|....*....|....*
gi 522130465 511 PRYVHVVdEFPMTVTGKVRKVEMRE 535
Cdd:cd05974 407 IRRLEFA-ELPKTISGKIRRVELRR 430
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
32-528 |
3.32e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 126.61 E-value: 3.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 32 VAAFGDRDALVdrAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSH 111
Cdd:PRK12316 2013 AARAPEAIAVV--FGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAE 2090
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 112 ELEYVLDQAGIRLLVASdkfktsdypamvEEVREKCARLEHVVVLGGESWQELMDAGrRGDPAQLAHlraglsADDPINI 191
Cdd:PRK12316 2091 RLAYMLEDSGAALLLTQ------------RHLLERLPLPAGVARLPLDRDAEWADYP-DTAPAVQLA------GENLAYV 2151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 192 QYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFyhCF-GMVMGNLACTSHGACMVI-PAPAFDPRATL 269
Cdd:PRK12316 2152 IYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSF--SFdGAHEQWFHPLLNGARVLIrDDELWDPEQLY 2229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 270 EAVAAERCTSLYGVPTMFIAELNHPDFgEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSICYGMTET--SPVSTQT 347
Cdd:PRK12316 2230 DEMERHGVTILDFPPVYLQQLAEHAER-DGRPPAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAvvTPLLWKC 2308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 348 RADDSIERRVSTVGRVGPHLEVKVVDPESGLtVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDA-------ARWMHTGD 420
Cdd:PRK12316 2309 RPQDPCGAAYVPIGRALGNRRAYILDADLNL-LAPGMAGELYLGGEGLARGYLNRPGLTAERFVPdpfsasgERLYRTGD 2387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 421 LAVMDGDGYVNITGRIKDMV-IRGGEnLYPREIEEFLYTHPDVLDAQVIGVpDEKYGEELMAWVRMREGASPLTAEkVRE 499
Cdd:PRK12316 2388 LARYRADGVVEYLGRIDHQVkIRGFR-IELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAAEDLLAE-LRA 2464
|
490 500
....*....|....*....|....*....
gi 522130465 500 FCSGKLAHYKIPRYVHVVDEFPMTVTGKV 528
Cdd:PRK12316 2465 WLAARLPAYMVPAHWVVLERLPLNPNGKL 2493
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
20-463 |
1.34e-29 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 124.90 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 20 LGDTIGDNFDRTVAAFGDRDAL---VDRAAGGR-WTYRELAGEVTALALGLVARGiGKGDRVGIWSPNRAEWTFLQYATA 95
Cdd:PRK05691 7 LPLTLVQALQRRAAQTPDRLALrflADDPGEGVvLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 96 KIGAILVninPAY-----RSHELEYVL---DQAGIRLLVAsdkfktsdypamVEEVREKCARLEHvvvLGGESWQELMdA 167
Cdd:PRK05691 86 YAGVIAV---PAYppesaRRHHQERLLsiiADAEPRLLLT------------VADLRDSLLQMEE---LAAANAPELL-C 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 168 GRRGDPAQLAHLRA-GLSADDPINIQYTSGTTGFPKGATLSHHNILNNGYFV--GELCNYTEEDKVCIPVPFYHCFGMVM 244
Cdd:PRK05691 147 VDTLDPALAEAWQEpALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIrhGFGIDLNPDDVIVSWLPLYHDMGLIG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 245 GNLACTSHGACMVIPAPAF---DPRATLEAVAAERCTsLYGVPTmFIAELNHPDFGE-----FDLSSLRTGIMAGSPCPV 316
Cdd:PRK05691 227 GLLQPIFSGVPCVLMSPAYfleRPLRWLEAISEYGGT-ISGGPD-FAYRLCSERVSEsalerLDLSRWRVAYSGSEPIRQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 317 EVMKQVIDRM---GMAEVSI--CYGMTE-TSPVS------------------TQTRADDSIERRVSTVGRVGPHLEVKVV 372
Cdd:PRK05691 305 DSLERFAEKFaacGFDPDSFfaSYGLAEaTLFVSggrrgqgipaleldaealARNRAEPGTGSVLMSCGRSQPGHAVLIV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 373 DPESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAI---DAARWMHTGDLAVMDgDGYVNITGRIKDMVIRGGENLYP 449
Cdd:PRK05691 385 DPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFvehDGRTWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYP 463
|
490
....*....|....
gi 522130465 450 REIEEFLYTHPDVL 463
Cdd:PRK05691 464 QDIEKTVEREVEVV 477
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
29-528 |
1.51e-29 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 123.13 E-value: 1.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 29 DRTVAAFGDRDALV------DRAAggRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILV 102
Cdd:PRK10524 60 DRHLAKRPEQLALIavstetDEER--TYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHS 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 103 NINPAYRSHELEYVLDQAGIRLLVASDK----FKTSDYPAMVEEVREKCA-RLEHVVVLGGESWQELMDAGRRGDPAQL- 176
Cdd:PRK10524 138 VVFGGFASHSLAARIDDAKPVLIVSADAgsrgGKVVPYKPLLDEAIALAQhKPRHVLLVDRGLAPMARVAGRDVDYATLr 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 177 -AHLRAG-----LSADDPINIQYTSGTTGFPKGATLShhnilNNGYfvgelcnyteedKVCIPVPFYHCFGMVMGN-LAC 249
Cdd:PRK10524 218 aQHLGARvpvewLESNEPSYILYTSGTTGKPKGVQRD-----TGGY------------AVALATSMDTIFGGKAGEtFFC 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 250 TSH-----GACMVIPAPAFDPRATL---------EAVAAERCTSLYGVPTMFIA-------ELNHPDF-GEFDLSSLRTG 307
Cdd:PRK10524 281 ASDigwvvGHSYIVYAPLLAGMATImyeglptrpDAGIWWRIVEKYKVNRMFSAptairvlKKQDPALlRKHDLSSLRAL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 308 IMAGSPC--PV------EVMKQVIDRmgmaevsicYGMTETS-PVSTQTRADDSIERRVSTVGRVGPHLEVKVVDPESGL 378
Cdd:PRK10524 361 FLAGEPLdePTaswiseALGVPVIDN---------YWQTETGwPILAIARGVEDRPTRLGSPGVPMYGYNVKLLNEVTGE 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 379 TVPRGEPGELCTRG------YSVMLG--------YWEQPDKTAEAidaarwmhTGDLAVMDGDGYVNITGRIKDMVIRGG 444
Cdd:PRK10524 432 PCGPNEKGVLVIEGplppgcMQTVWGdddrfvktYWSLFGRQVYS--------TFDWGIRDADGYYFILGRTDDVINVAG 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 445 ENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASPLTAEK-------VREFCSGKLAHYKIPRYVHVV 517
Cdd:PRK10524 504 HRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADREArlalekeIMALVDSQLGAVARPARVWFV 583
|
570
....*....|.
gi 522130465 518 DEFPMTVTGKV 528
Cdd:PRK10524 584 SALPKTRSGKL 594
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
51-519 |
2.85e-29 |
|
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: 121.17 E-value: 2.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 51 TYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNinpAYRS---HELEYVLDQAGIRLLVA 127
Cdd:cd17639 7 SYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVT---VYATlgeDALIHSLNETECSAIFT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 128 SDKfktsdypamveevrekcarlehvvvlggeswqelmdagrrgdpaqlahlraglsADDPINIQYTSGTTGFPKGATLS 207
Cdd:cd17639 84 DGK------------------------------------------------------PDDLACIMYTSGSTGNPKGVMLT 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 208 HHNILNN----GYFVGELCNytEEDKVCIPVPFYHCFGMVMGNLaCTSHGACMvipapAF-DPRaTLEAVAAERC----- 277
Cdd:cd17639 110 HGNLVAGiaglGDRVPELLG--PDDRYLAYLPLAHIFELAAENV-CLYRGGTI-----GYgSPR-TLTDKSKRGCkgdlt 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 278 ----TSLYGVPTMF-------IAELNHPDF---GEFD------LSSLRTGImaGSP-CPVEVMKQVIDRMG--------- 327
Cdd:cd17639 181 efkpTLMVGVPAIWdtirkgvLAKLNPMGGlkrTLFWtayqskLKALKEGP--GTPlLDELVFKKVRAALGgrlrymlsg 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 328 ---------------MAEVSICYGMTETSPVSTQTRADDSierRVSTVGRVGPHLEVKVVD-PESGLTVPRGEP-GELCT 390
Cdd:cd17639 259 gaplsadtqeflnivLCPVIQGYGLTETCAGGTVQDPGDL---ETGRVGPPLPCCEIKLVDwEEGGYSTDKPPPrGEILI 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 391 RGYSVMLGYWEQPDKTAEAIDAARWMHTGDLAVMDGDGYVNITGRIKDMV-IRGGENLYPREIEEFLYTHPDVLDAQVIG 469
Cdd:cd17639 336 RGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVkLQNGEYIALEKLESIYRSNPLVNNICVYA 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522130465 470 VPDEKYgeeLMAWVRMREG-ASPLTAEKVREFC------------------------SGKLAHYKIPRYVHVVDE 519
Cdd:cd17639 416 DPDKSY---PVAIVVPNEKhLTKLAEKHGVINSeweelcedkklqkavlkslaetarAAGLEKFEIPQGVVLLDE 487
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
51-471 |
7.49e-29 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 120.39 E-value: 7.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 51 TYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQA------GI-R 123
Cdd:PRK09274 43 SFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAqpdafiGIpK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 124 LLVASDKFktsdypamveevREKCARLEHVVVLGGESWQE---LMDAGRRGDPAQLAhlRAGLSADDPINIQYTSGTTGF 200
Cdd:PRK09274 123 AHLARRLF------------GWGKPSVRRLVTVGGRLLWGgttLATLLRDGAAAPFP--MADLAPDDMAAILFTSGSTGT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 201 PKGATLSHHNilnngyFVGEL----CNYTEE----DKVCIPVpfyhcfgMVMGNLACtshGACMVIPA-----PAF-DPR 266
Cdd:PRK09274 189 PKGVVYTHGM------FEAQIealrEDYGIEpgeiDLPTFPL-------FALFGPAL---GMTSVIPDmdptrPATvDPA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 267 ATLEAVAAERCTSLYGVP------TMFIAELNHPdfgefdLSSLRTGIMAGSPCPVEVMKQVIDRMG-MAEVSICYGMTE 339
Cdd:PRK09274 253 KLFAAIERYGVTNLFGSPallerlGRYGEANGIK------LPSLRRVISAGAPVPIAVIERFRAMLPpDAEILTPYGATE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 340 TSPVSTQTRADDSIERRVST-------VGRVGPHLEVKVVDPESG--------LTVPRGEPGELCTRGYSVMLGYWEQPD 404
Cdd:PRK09274 327 ALPISSIESREILFATRAATdngagicVGRPVDGVEVRIIAISDApipewddaLRLATGEIGEIVVAGPMVTRSYYNRPE 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522130465 405 KTAEA--IDAAR--WMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVP 471
Cdd:PRK09274 407 ATRLAkiPDGQGdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVG 477
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
39-528 |
5.34e-28 |
|
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: 116.77 E-value: 5.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 39 DALVDRAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLD 118
Cdd:cd17644 15 DAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYILE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 119 QAGIRLLVASdkfktsdypamveevrekcarlehvvvlggeswqelmdagrrgdPAQLAHlraglsaddpinIQYTSGTT 198
Cdd:cd17644 95 DAQISVLLTQ--------------------------------------------PENLAY------------VIYTSGST 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 199 GFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFyhCFGMVMGNLACT-SHGACMVI-PAPAFDPRATLEAVAAER 276
Cdd:cd17644 119 GKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASI--AFDVAAEEIYVTlLSGATLVLrPEEMRSSLEDFVQYIQQW 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 277 CTSLYGVPTMFIAELnhPDFGEFDL----SSLRTGIMAGS---PCPVEVMKQVI-DRMGMAEVsicYGMTETSPVSTQTR 348
Cdd:cd17644 197 QLTVLSLPPAYWHLL--VLELLLSTidlpSSLRLVIVGGEavqPELVRQWQKNVgNFIQLINV---YGPTEATIAATVCR 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 349 ADDSIERRVS--TVGRVGPHLEVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAI--------DAARWMHT 418
Cdd:cd17644 272 LTQLTERNITsvPIGRPIANTQVYILD-ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFishpfnssESERLYKT 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 419 GDLAVMDGDGYVNITGRIKDMV-IRG-----GEnlypreIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASPL 492
Cdd:cd17644 351 GDLARYLPDGNIEYLGRIDNQVkIRGfrielGE------IEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPS 424
|
490 500 510
....*....|....*....|....*....|....*.
gi 522130465 493 TAEkVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKV 528
Cdd:cd17644 425 TVE-LRQFLKAKLPDYMIPSAFVVLEELPLTPNGKI 459
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
37-528 |
1.17e-27 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 118.73 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 37 DRDALVdrAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYV 116
Cdd:PRK05691 1146 ERIALV--WDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYM 1223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 117 LDQAGIRLLVASdkfktSDYPAMVEEVREKCA-RLEHvvvLGGESWqelmdagrrgdPAQLAHLRagLSADDPINIQYTS 195
Cdd:PRK05691 1224 LADSGVELLLTQ-----SHLLERLPQAEGVSAiALDS---LHLDSW-----------PSQAPGLH--LHGDNLAYVIYTS 1282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 196 GTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVC--IPVPF----YHCFGMVMGnlactshGACMVIPAPA--FDPRA 267
Cdd:PRK05691 1283 GSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMqkAPISFdvsvWECFWPLIT-------GCRLVLAGPGehRDPQR 1355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 268 TLEAVAAERCTSLYGVPTMFIAELNHPDFGEfdLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSICYGMTETSPVST-- 345
Cdd:PRK05691 1356 IAELVQQYGVTTLHFVPPLLQLFIDEPLAAA--CTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVThw 1433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 346 QTRADDSiERrvSTVGRVGPHLEVKVVDPESGLtVPRGEPGELCTRGYSVMLGYWEQPDKTAE-------AIDAARWMHT 418
Cdd:PRK05691 1434 QCQAEDG-ER--SPIGRPLGNVLCRVLDAELNL-LPPGVAGELCIGGAGLARGYLGRPALTAErfvpdplGEDGARLYRT 1509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 419 GDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIgVPDEKYGEELMAWVRMrEGASPLTAEKVR 498
Cdd:PRK05691 1510 GDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-VREGAAGAQLVGYYTG-EAGQEAEAERLK 1587
|
490 500 510
....*....|....*....|....*....|
gi 522130465 499 EFCSGKLAHYKIPRYVHVVDEFPMTVTGKV 528
Cdd:PRK05691 1588 AALAAELPEYMVPAQLIRLDQMPLGPSGKL 1617
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
230-544 |
1.52e-27 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 115.48 E-value: 1.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 230 VCIpVPFYHCFGMVMGNLACTSHGACMVIPAPAFDPRATLEAVAAERCTSLygVPTMFIAEL-NHPDFgefdLSSLRTGI 308
Cdd:PRK07445 164 FCV-LPLYHVSGLMQFMRSFLTGGKLVILPYKRLKSGQELPPNPSDFFLSL--VPTQLQRLLqLRPQW----LAQFRTIL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 309 MAGSPCPVEVMKQVidRMGMAEVSICYGMTET-SPVSTQTRAD-----DSierrvstVGRVGPHLEVKVVDPESGLTVPR 382
Cdd:PRK07445 237 LGGAPAWPSLLEQA--RQLQLRLAPTYGMTETaSQIATLKPDDflagnNS-------SGQVLPHAQITIPANQTGNITIQ 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 383 GEpgelctrgySVMLGYWEQpdktaeAIDAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDV 462
Cdd:PRK07445 308 AQ---------SLALGYYPQ------ILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLV 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 463 LDAQVIGVPDEKYGEELMAWVRMRegASPLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMREKSITLLG 542
Cdd:PRK07445 373 QDVCVLGLPDPHWGEVVTAIYVPK--DPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQRLG 450
|
..
gi 522130465 543 LE 544
Cdd:PRK07445 451 LP 452
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
29-534 |
6.74e-27 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 115.24 E-value: 6.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 29 DRTVAAFGDRDALV----DRAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNI 104
Cdd:PRK00174 74 DRHLKTRGDKVAIIwegdDPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 105 NPAYRSHEL-EYVLDqAGIRLLVASDKF----KTSDYPAMVEEVREKCARLEHVVVL---GGE---------SWQELMDa 167
Cdd:PRK00174 154 FGGFSAEALaDRIID-AGAKLVITADEGvrggKPIPLKANVDEALANCPSVEKVIVVrrtGGDvdwvegrdlWWHELVA- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 168 grrgdPAQLAHLRAGLSADDPINIQYTSGTTGFPKG-----------ATLSHHNILNngyfvgelcnYTEEDkvcipvpF 236
Cdd:PRK00174 232 -----GASDECEPEPMDAEDPLFILYTSGSTGKPKGvlhttggylvyAAMTMKYVFD----------YKDGD-------V 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 237 YHC---FG-------MVMGNLACtshGACMVI--PAPAF-DPRATLEAVAAERCTSLYGVPT---MFIAELNHPdFGEFD 300
Cdd:PRK00174 290 YWCtadVGwvtghsyIVYGPLAN---GATTLMfeGVPNYpDPGRFWEVIDKHKVTIFYTAPTairALMKEGDEH-PKKYD 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 301 LSSLRtgIMA--GSP-----------------CPVevmkqvIDrmgmaevsiCYGMTET-----SPV--STQTRAddsie 354
Cdd:PRK00174 366 LSSLR--LLGsvGEPinpeawewyykvvggerCPI------VD---------TWWQTETggimiTPLpgATPLKP----- 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 355 rrvSTVGRVGPHLEVKVVDpESGLTVPRGEPGELC-TRGY-SVMLGYWEQPD---KTaeaidaaRWMH------TGDLAV 423
Cdd:PRK00174 424 ---GSATRPLPGIQPAVVD-EEGNPLEGGEGGNLViKDPWpGMMRTIYGDHErfvKT-------YFSTfkgmyfTGDGAR 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 424 MDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASP---LTAEkVREF 500
Cdd:PRK00174 493 RDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPsdeLRKE-LRNW 571
|
570 580 590
....*....|....*....|....*....|....*..
gi 522130465 501 CS---GKLAhykIPRYVHVVDEFPMTVTGKVrkveMR 534
Cdd:PRK00174 572 VRkeiGPIA---KPDVIQFAPGLPKTRSGKI----MR 601
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
172-528 |
8.21e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 111.68 E-value: 8.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 172 DPAQLAHLRAGLSADDPIN-----IQYTSGTTGFPKGATLSHHNILNNG----YFVGElcnyteEDKVCIPVPFYHCFGM 242
Cdd:PRK07824 16 DERRAALLRDALRVGEPIDddvalVVATSGTTGTPKGAMLTAAALTASAdathDRLGG------PGQWLLALPAHHIAGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 243 --VMGNLACTSHGACMVIPApAFDPRATLEAVAA----ERCTSLygVPTMFIAELNHPDFGEfDLSSLRTGIMAGSPCPv 316
Cdd:PRK07824 90 qvLVRSVIAGSEPVELDVSA-GFDPTALPRAVAElgggRRYTSL--VPMQLAKALDDPAATA-ALAELDAVLVGGGPAP- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 317 evmKQVIDRMGMAEVSIC--YGMTETSP-VSTQTRADDSIERRVSTvGRVgpHLevkvvdpeSGLTVPRGEPGElctrgy 393
Cdd:PRK07824 165 ---APVLDAAAAAGINVVrtYGMSETSGgCVYDGVPLDGVRVRVED-GRI--AL--------GGPTLAKGYRNP------ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 394 svmlgywEQPDKTAEAidaaRWMHTGDLAVMDgDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDE 473
Cdd:PRK07824 225 -------VDPDPFAEP----GWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDD 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 522130465 474 KYGEELMAWVRMREGASPlTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKV 528
Cdd:PRK07824 293 RLGQRVVAAVVGDGGPAP-TLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKV 346
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
37-528 |
9.81e-27 |
|
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: 112.88 E-value: 9.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 37 DRDALVDRAAggRWTYRELAGEVTALALGLVARGIGKGD-RVGIWSpNRAEWTFLQ-YATAKIGAILVNINPAYRSHELE 114
Cdd:cd17648 2 DRVAVVYGDK--RLTYRELNERANRLAHYLLSVAEIRPDdLVGLVL-DKSELMIIAiLAVWKAGAAYVPIDPSYPDERIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 115 YVLDQAGIRLLVAsdkfktsdypamveevrekcarlehvvvlggeswqelmdagrrgDPAQLAHlraglsaddpinIQYT 194
Cdd:cd17648 79 FILEDTGARVVIT--------------------------------------------NSTDLAY------------AIYT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 195 SGTTGFPKGATLSHHNILNngyFVGELCNY----TEEDKVCIPVPFY----HCFGMVMGNLActshGACMVIPAP--AFD 264
Cdd:cd17648 103 SGTTGKPKGVLVEHGSVVN---LRTSLSERyfgrDNGDEAVLFFSNYvfdfFVEQMTLALLN----GQKLVVPPDemRFD 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 265 PRATLEAVAAERCTSLYGVPTMfiaeLNHPDFGEfdLSSLRTGIMAGSPCPVEVMKQVIDRMGmAEVSICYGMTETS--- 341
Cdd:cd17648 176 PDRFYAYINREKVTYLSGTPSV----LQQYDLAR--LPHLKRVDAAGEEFTAPVFEKLRSRFA-GLIINAYGPTETTvtn 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 342 ---PVSTQTRADDSIERRVstvgrvgPHLEVKVVDPESGLtVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDA------ 412
Cdd:cd17648 249 hkrFFPGDQRFDKSLGRPV-------RNTKCYVLNDAMKR-VPVGAVGELYLGGDGVARGYLNRPELTAERFLPnpfqte 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 413 --------ARWMHTGDLAVMDGDGYVNITGRiKDMVIR-GGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEE----- 478
Cdd:cd17648 321 qerargrnARLYKTGDLVRWLPSGELEYLGR-NDFQVKiRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSriqky 399
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 522130465 479 LMAWVRMREGAspLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKV 528
Cdd:cd17648 400 LVGYYLPEPGH--VPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
49-470 |
1.54e-26 |
|
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: 112.55 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 49 RWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAgirllvAS 128
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEA------EP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 129 DKFKtsdypamveevrekcarlehvvvlggeswqelmdagrrGDPaqlahlraglSADDPINIQYTSGTTGFPKGATLSH 208
Cdd:cd05910 76 DAFI--------------------------------------GIP----------KADEPAAILFTSGSTGTPKGVVYRH 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 209 HNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGnlaCTShgacmVIP-----APA-FDPRATLEAVAAERCTSLYG 282
Cdd:cd05910 108 GTFAAQIDALRQLYGIRPGEVDLATFPLFALFGPALG---LTS-----VIPdmdptRPArADPQKLVGAIRQYGVSIVFG 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 283 VPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQvIDRM--GMAEVSICYGMTETSPVSTQTRADDSIERRVST- 359
Cdd:cd05910 180 SPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAAR-LRKMlsDEAEILTPYGATEALPVSSIGSRELLATTTAATs 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 360 ------VGRVGPHLEVKVVDPESG--------LTVPRGEPGELCTRGYSVMLGYWEQPDKTAEA-IDAAR---WMHTGDL 421
Cdd:cd05910 259 ggagtcVGRPIPGVRVRIIEIDDEpiaewddtLELPRGEIGEITVTGPTVTPTYVNRPVATALAkIDDNSegfWHRMGDL 338
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 522130465 422 AVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGV 470
Cdd:cd05910 339 GYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV 387
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
182-535 |
7.42e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 109.74 E-value: 7.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 182 GLSADDPINIQYTSGTTGFPKGATLSHHNILNngyfvgELCNYTE---EDKVCIPV---PFYHCFGMVMGNLACTSHGAC 255
Cdd:PRK08308 97 NYLAEEPSLLQYSSGTTGEPKLIRRSWTEIDR------EIEAYNEalnCEQDETPIvacPVTHSYGLICGVLAALTRGSK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 256 MVIPAPAfDPRATLEAVAAERCTSLYGVPTMF--IAELNHpdfGEFDLSSLRTgimAGSPCPVEVM-------KQVIDRM 326
Cdd:PRK08308 171 PVIITNK-NPKFALNILRNTPQHILYAVPLMLhiLGRLLP---GTFQFHAVMT---SGTPLPEAWFyklrertTYMMQQY 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 327 GMAE---VSICYGMTEtspvstqtrADDsierrvstVGRVGPHLEVkvvdpESGLTvpRGEPGELCTRgysvmlgyweqp 403
Cdd:PRK08308 244 GCSEagcVSICPDMKS---------HLD--------LGNPLPHVSV-----SAGSD--ENAPEEIVVK------------ 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 404 dktaeaiDAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWV 483
Cdd:PRK08308 288 -------MGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKV 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 522130465 484 RMREGASPltaEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKV--RKVEMRE 535
Cdd:PRK08308 361 ISHEEIDP---VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVsrKLLELGE 411
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
47-534 |
2.57e-25 |
|
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: 109.05 E-value: 2.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 47 GGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLV 126
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 127 asdkfktsdypamveevrekcarLEHVVVLGGESWQELmdagrrgdPAQlahlrAGLSADDPINIQYTSGTTGFPKGATL 206
Cdd:cd05939 81 -----------------------FNLLDPLLTQSSTEP--------PSQ-----DDVNFRDKLFYIYTSGTTGLPKAAVI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 207 SHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGACMVIpAPAFDPRATLEAVAAERCTSlygvpTM 286
Cdd:cd05939 125 VHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVI-RKKFSASNFWDDCVKYNCTI-----VQ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 287 FIAE-----LNHPDFGEFDLSSLRtgIMAGSPCPVEVMKQVIDRMGMAEVSICYGMTE-TSPVStqtraddSIERRVSTV 360
Cdd:cd05939 199 YIGEicrylLAQPPSEEEQKHNVR--LAVGNGLRPQIWEQFVRRFGIPQIGEFYGATEgNSSLV-------NIDNHVGAC 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 361 G---RVGPHL-EVKV--VDPES--------GLTVP--RGEPGELCTR-----GYSVMLGYWEQPDkTAEAIDAARWMH-- 417
Cdd:cd05939 270 GfnsRILPSVyPIRLikVDEDTgelirdsdGLCIPcqPGEPGLLVGKiiqndPLRRFDGYVNEGA-TNKKIARDVFKKgd 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 418 ----TGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGV--PDEKyGEELMAWVRMREGASP 491
Cdd:cd05939 349 saflSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVevPGVE-GRAGMAAIVDPERKVD 427
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 522130465 492 LtaEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKVRKVEMR 534
Cdd:cd05939 428 L--DRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQ 468
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
28-530 |
3.06e-25 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 111.03 E-value: 3.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 28 FDRTVAAFGDRdaLVDRAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPA 107
Cdd:PRK05691 3726 FEAQVAAHPQR--IAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPG 3803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 108 YRSHELEYVLDQAGIRLLVASDkfktsdypAMVEEVREKCARLEHVVVLGGESWQELM-------DAGRRGDPAQLAHlr 180
Cdd:PRK05691 3804 LPAQRLQRIIELSRTPVLVCSA--------ACREQARALLDELGCANRPRLLVWEEVQagevashNPGIYSGPDNLAY-- 3873
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 181 aglsaddpinIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDkvCIPVPFYHCFGM-VMGNLACTSHGACMVI- 258
Cdd:PRK05691 3874 ----------VIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEAD--VIAQTASQSFDIsVWQFLAAPLFGARVEIv 3941
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 259 P-APAFDPRATLEAVAAERCTSLYGVPTMFIAELNHPDFGefdLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSICYGM 337
Cdd:PRK05691 3942 PnAIAHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQA---LDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGP 4018
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 338 TETSpvstqtraDDSIERRVSTVGRVGPHLEVK---------VVDPESGLtVPRGEPGELCTRGYSVMLGYWEQPDKTAE 408
Cdd:PRK05691 4019 AECS--------DDVAFFRVDLASTRGSYLPIGsptdnnrlyLLDEALEL-VPLGAVGELCVAGTGVGRGYVGDPLRTAL 4089
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 409 AI-------DAARWMHTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQViGVPDEKYGEELMA 481
Cdd:PRK05691 4090 AFvphpfgaPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAV-AVQEGVNGKHLVG 4168
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 522130465 482 WVRMREGASPLTA--EKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKV-RK 530
Cdd:PRK05691 4169 YLVPHQTVLAQGAllERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLdRK 4220
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
186-453 |
5.49e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 109.05 E-value: 5.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 186 DDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGACMVIPAPAF-- 263
Cdd:PRK07769 180 DTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFvr 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 264 DPRATLEAVAAERctslYGVPTMFIAELN----H------PDFGE--FDLSSLRtGIMAGS-PCPVEVMKQVIDRM---G 327
Cdd:PRK07769 260 RPGRWIRELARKP----GGTGGTFSAAPNfafeHaaarglPKDGEppLDLSNVK-GLLNGSePVSPASMRKFNEAFapyG 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 328 MAEVSI--CYGMTE-TSPVSTqTRADDsiERRVSTVGR--VGPHLEVKV------------------------VDPESGL 378
Cdd:PRK07769 335 LPPTAIkpSYGMAEaTLFVST-TPMDE--EPTVIYVDRdeLNAGRFVEVpadapnavaqvsagkvgvsewaviVDPETAS 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 379 TVPRGEPGELCTRGYSVMLGYWEQPDKTAE-----------------AIDAARWMHTGDLAV-MDGDGYvnITGRIKDMV 440
Cdd:PRK07769 412 ELPDGQIGEIWLHGNNIGTGYWGKPEETAAtfqnilksrlseshaegAPDDALWVRTGDYGVyFDGELY--ITGRVKDLV 489
|
330
....*....|...
gi 522130465 441 IRGGENLYPREIE 453
Cdd:PRK07769 490 IIDGRNHYPQDLE 502
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
48-527 |
1.54e-24 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 107.21 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 48 GRWTYRELAGEVTALALGLVARgigKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVA 127
Cdd:PRK06334 44 GKLSYNQVRKAVIALATKVSKY---PDQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 128 SDKF---------KTSDYPAMV---EEVREKCArlehvvvlggeswqeLMDAGRRGDPAQLAH---LR----AGLSADDP 188
Cdd:PRK06334 121 SKQLmqhlaqthgEDAEYPFSLiymEEVRKELS---------------FWEKCRIGIYMSIPFewlMRwfgvSDKDPEDV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 189 INIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGACMVIPAPAFDPRAT 268
Cdd:PRK06334 186 AVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAYNPLYPKKI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 269 LEAVAAERCTSLYGVPTMFIAELNHPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSICYGMTETSPVSTQTR 348
Cdd:PRK06334 266 VEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTTECSPVITINT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 349 ADDSieRRVSTVGRVGPHLEVKVVDPESGLTVPRGEPGELCTRGYSVMLGYW-EQPDKTAEAIDAARWMHTGDLAVMDGD 427
Cdd:PRK06334 346 VNSP--KHESCVGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRH 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 428 GYVNITGRIKDMVIRGGENLYPREIEEFLYTH------PDVLDAQVIGVPDEKygEELMAWVRMregasPLTAEKVREFC 501
Cdd:PRK06334 424 GELFLKGRLSRFVKIGAEMVSLEALESILMEGfgqnaaDHAGPLVVCGLPGEK--VRLCLFTTF-----PTSISEVNDIL 496
|
490 500
....*....|....*....|....*..
gi 522130465 502 -SGKLAHYKIPRYVHVVDEFPMTVTGK 527
Cdd:PRK06334 497 kNSKTSSILKISYHHQVESIPMLGTGK 523
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
73-535 |
2.66e-24 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 107.49 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 73 KGDRVGIWSPNrAEWTflqyATAKIGAILVNINPAYRSHE-----LEYVLDQAGIRLLVAS----DKFKTSDYPAMVEEV 143
Cdd:PRK08043 254 EGERIGLMLPN-ATIS----AAVIFGASLRRRIPAMMNYTagvkgLTSAITAAEIKTIFTSrqflDKGKLWHLPEQLTQV 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 144 RekcarlehvvvlggesW---QELMDAGRRGDPAQ-LAHL----RAGLS--ADDPINIQYTSGTTGFPKGATLSHHNILN 213
Cdd:PRK08043 329 R----------------WvylEDLKDDVTTADKLWiFAHLlmprLAQVKqqPEDAALILFTSGSEGHPKGVVHSHKSLLA 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 214 NGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGA-CMVIPAPaFDPRATLEAVAAERCTSLYGVPTMF--IAE 290
Cdd:PRK08043 393 NVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAeVFLYPSP-LHYRIVPELVYDRNCTVLFGTSTFLgnYAR 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 291 LNHPdfgeFDLSSLRTgIMAGSPCPVEVMKQV-IDRMGMaEVSICYGMTETSPVStqtraddSIE----RRVSTVGRVGP 365
Cdd:PRK08043 472 FANP----YDFARLRY-VVAGAEKLQESTKQLwQDKFGL-RILEGYGVTECAPVV-------SINvpmaAKPGTVGRILP 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 366 HLEVKVVdPESGLTvprgEPGELCTRGYSVMLGYW--EQPDK-------TAEAIDAARWMHTGDLAVMDGDGYVNITGRI 436
Cdd:PRK08043 539 GMDARLL-SVPGIE----QGGRLQLKGPNIMNGYLrvEKPGVlevptaeNARGEMERGWYDTGDIVRFDEQGFVQIQGRA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 437 KDMVIRGGENLYPREIEEF-LYTHPDVLDAQVIgVPDEKYGEELMAWVRMREgaspLTAEKV----REFCSGKLAhykIP 511
Cdd:PRK08043 614 KRFAKIAGEMVSLEMVEQLaLGVSPDKQHATAI-KSDASKGEALVLFTTDSE----LTREKLqqyaREHGVPELA---VP 685
|
490 500
....*....|....*....|....
gi 522130465 512 RYVHVVDEFPMTVTGKVRKVEMRE 535
Cdd:PRK08043 686 RDIRYLKQLPLLGSGKPDFVTLKS 709
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
39-535 |
4.98e-24 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 105.36 E-value: 4.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 39 DALVDRAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEW--TFLqyATAKIGAILVNIN---PAYRsheL 113
Cdd:PRK04813 17 DFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMlaTFL--GAVKAGHAYIPVDvssPAER---I 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 114 EYVLDQAGIRLLVAsdkfkTSDYPAMVEEVRekcarlehvvVLggeSWQELMDAGRRGDPAQLAHLragLSADDPINIQY 193
Cdd:PRK04813 92 EMIIEVAKPSLIIA-----TEELPLEILGIP----------VI---TLDELKDIFATGNPYDFDHA---VKGDDNYYIIF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 194 TSGTTGFPKGATLSHHNILNngyFVGELCN--YTEEDKVCIPVPFYHcFGM-VMGNLAC-TSHGACMVIP-APAFDPR-- 266
Cdd:PRK04813 151 TSGTTGKPKGVQISHDNLVS---FTNWMLEdfALPEGPQFLNQAPYS-FDLsVMDLYPTlASGGTLVALPkDMTANFKql 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 267 -ATLEAVAAERCTSlygVPT-MFIAELNhPDFGEFDLSSLRTGIMAGSPCPVEVMKQVIDRMGMAEVSICYGMTETSPVS 344
Cdd:PRK04813 227 fETLPQLPINVWVS---TPSfADMCLLD-PSFNEEHLPNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATVAV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 345 TQTRADDSIERRVST--VGRVGPHLEVKVVDpESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEA---IDAARWMHTG 419
Cdd:PRK04813 303 TSIEITDEMLDQYKRlpIGYAKPDSPLLIID-EEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAfftFDGQPAYHTG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 420 DLAVMDgDGYVNITGRIkDMVIR-GGENLYPREIEEFLYTHPDVLDAQVIGV-PDEKYgEELMAWVRMREG----ASPLT 493
Cdd:PRK04813 382 DAGYLE-DGLLFYQGRI-DFQIKlNGYRIELEEIEQNLRQSSYVESAVVVPYnKDHKV-QYLIAYVVPKEEdferEFELT 458
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 522130465 494 AEkVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKV-RKVEMRE 535
Cdd:PRK04813 459 KA-IKKELKERLMEYMIPRKFIYRDSLPLTPNGKIdRKALIEE 500
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
23-420 |
5.60e-24 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 106.12 E-value: 5.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 23 TIGDNFDRTVAAFGDRDALVDRAAGGRW---TYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGA 99
Cdd:PRK08180 40 RLTDRLVHWAQEAPDRVFLAERGADGGWrrlTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 100 ILVNINPAY--RSHE---LEYVLDQAGIRLLVASDKFKTSDYPAMVEEvrekcARLEHVVVLGGE------SWQELMDAG 168
Cdd:PRK08180 120 PYAPVSPAYslVSQDfgkLRHVLELLTPGLVFADDGAAFARALAAVVP-----ADVEVVAVRGAVpgraatPFAALLATP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 169 RRGDpAQLAHLRAGlsADDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDKvciPV-----PFYHCFGmv 243
Cdd:PRK08180 195 PTAA-VDAAHAAVG--PDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEP---PVlvdwlPWNHTFG-- 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 244 mGN------LActsHGACMVI----PAPA-FDprATLEAVAAERCTSLYGVPT---MFIAELNH-PDFGEFDLSSLRTGI 308
Cdd:PRK08180 267 -GNhnlgivLY---NGGTLYIddgkPTPGgFD--ETLRNLREISPTVYFNVPKgweMLVPALERdAALRRRFFSRLKLLF 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 309 MAGSPCPVEVMKQvIDRMGMAEV------SICYGMTETSPVSTqtraddSIERRVSTVGRVG---PHLEVKVvdpesglt 379
Cdd:PRK08180 341 YAGAALSQDVWDR-LDRVAEATCgerirmMTGLGMTETAPSAT------FTTGPLSRAGNIGlpaPGCEVKL-------- 405
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 522130465 380 VPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDAARWMHTGD 420
Cdd:PRK08180 406 VPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGD 446
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
194-534 |
3.24e-23 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 102.15 E-value: 3.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 194 TSGTTGFPKGATLSHHNILNNGYFVG---ELCNYTEEDKVCIPVPFyhcfGMVMGNLACTShGA----CMVIPAPAFDPR 266
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDLDRWAELFArslRAAGVRPGDRVQNAFGY----GLFTGGLGLHY-GAerlgATVIPAGGGNTE 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 267 ATLEAVAAERCTSLYGVPTMFI-----AELNHPDFGEfdlSSLRTGIMAGSPCPvEVMKQVI-DRMGmAEVSICYGMTET 340
Cdd:COG1541 166 RQLRLMQDFGPTVLVGTPSYLLylaevAEEEGIDPRD---LSLKKGIFGGEPWS-EEMRKEIeERWG-IKAYDIYGLTEV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 341 SP-VSTQTRADDsierrvstvgrvGPHL-E----VKVVDPESGLTVPRGEPGEL----CTRGYSVMLGYweqpdktaeai 410
Cdd:COG1541 241 GPgVAYECEAQD------------GLHIwEdhflVEIIDPETGEPVPEGEEGELvvttLTKEAMPLIRY----------- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 411 daarwmHTGDLAVMDGD----GYVN-----ITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKYGEELMA 481
Cdd:COG1541 298 ------RTGDLTRLLPEpcpcGRTHprigrILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTV 371
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 522130465 482 WVRMREGASPltaEKVREFCSGKL-AHYKIPRYVHVV--DEFPMTvTGKVRKVEMR 534
Cdd:COG1541 372 RVELAPGASL---EALAEAIAAALkAVLGLRAEVELVepGSLPRS-EGKAKRVIDR 423
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
20-528 |
4.18e-23 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 104.48 E-value: 4.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 20 LGDTIGDNFDRTVAAFGDRDALVdrAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGA 99
Cdd:PRK05691 2186 LDQTLHGLFAAQAARTPQAPALT--FAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGG 2263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 100 ILVNINPAYRSHELEYVLDQAGIRLLVAsdkfktsdYPAMVEEVREKCArlehvvvlGGESWQeLMDagrrgDPAQLAHL 179
Cdd:PRK05691 2264 AYVPLDPEYPLERLHYMIEDSGIGLLLS--------DRALFEALGELPA--------GVARWC-LED-----DAAALAAY 2321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 180 raglSADDPINIQ---------YTSGTTGFPKGATLSHhnilnngyfvGELCnyteedkvcipvpfYHC------FGMVM 244
Cdd:PRK05691 2322 ----SDAPLPFLSlpqhqayliYTSGSTGKPKGVVVSH----------GEIA--------------MHCqavierFGMRA 2373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 245 GNlaCTSH-------------------GACMVIPAPA-FDPRATLEAVAAERCTSLYGVPTmFIAELNHPDFGEFDLSSL 304
Cdd:PRK05691 2374 DD--CELHfysinfdaaserllvpllcGARVVLRAQGqWGAEEICQLIREQQVSILGFTPS-YGSQLAQWLAGQGEQLPV 2450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 305 RTGIMAGSPCPVEVMKQVIDRMGMAEVSICYGMTETSPVSTQTRADDSIERRVSTV--GRVGPHLEVKVVDPESGLtVPR 382
Cdd:PRK05691 2451 RMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTETVVMPLACLAPEQLEEGAASVpiGRVVGARVAYILDADLAL-VPQ 2529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 383 GEPGELCTRGYSVMLGYWEQPDKTAE-------AIDAARWMHTGDLAVMDGDGYVNITGRIKDMV-IRGGEnLYPREIEE 454
Cdd:PRK05691 2530 GATGELYVGGAGLAQGYHDRPGLTAErfvadpfAADGGRLYRTGDLVRLRADGLVEYVGRIDHQVkIRGFR-IELGEIES 2608
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522130465 455 FLYTHPDVLDAQVIGVpDEKYGEELMAWV-----RMREGASPLTAEKVREFCSGKLAHYKIPRYVHVVDEFPMTVTGKV 528
Cdd:PRK05691 2609 RLLEHPAVREAVVLAL-DTPSGKQLAGYLvsavaGQDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKL 2686
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
22-540 |
2.41e-22 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 101.05 E-value: 2.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 22 DTIGDNFDRTVAAFGDRDAL-----VDRAAGG-RW-TYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYAT 94
Cdd:PLN02430 42 TTAWDIFSKSVEKYPDNKMLgwrriVDGKVGPyMWkTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEAC 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 95 AKIGAILVNINPAYRSHELEYVLDQAGIRLLVASDKfktsdypaMVEEVRE---KCA-RLEHVVVL--GGE--------- 159
Cdd:PLN02430 122 AAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDK--------KIKELLEpdcKSAkRLKAIVSFtsVTEeesdkasqi 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 160 -----SWQELMDAGRRgDPAQLahlraglSADDPIN---IQYTSGTTGFPKGATLSHHNILNngYFVG-ELCNYTEEDKV 230
Cdd:PLN02430 194 gvktySWIDFLHMGKE-NPSET-------NPPKPLDictIMYTSGTSGDPKGVVLTHEAVAT--FVRGvDLFMEQFEDKM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 231 CIP------VPFYHCFGMVM-------GNLACTSHGacmvipapafDPRATLEAVAAERCTSLYGVPTMF---------- 287
Cdd:PLN02430 264 THDdvylsfLPLAHILDRMIeeyffrkGASVGYYHG----------DLNALRDDLMELKPTLLAGVPRVFerihegiqka 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 288 IAELNHPDFGEFD------LSSLRTGIMAGSPCPVEVM---KQVIDRMG-------------------MAEVSIC----- 334
Cdd:PLN02430 334 LQELNPRRRLIFNalykykLAWMNRGYSHKKASPMADFlafRKVKAKLGgrlrllisggaplsteieeFLRVTSCafvvq 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 335 -YGMTETSPVSTQTRADDSIerRVSTVGRVGPHLEVKVVD-PESGLTvPRGEP--GELCTRGYSVMLGYWEQPDKTAEAI 410
Cdd:PLN02430 414 gYGLTETLGPTTLGFPDEMC--MLGTVGAPAVYNELRLEEvPEMGYD-PLGEPprGEICVRGKCLFSGYYKNPELTEEVM 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 411 dAARWMHTGDLAVMDGDGYVNITGRIKDMV-IRGGENLYPREIEEFLYTHPDVLDAQVIG-----------VPDEkygEE 478
Cdd:PLN02430 491 -KDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEYLENVYGQNPIVEDIWVYGdsfksmlvavvVPNE---EN 566
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522130465 479 LMAWVRMREGASPLTaekvrEFCSGKLAHYkipryvHVVDEFPMTVT-GKVRKVEmREKSITL 540
Cdd:PLN02430 567 TNKWAKDNGFTGSFE-----ELCSLPELKE------HILSELKSTAEkNKLRGFE-YIKGVIL 617
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
451-527 |
3.37e-21 |
|
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: 87.60 E-value: 3.37e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522130465 451 EIEEFLYTHPDVLDAQVIGVPDEKYGEELMAWVRMREGASPLTAEkVREFCSGKLAHYKIPRYVHVVDEFPMTVTGK 527
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEE-LVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
51-437 |
9.20e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 96.20 E-value: 9.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 51 TYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVASDK 130
Cdd:PTZ00216 123 TYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGK 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 131 fKTSDYPAMVEEVREKCARL------------EHVVVLggeSWQELMDAGRrGDPAQLAhLRAGLSADDPINIQYTSGTT 198
Cdd:PTZ00216 203 -NVPNLLRLMKSGGMPNTTIiyldslpasvdtEGCRLV---AWTDVVAKGH-SAGSHHP-LNIPENNDDLALIMYTSGTT 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 199 GFPKGATLSHHNI----LNNGYFVGELCNYTEEDKV-CIPVPFYHCFgmvmgNLACTS----HGA--CMVIPAPAFD--- 264
Cdd:PTZ00216 277 GDPKGVMHTHGSLtagiLALEDRLNDLIGPPEEDETyCSYLPLAHIM-----EFGVTNiflaRGAliGFGSPRTLTDtfa 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 265 -PRATLEAVaaeRCTSLYGVPTMF-----IAELNHPDFGE-----FD------LSSLRTG----------------IMAG 311
Cdd:PTZ00216 352 rPHGDLTEF---RPVFLIGVPRIFdtikkAVEAKLPPVGSlkrrvFDhayqsrLRALKEGkdtpywnekvfsapraVLGG 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 312 ------------SPCPVEVMKQVidrMGMaeVSICYGMTETSPVSTQTRADDsIErrVSTVGRVGPHLEVKVVD------ 373
Cdd:PTZ00216 429 rvramlsgggplSAATQEFVNVV---FGM--VIQGWGLTETVCCGGIQRTGD-LE--PNAVGQLLKGVEMKLLDteeykh 500
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522130465 374 ---PEsgltvPRGEpgeLCTRGYSVMLGYWEQPDKTAEAIDAARWMHTGDLAVMDGDGYVNITGRIK 437
Cdd:PTZ00216 501 tdtPE-----PRGE---ILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVK 559
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
21-453 |
1.26e-20 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 95.58 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 21 GDTIGDNFDRTVAAFGDRDAL----VDRAAGGRwtyrelAGEVTALALGLVARGIG--------KGDRVGIWSPNRAEWT 88
Cdd:PRK12476 33 GTTLISLIERNIANVGDTVAYryldHSHSAAGC------AVELTWTQLGVRLRAVGarlqqvagPGDRVAILAPQGIDYV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 89 FLQYATAKIGAILVNI-NPAYRSH--ELEYVLDQAGIRLLVASDkfktsdypAMVEEVREKCARLEH-----VVVLgges 160
Cdd:PRK12476 107 AGFFAAIKAGTIAVPLfAPELPGHaeRLDTALRDAEPTVVLTTT--------AAAEAVEGFLRNLPRlrrprVIAI---- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 161 wqelmDAgrrgDPAQLAHL--RAGLSADDPINIQYTSGTTGFPKGATLSHH----NILNNGYFVGELCNYTEEdkvCIPV 234
Cdd:PRK12476 175 -----DA----IPDSAGESfvPVELDTDDVSHLQYTSGSTRPPVGVEITHRavgtNLVQMILSIDLLDRNTHG---VSWL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 235 PFYHCFG--MVMGNLACTSHGACMVIPAPAFDPRATLEAVAAE-RCTSLYGVPTMFIAELNH-----PDFGEFDLSS--L 304
Cdd:PRK12476 243 PLYHDMGlsMIGFPAVYGGHSTLMSPTAFVRRPQRWIKALSEGsRTGRVVTAAPNFAYEWAAqrglpAEGDDIDLSNvvL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 305 RTGIMAGSPCPVEVMKQVIDRMGMAEVSI--CYGMTE-TSPVST---------------------QTRADDSIERRVSTV 360
Cdd:PRK12476 323 IIGSEPVSIDAVTTFNKAFAPYGLPRTAFkpSYGIAEaTLFVATiapdaepsvvyldreqlgagrAVRVAADAPNAVAHV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 361 --GRVGPHLEVKVVDPESGLTVPRGEPGELCTRGYSVMLGYWEQPDKT------------------AEAIDAARWMHTGD 420
Cdd:PRK12476 403 scGQVARSQWAVIVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETertfgaklqsrlaegshaDGAADDGTWLRTGD 482
|
490 500 510
....*....|....*....|....*....|....
gi 522130465 421 LAV-MDGDGYvnITGRIKDMVIRGGENLYPREIE 453
Cdd:PRK12476 483 LGVyLDGELY--ITGRIADLIVIDGRNHYPQDIE 514
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
51-439 |
3.37e-20 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 94.52 E-value: 3.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 51 TYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVASDk 130
Cdd:PLN02861 79 TYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQE- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 131 fktSDYPAMVEEVREKCARLEHVVVLGGESWQELMDAGRRG-------DPAQLAHLRAGLSA---DDPINIQYTSGTTGF 200
Cdd:PLN02861 158 ---SKISSILSCLPKCSSNLKTIVSFGDVSSEQKEEAEELGvscfsweEFSLMGSLDCELPPkqkTDICTIMYTSGTTGE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 201 PKGAtlshhnILNNGYFVGELCNY-----------TEEDKVCIPVPFYHCFGMVMGNLaCTSHGACmvIPAPAFDPRATL 269
Cdd:PLN02861 235 PKGV------ILTNRAIIAEVLSTdhllkvtdrvaTEEDSYFSYLPLAHVYDQVIETY-CISKGAS--IGFWQGDIRYLM 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 270 EAVAAERCTSLYGVPTMF-------IAELNHP--------DFG-EFDLSSLRTGIMAGSPCP-----------------V 316
Cdd:PLN02861 306 EDVQALKPTIFCGVPRVYdriytgiMQKISSGgmlrkklfDFAyNYKLGNLRKGLKQEEASPrldrlvfdkikeglggrV 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 317 EVM--------KQVIDRMGMAEVSIC---YGMTETSPVSTQTRADdsIERRVSTVGRVGPHLEVKVVD-PESGL----TV 380
Cdd:PLN02861 386 RLLlsgaaplpRHVEEFLRVTSCSVLsqgYGLTESCGGCFTSIAN--VFSMVGTVGVPMTTIEARLESvPEMGYdalsDV 463
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 381 PRgepGELCTRGYSVMLGYWEQPDKTAEA-IDAarWMHTGDLAVMDGDGYVNITGRIKDM 439
Cdd:PLN02861 464 PR---GEICLRGNTLFSGYHKRQDLTEEVlIDG--WFHTGDIGEWQPNGAMKIIDRKKNI 518
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
37-423 |
8.56e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 93.19 E-value: 8.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 37 DRDALVDRAAGGR-W---TYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYR--S 110
Cdd:PRK12582 64 DRPWLAQREPGHGqWrkvTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSlmS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 111 HE---LEYVLDQAGIRLLVASDkfkTSDYPAMVEEVREKCARLEHVVVLG-GESWQELMDAGRRGDPAQLAHLRAGLSAD 186
Cdd:PRK12582 144 HDhakLKHLFDLVKPRVVFAQS---GAPFARALAALDLLDVTVVHVTGPGeGIASIAFADLAATPPTAAVAAAIAAITPD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 187 DPINIQYTSGTTGFPKGATLSHHNILNNgyFVGELCNYTEEDKVCIPV-----PFYHCFGmvmGNLACTS---HGACMVI 258
Cdd:PRK12582 221 TVAKYLFTSGSTGMPKAVINTQRMMCAN--IAMQEQLRPREPDPPPPVsldwmPWNHTMG---GNANFNGllwGGGTLYI 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 259 ----PAPA-FDPraTLEAVAAERCTSLYGVP---TMFIAEL-NHPDFGEFDLSSLRTGIMAGSPCPVEVMkqviDRMGMA 329
Cdd:PRK12582 296 ddgkPLPGmFEE--TIRNLREISPTVYGNVPagyAMLAEAMeKDDALRRSFFKNLRLMAYGGATLSDDLY----ERMQAL 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 330 EVSIC---------YGMTETSPVSTQTRADdsiERRVSTVGRVGPHLEVKVVdpesgltvPRGEPGELCTRGYSVMLGYW 400
Cdd:PRK12582 370 AVRTTghripfytgYGATETAPTTTGTHWD---TERVGLIGLPLPGVELKLA--------PVGDKYEVRVKGPNVTPGYH 438
|
410 420
....*....|....*....|...
gi 522130465 401 EQPDKTAEAIDAARWMHTGDLAV 423
Cdd:PRK12582 439 KDPELTAAAFDEEGFYRLGDAAR 461
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
192-530 |
8.04e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 90.00 E-value: 8.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 192 QYTSGTTGFPKGATLSHHNILNN------GYFVGELCNYTEEDKVCIPVPFYHCFGMVMGnlactshgACMVI----PAP 261
Cdd:PRK05850 166 QYTSGSTRTPAGVMVSHRNVIANfeqlmsDYFGDTGGVPPPDTTVVSWLPFYHDMGLVLG--------VCAPIlggcPAV 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 262 AFDPRATLEAVA------AERctslygvPTMFIAElnhPDFGeFDLSSLRT--------------GIMAGSPcPVEV--M 319
Cdd:PRK05850 238 LTSPVAFLQRPArwmqllASN-------PHAFSAA---PNFA-FELAVRKTsdddmagldlggvlGIISGSE-RVHPatL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 320 KQVIDRM---GMAEVSI--CYGMTE-TSPVSTQTRADDSIERRVS----TVGRV-------GPHL---------EVKVVD 373
Cdd:PRK05850 306 KRFADRFapfNLRETAIrpSYGLAEaTVYVATREPGQPPESVRFDyeklSAGHAkrcetggGTPLvsygsprspTVRIVD 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 374 PESGLTVPRGEPGELCTRGYSVMLGYWEQPDKTAEAIDA-----------ARWMHTGDLAVMDgDGYVNITGRIKDMVIR 442
Cdd:PRK05850 386 PDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGAtlvdpspgtpeGPWLRTGDLGFIS-EGELFIVGRIKDLLIV 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 443 GGENLYPREIE----EFlyTHPDVldaQVIGVPDEKyGEELMAWVRMREGASPlTAEKVREFCSGKL--------AHyki 510
Cdd:PRK05850 465 DGRNHYPDDIEatiqEI--TGGRV---AAISVPDDG-TEKLVAIIELKKRGDS-DEEAMDRLRTVKRevtsaiskSH--- 534
|
410 420
....*....|....*....|....*..
gi 522130465 511 prYVHVVD-------EFPMTVTGKVRK 530
Cdd:PRK05850 535 --GLSVADlvlvapgSIPITTSGKIRR 559
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
37-420 |
2.47e-17 |
|
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: 85.18 E-value: 2.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 37 DRDALVDRAAGGRW---TYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAY--RSH 111
Cdd:cd05921 10 DRTWLAEREGNGGWrrvTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYslMSQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 112 E---LEYVLDQAGIRLLVASDKFKTSDYPAMVEEvrekcARLEHVVVLGGE------SWQELMDAGRRGDpaqLAHLRAG 182
Cdd:cd05921 90 DlakLKHLFELLKPGLVFAQDAAPFARALAAIFP-----LGTPLVVSRNAVagrgaiSFAELAATPPTAA---VDAAFAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 183 LSADDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNY-TEEDKVCIP-VPFYHCFG------MVMGNlactshGA 254
Cdd:cd05921 162 VGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFfGEEPPVLVDwLPWNHTFGgnhnfnLVLYN------GG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 255 CMVI----PAPA-FDprATLEAVAAERCTSLYGVP---TMFIAEL-NHPDFGEFDLSSLRTGIMAGSPCPVEVMKQvIDR 325
Cdd:cd05921 236 TLYIddgkPMPGgFE--ETLRNLREISPTVYFNVPagwEMLVAALeKDEALRRRFFKRLKLMFYAGAGLSQDVWDR-LQA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 326 MGMAEVS------ICYGMTETSPVSTQTRADDSierRVSTVGRVGPHLEVKVvdpesgltVPRGEPGELCTRGYSVMLGY 399
Cdd:cd05921 313 LAVATVGeripmmAGLGATETAPTATFTHWPTE---RSGLIGLPAPGTELKL--------VPSGGKYEVRVKGPNVTPGY 381
|
410 420
....*....|....*....|.
gi 522130465 400 WEQPDKTAEAIDAARWMHTGD 420
Cdd:cd05921 382 WRQPELTAQAFDEEGFYCLGD 402
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
50-462 |
4.90e-17 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 84.40 E-value: 4.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 50 W-TYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEW------TFLQ-------YATAKIGAILVNINpayrshELE- 114
Cdd:PLN02387 106 WiTYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWlialqgCFRQnitvvtiYASLGEEALCHSLN------ETEv 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 115 --YVLDQAGIRLLVA-SDKFKT-SDYPAMVEEVREKCARLEHVVVLGGESWQELMDAGRrGDPAQlAHLRaglSADDPIN 190
Cdd:PLN02387 180 ttVICDSKQLKKLIDiSSQLETvKRVIYMDDEGVDSDSSLSGSSNWTVSSFSEVEKLGK-ENPVD-PDLP---SPNDIAV 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 191 IQYTSGTTGFPKGATLSHhnilnngyfvgelcnyteedkvcipvpfyhcfgmvmGNLACTSHGACMVIPA-------PAF 263
Cdd:PLN02387 255 IMYTSGSTGLPKGVMMTH------------------------------------GNIVATVAGVMTVVPKlgkndvyLAY 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 264 DPRATLEAVAAER------CTSLYGVPTMFIAELNHPDFG-EFDLSSLRTGIMAGSPCPVE-----VMKQVIDRMGMAE- 330
Cdd:PLN02387 299 LPLAHILELAAESvmaavgAAIGYGSPLTLTDTSNKIKKGtKGDASALKPTLMTAVPAILDrvrdgVRKKVDAKGGLAKk 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 331 -------------------------------------------------------------VSIC--------YGMTETS 341
Cdd:PLN02387 379 lfdiaykrrlaaiegswfgawglekllwdalvfkkiravlggrirfmlsggaplsgdtqrfINIClgapigqgYGLTETC 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 342 PVSTQTRADDSierrvsTVGRVG---PHLEVKVVD-PESGLTV-----PRGEpgeLCTRGYSVMLGYWEQPDKTAEA--I 410
Cdd:PLN02387 459 AGATFSEWDDT------SVGRVGpplPCCYVKLVSwEEGGYLIsdkpmPRGE---IVIGGPSVTLGYFKNQEKTDEVykV 529
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 522130465 411 D--AARWMHTGDLAVMDGDGYVNITGRIKDMV-IRGGENLYPREIEEFLYTHPDV 462
Cdd:PLN02387 530 DerGMRWFYTGDIGQFHPDGCLEIIDRKKDIVkLQHGEYVSLGKVEAALSVSPYV 584
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
171-470 |
5.44e-17 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 84.05 E-value: 5.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 171 GDPAQLAHLR-----AGLSADDPINIQYTSGTTGFPKGATLSHHNILNNGYFVGELCNYTE-EDKVCIPVPFYHCFGM-- 242
Cdd:PRK05851 132 HDLATAAHTNrsaslTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAaTDVGCSWLPLYHDMGLaf 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 243 -VMGNLActshGACM-VIPAPAF------------DPRATLeaVAAERCTslYGVPTMFIAELNhpdfgEFDLSSLRTGI 308
Cdd:PRK05851 212 lLTAALA----GAPLwLAPTTAFsaspfrwlswlsDSRATL--TAAPNFA--YNLIGKYARRVS-----DVDLGALRVAL 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 309 MAGSPCPVEVMKQVIDRMG-----MAEVSICYGMTE-----TSPV-STQTRADD------SIERRVSTVGRVGPHLEVKV 371
Cdd:PRK05851 279 NGGEPVDCDGFERFATAMApfgfdAGAAAPSYGLAEstcavTVPVpGIGLRVDEvttddgSGARRHAVLGNPIPGMEVRI 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 372 VDPESGLTVPRGEPGELCTRGYSVMLGYWEQPdktaeAIDAARWMHTGDLAVMDGDGYVnITGRIKDMVIRGGENLYPRE 451
Cdd:PRK05851 359 SPGDGAAGVAGREIGEIEIRGASMMSGYLGQA-----PIDPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTE 432
|
330
....*....|....*....
gi 522130465 452 IEEflythpdvLDAQVIGV 470
Cdd:PRK05851 433 IER--------VAAQVRGV 443
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
3-421 |
7.64e-17 |
|
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: 83.66 E-value: 7.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 3 DAPALPSYASGISEVPL-LGDTIgdnfDRTVAAFGDRDALVDRAAG-------GRWTYRELAGEVTALALGLVARG---- 70
Cdd:cd17632 6 AAAPLEAVTEAIRRPGLrLAQII----ATVMTGYADRPALGQRATElvtdpatGRTTLRLLPRFETITYAELWERVgava 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 71 --------IGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVASdkfkTSDYPAMVEE 142
Cdd:cd17632 82 aahdpeqpVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVS----AEHLDLAVEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 143 VREKCArLEHVVVLGG-----------ESWQE------------LMDAGRRGDPAQLAHLRAGLSADDPINIQYTSGTTG 199
Cdd:cd17632 158 VLEGGT-PPRLVVFDHrpevdahraalESARErlaavgipvttlTLIAVRGRDLPPAPLFRPEPDDDPLALLIYTSGSTG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 200 FPKGATLSHHNILNNG-YFVGELCNYTEEDKVCIPVPFYHCFG--MVMGNLActSHGACMVIPAPafDPRATLEAVAAER 276
Cdd:cd17632 237 TPKGAMYTERLVATFWlKVSSIQDIRPPASITLNFMPMSHIAGriSLYGTLA--RGGTAYFAAAS--DMSTLFDDLALVR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 277 CTSLYGVPTM-------FIAELNHPDFGEFDLSS--------LR---------TGIMAGSPCPVEvMKQVIDRMGMAEVS 332
Cdd:cd17632 313 PTELFLVPRVcdmlfqrYQAELDRRSVAGADAETlaervkaeLRervlggrllAAVCGSAPLSAE-MKAFMESLLDLDLH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 333 ICYGMTETSPVSTqtraDDSIERRvstvgrvgPHLEVKVVD-PESG-LTVPRGEP-GELCTRGYSVMLGYWEQPDKTAEA 409
Cdd:cd17632 392 DGYGSTEAGAVIL----DGVIVRP--------PVLDYKLVDvPELGyFRTDRPHPrGELLVKTDTLFPGYYKRPEVTAEV 459
|
490
....*....|..
gi 522130465 410 IDAARWMHTGDL 421
Cdd:cd17632 460 FDEDGFYRTGDV 471
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
38-465 |
2.48e-14 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 75.83 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 38 RDALVDRAAGGR-W-TYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEY 115
Cdd:PLN02614 66 RREIVDGKPGKYvWqTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEF 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 116 VLDQAGIRLLVASDKfktsDYPAMVEEVREKCARLEHVVVLGGESWQELMDAGRRG----DPAQLAHLRAGLSADDPI-- 189
Cdd:PLN02614 146 IISHSEVSIVFVEEK----KISELFKTCPNSTEYMKTVVSFGGVSREQKEEAETFGlviyAWDEFLKLGEGKQYDLPIkk 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 190 -----NIQYTSGTTGFPKGATLSHHNI--LNNG--YFVGEL-CNYTEEDKVCIPVPFYHCFGMVMGNlACTSHGACMvip 259
Cdd:PLN02614 222 ksdicTIMYTSGTTGDPKGVMISNESIvtLIAGviRLLKSAnAALTVKDVYLSYLPLAHIFDRVIEE-CFIQHGAAI--- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 260 apAF---DPRATLEAVAAERCTSLYGVP-------TMFIAELNHPDFGE---FDLS-SLRTGIM-------AGSP-CPVE 317
Cdd:PLN02614 298 --GFwrgDVKLLIEDLGELKPTIFCAVPrvldrvySGLQKKLSDGGFLKkfvFDSAfSYKFGNMkkgqshvEASPlCDKL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 318 VMKQVIDRMG--------------------MAEVSIC-----YGMTETSPVSTQTRADDSieRRVSTVGRVGPHLEVKVV 372
Cdd:PLN02614 376 VFNKVKQGLGgnvriilsgaaplashvesfLRVVACChvlqgYGLTESCAGTFVSLPDEL--DMLGTVGPPVPNVDIRLE 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 373 D-PESGLTVPRGEP-GELCTRGYSVMLGYWEQPDKTAEA-IDAarWMHTGDLAVMDGDGYVNITGRIKDMV-IRGGENLY 448
Cdd:PLN02614 454 SvPEMEYDALASTPrGEICIRGKTLFSGYYKREDLTKEVlIDG--WLHTGDVGEWQPNGSMKIIDRKKNIFkLSQGEYVA 531
|
490
....*....|....*..
gi 522130465 449 PREIEEfLYTHPDVLDA 465
Cdd:PLN02614 532 VENIEN-IYGEVQAVDS 547
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
29-535 |
1.11e-12 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 70.70 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 29 DRTV-AAFGDRDALV----DRAAGGRWTYRELAGEVTALALGLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVN 103
Cdd:PLN02654 95 DRNVeAGNGDKIAIYwegnEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 104 INPAYRSHELEYVLDQAGIRLLVASDKFKTSDYP---------AMVEEVREK-----CARLEHVVVLGGES--WQELMDA 167
Cdd:PLN02654 175 VFAGFSAESLAQRIVDCKPKVVITCNAVKRGPKTinlkdivdaALDESAKNGvsvgiCLTYENQLAMKREDtkWQEGRDV 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 168 GRRGDPAQLAHL--RAGLSADDPINIQYTSGTTGFPKGATLShhnilNNGYFV--GELCNYTEEDKvciPVPFYHCF--- 240
Cdd:PLN02654 255 WWQDVVPNYPTKceVEWVDAEDPLFLLYTSGSTGKPKGVLHT-----TGGYMVytATTFKYAFDYK---PTDVYWCTadc 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 241 GMVMGNLACTS----HGACMVI--PAPAF-DPRATLEAVAAERCTSLYGVPTMFIAELNHPD--FGEFDLSSLRTGIMAG 311
Cdd:PLN02654 327 GWITGHSYVTYgpmlNGATVLVfeGAPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDeyVTRHSRKSLRVLGSVG 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 312 SPCPVEVMKQVIDRMGMAE--VSICYGMTETSPVSTQTRADDSIERRVSTVGrvgPHLEVK--VVDpESGLTVPRGEPGE 387
Cdd:PLN02654 407 EPINPSAWRWFFNVVGDSRcpISDTWWQTETGGFMITPLPGAWPQKPGSATF---PFFGVQpvIVD-EKGKEIEGECSGY 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 388 LCTRG-----YSVMLGYWEQPDKTAEAIDAARWMhTGDLAVMDGDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDV 462
Cdd:PLN02654 483 LCVKKswpgaFRTLYGDHERYETTYFKPFAGYYF-SGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQC 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 463 LDAQVIGVPDEKYGEELMAWVRMREGAsPLTAEKVREFCS---GKLAHYKIPRYVHVVDEFPMTVTGKV-----RKVEMR 534
Cdd:PLN02654 562 AEAAVVGIEHEVKGQGIYAFVTLVEGV-PYSEELRKSLILtvrNQIGAFAAPDKIHWAPGLPKTRSGKImrrilRKIASR 640
|
.
gi 522130465 535 E 535
Cdd:PLN02654 641 Q 641
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
178-462 |
1.50e-12 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 69.58 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 178 HLRAGlSADDPINIQYTSGTTGFPKGATLSHHNILNNGYFVG---ELCNYTEEDKVCIpVPFYHCFgmvMGNLACtsH-G 253
Cdd:cd05913 71 GLFAV-PREKVVRIHASSGTTGKPTVVGYTKNDLDVWAELVArclDAAGVTPGDRVQN-AYGYGLF---TGGLGF--HyG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 254 A----CMVIPAPAFDPRATLEAVAAERCTSLYGVPTM--FIAELNHPDFGEFDLSSLRTGIMAGSPCpVEVMKQVIDRMG 327
Cdd:cd05913 144 AerlgALVIPAGGGNTERQLQLIKDFGPTVLCCTPSYalYLAEEAEEEGIDPRELSLKVGIFGAEPW-TEEMRKRIERRL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 328 MAEVSICYGMTETSPVSTqtrADDSIERRVSTVgrVGPHLEVKVVDPESGLTVPRGEPGELC----TRGYSVMLGYWeqp 403
Cdd:cd05913 223 GIKAYDIYGLTEIIGPGV---AFECEEKDGLHI--WEDHFIPEIIDPETGEPVPPGEVGELVfttlTKEAMPLIRYR--- 294
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522130465 404 dktaeaidaarwmhTGDLAVMDGD----GYVN-----ITGRIKDMVIRGGENLYPREIEEFLYTHPDV 462
Cdd:cd05913 295 --------------TRDITRLLPGpcpcGRTHrridrITGRSDDMLIIRGVNVFPSQIEDVLLKIPGL 348
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
194-533 |
3.91e-10 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 62.10 E-value: 3.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 194 TSGTTGFPKGATLSHHNILNNGYFVGELCNYTEEDkVCIPVPFYHCFGMVMGNLACTSHGACMVI-PAPAFDPRATLEAV 272
Cdd:cd17654 126 TSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSED-ILFLTSPLTFDPSVVEIFLSLSSGATLLIvPTSVKVLPSKLADI 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 273 AAER--CTSLYGVPTMFiAELNHPDFGEFDLS---SLRTGIMAGSPCPVEVMKQVIDRMGMaEVSIC--YGMTETSPVST 345
Cdd:cd17654 205 LFKRhrITVLQATPTLF-RRFGSQSIKSTVLSatsSLRVLALGGEPFPSLVILSSWRGKGN-RTRIFniYGITEVSCWAL 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 346 QTRaddsIERRVSTVgRVGPHLEVKVVdpESGLTVPRGEPGELCTRGYSvMLGYWEQPDKTAEAIdaarWMHTGDLaVMD 425
Cdd:cd17654 283 AYK----VPEEDSPV-QLGSPLLGTVI--EVRDQNGSEGTGQVFLGGLN-RVCILDDEVTVPKGT----MRATGDF-VTV 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 426 GDGYVNITGRIKDMVIRGGENLYPREIEEFLYTHPDVLDAQVIGVPDEKygeeLMAWVRMREGASPLTAEKVREfcsgKL 505
Cdd:cd17654 350 KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQR----LIAFIVGESSSSRIHKELQLT----LL 421
|
330 340
....*....|....*....|....*...
gi 522130465 506 AHYKIPRYVHVVDEFPMTVTGKVRKVEM 533
Cdd:cd17654 422 SSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
51-462 |
2.04e-05 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 47.34 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 51 TYRELAGEVTALALGLVAR-GIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPAYRSHELEYVLDQAGIRLLVASD 129
Cdd:cd05905 16 TWGKLLSRAEKIAAVLQKKvGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVALTVE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 130 KFkTSDYPAMVEEVREKCARLEHVVvlggesWQELMDAG----RRGDPAQLAHLRAGLSADDPINIQYTSGTTGFPKGAT 205
Cdd:cd05905 96 AC-LKGLPKKLLKSKTAAEIAKKKG------WPKILDFVkipkSKRSKLKKWGPHPPTRDGDTAYIEYSFSSDGSLSGVA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 206 LSHHNILNNGYFVGELCNYTEEDKVCIPVPFYHCFGMVMGNLACTSHGACMVIPAPAF---DPRATLEAVAAERCTSLYG 282
Cdd:cd05905 169 VSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELmktNPLLWLQTLSQYKVRDAYV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 283 -VPTMFIAELNHPDFGEF------DLSSLRTgIMAgsPCPVEVMKQVIDR-------------------MGMAEVSICYG 336
Cdd:cd05905 249 kLRTLHWCLKDLSSTLASlknrdvNLSSLRM-CMV--PCENRPRISSCDSflklfqtlglspravstefGTRVNPFICWQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 337 MTETSPVSTQ-----------TRADDSIERRVSTV---GRVGPHLEVKVVDPESGLTVPRGEPGELCTRGYSVMLGYWEQ 402
Cdd:cd05905 326 GTSGPEPSRVyldmralrhgvVRLDERDKPNSLPLqdsGKVLPGAQVAIVNPETKGLCKDGEIGEIWVNSPANASGYFLL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 403 PDKT------------AEAIDAARWMHTGDL----------AVMDGDGYVNITGRIKD-MVIRgGENLYPREIEE-FLYT 458
Cdd:cd05905 406 DGETndtfkvfpstrlSTGITNNSYARTGLLgflrptkctdLNVEEHDLLFVVGSIDEtLEVR-GLRHHPSDIEAtVMRV 484
|
....
gi 522130465 459 HPDV 462
Cdd:cd05905 485 HPYR 488
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
331-440 |
3.04e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 47.02 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 331 VSIC--YGMTETS-PVSTQTRADDSIErrvSTVGRVGPHLEVKVVDPE---SGLTVPRGEpgeLCTRGYSVMLGYWEQPD 404
Cdd:PTZ00342 487 VNYYqgYGLTETTgPIFVQHADDNNTE---SIGGPISPNTKYKVRTWEtykATDTLPKGE---LLIKSDSIFSGYFLEKE 560
|
90 100 110
....*....|....*....|....*....|....*.
gi 522130465 405 KTAEAIDAARWMHTGDLAVMDGDGYVNITGRIKDMV 440
Cdd:PTZ00342 561 QTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLV 596
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
65-525 |
4.43e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 40.09 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 65 GLVARGIGKGDRVGIWSPNRAEWTFLQYATAKIGAILVNINPayrSHELEYVLDQAGIRLLVASdkfktsdyPAMVEEVR 144
Cdd:PRK07868 488 GLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLMPP---DTDLAAAVRLGGVTEIITD--------PTNLEAAR 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 145 EKCARlehVVVLGG--------ESWQELMDAgRRGDPAQLAHLR-----AGLSADDPINIQYTSGTTGFPKGATlsHHNI 211
Cdd:PRK07868 557 QLPGR---VLVLGGgesrdldlPDDADVIDM-EKIDPDAVELPGwyrpnPGLARDLAFIAFSTAGGELVAKQIT--NYRW 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 212 LNNGYFVGELCNYTEEDKV-CIPvPFYHCFGMvMGNLACTSHGACMVIPAPAFDPRATLEAVAAerctslYGVP------ 284
Cdd:PRK07868 631 ALSAFGTASAAALDRRDTVyCLT-PLHHESGL-LVSLGGAVVGGSRIALSRGLDPDRFVQEVRQ------YGVTvvsytw 702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 285 TMFIAELNHPDFGEFDLSSLRTGImaGSPCPVEVMKQVIDRMGMAEVSICYGMTETSPVSTQTRAD--DSIERRVSTVGR 362
Cdd:PRK07868 703 AMLREVVDDPAFVLHGNHPVRLFI--GSGMPTGLWERVVEAFAPAHVVEFFATTDGQAVLANVSGAkiGSKGRPLPGAGR 780
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 363 VgphlEVKVVDPESGLT-------VPRGEPGELctrgySVMLGYWEQP-DKTAEAI-----DAARWMHTGDLAVMDGDGY 429
Cdd:PRK07868 781 V----ELAAYDPEHDLIleddrgfVRRAEVNEV-----GVLLARARGPiDPTASVKrgvfaPADTWISTEYLFRRDDDGD 851
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 430 VNITGRiKDMVIRGgenlyPREIeefLYTHPdVLDA--QVIGVPDE-KYGEEL------MAWVRMREGASpLTAEKVREF 500
Cdd:PRK07868 852 YWLVDR-RGSVIRT-----ARGP---VYTEP-VTDAlgRIGGVDLAvTYGVEVggrqlaVAAVTLRPGAA-ITAADLTEA 920
|
490 500
....*....|....*....|....*
gi 522130465 501 CSGkLAHYKIPRYVHVVDEFPMTVT 525
Cdd:PRK07868 921 LAS-LPVGLGPDIVHVVPEIPLSAT 944
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
98-317 |
7.43e-03 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 39.03 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 98 GAILVNINPAYRSHELEYVLDQAGIRLLVASDKF-----KTSDYPAMVEEVREKCARLEhvvVLGGESWQELmdagRRGD 172
Cdd:PLN03051 18 GCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVlrggrALPLYSKVVEAAPAKAIVLP---AAGEPVAVPL----REQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 173 PAQLAHLRAG---------------LSADDPINIQYTSGTTGFPKGATLSHHNIL---NNGYFVGELcnyTEEDKVCIPV 234
Cdd:PLN03051 91 LSWCDFLGVAaaqgsvggneyspvyAPVESVTNILFSSGTTGEPKAIPWTHLSPLrcaSDGWAHMDI---QPGDVVCWPT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522130465 235 PfyhcFGMVMGNL---ACTSHGACMVIPAPAFDPRATLEAVAAERCTSLYGVPTMFIA--ELNHPDFGEFDLSSLRTGIM 309
Cdd:PLN03051 168 N----LGWMMGPWllySAFLNGATLALYGGAPLGRGFGKFVQDAGVTVLGLVPSIVKAwrHTGAFAMEGLDWSKLRVFAS 243
|
....*...
gi 522130465 310 AGSPCPVE 317
Cdd:PLN03051 244 TGEASAVD 251
|
|
| |
