|
Name |
Accession |
Description |
Interval |
E-value |
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
2-498 |
0e+00 |
|
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: 807.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 2 QTVNEMLRRAATRAPDHCALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVP 81
Cdd:cd05923 1 QTVFEMLRRAASRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 82 ALLNPRLKSAELAELIKRGEMTAAVIAVGRQVADAIFQSGsgARIIFLGDLVRDGEPYSYGPPIEDPQREPAQPAFIFYT 161
Cdd:cd05923 81 ALINPRLKAAELAELIERGEMTAAVIAVDAQVMDAIFQSG--VRVLALSDLVGLGEPESAGPLIEDPPREPEQPAFVFYT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 162 SGTTGLPKAAIIPQRAAESRVLFMSTQVGLRHGRHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFRPVDALQLVQ 241
Cdd:cd05923 159 SGTTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPADALKLIE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 242 QEQVTSLFATPThlDALAAAAAHAGSSLKLDSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTEAMNSLYMRQPKTG 321
Cdd:cd05923 239 QERVTSLFATPT--HLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAMNSLYMRDARTG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 322 TEMAPGFFSEVRIVRIGGGVDEIVANGEEGELIVAAS-DSAFVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGR 400
Cdd:cd05923 317 TEMRPGFFSEVRIVRIGGSPDEALANGEEGELIVAAAaDAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 401 VDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGeTLSADALDTFCRSSELADFKRPKRYF 480
Cdd:cd05923 397 VDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG-TLSADELDQFCRASELADFKRPRRYF 475
|
490
....*....|....*...
1T5D_X 481 ILDQLPKNALNKVLRRQL 498
Cdd:cd05923 476 FLDELPKNAMNKVLRRQL 493
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
4-502 |
1.49e-133 |
|
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: 394.18 E-value: 1.49e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 4 VNEMLRRAATRAPDHCALAVPARglRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPAL 83
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGR--RLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 84 LNPRLKSAELAELIKRgemtaaviavgrqvadaifqsgSGARIIFLgdlvrdgepysygppiedpqrepaqpAFIFYTSG 163
Cdd:COG0318 79 LNPRLTAEELAYILED----------------------SGARALVT--------------------------ALILYTSG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 164 TTGLPKAAIIPQRAAESRVLFMSTQVGLRHGrhNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFRPVDALQLVQQE 243
Cdd:COG0318 111 TTGRPKGVMLTHRNLLANAAAIAAALGLTPG--DVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVLELIERE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 244 QVTSLFATPTHLDALAAAAAHAGssLKLDSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTEA-----MNSLYMRQP 318
Cdd:COG0318 189 RVTVLFGVPTMLARLLRHPEFAR--YDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETspvvtVNPEDPGER 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 319 KTGTEMAPGFFSEVRIVRIGGgvdEIVANGEEGELIVAaSDSAFVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRIL 398
Cdd:COG0318 267 RPGSVGRPLPGVEVRIVDEDG---RELPPGEVGEIVVR-GPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 399 GRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCRsSELADFKRPKR 478
Cdd:COG0318 343 GRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLR-ERLARYKVPRR 421
|
490 500
....*....|....*....|....
1T5D_X 479 YFILDQLPKNALNKVLRRQLVQQV 502
Cdd:COG0318 422 VEFVDELPRTASGKIDRRALRERY 445
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
8-495 |
7.68e-107 |
|
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: 325.33 E-value: 7.68e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 8 LRRAATRAPDhcALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPR 87
Cdd:cd17631 1 LRRRARRHPD--RTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 88 LKSAELAElikrgemtaaviavgrQVADaifqsgSGARIIFlgdlvrdgepysygppiedpqrepAQPAFIFYTSGTTGL 167
Cdd:cd17631 79 LTPPEVAY----------------ILAD------SGAKVLF------------------------DDLALLMYTSGTTGR 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 168 PKAAIIPQRAAESRVlfMSTQVGLRHGRHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFRPVDALQLVQQEQVTS 247
Cdd:cd17631 113 PKGAMLTHRNLLWNA--VNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIERHRVTS 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 248 LFATPTHLDALAAAAAHagSSLKLDSLRHVTFAGATMPDAVLETVhQHLPGEKVNIYGTTEAMNSLYMRQP-----KTGT 322
Cdd:cd17631 191 FFLVPTMIQALLQHPRF--ATTDLSSLRAVIYGGAPMPERLLRAL-QARGVKFVQGYGMTETSPGVTFLSPedhrrKLGS 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 323 EMAPGFFSEVRIVRIGGgvdEIVANGEEGElIVAASDSAFVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGRVD 402
Cdd:cd17631 268 AGRPVFFVEVRIVDPDG---REVPPGEVGE-IVVRGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKK 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 403 DMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCRsSELADFKRPKRYFIL 482
Cdd:cd17631 344 DMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCR-ERLARYKIPKSVEFV 422
|
490
....*....|...
1T5D_X 483 DQLPKNALNKVLR 495
Cdd:cd17631 423 DALPRNATGKILK 435
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
6-499 |
2.51e-106 |
|
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: 325.29 E-value: 2.51e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 6 EMLRRAATRAPDHCALAVParGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLN 85
Cdd:cd05936 3 DLLEEAARRFPDKTALIFM--GRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 86 PRLKSAELAELIKRGEMTAAVIAVGRQvadaifqsgsgariiflgDLVRDGEPYSYGPpiedpQREPAQPAFIFYTSGTT 165
Cdd:cd05936 81 PLYTPRELEHILNDSGAKALIVAVSFT------------------DLLAAGAPLGERV-----ALTPEDVAVLQYTSGTT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 166 GLPKAAIIPQRAAESRVLFMSTQVGLRHGRHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFRPVDALQLVQQEQV 245
Cdd:cd05936 138 GVPKGAMLTHRNLVANALQIKAWLEDLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGVLKEIRKHRV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 246 TSLFATPTHLDALAAAAAHAGSSLKldSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTEA-----MNSLYmRQPKT 320
Cdd:cd05936 218 TIFPGVPTMYIALLNAPEFKKRDFS--SLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETspvvaVNPLD-GPRKP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 321 GT--EMAPGffSEVRIVRIGGgvdEIVANGEEGELIVAAsDSAFVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRIL 398
Cdd:cd05936 295 GSigIPLPG--TEVKIVDDDG---EELPPGEVGELWVRG-PQVMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 399 GRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCRsSELADFKRPKR 478
Cdd:cd05936 369 DRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCR-EQLAGYKVPRQ 447
|
490 500
....*....|....*....|.
1T5D_X 479 YFILDQLPKNALNKVLRRQLV 499
Cdd:cd05936 448 VEFRDELPKSAVGKILRRELR 468
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
154-494 |
1.34e-101 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 308.45 E-value: 1.34e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 154 QPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGLRHgrHNVVLGLMPLYHVVGFFAVLvAALALDGTYVVVEEFRP 233
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTE--GDVFLSTLPLFHIGGLFGLL-GALLAGGTVVLLPKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 234 VDALQLVQQEQVTSLFATPTHLDALAAAAAHAGssLKLDSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTEAM--- 310
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKAPESAG--YDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGgtv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 311 --NSLYMRQPKTGTEMAPGFFSEVRIVRIGGGvdeIVANGEEGElIVAASDSAFVGYLNQPQATAEKLQDGWYRTSDVAV 388
Cdd:cd04433 156 atGPPDDDARKPGSVGRPVPGVEVRIVDPDGG---ELPPGEIGE-LVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 389 WTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCRsS 468
Cdd:cd04433 232 LDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVR-E 310
|
330 340
....*....|....*....|....*.
1T5D_X 469 ELADFKRPKRYFILDQLPKNALNKVL 494
Cdd:cd04433 311 RLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1-498 |
3.51e-100 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 310.68 E-value: 3.51e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 1 MQTVNEMLRRAATRAPDHcaLAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAV 80
Cdd:PRK07656 4 WMTLPELLARAARRFGDK--EAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 81 PALLNPRLKSAELAELIKRGEmTAAVIAVG------RQVADA--------IFQSGSGA----RIIFLGDLVRDGEPYSYG 142
Cdd:PRK07656 82 VVPLNTRYTADEAAYILARGD-AKALFVLGlflgvdYSATTRlpalehvvICETEEDDphteKMKTFTDFLAAGDPAERA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 143 PPIEdpqrePAQPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGLRHG-RHNVVLglmPLYHVVGFFAVLVAALAL 221
Cdd:PRK07656 161 PEVD-----PDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGdRYLAAN---PFFHVFGYKAGVNAPLMR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 222 DGTYVVVEEFRPVDALQLVQQEQVTSLFATPTHLDALAAAAAhaGSSLKLDSLRHVTFAGATMPDAVLETVHQHLPGEKV 301
Cdd:PRK07656 233 GATILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPD--RSAEDLSSLRLAVTGAASMPVALLERFESELGVDIV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 302 -NIYGTTEA-----MNSLYmRQPKT-----GTEMaPGFfsEVRIVRIGGgvdEIVANGEEGELIVAASdSAFVGYLNQPQ 370
Cdd:PRK07656 311 lTGYGLSEAsgvttFNRLD-DDRKTvagtiGTAI-AGV--ENKIVNELG---EEVPVGEVGELLVRGP-NVMKGYYDDPE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 371 ATAEKL-QDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVV 449
Cdd:PRK07656 383 ATAAAIdADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVV 462
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
1T5D_X 450 PRLGETLSADALDTFCRsSELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:PRK07656 463 LKPGAELTEEELIAYCR-EHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
2-501 |
1.93e-94 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 296.07 E-value: 1.93e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 2 QTVNEMLRRAATRAPDHcaLAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVP 81
Cdd:PRK08316 11 QTIGDILRRSARRYPDK--TALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 82 ALLNPRLKSAELAELIKRGEMTAAVIAVG-RQVADAIFQSGSGARIIFL--------GDLVRDGEPYSYGPPIEDPQREP 152
Cdd:PRK08316 89 VPVNFMLTGEELAYILDHSGARAFLVDPAlAPTAEAALALLPVDTLILSlvlggreaPGGWLDFADWAEAGSVAEPDVEL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 153 A--QPAFIFYTSGTTGLPKAAIIPQRA--AEsrvlFMSTQVGLRHGRHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVV 228
Cdd:PRK08316 169 AddDLAQILYTSGTESLPKGAMLTHRAliAE----YVSCIVAGDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVIL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 229 EEFRPVDALQLVQQEQVTSLFATPTHLDalaaaaahagsSL---------KLDSLRHVTFAGATMPDAVLETVHQHLPGE 299
Cdd:PRK08316 245 DAPDPELILRTIEAERITSFFAPPTVWI-----------SLlrhpdfdtrDLSSLRKGYYGASIMPVEVLKELRERLPGL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 300 KV-NIYGTTEaMNSLYM-RQP-----KTGTEMAPGFFSEVRIVRIGGgvdEIVANGEEGElIVAASDSAFVGYLNQPQAT 372
Cdd:PRK08316 314 RFyNCYGQTE-IAPLATvLGPeehlrRPGSAGRPVLNVETRVVDDDG---NDVAPGEVGE-IVHRSPQLMLGYWDDPEKT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 373 AEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRL 452
Cdd:PRK08316 389 AEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKA 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
1T5D_X 453 GETLSADALDTFCRSSeLADFKRPKRYFILDQLPKNALNKVLRRQLVQQ 501
Cdd:PRK08316 469 GATVTEDELIAHCRAR-LAGFKVPKRVIFVDELPRNPSGKILKRELRER 516
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
1-503 |
2.49e-93 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 293.25 E-value: 2.49e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 1 MQTVNEMLRRAATRAPDhcALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAV 80
Cdd:PRK06187 5 PLTIGRILRHGARKHPD--KEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 81 PALLNPRLKSAELAELIKRGEmtAAVIAVGRQVADAIF----QSGSGARIIFLGDLVRDGEPYSYG----------PPIE 146
Cdd:PRK06187 83 LHPINIRLKPEEIAYILNDAE--DRVVLVDSEFVPLLAailpQLPTVRTVIVEGDGPAAPLAPEVGeyeellaaasDTFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 147 DPQREPAQPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGLRHGrhNVVLGLMPLYHVVGFfAVLVAALALDGTYV 226
Cdd:PRK06187 161 FPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRD--DVYLVIVPMFHVHAW-GLPYLALMAGAKQV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 227 VVEEFRPVDALQLVQQEQVTSLFATPTHLDALAAAAAHAGssLKLDSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGT 306
Cdd:PRK06187 238 IPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYF--VDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 307 TE-----AMNSL---------YMRqpKTGTemaPGFFSEVRIVRIGGgvDEIVANGEE-GELIVAAsDSAFVGYLNQPQA 371
Cdd:PRK06187 316 TEtspvvSVLPPedqlpgqwtKRR--SAGR---PLPGVEARIVDDDG--DELPPDGGEvGEIIVRG-PWLMQGYWNRPEA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 372 TAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPR 451
Cdd:PRK06187 388 TAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLK 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
1T5D_X 452 LGETLSADALDTFCRsSELADFKRPKRYFILDQLPKNALNKVLRRQLVQQVS 503
Cdd:PRK06187 468 PGATLDAKELRAFLR-GRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQYA 518
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
8-408 |
4.18e-83 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 263.40 E-value: 4.18e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 8 LRRAATRAPDHCALaVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPR 87
Cdd:pfam00501 1 LERQAARTPDKTAL-EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 88 LKSAELAELIKRGEMTAAVIAVGRQVADAIFQSGSGARI----------IFLGDLVRDGEPYSYGPPIEDPQREPAQPAF 157
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVklvlvldrdpVLKEEPLPEEAKPADVPPPPPPPPDPDDLAY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 158 IFYTSGTTGLPKAAIIPQRAAESRVLFMS--TQVGLRHGRHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFRPVD 235
Cdd:pfam00501 160 IIYTSGTTGKPKGVMLTHRNLVANVLSIKrvRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPALD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 236 A---LQLVQQEQVTSLFATPTHLDALAAAAAHAGssLKLDSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTEA--- 309
Cdd:pfam00501 240 PaalLELIERYKVTVLYGVPTLLNMLLEAGAPKR--ALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETtgv 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 310 -MNSLYM--RQPKTGTEMAPGFFSEVRIVRIGGGvdEIVANGEEGELIVaASDSAFVGYLNQPQATAEKL-QDGWYRTSD 385
Cdd:pfam00501 318 vTTPLPLdeDLRSLGSVGRPLPGTEVKIVDDETG--EPVPPGEPGELCV-RGPGVMKGYLNDPELTAEAFdEDGWYRTGD 394
|
410 420
....*....|....*....|...
1T5D_X 386 VAVWTPEGTVRILGRVDDMIISG 408
Cdd:pfam00501 395 LGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
16-500 |
1.98e-80 |
|
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: 258.78 E-value: 1.98e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 16 PDHCALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAE 95
Cdd:cd05926 1 PDAPALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 96 LIKRGEMTAAVIAVGRQVADAIFQSGSGARIIFLG------DLVRDGEPYSYGPPIEDPQREPAQP-----AFIFYTSGT 164
Cdd:cd05926 81 YLADLGSKLVLTPKGELGPASRAASKLGLAILELAldvgvlIRAPSAESLSNLLADKKNAKSEGVPlpddlALILHTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 165 TGLPKAAIIPQRAAESRVLFMSTqvGLRHGRHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFRPVDALQLVQQEQ 244
Cdd:cd05926 161 TGRPKGVPLTHRNLAASATNITN--TYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDVRDYN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 245 VTSLFATPTHLDALAAAAAHAGSSlKLDSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTEA-----MNSLYMRQPK 319
Cdd:cd05926 239 ATWYTAVPTIHQILLNRPEPNPES-PPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAahqmtSNPLPPGPRK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 320 TGTeMAPGFFSEVRIVRIGGgvdEIVANGEEGElIVAASDSAFVGYLNQPQATAEK-LQDGWYRTSDVAVWTPEGTVRIL 398
Cdd:cd05926 318 PGS-VGKPVGVEVRILDEDG---EILPPGVVGE-ICLRGPNVTRGYLNNPEANAEAaFKDGWFRTGDLGYLDADGYLFLT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 399 GRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCRsSELADFKRPKR 478
Cdd:cd05926 393 GRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCR-KHLAAFKVPKK 471
|
490 500
....*....|....*....|..
1T5D_X 479 YFILDQLPKNALNKVLRRQLVQ 500
Cdd:cd05926 472 VYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1-503 |
3.50e-78 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 252.58 E-value: 3.50e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 1 MQTVNEMLRRAATRAPDHCALAvpARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAV 80
Cdd:PRK03640 1 METMPNWLKQRAFLTPDRTAIE--FEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 81 PALLNPRLKSAELAELIKrgemTAAVIAVgrqVADAIFQS--GSGARIIFlGDLVrdGEPYSYGPPIEDPQREPAqpAFI 158
Cdd:PRK03640 79 AVLLNTRLSREELLWQLD----DAEVKCL---ITDDDFEAklIPGISVKF-AELM--NGPKEEAEIQEEFDLDEV--ATI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 159 FYTSGTTGLPKAAIipQR------AAESRVLFMstqvGLRHgrHNVVLGLMPLYHVVGFfAVLVAALALDGTYVVVEEFR 232
Cdd:PRK03640 147 MYTSGTTGKPKGVI--QTygnhwwSAVGSALNL----GLTE--DDCWLAAVPIFHISGL-SILMRSVIYGMRVVLVEKFD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 233 PVDALQLVQQEQVTSLFATPTHLDALAAAAAHAGSSlklDSLRHVTFAGATMPDAVLET-VHQHLPgeKVNIYGTTE--- 308
Cdd:PRK03640 218 AEKINKLLQTGGVTIISVVSTMLQRLLERLGEGTYP---SSFRCMLLGGGPAPKPLLEQcKEKGIP--VYQSYGMTEtas 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 309 ---AMNSLYMRQpKTGTEMAPGFFSEVRIVRIGggvdEIVANGEEGElIVAASDSAFVGYLNQPQATAEKLQDGWYRTSD 385
Cdd:PRK03640 293 qivTLSPEDALT-KLGSAGKPLFPCELKIEKDG----VVVPPFEEGE-IVVKGPNVTKGYLNREDATRETFQDGWFKTGD 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 386 VAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVprLGETLSADALDTFC 465
Cdd:PRK03640 367 IGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVV--KSGEVTEEELRHFC 444
|
490 500 510
....*....|....*....|....*....|....*...
1T5D_X 466 RsSELADFKRPKRYFILDQLPKNALNKVLRRQLVQQVS 503
Cdd:PRK03640 445 E-EKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVE 481
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
30-494 |
1.45e-77 |
|
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: 251.36 E-value: 1.45e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 30 LTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIKRGEMTAAVIAV 109
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 110 GRQ--VADAIFQSGSGARIIFLGDLV------------RDGEPYSYGPPieDPQREPAQPAFIFYTSGTTGLPKAAIIPQ 175
Cdd:cd05911 91 DGLekVKEAAKELGPKDKIIVLDDKPdgvlsiedllspTLGEEDEDLPP--PLKDGKDDTAAILYSSGTTGLPKGVCLSH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 176 RAAESRVLFMSTQVGLRHGRHNVVLGLMPLYHVVGFFAvLVAALALDGTYVVVEEFRPVDALQLVQQEQVTSLFATPTHL 255
Cdd:cd05911 169 RNLIANLSQVQTFLYGNDGSNDVILGFLPLYHIYGLFT-TLASLLNGATVIIMPKFDSELFLDLIEKYKITFLYLVPPIA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 256 DALAAAAAHAGSSLKldSLRHVTFAGATMPDAVLETVHQHLPGEKVN-IYGTTE-----AMNSLYMRQPKTGTEMAPGFf 329
Cdd:cd05911 248 AALAKSPLLDKYDLS--SLRVILSGGAPLSKELQELLAKRFPNATIKqGYGMTEtggilTVNPDGDDKPGSVGRLLPNV- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 330 sEVRIVRIGGGvdEIVANGEEGELIVAaSDSAFVGYLNQPQATAEKL-QDGWYRTSDVAVWTPEGTVRILGRVDDMIISG 408
Cdd:cd05911 325 -EAKIVDDDGK--DSLGPNEPGEICVR-GPQVMKGYYNNPEATKETFdEDGWLHTGDIGYFDEDGYLYIVDRKKELIKYK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 409 GENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCRSSeLADFKR-PKRYFILDQLPK 487
Cdd:cd05911 401 GFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKK-VASYKQlRGGVVFVDEIPK 479
|
....*..
1T5D_X 488 NALNKVL 494
Cdd:cd05911 480 SASGKIL 486
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
6-498 |
5.37e-76 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 249.26 E-value: 5.37e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 6 EMLRRAATRAPDHCAL---AVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPA 82
Cdd:COG0365 13 NCLDRHAEGRGDKVALiweGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 83 LLNPRLKSAELAELIKRGEMTAAVIAVG-----------RQVADAIFQSGSGARIIFLGDLVRDGEP---YSY------- 141
Cdd:COG0365 93 PVFPGFGAEALADRIEDAEAKVLITADGglrggkvidlkEKVDEALEELPSLEHVIVVGRTGADVPMegdLDWdellaaa 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 142 GPPIEDPQREPAQPAFIFYTSGTTGLPKAAIIPQRAAesrVLFMSTQVGLrhgrhnvVLGLMP--LYH-------VVGFF 212
Cdd:COG0365 173 SAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGY---LVHAATTAKY-------VLDLKPgdVFWctadigwATGHS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 213 AVLVAALALDGTyVVVEEFRPV--DA---LQLVQQEQVTSLFATPTHLDALAAAAAHAGSSLKLDSLRHVTFAGATMPDA 287
Cdd:COG0365 243 YIVYGPLLNGAT-VVLYEGRPDfpDPgrlWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAGEPLNPE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 288 VLETVHQHLPGEKVNIYGTTEA----MNSLYMRQPKTGtEM---APGFfsEVRIVrigggvDE---IVANGEEGELIVAA 357
Cdd:COG0365 322 VWEWWYEAVGVPIVDGWGQTETggifISNLPGLPVKPG-SMgkpVPGY--DVAVV------DEdgnPVPPGEEGELVIKG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 358 SD-SAFVGYLNQPQATAEKLQD---GWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVI 433
Cdd:COG0365 393 PWpGMFRGYWNDPERYRETYFGrfpGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVV 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1T5D_X 434 GLADQRWGQSVTACVVPRLGETLS---ADALDTFCRsSELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:COG0365 473 GVPDEIRGQVVKAFVVLKPGVEPSdelAKELQAHVR-EELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
3-497 |
1.46e-74 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 245.68 E-value: 1.46e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 3 TVNEMLRRAATRAPDHCALAVpaRGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPA 82
Cdd:PRK05605 33 TLVDLYDNAVARFGDRPALDF--FGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 83 LLNPRLKSAELAELIKrgEMTAAVIAVGRQVADAIFQ--SGSGARIIFLGDLVR-------------------------- 134
Cdd:PRK05605 111 EHNPLYTAHELEHPFE--DHGARVAIVWDKVAPTVERlrRTTPLETIVSVNMIAampllqrlalrlpipalrkaraaltg 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 135 ------------DGEPYSYGPPIEDPQREPAQPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQV-GLRHGRHnVVLG 201
Cdd:PRK05605 189 papgtvpwetlvDAAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVpGLGDGPE-RVLA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 202 LMPLYHVVGFFAVLVAALALDGTYVVVEEFRPVDALQLVQQEQVTSLFATPTHLDALAAAAAHAGSSLKldSLRhVTFAG 281
Cdd:PRK05605 268 ALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLS--GVR-NAFSG 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 282 A-TMPDAVLETVHQHLPGEKVNIYGTTEA--------MNSlyMRQPktGTEMAPGFFSEVRIVRiGGGVDEIVANGEEGE 352
Cdd:PRK05605 345 AmALPVSTVELWEKLTGGLLVEGYGLTETspiivgnpMSD--DRRP--GYVGVPFPDTEVRIVD-PEDPDETMPDGEEGE 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 353 LIVAASdSAFVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVV 432
Cdd:PRK05605 420 LLVRGP-QVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAV 498
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
1T5D_X 433 IGLADQRWGQSVTACVVPRLGETLSADALDTFCRsSELADFKRPKRYFILDQLPKNALNKVLRRQ 497
Cdd:PRK05605 499 VGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCR-EHLTRYKVPRRFYHVDELPRDQLGKVRRRE 562
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
2-501 |
1.12e-73 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 243.18 E-value: 1.12e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 2 QTVNEMLRRAATRAPDHCALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVP 81
Cdd:PRK08315 16 QTIGQLLDRTAARYPDREALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 82 ALLNPRLKSAELAELIKRGEMTAAVIAVG----------RQVADAIFQSGSGA----------RIIFLG----------- 130
Cdd:PRK08315 96 VTINPAYRLSELEYALNQSGCKALIAADGfkdsdyvamlYELAPELATCEPGQlqsarlpelrRVIFLGdekhpgmlnfd 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 131 DLVRDGEPYSYgPPIEDPQRE--PAQPAFIFYTSGTTGLPKAAIipqraaesrvlfmstqvgLRHgrHNVV--------- 199
Cdd:PRK08315 176 ELLALGRAVDD-AELAARQATldPDDPINIQYTSGTTGFPKGAT------------------LTH--RNILnngyfigea 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 200 LGL---------MPLYHVVGF-FAVLvAALALDGTYVV-VEEFRPVDALQLVQQEQVTSLFATPTHLDALAAAAAHagSS 268
Cdd:PRK08315 235 MKLteedrlcipVPLYHCFGMvLGNL-ACVTHGATMVYpGEGFDPLATLAAVEEERCTALYGVPTMFIAELDHPDF--AR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 269 LKLDSLRHVTFAGATMPDAVLETVHQHLPGEKVNI-YGTTEAmnSLYMRQPKT-----------GTEMApgfFSEVRIVR 336
Cdd:PRK08315 312 FDLSSLRTGIMAGSPCPIEVMKRVIDKMHMSEVTIaYGMTET--SPVSTQTRTddplekrvttvGRALP---HLEVKIVD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 337 IGGGvdEIVANGEEGELiVAASDSAFVGYLNQPQATAEKL-QDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPS 415
Cdd:PRK08315 387 PETG--ETVPRGEQGEL-CTRGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 416 EIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCRsSELADFKRPKRYFILDQLPKNALNKV-- 493
Cdd:PRK08315 464 EIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCR-GKIAHYKIPRYIRFVDEFPMTVTGKIqk 542
|
570
....*....|
1T5D_X 494 --LRRQLVQQ 501
Cdd:PRK08315 543 fkMREMMIEE 552
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
30-500 |
1.03e-72 |
|
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: 236.47 E-value: 1.03e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 30 LTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAElikrgemtaaviav 109
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAF-------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 110 grQVADAifqsgsgariiflgdlvrdgepysygppieDPQREPAqpAFIFYTSGTTGLPKAAIIPQR----AAESRVLFM 185
Cdd:cd05912 68 --QLKDS------------------------------DVKLDDI--ATIMYTSGTTGKPKGVQQTFGnhwwSAIGSALNL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 186 stqvGLRhgRHNVVLGLMPLYHVVGFfAVLVAALALDGTYVVVEEFRPVDALQLVQQEQVTSLFATPTHLDALAAAAAHA 265
Cdd:cd05912 114 ----GLT--EDDNWLCALPLFHISGL-SILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEG 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 266 GSSlkldSLRHVTFAGATMPDAVLETVHQH-LPgeKVNIYGTTE------AMNSLYMRQpKTGTEMAPGFFSEVRIVRIG 338
Cdd:cd05912 187 YPN----NLRCILLGGGPAPKPLLEQCKEKgIP--VYQSYGMTEtcsqivTLSPEDALN-KIGSAGKPLFPVELKIEDDG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 339 GgvdeivANGEEGELIVAASdSAFVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIE 418
Cdd:cd05912 260 Q------PPYEVGEILLKGP-NVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIE 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 419 RVLGTAPGVTEVVVIGLADQRWGQSVTACVVprLGETLSADALDTFCRsSELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:cd05912 333 EVLLSHPAIKEAGVVGIPDDKWGQVPVAFVV--SERPISEEELIAYCS-EKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
..
1T5D_X 499 VQ 500
Cdd:cd05912 410 KQ 411
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
2-502 |
1.62e-72 |
|
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: 239.28 E-value: 1.62e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 2 QTVNEMLRRAATRAPDHCALAVPARglRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVP 81
Cdd:COG1021 25 ETLGDLLRRRAERHPDRIAVVDGER--RLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 82 ALLNPRLKSAELAELIKRGEMTAAVIAVG------RQVADAIFQSGSGAR-IIFLGDlVRDGEPYS--YGPPIEDPQREP 152
Cdd:COG1021 103 VFALPAHRRAEISHFAEQSEAVAYIIPDRhrgfdyRALARELQAEVPSLRhVLVVGD-AGEFTSLDalLAAPADLSEPRP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 153 A--QPAFIFYTSGTTGLPKaaIIP----------QRAAESrvlfmstqVGLrhGRHNVVLGLMPLYH-----VVGFFAVL 215
Cdd:COG1021 182 DpdDVAFFQLSGGTTGLPK--LIPrthddylysvRASAEI--------CGL--DADTVYLAALPAAHnfplsSPGVLGVL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 216 VAAlaldGTYVVVEEFRPVDALQLVQQEQVTSLFATPTHLDALAAAAAHAGSslKLDSLRHVTFAGATMPDAVLETVHQH 295
Cdd:COG1021 250 YAG----GTVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRY--DLSSLRVLQVGGAKLSPELARRVRPA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 296 LPGEKVNIYGTTEAM-NslYMR-----------QpktGTEMAPGffSEVRIVrigGGVDEIVANGEEGELIVAASdSAFV 363
Cdd:COG1021 324 LGCTLQQVFGMAEGLvN--YTRlddpeevilttQ---GRPISPD--DEVRIV---DEDGNPVPPGEVGELLTRGP-YTIR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 364 GYLNQPQATAEKL-QDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQ 442
Cdd:COG1021 393 GYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGE 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 443 SVTACVVPRlGETLSADALDTFCRSSELADFKRPKRYFILDQLPKNALNKVLRRQLVQQV 502
Cdd:COG1021 473 RSCAFVVPR-GEPLTLAELRRFLRERGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAAL 531
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
1-504 |
5.78e-72 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 237.07 E-value: 5.78e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 1 MQTVNEMLRRAATRAPDHcaLAVPARGLRLTHAELRARVEAVAARL-HADGLRPQQRVAVVAPNSADVVIAILALHRLGA 79
Cdd:PRK06839 1 MQGIAYWIEKRAYLHPDR--IAIITEEEEMTYKQLHEYVSKVAAYLiYELNVKKGERIAILSQNSLEYIVLLFAIAKVEC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 80 VPALLNPRLKSAELAELIKRGEMTAAVIAVGRQVADAIFQSGSG-ARIIFLGDL--VRDGEPYSYGPPIEDpqrepaQPA 156
Cdd:PRK06839 79 IAVPLNIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYvQRVISITSLkeIEDRKIDNFVEKNES------ASF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 157 FIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGLRhgRHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFRPVDA 236
Cdd:PRK06839 153 IICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLT--MHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 237 LQLVQQEQVTSLFATPTHLDALAAAAAHAGSSLklDSLRHVTFAGATMPDAVLETVHQ--HLPGEKvniYGTTEAMNSLY 314
Cdd:PRK06839 231 LSMIEKHKVTVVMGVPTIHQALINCSKFETTNL--QSVRWFYNGGAPCPEELMREFIDrgFLFGQG---FGMTETSPTVF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 315 M-----RQPKTGTEMAPGFFSEVRIVRIGGGVdeiVANGEEGELIVAASDsAFVGYLNQPQATAEKLQDGWYRTSDVAVW 389
Cdd:PRK06839 306 MlseedARRKVGSIGKPVLFCDYELIDENKNK---VEVGEVGELLIRGPN-VMKEYWNRPDATEETIQDGWLCTGDLARV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 390 TPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCRsSE 469
Cdd:PRK06839 382 DEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCR-LF 460
|
490 500 510
....*....|....*....|....*....|....*
1T5D_X 470 LADFKRPKRYFILDQLPKNALNKVLRRQLVQQVSS 504
Cdd:PRK06839 461 LAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLKS 495
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
20-500 |
1.41e-70 |
|
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: 231.80 E-value: 1.41e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 20 ALAVPARGLRLTHAELRARVEAVAARLHA-DGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIK 98
Cdd:cd05941 2 RIAIVDDGDSITYADLVARAARLANRLLAlGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 99 RGEMTAAViavgrqvadaifqsgsgariiflgdlvrdgepysygppiedpqrepaQPAFIFYTSGTTGLPKAAIIPQRAA 178
Cdd:cd05941 82 DSEPSLVL-----------------------------------------------DPALILYTSGTTGRPKGVVLTHANL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 179 ESRVLFMSTQVGLRhgRHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFRPVDALQLVQQEQVTSLFATPT----- 253
Cdd:cd05941 115 AANVRALVDAWRWT--EDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRLMPSITVFMGVPTiytrl 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 254 -HLDALAAAAAHAGSSLKLDSLRHVTFAGATMPDAVLETVHQ---HLPGEKvniYGTTEA-MNslyMRQPKTGtEMAPGF 328
Cdd:cd05941 193 lQYYEAHFTDPQFARAAAAERLRLMVSGSAALPVPTLEEWEAitgHTLLER---YGMTEIgMA---LSNPLDG-ERRPGT 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 329 FS------EVRIVRIGGGvdEIVANGEEGELIVAaSDSAFVGYLNQPQATAEKLQ-DGWYRTSDVAVWTPEGTVRILGRV 401
Cdd:cd05941 266 VGmplpgvQARIVDEETG--EPLPRGEVGEIQVR-GPSVFKEYWNKPEATKEEFTdDGWFKTGDLGVVDEDGYYWILGRS 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 402 DDMII-SGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLG-ETLSADALDTFCRsSELADFKRPKRY 479
Cdd:cd05941 343 SVDIIkSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGaAALSLEELKEWAK-QRLAPYKRPRRL 421
|
490 500
....*....|....*....|.
1T5D_X 480 FILDQLPKNALNKVLRRQLVQ 500
Cdd:cd05941 422 ILVDELPRNAMGKVNKKELRK 442
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
29-498 |
2.01e-68 |
|
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: 225.72 E-value: 2.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 29 RLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIKRGEmtaavia 108
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAK------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 109 vgrqvadaifqsgsgARIIFLGDLVRDgepysygppiEDPQREPAQPAFIFYTSGTTGLPKAAIipqraAESRVLFMSTQ 188
Cdd:cd05903 74 ---------------AKVFVVPERFRQ----------FDPAAMPDAVALLLFTSGTTGEPKGVM-----HSHNTLSASIR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 189 VGLRH---GRHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFRPVDALQLVQQEQVTSLFATPTHLDALAAAAAHA 265
Cdd:cd05903 124 QYAERlglGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 266 GSSLKldSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTEAMNSLYMRQP-----KTGTEMAPGFFSEVRIVRIGGG 340
Cdd:cd05903 204 GEPLS--RLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPapedrRLYTDGRPLPGVEIKVVDDTGA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 341 VdeiVANGEEGElIVAASDSAFVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERV 420
Cdd:cd05903 282 T---LAPGVEGE-LLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDL 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1T5D_X 421 LGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCRSSELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:cd05903 358 LLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRL 435
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
7-501 |
9.11e-68 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 226.85 E-value: 9.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 7 MLRRAATRAPDHCALAVPARglRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNP 86
Cdd:PRK07470 12 FLRQAARRFPDRIALVWGDR--SWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 87 RLKSAELAELIKRGEMTAAVIAVG-RQVADAIFQSGSGARIIFLGDLVRDGEPYS------YGPPIEDPQREPAQPAFIF 159
Cdd:PRK07470 90 RQTPDEVAYLAEASGARAMICHADfPEHAAAVRAASPDLTHVVAIGGARAGLDYEalvarhLGARVANAAVDHDDPCWFF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 160 YTSGTTGLPKAAIIP--QRAaesrvlFMSTQ------VGLRHgrHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEF 231
Cdd:PRK07470 170 FTSGTTGRPKAAVLThgQMA------FVITNhladlmPGTTE--QDASLVVAPLSHGAGIHQLCQVARGAATVLLPSERF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 232 RPVDALQLVQQEQVTSLFATPTHldalaaaaahagssLKL------------DSLRHVTFAGATMPDAVLETVHQHLPGE 299
Cdd:PRK07470 242 DPAEVWALVERHRVTNLFTVPTI--------------LKMlvehpavdrydhSSLRYVIYAGAPMYRADQKRALAKLGKV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 300 KVNIYGTTEAmnslymrqpkTG--TEMAPGFFS-----EVRI-----------VRIGGGVDEIVANGEEGElIVAASDSA 361
Cdd:PRK07470 308 LVQYFGLGEV----------TGniTVLPPALHDaedgpDARIgtcgfertgmeVQIQDDEGRELPPGETGE-ICVIGPAV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 362 FVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWG 441
Cdd:PRK07470 377 FAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWG 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 442 QSVTACVVPRLGETLSADALDTFCrSSELADFKRPKRYFILDQLPKNALNKVLRRQLVQQ 501
Cdd:PRK07470 457 EVGVAVCVARDGAPVDEAELLAWL-DGKVARYKLPKRFFFWDALPKSGYGKITKKMVREE 515
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
31-498 |
1.19e-66 |
|
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: 221.17 E-value: 1.19e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 31 THAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIKRgemtaavIAVG 110
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLED-------LDVQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 111 RQVADAIFQsgsgARIIFLGDLVRDGEPYSYGPPIEdPQREPAQPAFIFYTSGTTGLPKAAiiPQRAAESRVLFMSTQVG 190
Cdd:TIGR01923 74 LLLTDSLLE----EKDFQADSLDRIEAAGRYETSLS-ASFNMDQIATLMFTSGTTGKPKAV--PHTFRNHYASAVGSKEN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 191 LRHGRHNVVLGLMPLYHVVGFfAVLVAALALDGTYVVVEEFRpvDALQLVQQEQVTSLFATPTHLDALAAaaahagSSLK 270
Cdd:TIGR01923 147 LGFTEDDNWLLSLPLYHISGL-SILFRWLIEGATLRIVDKFN--QLLEMIANERVTHISLVPTQLNRLLD------EGGH 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 271 LDSLRHVTFAGATMPDAVLETVHQH-LPgeKVNIYGTTEAMNSLYMRQP-----KTGTEMaPGFFSEVRIvriggGVDEI 344
Cdd:TIGR01923 218 NENLRKILLGGSAIPAPLIEEAQQYgLP--IYLSYGMTETCSQVTTATPemlhaRPDVGR-PLAGREIKI-----KVDNK 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 345 VANGEegelIVAASDSAFVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTA 424
Cdd:TIGR01923 290 EGHGE----IMVKGANLMKGYLYQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQH 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1T5D_X 425 PGVTEVVVIGLADQRWGQSVTACVVPRlgETLSADALDTFCrSSELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:TIGR01923 366 PGIQEAVVVPKPDAEWGQVPVAYIVSE--SDISQAKLIAYL-TEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
11-498 |
4.76e-66 |
|
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: 221.34 E-value: 4.76e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 11 AATRAPDHCALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKS 90
Cdd:cd05904 14 FASAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 91 AELAELIKrgEMTAAVIAVGRQVADAIfqSGSGARIIFLGDLVRDGEPYSYgPPIEDPQREPAQP-------AFIFYTSG 163
Cdd:cd05904 94 AEIAKQVK--DSGAKLAFTTAELAEKL--ASLALPVVLLDSAEFDSLSFSD-LLFEADEAEPPVVvikqddvAALLYSSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 164 TTGLPKAAIIPQRAAESRVLFMSTQVGLRHGRHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFRPVDALQLVQQE 243
Cdd:cd05904 169 TTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPRFDLEELLAAIERY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 244 QVTSLFATPTHLDALAAAAAHAGSSLKldSLRHVTFAGATMPDAVLETVHQHLPgeKVNI---YGTTE-----AMNSLYM 315
Cdd:cd05904 249 KVTHLPVVPPIVLALVKSPIVDKYDLS--SLRQIMSGAAPLGKELIEAFRAKFP--NVDLgqgYGMTEstgvvAMCFAPE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 316 RQPK----TGTeMAPGFfsEVRIVRIGGGvdEIVANGEEGELIVaASDSAFVGYLNQPQATAEKL-QDGWYRTSDVAVWT 390
Cdd:cd05904 325 KDRAkygsVGR-LVPNV--EAKIVDPETG--ESLPPNQTGELWI-RGPSIMKGYLNNPEATAATIdKEGWLHTGDLCYID 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 391 PEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCrSSEL 470
Cdd:cd05904 399 EDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFV-AKQV 477
|
490 500
....*....|....*....|....*...
1T5D_X 471 ADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:cd05904 478 APYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
29-498 |
8.19e-65 |
|
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: 216.19 E-value: 8.19e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 29 RLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIKRGEMTAAVIa 108
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 109 vgrqvadaifqsGSGariifLGDLvrdgepysygppiedpqrepaqpAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQ 188
Cdd:cd05935 80 ------------GSE-----LDDL-----------------------ALIPYTSGTTGLPKGCMHTHFSAAANALQSAVW 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 189 VGLRHGrhNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFRPVDALQLVQQEQVTSLFATPTHLDALAAAAAHAGSS 268
Cdd:cd05935 120 TGLTPS--DVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRD 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 269 LKldSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTEAMNSLYMR---QPKTGTEMAPGFFSEVRIVRIGGGvdEIV 345
Cdd:cd05935 198 LS--SLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNpplRPKLQCLGIP*FGVDARVIDIETG--REL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 346 ANGEEGElIVAASDSAFVGYLNQPQATAEKL--QDG--WYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVL 421
Cdd:cd05935 274 PPNEVGE-IVVRGPQIFKGYWNRPEETEESFieIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKL 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1T5D_X 422 GTAPGVTEVVVIGLADQRWGQSVTACVV--PRLGETLSADALDTFCRsSELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:cd05935 353 YKHPAI*EVCVISVPDERVGEEVKAFIVlrPEYRGKVTEEDIIEWAR-EQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
2-493 |
3.02e-64 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 218.10 E-value: 3.02e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 2 QTVNEMLRRAATRAPDHCALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVP 81
Cdd:PRK12583 18 QTIGDAFDATVARFPDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 82 ALLNPRLKSAELAELIKRGEMTAAVIAVGRQVAD--AIFQ--------SGSGA----RIIFLGDLVR-DGEP-------- 138
Cdd:PRK12583 98 VNINPAYRASELEYALGQSGVRWVICADAFKTSDyhAMLQellpglaeGQPGAlaceRLPELRGVVSlAPAPppgflawh 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 139 --YSYGPPIEDPQREPAQPAF-------IFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGLrhGRHNVVLGLMPLYHVV 209
Cdd:PRK12583 178 elQARGETVSREALAERQASLdrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGL--TEHDRLCVPVPLYHCF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 210 GFFAVLVAALALDGTYVV-VEEFRPVDALQLVQQEQVTSLFATPTHLDALAAAAAHagSSLKLDSLRHVTFAGATMPDAV 288
Cdd:PRK12583 256 GMVLANLGCMTVGACLVYpNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQR--GNFDLSSLRTGIMAGAPCPIEV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 289 LETVHQHLPGEKVNI-YGTTE---------AMNSLYMRQPKTGTEMApgfFSEVRIVRIGGgvdEIVANGEEGELIVAAS 358
Cdd:PRK12583 334 MRRVMDEMHMAEVQIaYGMTEtspvslqttAADDLERRVETVGRTQP---HLEVKVVDPDG---ATVPRGEIGELCTRGY 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 359 dSAFVGYLNQPQATAEKL-QDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLAD 437
Cdd:PRK12583 408 -SVMKGYWNNPEATAESIdEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPD 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
1T5D_X 438 QRWGQSVTACVVPRLGETLSADALDTFCRsSELADFKRPKRYFILDQLPKNALNKV 493
Cdd:PRK12583 487 EKYGEEIVAWVRLHPGHAASEEELREFCK-ARIAHFKVPRYFRFVDEFPMTVTGKV 541
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
16-498 |
7.68e-64 |
|
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: 213.93 E-value: 7.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 16 PDhcALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAE 95
Cdd:cd05930 1 PD--AVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 96 LIKRgemtaaviavgrqvadaifqsgSGARIIFlgdlvrdgepysygppiedpqREPAQPAFIFYTSGTTGLPKAAIIPQ 175
Cdd:cd05930 79 ILED----------------------SGAKLVL---------------------TDPDDLAYVIYTSGSTGKPKGVMVEH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 176 RAAESRVLFMSTQVGLRHGRhnVVLGLMPLYHVVGFFAVLvAALALDGTYVVVEE---FRPVDALQLVQQEQVTSLFATP 252
Cdd:cd05930 116 RGLVNLLLWMQEAYPLTPGD--RVLQFTSFSFDVSVWEIF-GALLAGATLVVLPEevrKDPEALADLLAEEGITVLHLTP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 253 ThldaLAAAAAHAGSSLKLDSLRHVTFAGATMPDAVLETVHQHLPGEKV-NIYGTTEA-MNSLYMRQPKTGTemapgffs 330
Cdd:cd05930 193 S----LLRLLLQELELAALPSLRLVLVGGEALPPDLVRRWRELLPGARLvNLYGPTEAtVDATYYRVPPDDE-------- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 331 EVRIVRIGGGVD-----------EIVANGEEGELIVaASDSAFVGYLNQPQATAEK-LQDGW------YRTSDVAVWTPE 392
Cdd:cd05930 261 EDGRVPIGRPIPntrvyvldenlRPVPPGVPGELYI-GGAGLARGYLNRPELTAERfVPNPFgpgermYRTGDLVRWLPD 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 393 GTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCRsSELAD 472
Cdd:cd05930 340 GNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLA-ERLPD 418
|
490 500
....*....|....*....|....*.
1T5D_X 473 FKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:cd05930 419 YMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
152-493 |
2.13e-63 |
|
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: 209.83 E-value: 2.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 152 PAQPAFIFYTSGTTGLPKAAIIPQRaaesRVLFMSTQVGLRHG-RHNVVLGL-MPLYHVVGFFAVLVAALALDGTYVVVE 229
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHH----NIVNNGYFIGERLGlTEQDRLCIpVPLFHCFGSVLGVLACLTHGATMVFPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 230 E-FRPVDALQLVQQEQVTSLFATPTHLDALAAAAAHagSSLKLDSLRHVTFAGATMPDAVLETVHQHLPGEKVNI-YGTT 307
Cdd:cd05917 77 PsFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDF--DKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIaYGMT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 308 EAMNSLYMRQP------KTGTEMAPGFFSEVRIVRIGGGvdEIVANGEEGELIVAASdSAFVGYLNQPQATAEKL-QDGW 380
Cdd:cd05917 155 ETSPVSTQTRTddsiekRVNTVGRIMPHTEAKIVDPEGG--IVPPVGVPGELCIRGY-SVMKGYWNDPEKTAEAIdGDGW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 381 YRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADA 460
Cdd:cd05917 232 LHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEED 311
|
330 340 350
....*....|....*....|....*....|...
1T5D_X 461 LDTFCRSSeLADFKRPKRYFILDQLPKNALNKV 493
Cdd:cd05917 312 IKAYCKGK-IAHYKVPRYVFFVDEFPLTVSGKI 343
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
8-493 |
1.39e-61 |
|
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: 209.08 E-value: 1.39e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 8 LRRAATRAPDHcaLAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPR 87
Cdd:cd12118 10 LERAAAVYPDR--TSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 88 LKSAELAELIKRGEmtAAVIAVGRQvadaifqsgsgariiFLG-DLVRDGEPYsygPPIEDPQREpAQPAFIFYTSGTTG 166
Cdd:cd12118 88 LDAEEIAFILRHSE--AKVLFVDRE---------------FEYeDLLAEGDPD---FEWIPPADE-WDPIALNYTSGTTG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 167 LPKAAIIPQRAAesRVLFMSTQVGLRHGRHNVVLGLMPLYHVVGF-FAVLVAALAldGTYVVVEEFRPVDALQLVQQEQV 245
Cdd:cd12118 147 RPKGVVYHHRGA--YLNALANILEWEMKQHPVYLWTLPMFHCNGWcFPWTVAAVG--GTNVCLRKVDAKAIYDLIEKHKV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 246 TSLFATPTHLDALAAAAAHagSSLKLDSLRHVTFAGATMPDAVLETVHQHlpGEKVNI-YGTTEAM------------NS 312
Cdd:cd12118 223 THFCGAPTVLNMLANAPPS--DARPLPHRVHVMTAGAPPPAAVLAKMEEL--GFDVTHvYGLTETYgpatvcawkpewDE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 313 L-----YMRQPKTGTEMApgFFSEVRIVRIGGGVDeIVANGEE-GElIVAASDSAFVGYLNQPQATAEKLQDGWYRTSDV 386
Cdd:cd12118 299 LpteerARLKARQGVRYV--GLEEVDVLDPETMKP-VPRDGKTiGE-IVFRGNIVMKGYLKNPEATAEAFRGGWFHSGDL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 387 AVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCR 466
Cdd:cd12118 375 AVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEEEIIAFCR 454
|
490 500
....*....|....*....|....*..
1T5D_X 467 sSELADFKRPKRYfILDQLPKNALNKV 493
Cdd:cd12118 455 -EHLAGFMVPKTV-VFGELPKTSTGKI 479
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
27-498 |
1.82e-61 |
|
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: 207.14 E-value: 1.82e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 27 GLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIKRGEMTAAV 106
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 107 IAvgrqvadaifqsgsgariiflgdlvrdgepysygppiedpqrepaqPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMS 186
Cdd:cd05934 81 VD----------------------------------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 187 TQVGLRHGrhNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFRPVDALQLVQQEQVT----------SLFATPTHLD 256
Cdd:cd05934 115 RRFGLGED--DVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATvtnylgamlsYLLAQPPSPD 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 257 ALaaaaahagsslklDSLRHVTFAGATMPDavletvhQHLPGEK------VNIYGTTEA----MNSLYMRQPkTGTEMAP 326
Cdd:cd05934 193 DR-------------AHRLRAAYGAPNPPE-------LHEEFEErfgvrlLEGYGMTETivgvIGPRDEPRR-PGSIGRP 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 327 GFFSEVRIVrigGGVDEIVANGEEGELIVAAS--DSAFVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDM 404
Cdd:cd05934 252 APGYEVRIV---DDDGQELPAGEPGELVIRGLrgWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDM 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 405 IISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCRSSeLADFKRPKRYFILDQ 484
Cdd:cd05934 329 IRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQ-LAYFKVPRYIRFVDD 407
|
490
....*....|....
1T5D_X 485 LPKNALNKVLRRQL 498
Cdd:cd05934 408 LPKTPTEKVAKAQL 421
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
11-498 |
8.18e-61 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 208.63 E-value: 8.18e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 11 AATRAPDHCALaVPARGlRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKS 90
Cdd:PRK07788 58 AARRAPDRAAL-IDERG-TLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 91 AELAELIKRGEMTAAVI-----AVGRQVADAIfqsgsgARIIFLGDLVRDGEPYSYGPPIED---------PQREPAQPA 156
Cdd:PRK07788 136 PQLAEVAAREGVKALVYddeftDLLSALPPDL------GRLRAWGGNPDDDEPSGSTDETLDdliagsstaPLPKPPKPG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 157 -FIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGLRhgRHNVVLGLMPLYHVVGFfAVLVAALALDGTYVVVEEFRPVD 235
Cdd:PRK07788 210 gIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFR--AGETTLLPAPMFHATGW-AHLTLAMALGSTVVLRRRFDPEA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 236 ALQLVQQEQVTSLFATPTHLDALAAAAAHAGSSLKLDSLRHVTFAGATMPDAVLETVHQHLpGEKV-NIYGTTEA----- 309
Cdd:PRK07788 287 TLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAF-GPVLyNLYGSTEVafati 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 310 --MNSLyMRQPKTGTEMAPGffseVRiVRIGGGVDEIVANGEEGELIVAaSDSAFVGYLNQPQataEKLQDGWYRTSDVA 387
Cdd:PRK07788 366 atPEDL-AEAPGTVGRPPKG----VT-VKILDENGNEVPRGVVGRIFVG-NGFPFEGYTDGRD---KQIIDGLLSSGDVG 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 388 VWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCRS 467
Cdd:PRK07788 436 YFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRD 515
|
490 500 510
....*....|....*....|....*....|.
1T5D_X 468 SeLADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:PRK07788 516 N-LARYKVPRDVVFLDELPRNPTGKVLKREL 545
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
11-498 |
5.86e-59 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 203.45 E-value: 5.86e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 11 AATRAPDHCALaVPARGLrLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKS 90
Cdd:PRK13382 52 AAQRCPDRPGL-IDELGT-LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 91 AELAELIKRGEMTAAVI------AVGRQVADAifqsGSGARIIFLGDLVRDG--EPYSYGPPIEDPQREPAQPAFIFYTS 162
Cdd:PRK13382 130 PALAEVVTREGVDTVIYdeefsaTVDRALADC----PQATRIVAWTDEDHDLtvEVLIAAHAGQRPEPTGRKGRVILLTS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 163 GTTGLPKAAIIPQRAAESRVLFMSTQVGLRHGRHNVVLGlmPLYHVVGFfAVLVAALALDGTYVVVEEFRPVDALQLVQQ 242
Cdd:PRK13382 206 GTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVA--PMFHAWGF-SQLVLAASLACTIVTRRRFDPEATLDLIDR 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 243 EQVTSLFATPTHLDALAAAAAHAGSSLKLDSLRHVTFAGATM-PDAVLETVHQHlpGEKV-NIYGTTEA-MNSL-----Y 314
Cdd:PRK13382 283 HRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMrPDVVIAFMDQF--GDVIyNNYNATEAgMIATatpadL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 315 MRQPKTGTEMAPGffSEVRIVRIGGgvdEIVANGEEGELIVAaSDSAFVGYLNqpqATAEKLQDGWYRTSDVAVWTPEGT 394
Cdd:PRK13382 361 RAAPDTAGRPAEG--TEIRILDQDF---REVPTGEVGTIFVR-NDTQFDGYTS---GSTKDFHDGFMASGDVGYLDENGR 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 395 VRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCRSSeLADFK 474
Cdd:PRK13382 432 LFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDN-LANYK 510
|
490 500
....*....|....*....|....
1T5D_X 475 RPKRYFILDQLPKNALNKVLRRQL 498
Cdd:PRK13382 511 VPRDIVVLDELPRGATGKILRREL 534
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
5-504 |
1.91e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 202.31 E-value: 1.91e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 5 NEMLRRAATRAPDHCALAVpaRGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALL 84
Cdd:PRK07786 20 VNQLARHALMQPDAPALRF--LGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 85 NPRLKSAELAELIKRGEMTAAVI-AVGRQVADAIFQSGSG-ARIIFLGDLVRDG---------EPYSYGPPIEDPQRepa 153
Cdd:PRK07786 98 NFRLTPPEIAFLVSDCGAHVVVTeAALAPVATAVRDIVPLlSTVVVAGGSSDDSvlgyedllaEAGPAHAPVDIPND--- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 154 QPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGLRHGrHNVVLGLMPLYHVVGFFAVLVAaLALDGTYVV--VEEF 231
Cdd:PRK07786 175 SPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADIN-SDVGFVGVPLFHIAGIGSMLPG-LLLGAPTVIypLGAF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 232 RPVDALQLVQQEQVTSLFATPTHLDALAAAAAHAGSSLKLdslRHVTFAGATMPDAVLETVHQHLPGEK-VNIYGTTEAM 310
Cdd:PRK07786 253 DPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLAL---RVLSWGAAPASDTLLRQMAATFPEAQiLAAFGQTEMS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 311 NSLYMRQ-----PKTGTEMAPGFFSEVRIVrigggvDEI---VANGEEGElIVAASDSAFVGYLNQPQATAEKLQDGWYR 382
Cdd:PRK07786 330 PVTCMLLgedaiRKLGSVGKVIPTVAARVV------DENmndVPVGEVGE-IVYRAPTLMSGYWNNPEATAEAFAGGWFH 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 383 TSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLG-ETLSADAL 461
Cdd:PRK07786 403 SGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDdAALTLEDL 482
|
490 500 510 520
....*....|....*....|....*....|....*....|...
1T5D_X 462 DTFCrSSELADFKRPKRYFILDQLPKNALNKVLRRQLVQQVSS 504
Cdd:PRK07786 483 AEFL-TDRLARYKHPKALEIVDALPRNPAGKVLKTELRERYGA 524
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
12-498 |
2.52e-58 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 200.80 E-value: 2.52e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 12 ATRAPDHCALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSA 91
Cdd:PRK09088 5 ARLQPQRLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 92 ELAELIKRGEmtAAVIavgrqVADAIFQSGsGARIIFLGDLVRDGEPYSygpPIEDPQREPAQPAFIFYTSGTTGLPKAA 171
Cdd:PRK09088 85 ELDALLQDAE--PRLL-----LGDDAVAAG-RTDVEDLAAFIASADALE---PADTPSIPPERVSLILFTSGTSGQPKGV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 172 IIPQRAAESRVLFMStqVGLRHGRHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFRPVDALQLVQQEQ--VTSLF 249
Cdd:PRK09088 154 MLSERNLQQTAHNFG--VLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLGDPAlgITHYF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 250 ATPTHLDALAAAAAHAGSSLKldSLRHVTFAGATMP-DAVLETVHQHLPgeKVNIYGTTEAMNSLYMR------QPKTGT 322
Cdd:PRK09088 232 CVPQMAQAFRAQPGFDAAALR--HLTALFTGGAPHAaEDILGWLDDGIP--MVDGFGMSEAGTVFGMSvdcdviRAKAGA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 323 EMAPGFFSEVRIVRIGGgvdEIVANGEEGELIVAAsDSAFVGYLNQPQATAEKL-QDGWYRTSDVAVWTPEGTVRILGRV 401
Cdd:PRK09088 308 AGIPTPTVQTRVVDDQG---NDCPAGVPGELLLRG-PNLSPGYWRRPQATARAFtGDGWFRTGDIARRDADGFFWVVDRK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 402 DDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCrSSELADFKRPKRYFI 481
Cdd:PRK09088 384 KDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHL-STRLAKYKVPKHLRL 462
|
490
....*....|....*..
1T5D_X 482 LDQLPKNALNKVLRRQL 498
Cdd:PRK09088 463 VDALPRTASGKLQKARL 479
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
2-501 |
3.37e-58 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 201.82 E-value: 3.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 2 QTVNEMLRRAATRAPDHCALAVPARGL----RLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRL 77
Cdd:PRK13295 24 RTINDDLDACVASCPDKTAVTAVRLGTgaprRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 78 GAVPALLNPRLKSAELAELIKRGEMTAAVI----------AVGRQVADAI-------FQSGSGARII--FLGDLVRDGEP 138
Cdd:PRK13295 104 GAVLNPLMPIFRERELSFMLKHAESKVLVVpktfrgfdhaAMARRLRPELpalrhvvVVGGDGADSFeaLLITPAWEQEP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 139 YSyGPPIEDPQREPAQPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGLrhGRHNVVLGLMPLYHVVGFFAVLVAA 218
Cdd:PRK13295 184 DA-PAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGL--GADDVILMASPMAHQTGFMYGLMMP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 219 LALDGTYVVVEEFRPVDALQLVQQEQVT-SLFATPTHLDALAAAAAhagSSLKLDSLRHVTFAGATMPDAVLETVHQHLP 297
Cdd:PRK13295 261 VMLGATAVLQDIWDPARAAELIRTEGVTfTMASTPFLTDLTRAVKE---SGRPVSSLRTFLCAGAPIPGALVERARAALG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 298 GEKVNIYGTTEamNSLYmrqpkTGTEMA--------------PGFfsEVRIVrigGGVDEIVANGEEGELIVAASdSAFV 363
Cdd:PRK13295 338 AKIVSAWGMTE--NGAV-----TLTKLDdpderasttdgcplPGV--EVRVV---DADGAPLPAGQIGRLQVRGC-SNFG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 364 GYLNQPQATAEkLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQS 443
Cdd:PRK13295 405 GYLKRPQLNGT-DADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGER 483
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
1T5D_X 444 VTACVVPRLGETLSADALDTFCRSSELADFKRPKRYFILDQLPKNALNKV----LRRQLVQQ 501
Cdd:PRK13295 484 ACAFVVPRPGQSLDFEEMVEFLKAQKVAKQYIPERLVVRDALPRTPSGKIqkfrLREMLRGE 545
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
3-498 |
7.64e-58 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 200.21 E-value: 7.64e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 3 TVNEMLRRAATRAPDHCALAVParGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPA 82
Cdd:PRK06188 13 TYGHLLVSALKRYPDRPALVLG--DTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 83 LLNPRLKSAELAELIKRGEMTAAVIAVGRQV--ADAIFQSGSGARIIFLGDLVRDGEPYSYGPPIEDPQR-----EPAQP 155
Cdd:PRK06188 91 ALHPLGSLDDHAYVLEDAGISTLIVDPAPFVerALALLARVPSLKHVLTLGPVPDGVDLLAAAAKFGPAPlvaaaLPPDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 156 AFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGLRhgRHNVVLGLMPLYHVVGffAVLVAALALDGTYVVVEEFRPVD 235
Cdd:PRK06188 171 AGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWP--ADPRFLMCTPLSHAGG--AFFLPTLLRGGTVIVLAKFDPAE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 236 ALQLVQQEQVTSLFATPTHLDALAAAAAHagSSLKLDSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTEA-MNSLY 314
Cdd:PRK06188 247 VLRAIEEQRITATFLVPTMIYALLDHPDL--RTRDLSSLETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEApMVITY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 315 MR-------QPKTGTEMA-PGFFSEVRIVrigGGVDEIVANGEEGELIVAASDSAfVGYLNQPQATAEKLQDGWYRTSDV 386
Cdd:PRK06188 325 LRkrdhdpdDPKRLTSCGrPTPGLRVALL---DEDGREVAQGEVGEICVRGPLVM-DGYWNRPEETAEAFRDGWLHTGDV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 387 AVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCR 466
Cdd:PRK06188 401 AREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVK 480
|
490 500 510
....*....|....*....|....*....|..
1T5D_X 467 SSELAdFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:PRK06188 481 ERKGS-VHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
2-498 |
1.11e-57 |
|
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: 198.71 E-value: 1.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 2 QTVNEMLRRAATRAPDHCALAVPARglRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVP 81
Cdd:cd05920 15 EPLGDLLARSAARHPDRIAVVDGDR--RLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 82 ALLNPRLKSAELAELIKRGEMTAAVIAvgrqvadaifqsgsgariiflgdlvRDGEPYSYGPPIEDPQREPAQPAFIFYT 161
Cdd:cd05920 93 VLALPSHRRSELSAFCAHAEAVAYIVP-------------------------DRHAGFDHRALARELAESIPEVALFLLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 162 SGTTGLPKAaiIPQRAAESRVLFMSTQVGLRHGRHNVVLGLMPLYHVvgfFAV----LVAALALDGTYVVVEEFRPVDAL 237
Cdd:cd05920 148 GGTTGTPKL--IPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHN---FPLacpgVLGTLLAGGRVVLAPDPSPDAAF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 238 QLVQQEQVTSLFATPTHLDALAAAAAHAGSSLKldSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTEAM-NSLYMR 316
Cdd:cd05920 223 PLIEREGVTVTALVPALVSLWLDAAASRRADLS--SLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLlNYTRLD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 317 QPK------TGTEMAPGffSEVRIVrigGGVDEIVANGEEGELIVAASDSaFVGYLNQPQATAEKL-QDGWYRTSDVAVW 389
Cdd:cd05920 301 DPDeviihtQGRPMSPD--DEIRVV---DEEGNPVPPGEEGELLTRGPYT-IRGYYRAPEHNARAFtPDGFYRTGDLVRR 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 390 TPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRlGETLSADALDTFCRSSE 469
Cdd:cd05920 375 TPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLR-DPPPSAAQLRRFLRERG 453
|
490 500
....*....|....*....|....*....
1T5D_X 470 LADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:cd05920 454 LAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
12-498 |
2.15e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 195.87 E-value: 2.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 12 ATRAPDHCALAVpaRGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSA 91
Cdd:PRK06145 12 ARRTPDRAALVY--RDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAAD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 92 ELAELIkrGEMTAAVIAVGRQVaDAIfqSGSGARIIFLG-----DLVRDGEPYSYGPPIEdpQREPAQPAFIFYTSGTTG 166
Cdd:PRK06145 90 EVAYIL--GDAGAKLLLVDEEF-DAI--VALETPKIVIDaaaqaDSRRLAQGGLEIPPQA--AVAPTDLVRLMYTSGTTD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 167 LPKAAIIPQRAAESRVLFMSTQVGLRHGRHNVVLGlmPLYHVVGFFAVLVAALALDGTYVVVEEFRPVDALQLVQQEQVT 246
Cdd:PRK06145 163 RPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVG--PLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLAAIERHRLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 247 SLFATPTHLDALAAAAAHagSSLKLDSLRHVTFAGATMPDAVLETVHQHLPGEK-VNIYGTTEAMN-SLYMRQPK----- 319
Cdd:PRK06145 241 CAWMAPVMLSRVLTVPDR--DRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARyIDAYGLTETCSgDTLMEAGReieki 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 320 --TGTEMApgfFSEVRIVRIGGGvdeIVANGEEGELIVAASDSAfVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRI 397
Cdd:PRK06145 319 gsTGRALA---HVEIRIADGAGR---WLPPNMKGEICMRGPKVT-KGYWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 398 LGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCRsSELADFKRPK 477
Cdd:PRK06145 392 TDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCR-QRLASFKVPR 470
|
490 500
....*....|....*....|.
1T5D_X 478 RYFILDQLPKNALNKVLRRQL 498
Cdd:PRK06145 471 QLKVRDELPRNPSGKVLKRVL 491
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
7-498 |
9.70e-56 |
|
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: 194.39 E-value: 9.70e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 7 MLRRAATRAPDH--CALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALL 84
Cdd:cd12119 1 LLEHAARLHGDReiVSRTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 85 NPRLKSAELAELIKRGEMTAAVI-----AVGRQVADAIfqsGSGARIIFLGDLVRDGEP-----YSY------GPPIED- 147
Cdd:cd12119 81 NPRLFPEQIAYIINHAEDRVVFVdrdflPLLEAIAPRL---PTVEHVVVMTDDAAMPEPagvgvLAYeellaaESPEYDw 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 148 PQREPAQPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGLRHGRHNVVLGLMPLYHV----VGFFAVLV-AALALD 222
Cdd:cd12119 158 PDFDENTAAAICYTSGTTGNPKGVVYSHRSLVLHAMAALLTDGLGLSESDVVLPVVPMFHVnawgLPYAAAMVgAKLVLP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 223 GTYVvveefRPVDALQLVQQEQVTSLFATPTHLDALAAAAAHAGssLKLDSLRHVTFAGATMPDAVLETVHQHLPgEKVN 302
Cdd:cd12119 238 GPYL-----DPASLAELIEREGVTFAAGVPTVWQGLLDHLEANG--RDLSSLRRVVIGGSAVPRSLIEAFEERGV-RVIH 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 303 IYGTTEAMNSLYMRQPKTGTEMAPG--------------FFSEVRIVRIGGGvdEIVANGEE-GELIVAAsdsAFV--GY 365
Cdd:cd12119 310 AWGMTETSPLGTVARPPSEHSNLSEdeqlalrakqgrpvPGVELRIVDDDGR--ELPWDGKAvGELQVRG---PWVtkSY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 366 LNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVT 445
Cdd:cd12119 385 YKNDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPL 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
1T5D_X 446 ACVVPRLGETLSADALDTFCRsSELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:cd12119 465 AVVVLKEGATVTAEELLEFLA-DKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
6-498 |
6.60e-55 |
|
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: 191.26 E-value: 6.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 6 EMLRRAATRAPDhcALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLN 85
Cdd:cd12117 1 ELFEEQAARTPD--AVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 86 PRLKSAELAELIKRGEMTAAVIavgrqvadaifQSGSGARIIFLGD-LVRDGEPYSYGPPIEDPQREPAQPAFIFYTSGT 164
Cdd:cd12117 79 PELPAERLAFMLADAGAKVLLT-----------DRSLAGRAGGLEVaVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 165 TGLPKAAIIPQRAAESRVLfmsTQVGLRHGRHNVVLGLMPLYHVVGFFAVLVAALAlDGTYVVVEEFRPVDALQL---VQ 241
Cdd:cd12117 148 TGRPKGVAVTHRGVVRLVK---NTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLN-GARLVLAPKGTLLDPDALgalIA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 242 QEQVTSLFATPTHLDALAAAAAHAgsslkLDSLRHVTFAGATMPDAVLETVHQHLPGEK-VNIYGTTE--------AMNS 312
Cdd:cd12117 224 EEGVTVLWLTAALFNQLADEDPEC-----FAGLRELLTGGEVVSPPHVRRVLAACPGLRlVNGYGPTEnttfttshVVTE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 313 LYMRQPKT--GTEMAPgffSEVRIVRIGGgvdEIVANGEEGELIVAASDSAFvGYLNQPQATAEKL-----QDG--WYRT 383
Cdd:cd12117 299 LDEVAGSIpiGRPIAN---TRVYVLDEDG---RPVPPGVPGELYVGGDGLAL-GYLNRPALTAERFvadpfGPGerLYRT 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 384 SDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRlgETLSADALDT 463
Cdd:cd12117 372 GDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAE--GALDAAELRA 449
|
490 500 510
....*....|....*....|....*....|....*
1T5D_X 464 FCRSSeLADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:cd12117 450 FLRER-LPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
6-498 |
1.07e-54 |
|
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: 190.95 E-value: 1.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 6 EMLRRAATRAPDhcALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLN 85
Cdd:cd17646 2 ALVAEQAARTPD--APAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 86 PRLKSAELAELIKRGemTAAVIAVGRQVADAIFQSGsgariifLGDLVRDGEPYSYGPPIEDPQREPAQPAFIFYTSGTT 165
Cdd:cd17646 80 PGYPADRLAYMLADA--GPAVVLTTADLAARLPAGG-------DVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGST 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 166 GLPKAAIIPQRAAESRVLFMSTQVGLRHGrhNVVLGLMPLYHVVGFFAVLVaALALDGTYVVVEEFRPVDA---LQLVQQ 242
Cdd:cd17646 151 GRPKGVMVTHAGIVNRLLWMQDEYPLGPG--DRVLQKTPLSFDVSVWELFW-PLVAGARLVVARPGGHRDPaylAALIRE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 243 EQVTSLFATPTHLDALAAAAAHAGsslkLDSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTEA-MNSLYMrqPKTG 321
Cdd:cd17646 228 HGVTTCHFVPSMLRVFLAEPAAGS----CASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAaIDVTHW--PVRG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 322 TEMAPGffseVRIVRIGGGVD--------EIVANGEEGELIVAASDSAFvGYLNQPQATAEKLQDGW-------YRTSDV 386
Cdd:cd17646 302 PAETPS----VPIGRPVPNTRlyvlddalRPVPVGVPGELYLGGVQLAR-GYLGRPALTAERFVPDPfgpgsrmYRTGDL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 387 AVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGET-LSADALDTFC 465
Cdd:cd17646 377 ARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAgPDTAALRAHL 456
|
490 500 510
....*....|....*....|....*....|...
1T5D_X 466 RSSeLADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:cd17646 457 AER-LPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
8-502 |
2.19e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 189.82 E-value: 2.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 8 LRRAATRAPDHCALAVPARGLRLTHAELRARVEAVAARLhadglRPQQRVAVVAPNSADVVIAILALHRLG--AVPalLN 85
Cdd:PRK07787 4 LNPAAVAAAADIADAVRIGGRVLSRSDLAGAATAVAERV-----AGARRVAVLATPTLATVLAVVGALIAGvpVVP--VP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 86 PRLKSAELAELIKRGEMTAAVIAVGRQVAdaifqsgsGARIIFLGDLVRDGEPYsygppiedPQREPAQPAFIFYTSGTT 165
Cdd:PRK07787 77 PDSGVAERRHILADSGAQAWLGPAPDDPA--------GLPHVPVRLHARSWHRY--------PEPDPDAPALIVYTSGTT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 166 GLPKAAIIPQRAAESRvLFMSTQVGLRHGRHNVVLGLmPLYHVVGFFAVLVAALALDGTYVVVEEFRPvDALQLVQQEQV 245
Cdd:PRK07787 141 GPPKGVVLSRRAIAAD-LDALAEAWQWTADDVLVHGL-PLFHVHGLVLGVLGPLRIGNRFVHTGRPTP-EAYAQALSEGG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 246 TSLFATPTHLDALAAAAahaGSSLKLDSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTEAMNSLYMR---QPKTGT 322
Cdd:PRK07787 218 TLYFGVPTVWSRIAADP---EAARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRadgERRPGW 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 323 EMAPGFFSEVRIVRIGGGvdEIVANGEE-GELIVAASdSAFVGYLNQPQATAEKL-QDGWYRTSDVAVWTPEGTVRILGR 400
Cdd:PRK07787 295 VGLPLAGVETRLVDEDGG--PVPHDGETvGELQVRGP-TLFDGYLNRPDATAAAFtADGWFRTGDVAVVDPDGMHRIVGR 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 401 VD-DMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPrlGETLSADALDTFCrSSELADFKRPKRY 479
Cdd:PRK07787 372 EStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVG--ADDVAADELIDFV-AQQLSVHKRPREV 448
|
490 500
....*....|....*....|...
1T5D_X 480 FILDQLPKNALNKVLRRQLVQQV 502
Cdd:PRK07787 449 RFVDALPRNAMGKVLKKQLLSEG 471
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
16-498 |
8.91e-54 |
|
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: 188.73 E-value: 8.91e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 16 PDHCALAVPARglRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAE 95
Cdd:cd05959 18 GDKTAFIDDAG--SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 96 LIKRGEMTAAViaVGRQVADAIFQSGSGARIIFLGDLVRDGEPYSYG-------PPIEDPQREPA-----QPAFIFYTSG 163
Cdd:cd05959 96 YLEDSRARVVV--VSGELAPVLAAALTKSEHTLVVLIVSGGAGPEAGalllaelVAAEAEQLKPAathadDPAFWLYSSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 164 TTGLPKAAIIPQRA-AESRVLFMSTQVGLRHGrhNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEfRPVDA--LQLV 240
Cdd:cd05959 174 STGRPKGVVHLHADiYWTAELYARNVLGIRED--DVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPE-RPTPAavFKRI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 241 QQEQVTSLFATPTHLDALAAAAAHagSSLKLDSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTEAM-----NSLYM 315
Cdd:cd05959 251 RRYRPTVFFGVPTLYAAMLAAPNL--PSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLhiflsNRPGR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 316 RQPKTGTEMAPGFfsEVRIVRIGGGvdeIVANGEEGELIVAAsDSAFVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTV 395
Cdd:cd05959 329 VRYGTTGKPVPGY--EVELRDEDGG---DVADGEPGELYVRG-PSSATMYWNNRDKTRDTFQGEWTRTGDKYVRDDDGFY 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 396 RILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLG---ETLSADALDTFCRsSELAD 472
Cdd:cd05959 403 TYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGyedSEALEEELKEFVK-DRLAP 481
|
490 500
....*....|....*....|....*.
1T5D_X 473 FKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:cd05959 482 YKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
8-501 |
1.43e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 189.02 E-value: 1.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 8 LRRAATRAPDHCALAVpaRGLRLTHAELRARVEAVAARLHAD-GLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNP 86
Cdd:PRK08314 16 LEVSARRYPDKTAIVF--YGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 87 RLKSAELAELIKRGEMTAAViaVGRQVADAIFQSGSGARIIFL-----GDLVRDGEPYSYgPPIEDPQREPAQP------ 155
Cdd:PRK08314 94 MNREEELAHYVTDSGARVAI--VGSELAPKVAPAVGNLRLRHVivaqySDYLPAEPEIAV-PAWLRAEPPLQALapggvv 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 156 ----------------------AFIFYTSGTTGLPKAAIIPQRAAESRVLfmSTQVGLRHGRHNVVLGLMPLYHVVGFFA 213
Cdd:PRK08314 171 awkealaaglappphtagpddlAVLPYTSGTTGVPKGCMHTHRTVMANAV--GSVLWSNSTPESVVLAVLPLFHVTGMVH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 214 VLVAALALDGTYVVVEEFRPVDALQLVQQEQVTSLFATPTHLDALAAAAAHAGSSLKldSLRHVTFAGATMPDAVLETVH 293
Cdd:PRK08314 249 SMNAPIYAGATVVLMPRWDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLS--SLRYIGGGGAAMPEAVAERLK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 294 QHLPGEKVNIYGTTEAMNSLYMR---QPKTGTEMAPGFFSEVRIVRIGGGvdEIVANGEEGELIVAASdSAFVGYLNQPQ 370
Cdd:PRK08314 327 ELTGLDYVEGYGLTETMAQTHSNppdRPKLQCLGIPTFGVDARVIDPETL--EELPPGEVGEIVVHGP-QVFKGYWNRPE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 371 ATAEKLQ--DG--WYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTA 446
Cdd:PRK08314 404 ATAEAFIeiDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKA 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
1T5D_X 447 CVVPRLGE--TLSADALDTFCRSSeLADFKRPKRYFILDQLPKNALNKVLRRQLVQQ 501
Cdd:PRK08314 484 VVVLRPEArgKTTEEEIIAWAREH-MAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQ 539
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
20-498 |
3.64e-53 |
|
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: 185.97 E-value: 3.64e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 20 ALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGA--VPalLNPRLKSAELAELi 97
Cdd:cd17643 3 AVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGayVP--IDPAYPVERIAFI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 98 krgemtaaviavgrqVADaifqsgSGARIIfLGDlvrdgepysygppiedpqrePAQPAFIFYTSGTTGLPKAAIIPQRA 177
Cdd:cd17643 80 ---------------LAD------SGPSLL-LTD--------------------PDDLAYVIYTSGSTGRPKGVVVSHAN 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 178 AesRVLFMSTQVGLRHGRHNVVLglmpLYHVVGF-FAV--LVAALALDGTYVVVEEF---RPVDALQLVQQEQVTSLFAT 251
Cdd:cd17643 118 V--LALFAATQRWFGFNEDDVWT----LFHSYAFdFSVweIWGALLHGGRLVVVPYEvarSPEDFARLLRDEGVTVLNQT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 252 PTHLDALAAAAAHAGSslKLDSLRHVTFAGATMPDAVLETVHQHLPGEK---VNIYGTTEAMNSLymrqpkTGTEMAPGF 328
Cdd:cd17643 192 PSAFYQLVEAADRDGR--DPLALRYVIFGGEALEAAMLRPWAGRFGLDRpqlVNMYGITETTVHV------TFRPLDAAD 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 329 FSEVRIVRIGGG--------VDE---IVANGEEGELIVAASDSAfVGYLNQPQATAEKLQDG--------WYRTSDVAVW 389
Cdd:cd17643 264 LPAAAASPIGRPlpglrvyvLDAdgrPVPPGVVGELYVSGAGVA-RGYLGRPELTAERFVANpfggpgsrMYRTGDLARR 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 390 TPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCRSSe 469
Cdd:cd17643 343 LPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKEL- 421
|
490 500
....*....|....*....|....*....
1T5D_X 470 LADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:cd17643 422 LPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
158-495 |
5.25e-53 |
|
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: 181.93 E-value: 5.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 158 IFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGLRHGRHNVVLGlmPLYHVVGFFAVLVAALALDGTYVVVEEFRPVDAL 237
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIIN--PFFHTFGYKAGIVACLLTGATVVPVAVFDVDAIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 238 QLVQQEQVTSLFATPTHLDALAAAAAHagSSLKLDSLRHVTFAGATMPDAVLETVHQHLPGEKV-NIYGTTEAMNSLYMR 316
Cdd:cd17638 83 EAIERERITVLPGPPTLFQSLLDHPGR--KKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVlTAYGLTEAGVATMCR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 317 QPKTGTEMA-------PGFfsEVRIVRIGggvdEIVANGEegelivaasdSAFVGYLNQPQATAEKL-QDGWYRTSDVAV 388
Cdd:cd17638 161 PGDDAETVAttcgracPGF--EVRIADDG----EVLVRGY----------NVMQGYLDDPEATAEAIdADGWLHTGDVGE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 389 WTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCRsS 468
Cdd:cd17638 225 LDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCR-E 303
|
330 340
....*....|....*....|....*..
1T5D_X 469 ELADFKRPKRYFILDQLPKNALNKVLR 495
Cdd:cd17638 304 RLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
31-432 |
1.34e-52 |
|
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: 183.24 E-value: 1.34e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 31 THAELRARVEAVAARLHAD-GLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIkrgEMTAAVIAV 109
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFIL---EDAGARLLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 110 GRQVADAIFQSGSGARIIFLGDLVRDGEPYSYGPPIEDPQRePAQPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQV 189
Cdd:TIGR01733 78 TDSALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSG-PDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 190 GLRHGrhNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFR---PVDALQLVQQEQVTSLFATPTHLDALAAAAAHAg 266
Cdd:TIGR01733 157 GLDPD--DRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEErddAALLAALIAEHPVTVLNLTPSLLALLAAALPPA- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 267 sslkLDSLRHVTFAGATMPDAVLETVHQHLPGEKV-NIYGTTEA----MNSLYMRQPKTGTEMAPgffsevrivrIGGGV 341
Cdd:TIGR01733 234 ----LASLRLVILGGEALTPALVDRWRARGPGARLiNLYGPTETtvwsTATLVDPDDAPRESPVP----------IGRPL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 342 D-----------EIVANGEEGELIVAAsDSAFVGYLNQPQATAEKL---------QDGWYRTSDVAVWTPEGTVRILGRV 401
Cdd:TIGR01733 300 AntrlyvldddlRPVPVGVVGELYIGG-PGVARGYLNRPELTAERFvpdpfaggdGARLYRTGDLVRYLPDGNLEFLGRI 378
|
410 420 430
....*....|....*....|....*....|.
1T5D_X 402 DDMIISGGENIHPSEIERVLGTAPGVTEVVV 432
Cdd:TIGR01733 379 DDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
29-501 |
3.30e-52 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 184.52 E-value: 3.30e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 29 RLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIK---------- 98
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEdsgarvliah 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 99 -------RGEMTAAV----------IAVGRQVADAIFQSGSGAriIFLGDLVRDGEPYSyGPPIEdpqrepaQPAFIFYT 161
Cdd:PRK12406 91 adllhglASALPAGVtvlsvptppeIAAAYRISPALLTPPAGA--IDWEGWLAQQEPYD-GPPVP-------QPQSMIYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 162 SGTTGLPK----AAIIPQRAAeSRVLFMSTQVGLRHGRHNVVLGlmPLYHVVGFfAVLVAALALDGTYVVVEEFRPVDAL 237
Cdd:PRK12406 161 SGTTGHPKgvrrAAPTPEQAA-AAEQMRALIYGLKPGIRALLTG--PLYHSAPN-AYGLRAGRLGGVLVLQPRFDPEELL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 238 QLVQQEQVTSLFATPTHLDALAAAAAHAGSSLKLDSLRHVTFAGATMPDAVLETVHQHLpGEKVN-IYGTTE------AM 310
Cdd:PRK12406 237 QLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAPCPADVKRAMIEWW-GPVIYeYYGSTEsgavtfAT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 311 NSLYMRQPKTGTEMAPGffSEVRIVrigGGVDEIVANGEEGELIVAASDSAFVGYLNQPQATAEKLQDGWYRTSDVAVWT 390
Cdd:PRK12406 316 SEDALSHPGTVGKAAPG--AELRFV---DEDGRPLPQGEIGEIYSRIAGNPDFTYHNKPEKRAEIDRGGFITSGDVGYLD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 391 PEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCRSSeL 470
Cdd:PRK12406 391 ADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKAR-L 469
|
490 500 510
....*....|....*....|....*....|.
1T5D_X 471 ADFKRPKRYFILDQLPKNALNKVLRRQLVQQ 501
Cdd:PRK12406 470 AGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
9-502 |
3.65e-52 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 185.34 E-value: 3.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 9 RRAATRAPDHCALaVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRL 88
Cdd:PRK06087 30 QQTARAMPDKIAV-VDNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 89 KSAELAELI--------------KRGEMTAAVIAVGRQV-----ADAIFQSGSGARIIFLGDLVRDGEPYSYGPPIEDPQ 149
Cdd:PRK06087 109 REAELVWVLnkcqakmffaptlfKQTRPVDLILPLQNQLpqlqqIVGVDKLAPATSSLSLSQIIADYEPLTTAITTHGDE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 150 RepaqpAFIFYTSGTTGLPKAAIIpqraAESRVLF--MSTQVGLRHGRHNVVLGLMPLYHVVGFFAVLVAALALDGTYVV 227
Cdd:PRK06087 189 L-----AAVLFTSGTEGLPKGVML----THNNILAseRAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 228 VEEFRPVDALQLVQQEQVT-SLFATPTHLDALAAAAAhagSSLKLDSLRHVTFAGATMPDAVLETVHQHlpGEKV-NIYG 305
Cdd:PRK06087 260 LDIFTPDACLALLEQQRCTcMLGATPFIYDLLNLLEK---QPADLSALRFFLCGGTTIPKKVARECQQR--GIKLlSVYG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 306 TTEAMNSLYMRQPK-------TGTEMAPGFfsEVRIVrigggvDE---IVANGEEGELIvAASDSAFVGYLNQPQATAEK 375
Cdd:PRK06087 335 STESSPHAVVNLDDplsrfmhTDGYAAAGV--EIKVV------DEarkTLPPGCEGEEA-SRGPNVFMGYLDEPELTARA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 376 L-QDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGE 454
Cdd:PRK06087 406 LdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPH 485
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
1T5D_X 455 -TLSADALDTFCRSSELADFKRPKRYFILDQLPKNALNKVLRRQLVQQV 502
Cdd:PRK06087 486 hSLTLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDI 534
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
11-492 |
7.73e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 184.32 E-value: 7.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 11 AATRAPDHCALAVPARglRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKS 90
Cdd:PRK07798 12 VADAVPDRVALVCGDR--RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 91 AELAELIKRGEMTAAViaVGRQVAD---AIFQSGSGAR-IIFLGD-----LVRDGEPYSYGPPIEDPQREPAQPA----F 157
Cdd:PRK07798 90 DELRYLLDDSDAVALV--YEREFAPrvaEVLPRLPKLRtLVVVEDgsgndLLPGAVDYEDALAAGSPERDFGERSpddlY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 158 IFYTSGTTGLPKAAIIPQ----RAAESRVLFMSTQV---------GLRHGRHNVVLGLMPLYHVVGFFAVLVAALAldGT 224
Cdd:PRK07798 168 LLYTGGTTGMPKGVMWRQedifRVLLGGRDFATGEPiedeeelakRAAAGPGMRRFPAPPLMHGAGQWAAFAALFS--GQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 225 YVV---VEEFRPVDALQLVQQEQVTSLFATPTHLDALAAAAAHAGSSLKLDSLRHVTFAGATMPDAVLETVHQHLPG-EK 300
Cdd:PRK07798 246 TVVllpDVRFDADEVWRTIEREKVNVITIVGDAMARPLLDALEARGPYDLSSLFAIASGGALFSPSVKEALLELLPNvVL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 301 VNIYGTTEA-MNSLYMRQPKTGTEMAPGFfsevrivRIGGG---VDE---IVANGEEGELIVAASDSAFVGYLNQPQATA 373
Cdd:PRK07798 326 TDSIGSSETgFGGSGTVAKGAVHTGGPRF-------TIGPRtvvLDEdgnPVEPGSGEIGWIARRGHIPLGYYKDPEKTA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 374 E--KLQDG--WYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVV 449
Cdd:PRK07798 399 EtfPTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQ 478
|
490 500 510 520
....*....|....*....|....*....|....*....|...
1T5D_X 450 PRLGETLSADALDTFCRsSELADFKRPKRYFILDQLPKNALNK 492
Cdd:PRK07798 479 LREGARPDLAELRAHCR-SSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
155-489 |
5.49e-51 |
|
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: 176.72 E-value: 5.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 155 PAFIFYTSGTTGLPKAAIIPQRAaesrVLFMSTQVGLRHG--RHNVVLGLMPLYHVvGFFAVLVAALALDGTYVVVEEFR 232
Cdd:cd17636 2 PVLAIYTAAFSGRPNGALLSHQA----LLAQALVLAVLQAidEGTVFLNSGPLFHI-GTLMFTLATFHAGGTNVFVRRVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 233 PVDALQLVQQEQVTSLFATPthLDALAAAAAHAGSSLKLDSLRhvtfAGATMPD-AVLETVHQHLPGEKVNIYGTTEAMN 311
Cdd:cd17636 77 AEEVLELIEAERCTHAFLLP--PTIDQIVELNADGLYDLSSLR----SSPAAPEwNDMATVDTSPWGRKPGGYGQTEVMG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 312 SL---YMRQPKTGTEMAPGFFSEVRIVrigGGVDEIVANGEEGElIVAASDSAFVGYLNQPQATAEKLQDGWYRTSDVAV 388
Cdd:cd17636 151 LAtfaALGGGAIGGAGRPSPLVQVRIL---DEDGREVPDGEVGE-IVARGPTVMAGYWNRPEVNARRTRGGWHHTNDLGR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 389 WTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCRsS 468
Cdd:cd17636 227 REPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCR-A 305
|
330 340
....*....|....*....|.
1T5D_X 469 ELADFKRPKRYFILDQLPKNA 489
Cdd:cd17636 306 RIASYKKPKSVEFADALPRTA 326
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
2-501 |
7.12e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 182.16 E-value: 7.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 2 QTVNEMLRRAATRAPDHCALAVpaRGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVP 81
Cdd:PRK06178 33 RPLTEYLRAWARERPQRPAIIF--YGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 82 ALLNPRLKSAELA-ELikrGEMTAAVIAVGRQVADAIFQ--SGSGARIIF---------------LGDLVRDGEPYSYG- 142
Cdd:PRK06178 111 VPVSPLFREHELSyEL---NDAGAEVLLALDQLAPVVEQvrAETSLRHVIvtsladvlpaeptlpLPDSLRAPRLAAAGa 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 143 ---------PPIEDPQREPA--QPAFIFYTSGTTGLPKAAIIPQR-----AAESrvlfmsTQVGLRHGRHNVVLGLMPLY 206
Cdd:PRK06178 188 idllpalraCTAPVPLPPPAldALAALNYTGGTTGMPKGCEHTQRdmvytAAAA------YAVAVVGGEDSVFLSFLPEF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 207 HVVGFFAVLVAALALDGTYVVVEEFRPVDALQLVQQEQVTSLFATPTHLDALAAAAAHagSSLKLDSLRHV---TFAGAT 283
Cdd:PRK06178 262 WIAGENFGLLFPLFSGATLVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRF--AEYDLSSLRQVrvvSFVKKL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 284 MPDavletvhqhLPGEKVNIYGTTEAMNSLYMRQPKTGTEMAPGF------------F-------SEVRIVRIGGGvdEI 344
Cdd:PRK06178 340 NPD---------YRQRWRALTGSVLAEAAWGMTETHTCDTFTAGFqdddfdllsqpvFvglpvpgTEFKICDFETG--EL 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 345 VANGEEGELIVAaSDSAFVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTA 424
Cdd:PRK06178 409 LPLGAEGEIVVR-TPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQH 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1T5D_X 425 PGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCRsSELADFKRPKRYfILDQLPKNALNKVLRRQLVQQ 501
Cdd:PRK06178 488 PAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCR-ENMAVYKVPEIR-IVDALPMTATGKVRKQDLQAL 562
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
2-498 |
7.35e-51 |
|
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: 186.99 E-value: 7.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 2 QTVNEMLRRAATRAPDhcALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGA-- 79
Cdd:COG1020 476 ATLHELFEAQAARTPD--AVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAay 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 80 VPalLNPRLKSAELAELIKRGEmtAAVIAVGRQVADAIfqSGSGARIIFLGDLVRDGEpysygpPIEDPQRE--PAQPAF 157
Cdd:COG1020 554 VP--LDPAYPAERLAYMLEDAG--ARLVLTQSALAARL--PELGVPVLALDALALAAE------PATNPPVPvtPDDLAY 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 158 IFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGLRHGRhnVVLGLMPLYHVVGFFAVLvAALALDGTYVVV--EEFRPVD 235
Cdd:COG1020 622 VIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGD--RVLQFASLSFDASVWEIF-GALLSGATLVLAppEARRDPA 698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 236 AL-QLVQQEQVTSLFATPTHLDALAAAAAHAgsslkLDSLRHVTFAGATMPDAVLETVHQHLPGEK-VNIYGTTEA-MNS 312
Cdd:COG1020 699 ALaELLARHRVTVLNLTPSLLRALLDAAPEA-----LPSLRLVLVGGEALPPELVRRWRARLPGARlVNLYGPTETtVDS 773
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 313 LYMRqpktgtemAPGFFSEVRIVRIGGGVD-----------EIVANGEEGELIVAasdSAFV--GYLNQPQATAEK---- 375
Cdd:COG1020 774 TYYE--------VTPPDADGGSVPIGRPIAntrvyvldahlQPVPVGVPGELYIG---GAGLarGYLNRPELTAERfvad 842
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 376 --LQDG--WYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPR 451
Cdd:COG1020 843 pfGFPGarLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPE 922
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
1T5D_X 452 LGETLSADALDTFcRSSELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:COG1020 923 AGAAAAAALLRLA-LALLLPPYMVPAAVVLLLPLPLTGNGKLDRLAL 968
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
6-501 |
1.04e-50 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 181.24 E-value: 1.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 6 EMLRRAATRAPDHCALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLN 85
Cdd:PRK05852 20 DLVEVAATRLPEAPALVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 86 PRLKSAElaELIKRGEMTAAVIAVGRQ--------------VADAIFQSGSGARIIFLGDLVRDGEPYsygPPIEDPQRE 151
Cdd:PRK05852 100 PALPIAE--QRVRSQAAGARVVLIDADgphdraepttrwwpLTVNVGGDSGPSGGTLSVHLDAATEPT---PATSTPEGL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 152 PAQPAFIFYTSGTTGLPKaaIIPQRAAESRVLFMSTQVGLRHGRHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVV--- 228
Cdd:PRK05852 175 RPDDAMIMFTGGTTGLPK--MVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLParg 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 229 --------EEFRPVDAlqlvqqeqvTSLFATPTHLDALAAAAAHAGSSLKLDSLRHVTFAGATMPDAVLETVHQHLPGEK 300
Cdd:PRK05852 253 rfsahtfwDDIKAVGA---------TWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFAAPV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 301 VNIYGTTEAMNSLYMRQPKTGTE-----MAPGFF-----SEVRIVRIGGGVdeiVANGEEGELIVAASdSAFVGYLNQPQ 370
Cdd:PRK05852 324 VCAFGMTEATHQVTTTQIEGIGQtenpvVSTGLVgrstgAQIRIVGSDGLP---LPAGAVGEVWLRGT-TVVRGYLGDPT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 371 ATAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVP 450
Cdd:PRK05852 400 ITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVP 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
1T5D_X 451 RLGETLSADALDTFCRsSELADFKRPKRYFILDQLPKNALNKVLRRQLVQQ 501
Cdd:PRK05852 480 RESAPPTAEELVQFCR-ERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQ 529
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
10-497 |
2.52e-50 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 179.30 E-value: 2.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 10 RAATRAPDHCALAVPArGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLK 89
Cdd:PRK07514 10 RAAFADRDAPFIETPD-GLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 90 SAELAELIKRGEMTAAVIAVGRQVADAIFQSGSGARIIFLGDLVRDGE----PYSYGPPIEDPQREPAQPAFIFYTSGTT 165
Cdd:PRK07514 89 LAELDYFIGDAEPALVVCDPANFAWLSKIAAAAGAPHVETLDADGTGSlleaAAAAPDDFETVPRGADDLAAILYTSGTT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 166 GLPKAAIIPQR--AAESRVLfmstQVGLRHGRHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFRPVDALQLVQQE 243
Cdd:PRK07514 169 GRSKGAMLSHGnlLSNALTL----VDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDPDAVLALMPRA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 244 QV--------TSLFATP--THLDALAAAAAHAGSS-LKLDSlrHVTFAGATmPDAVLETvhqhlpgekvniYGTTE-AMN 311
Cdd:PRK07514 245 TVmmgvptfyTRLLQEPrlTREAAAHMRLFISGSApLLAET--HREFQERT-GHAILER------------YGMTEtNMN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 312 SlymRQPKTGTEMA-------PGFfsEVRIVRIGGGvdEIVANGEEGELIVAASdSAFVGYLNQPQATAEKLQ-DGWYRT 383
Cdd:PRK07514 310 T---SNPYDGERRAgtvgfplPGV--SLRVTDPETG--AELPPGEIGMIEVKGP-NVFKGYWRMPEKTAEEFRaDGFFIT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 384 SDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDT 463
Cdd:PRK07514 382 GDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAILA 461
|
490 500 510
....*....|....*....|....*....|....*...
1T5D_X 464 FCRsSELADFKRPKRYFILDQLPKNALNKV----LRRQ 497
Cdd:PRK07514 462 ALK-GRLARFKQPKRVFFVDELPRNTMGKVqknlLREQ 498
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
2-498 |
6.92e-50 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 180.54 E-value: 6.92e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 2 QTVNEMLRRAATRAPDHCAL------AVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALH 75
Cdd:PRK07529 25 ASTYELLSRAAARHPDAPALsflldaDPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 76 RLGAVPALlNPRLKSAELAELIKRGE----MTAA-----------------------VIAVG--------RQVADAIFQS 120
Cdd:PRK07529 105 AAGIANPI-NPLLEPEQIAELLRAAGakvlVTLGpfpgtdiwqkvaevlaalpelrtVVEVDlarylpgpKRLAVPLIRR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 121 GSGARIIFLGDLVR--DGEPYSYGPPIEdpqrePAQPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGLRHGRhnV 198
Cdd:PRK07529 184 KAHARILDFDAELArqPGDRLFSGRPIG-----PDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGD--T 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 199 VLGLMPLYHVVGFFAVLVAALALDGTYV-----------VVEEFrpvdaLQLVQQEQVTSLFATPTHLDALAAAAAhagS 267
Cdd:PRK07529 257 VFCGLPLFHVNALLVTGLAPLARGAHVVlatpqgyrgpgVIANF-----WKIVERYRINFLSGVPTVYAALLQVPV---D 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 268 SLKLDSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTEAmNSLYMRQPKTGtEMAPGF------FSEVRIVRIG--G 339
Cdd:PRK07529 329 GHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEA-TCVSSVNPPDG-ERRIGSvglrlpYQRVRVVILDdaG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 340 GVDEIVANGEEGELIVAASdSAFVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIER 419
Cdd:PRK07529 407 RYLRDCAVDEVGVLCIAGP-NVFSGYLEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEE 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 420 VLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCRS--SELADFkrPKRYFILDQLPKNALNKVLRRQ 497
Cdd:PRK07529 486 ALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAELLAFARDhiAERAAV--PKHVRILDALPKTAVGKIFKPA 563
|
.
1T5D_X 498 L 498
Cdd:PRK07529 564 L 564
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
8-504 |
7.25e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 178.99 E-value: 7.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 8 LRRAATRAPDHcaLAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPR 87
Cdd:PRK08162 24 LERAAEVYPDR--PAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 88 LKSAELAELIKRGEmtAAVIAVGRQVADAIFQSGS---GARIIFLGDlvrDGEPYSYGPPIE-----------DPQREPA 153
Cdd:PRK08162 102 LDAASIAFMLRHGE--AKVLIVDTEFAEVAREALAllpGPKPLVIDV---DDPEYPGGRFIGaldyeaflasgDPDFAWT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 154 QPA------FIFYTSGTTGLPKAAIIPQRAAesRVLFMSTQVGLRHGRHNVVLGLMPLYHVVGF-FAVLVAALAldGTYV 226
Cdd:PRK08162 177 LPAdewdaiALNYTSGTTGNPKGVVYHHRGA--YLNALSNILAWGMPKHPVYLWTLPMFHCNGWcFPWTVAARA--GTNV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 227 VVEEFRPVDALQLVQQEQVTSLFATPTHLDALAAAAAHAGSslKLDSLRHVTFAGATMPDAVLETVHQHlpGEKVN-IYG 305
Cdd:PRK08162 253 CLRKVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRA--GIDHPVHAMVAGAAPPAAVIAKMEEI--GFDLThVYG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 306 TTE-----------------------AMNSlymRQ--------------PKTGTEMApgffsevrivRIGGGVDEIVANG 348
Cdd:PRK08162 329 LTEtygpatvcawqpewdalplderaQLKA---RQgvryplqegvtvldPDTMQPVP----------ADGETIGEIMFRG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 349 EegelIVAAsdsafvGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVT 428
Cdd:PRK08162 396 N----IVMK------GYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVL 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1T5D_X 429 EVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCRsSELADFKRPKRyFILDQLPKNALNKVLRRQLVQQVSS 504
Cdd:PRK08162 466 VAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCR-EHLAGFKVPKA-VVFGELPKTSTGKIQKFVLREQAKS 539
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
12-502 |
2.03e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 176.51 E-value: 2.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 12 ATRAPDHCALAVPARglRLTHAELRARVEAVAARLHADGLRPQqRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSA 91
Cdd:PRK07638 11 ASLQPNKIAIKENDR--VLTYKDWFESVCKVANWLNEKESKNK-TIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 92 ELAELIKRGEmtAAVIAVGRQVADAIfqSGSGARIIFLGDLVRDGEPYSYGP-PIEDPQREPaqpafiFY---TSGTTGL 167
Cdd:PRK07638 88 ELKERLAISN--ADMIVTERYKLNDL--PDEEGRVIEIDEWKRMIEKYLPTYaPIENVQNAP------FYmgfTSGSTGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 168 PKAAIipqRAAESRVLFMSTQV---GLRHGRHNVVLGlmPLYHVVGFFAVlVAALALDGTYVVVEEFRPVDALQLVQQEQ 244
Cdd:PRK07638 158 PKAFL---RAQQSWLHSFDCNVhdfHMKREDSVLIAG--TLVHSLFLYGA-ISTLYVGQTVHLMRKFIPNQVLDKLETEN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 245 VTSLFATPTHLDALAAAAAHAGSSLKLDSlrhvtfAGATMPDAVLETVHQHLPGEKV-NIYGTTEA--MNSLYMRQPKTG 321
Cdd:PRK07638 232 ISVMYTVPTMLESLYKENRVIENKMKIIS------SGAKWEAEAKEKIKNIFPYAKLyEFYGASELsfVTALVDEESERR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 322 TEMAPGFFSEVRI-VRIGGGvdEIVANGEEGELIVAaSDSAFVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGR 400
Cdd:PRK07638 306 PNSVGRPFHNVQVrICNEAG--EEVQKGEIGTVYVK-SPQFFMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 401 VDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVvprLGETlSADALDTFCRsSELADFKRPKRYF 480
Cdd:PRK07638 383 EKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---KGSA-TKQQLKSFCL-QRLSSFKIPKEWH 457
|
490 500
....*....|....*....|..
1T5D_X 481 ILDQLPKNALNKVLRRQLVQQV 502
Cdd:PRK07638 458 FVDEIPYTNSGKIARMEAKSWI 479
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
30-498 |
3.51e-49 |
|
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: 174.45 E-value: 3.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 30 LTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIKRgemtaaviav 109
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEA---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 110 grqvadaifqsgSGARIIFLGDlvrdgepysygppiEDPqrepaqpAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQV 189
Cdd:cd05972 71 ------------AGAKAIVTDA--------------EDP-------ALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 190 GLRHGrhNVVLGLMP---LYHVV-GFFAVLvaalaLDGTYVVVEEFRPVDA---LQLVQQEQVTSLFATPTHLDALAAAA 262
Cdd:cd05972 118 GLRPD--DIHWNIADpgwAKGAWsSFFGPW-----LLGATVFVYEGPRFDAeriLELLERYGVTSFCGPPTAYRMLIKQD 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 263 ahaGSSLKLDSLRHVTFAGATMPDAVLETVHQHLpGEKV-NIYGTTEA----MNSLYM--RQPKTGTEMaPGFfsEVRIV 335
Cdd:cd05972 191 ---LSSYKFSHLRLVVSAGEPLNPEVIEWWRAAT-GLPIrDGYGQTETgltvGNFPDMpvKPGSMGRPT-PGY--DVAII 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 336 RIGGgvdEIVANGEEGELIVAASD-SAFVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHP 414
Cdd:cd05972 264 DDDG---RELPPGEEGDIAIKLPPpGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGP 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 415 SEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLS---ADALDTFCRsSELADFKRPKRYFILDQLPKNALN 491
Cdd:cd05972 341 FEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSeelAEELQGHVK-KVLAPYKYPREIEFVEELPKTISG 419
|
....*..
1T5D_X 492 KVLRRQL 498
Cdd:cd05972 420 KIRRVEL 426
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
12-498 |
9.81e-49 |
|
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: 173.97 E-value: 9.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 12 ATRAPDhcALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGA--VPalLNPRLK 89
Cdd:cd05945 1 AAANPD--RPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHayVP--LDASSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 90 saelaelIKRGEMTAAVIAvgrqvADAIFQsgsgariiflgdlvrdgepysygppiedpqrEPAQPAFIFYTSGTTGLPK 169
Cdd:cd05945 77 -------AERIREILDAAK-----PALLIA-------------------------------DGDDNAYIIFTSGSTGRPK 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 170 AAIIPQRAAESRVLFMSTQVGLrhGRHNVVLGLMPLYHVVGFFAVLVAaLALDGTYVVVEEFRPVDALQLV---QQEQVT 246
Cdd:cd05945 114 GVQISHDNLVSFTNWMLSDFPL--GPGDVFLNQAPFSFDLSVMDLYPA-LASGATLVPVPRDATADPKQLFrflAEHGIT 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 247 SLFATPTHLDALAAAAAHAGSSLklDSLRHVTFAGATMPDAVLETVHQHLPGEKV-NIYGTTEA---------------- 309
Cdd:cd05945 191 VWVSTPSFAAMCLLSPTFTPESL--PSLRHFLFCGEVLPHKTARALQQRFPDARIyNTYGPTEAtvavtyievtpevldg 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 310 MNSLYMRQPKTGTEMApgffsevrIVRIGGgvdEIVANGEEGELIVAaSDSAFVGYLNQPQATAEKL--QDG--WYRTSD 385
Cdd:cd05945 269 YDRLPIGYAKPGAKLV--------ILDEDG---RPVPPGEKGELVIS-GPSVSKGYLNNPEKTAAAFfpDEGqrAYRTGD 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 386 VAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLG-ETLSADALDTF 464
Cdd:cd05945 337 LVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGaEAGLTKAIKAE 416
|
490 500 510
....*....|....*....|....*....|....
1T5D_X 465 CRsSELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:cd05945 417 LA-ERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
158-489 |
1.35e-47 |
|
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: 167.83 E-value: 1.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 158 IFYTSGTTGLPKAAIIPQR---AAEsrvlfMSTQVGLRHGRHNVVLGLMPLYHVVGFFAVLvAALALDGTYVVVEEFRPV 234
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGnliAAN-----LQLIHAMGLTEADVYLNMLPLFHIAGLNLAL-ATFHAGGANVVMEKFDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 235 DALQLVQQEQVTSLFATPTHLDALAAAAAHAGSSLklDSLRHVTfaGATMPDaVLETVHQHLPGEKVNIYGTTEAMNSLY 314
Cdd:cd17637 79 EALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDL--SSLRHVL--GLDAPE-TIQRFEETTGATFWSLYGQTETSGLVT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 315 MrQP---KTGTEMAPGFFSEVRIVrigGGVDEIVANGEEGElIVAASDSAFVGYLNQPQATAEKLQDGWYRTSDVAVWTP 391
Cdd:cd17637 154 L-SPyreRPGSAGRPGPLVRVRIV---DDNDRPVPAGETGE-IVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFDE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 392 EGTVRILGRV--DDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCrSSE 469
Cdd:cd17637 229 DGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFV-GSR 307
|
330 340
....*....|....*....|
1T5D_X 470 LADFKRPKRYFILDQLPKNA 489
Cdd:cd17637 308 IARYKKPRYVVFVEALPKTA 327
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
8-498 |
1.57e-47 |
|
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: 171.76 E-value: 1.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 8 LRRAATRAPDHCALAvpARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPR 87
Cdd:cd17651 1 FERQAARTPDAPALV--AEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 88 LKSAELAELIKRGEMTAAviavgrqVADAIFQSGSGARIIFLGDLVRDGEPySYGPPIEDPQREPAQPAFIFYTSGTTGL 167
Cdd:cd17651 79 YPAERLAFMLADAGPVLV-------LTHPALAGELAVELVAVTLLDQPGAA-AGADAEPDPALDADDLAYVIYTSGSTGR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 168 PKAAIIPQRAAESRVLFMSTQVGLRHGRHnvVLGLMPLYHVVGFFAVLvAALALDGTYVVV-EEFRPVDA--LQLVQQEQ 244
Cdd:cd17651 151 PKGVVMPHRSLANLVAWQARASSLGPGAR--TLQFAGLGFDVSVQEIF-STLCAGATLVLPpEEVRTDPPalAAWLDEQR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 245 VTSLFAtPTHLDALAAAAAHAGSSLkLDSLRHVTFAGATMP-DAVLETVHQHLPGEKV-NIYGTTE----------AMNS 312
Cdd:cd17651 228 ISRVFL-PTVALRALAEHGRPLGVR-LAALRYLLTGGEQLVlTEDLREFCAGLPGLRLhNHYGPTEthvvtalslpGDPA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 313 LYMRQPKTGTEMApgffsEVRiVRIGGGVDEIVANGEEGELIVAASDSAfVGYLNQPQATAEKLQDG-------WYRTSD 385
Cdd:cd17651 306 AWPAPPPIGRPID-----NTR-VYVLDAALRPVPPGVPGELYIGGAGLA-RGYLNRPELTAERFVPDpfvpgarMYRTGD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 386 VAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFC 465
Cdd:cd17651 379 LARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAAL 458
|
490 500 510
....*....|....*....|....*....|...
1T5D_X 466 RsSELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:cd17651 459 A-THLPEYMVPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
154-500 |
1.95e-47 |
|
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: 167.12 E-value: 1.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 154 QPAFIFYTSGTTGLPKAAIIPQRAAESRvlFMSTQVGLRHGRHNVVLGLMPLYHVVGFfAVLVAALALDGTYVVVEEFRP 233
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLAS--AAGLHSRLGFGGGDSWLLSLPLYHVGGL-AILVRSLLAGAELVLLERNQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 234 vdALQLVQQEQVTSLFATPTHLDALAAAAAHAGSslkLDSLRHVTFAGATMPDAVLETV-HQHLPGekVNIYGTTEAMNS 312
Cdd:cd17630 78 --LAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAA---LKSLRAVLLGGAPIPPELLERAaDRGIPL--YTTYGMTETASQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 313 LYMRQPKTGTEMAPGFFSEVRIVRIgggvdeiVANGEegelIVAASDSAFVGYLNqPQATAEKLQDGWYRTSDVAVWTPE 392
Cdd:cd17630 151 VATKRPDGFGRGGVGVLLPGRELRI-------VEDGE----IWVGGASLAMGYLR-GQLVPEFNEDGWFTTKDLGELHAD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 393 GTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGetLSADALDTFCRsSELAD 472
Cdd:cd17630 219 GRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGP--ADPAELRAWLK-DKLAR 295
|
330 340
....*....|....*....|....*...
1T5D_X 473 FKRPKRYFILDQLPKNALNKVLRRQLVQ 500
Cdd:cd17630 296 FKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
12-486 |
2.11e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 172.24 E-value: 2.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 12 ATRAPDHCALAvpARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSA 91
Cdd:PRK06164 20 ARARPDAVALI--DEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 92 ELAELIKRGEMTAAVIAVG-------RQVADAIFQSGSGARIIFLGDLVRDGEP------------YSYGPPI---EDPQ 149
Cdd:PRK06164 98 EVAHILGRGRARWLVVWPGfkgidfaAILAAVPPDALPPLRAIAVVDDAADATPapapgarvqlfaLPDPAPPaaaGERA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 150 REPAQPAFIFYTSGTTGLPKAAIIPQRAAesrvlfmstqvgLRHGR----------HNVVLGLMPLYHVVGfFAVLVAAL 219
Cdd:PRK06164 178 ADPDAGALLFTTSGTTSGPKLVLHRQATL------------LRHARaiaraygydpGAVLLAALPFCGVFG-FSTLLGAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 220 ALDGTYVVVEEFRPVDALQLVQQEQVTSLFATpthLDALAAAAAHAGSSLKLDSLRHVTFAG-ATMPDAVLETVHQH--- 295
Cdd:PRK06164 245 AGGAPLVCEPVFDAARTARALRRHRVTHTFGN---DEMLRRILDTAGERADFPSARLFGFASfAPALGELAALARARgvp 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 296 LPGekvnIYGTTEAMnSLYMRQPKT----------GTEMAPGffSEVRIVRIGGGvdEIVANGEEGELIVAASdSAFVGY 365
Cdd:PRK06164 322 LTG----LYGSSEVQ-ALVALQPATdpvsvrieggGRPASPE--ARVRARDPQDG--ALLPDGESGEIEIRAP-SLMRGY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 366 LNQPQATAEKLQ-DGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLadQRWGQSV 444
Cdd:PRK06164 392 LDNPDATARALTdDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKTV 469
|
490 500 510 520
....*....|....*....|....*....|....*....|...
1T5D_X 445 -TACVVPRLGETLSADALDTFCRSSeLADFKRPKRYFILDQLP 486
Cdd:PRK06164 470 pVAFVIPTDGASPDEAGLMAACREA-LAGFKVPARVQVVEAFP 511
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
29-500 |
4.26e-47 |
|
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: 169.15 E-value: 4.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 29 RLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVpALLNPRLKSAElaelikrgemtaaviA 108
Cdd:cd05971 6 KVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAI-AVPLFALFGPE---------------A 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 109 VGRQVADaifqsgSGARIIflgdlVRDGepysygppiedpqrePAQPAFIFYTSGTTGLPKAAIipqraaesrvlfmstq 188
Cdd:cd05971 70 LEYRLSN------SGASAL-----VTDG---------------SDDPALIIYTSGTTGPPKGAL---------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 189 vglrHGrHNVVLGLMP---LYH------------------VVGFFAVLVAALaLDGTYVVVEEFRPVD---ALQLVQQEQ 244
Cdd:cd05971 108 ----HA-HRVLLGHLPgvqFPFnlfprdgdlywtpadwawIGGLLDVLLPSL-YFGVPVLAHRMTKFDpkaALDLMSRYG 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 245 VTSLFATPTHLDALAAAAAHAgsSLKLDSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTEA----MNSLYMRQPKT 320
Cdd:cd05971 182 VTTAFLPPTALKMMRQQGEQL--KHAQVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECnlviGNCSALFPIKP 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 321 GTEMAPGFFSEVRIVRIGGgvdEIVANGEEGELIVAASDS-AFVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILG 399
Cdd:cd05971 260 GSMGKPIPGHRVAIVDDNG---TPLPPGEVGEIAVELPDPvAFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 400 RVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLS---ADALDTFCRsSELADFKRP 476
Cdd:cd05971 337 RDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSdalAREIQELVK-TRLAAHEYP 415
|
490 500
....*....|....*....|....
1T5D_X 477 KRYFILDQLPKNALNKVLRRQLVQ 500
Cdd:cd05971 416 REIEFVNELPRTATGKIRRRELRA 439
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
20-498 |
1.66e-46 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 167.66 E-value: 1.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 20 ALAVPARglRLTHAELRARVEAVA-ARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIK 98
Cdd:cd05958 3 CLRSPER--EWTYRDLLALANRIAnVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 99 RGEMTAAVIAVGRQVADAIfqsgsgariiflgdlvrdgepysygppiedpqrepaqpAFIFYTSGTTGLPKAAIIPQRAA 178
Cdd:cd05958 81 KARITVALCAHALTASDDI--------------------------------------CILAFTSGTTGAPKATMHFHRDP 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 179 ESRVLFMSTQVgLRHGRHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFRPVDALQLVQQEQVTSLFATPTHLDAL 258
Cdd:cd05958 123 LASADRYAVNV-LRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYKPTVLFTAPTAYRAM 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 259 AAAAAHAGSSLKldSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTEAMNSLYMRQP------KTGTEMaPGFFSEV 332
Cdd:cd05958 202 LAHPDAAGPDLS--SLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPgdarpgATGKPV-PGYEAKV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 333 rivrigggVDEI---VANGEEGELIVAaSDSAFVGYLNQPQATAekLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGG 409
Cdd:cd05958 279 --------VDDEgnpVPDGTIGRLAVR-GPTGCRYLADKRQRTY--VQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGG 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 410 ENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSAD---ALDTFCRsSELADFKRPKRYFILDQLP 486
Cdd:cd05958 348 YNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVlarELQDHAK-AHIAPYKYPRAIEFVTELP 426
|
490
....*....|..
1T5D_X 487 KNALNKVLRRQL 498
Cdd:cd05958 427 RTATGKLQRFAL 438
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
8-504 |
4.99e-46 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 168.82 E-value: 4.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 8 LRRAATRAPDhcALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPR 87
Cdd:PLN02860 13 LTRLATLRGN--AVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 88 LKSAELAELIkrgEMTAAVIAVGRQVADAIFQSGSGARI------IFLGDLVRDGEP-------------YSYGPPIEDP 148
Cdd:PLN02860 91 WSFEEAKSAM---LLVRPVMLVTDETCSSWYEELQNDRLpslmwqVFLESPSSSVFIflnsflttemlkqRALGTTELDY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 149 QREPAQPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGlrHGRHNVVLGLMPLYHVVGFFAVLvAALALDGTYVVV 228
Cdd:PLN02860 168 AWAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVG--YGEDDVYLHTAPLCHIGGLSSAL-AMLMVGACHVLL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 229 EEFRPVDALQLVQQEQVTSLFATPTHLDALAAAAAHAGSSLKLDSLRHVTFAGATMPDAVLETVHQHLPGEKV-NIYGTT 307
Cdd:PLN02860 245 PKFDAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLfSAYGMT 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 308 EAMNSL-YMR-QPKTGTEMAPGFFSEVRIVRIGGGVDEIVANGEEG---ELIVAASDSAFVG------------YLNQPQ 370
Cdd:PLN02860 325 EACSSLtFMTlHDPTLESPKQTLQTVNQTKSSSVHQPQGVCVGKPAphvELKIGLDESSRVGriltrgphvmlgYWGQNS 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 371 ATAEKL-QDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVv 449
Cdd:PLN02860 405 ETASVLsNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACV- 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1T5D_X 450 pRLGE----------------TLSADALDTFCRSSELADFKRPKRYFIL-DQLPKNALNKVLRRQLVQQVSS 504
Cdd:PLN02860 484 -RLRDgwiwsdnekenakknlTLSSETLRHHCREKNLSRFKIPKLFVQWrKPFPLTTTGKIRRDEVRREVLS 554
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
30-498 |
7.95e-46 |
|
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: 165.71 E-value: 7.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 30 LTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIKRGEMTAAVIAv 109
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTS- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 110 grqvADAIfqsgsgariiflgdlvrdgepysygppiedpqrepaqpAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQV 189
Cdd:cd05919 90 ----ADDI--------------------------------------AYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 190 -GLRHGrhNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFR-PVDALQLVQQEQVTSLFATPTHLDALAAAAAhaGS 267
Cdd:cd05919 128 lGLTPG--DRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWPtAERVLATLARFRPTVLYGVPTFYANLLDSCA--GS 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 268 SLKLDSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTEAMNSLYMRQP---KTGTEMAPGFFSEVRIVRIGGgvdEI 344
Cdd:cd05919 204 PDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPgawRLGSTGRPVPGYEIRLVDEEG---HT 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 345 VANGEEGELIVAaSDSAFVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTA 424
Cdd:cd05919 281 IPPGEEGDLLVR-GPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQH 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1T5D_X 425 PGVTEVVVIGLADQRWGQSVTACVVPRLGETLS---ADALDTFCRsSELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:cd05919 360 PAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQeslARDIHRHLL-ERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
12-501 |
1.05e-45 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 167.18 E-value: 1.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 12 ATRAPDHCALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSA 91
Cdd:PRK13391 7 AQTTPDKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 92 ELAELIKRGEMTAAVIAVG-RQVADAIFQSGSGARIIFLGDLVRDGEPY-SYGPPIED----PQREPAQPAFIFYTSGTT 165
Cdd:PRK13391 87 EAAYIVDDSGARALITSAAkLDVARALLKQCPGVRHRLVLDGDGELEGFvGYAEAVAGlpatPIADESLGTDMLYSSGTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 166 GLPKAAIIP---QRAAESRVLFMSTQVGLRHGRHNVVLGLMPLYHVVGFFAVLVAaLALDGTYVVVEEFRPVDALQLVQQ 242
Cdd:PRK13391 167 GRPKGIKRPlpeQPPDTPLPLTAFLQRLWGFRSDMVYLSPAPLYHSAPQRAVMLV-IRLGGTVIVMEHFDAEQYLALIEE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 243 EQVTSLFATPTHLDALAAAAAHAGSSLKLDSLRHVTFAGATMPDAVLET--------VHQHlpgekvniYGTTEAMNSLY 314
Cdd:PRK13391 246 YGVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHAAAPCPPQVKEQmidwwgpiIHEY--------YAATEGLGFTA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 315 MRQP----KTGTeMAPGFFSEVRIVRIGGgvdEIVANGEEGElIVAASDSAFVgYLNQPQATAEKL--QDGWYRTSDVAV 388
Cdd:PRK13391 318 CDSEewlaHPGT-VGRAMFGDLHILDDDG---AELPPGEPGT-IWFEGGRPFE-YLNDPAKTAEARhpDGTWSTVGDIGY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 389 WTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSAD---ALDTFC 465
Cdd:PRK13391 392 VDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPAlaaELIAFC 471
|
490 500 510
....*....|....*....|....*....|....*.
1T5D_X 466 RSSeLADFKRPKRYFILDQLPKNALNKVLRRQLVQQ 501
Cdd:PRK13391 472 RQR-LSRQKCPRSIDFEDELPRLPTGKLYKRLLRDR 506
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
27-498 |
3.74e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 165.46 E-value: 3.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 27 GLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIKRGE----- 101
Cdd:PRK08276 9 GEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGakvli 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 102 MTAAVIAVGRQVADAIfqsGSGARIIFLGDLVRDG-EPYSY---GPPIEDPQREPAQpAFIFYTSGTTGLPKAAIIPQRA 177
Cdd:PRK08276 89 VSAALADTAAELAAEL---PAGVPLLLVVAGPVPGfRSYEEalaAQPDTPIADETAG-ADMLYSSGTTGRPKGIKRPLPG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 178 A--ESRVLFMSTQVGLRHGRH--NVVLGLMPLYHVvgffAVLV---AALALDGTYVVVEEFRPVDALQLVQQEQVTSLFA 250
Cdd:PRK08276 165 LdpDEAPGMMLALLGFGMYGGpdSVYLSPAPLYHT----APLRfgmSALALGGTVVVMEKFDAEEALALIERYRVTHSQL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 251 TPTHLDALAAAAAHAGSSLKLDSLRHVTFAGATMPDAVLE--------TVHQHlpgekvniYGTTEA-----MNSL-YMR 316
Cdd:PRK08276 241 VPTMFVRMLKLPEEVRARYDVSSLRVAIHAAAPCPVEVKRamidwwgpIIHEY--------YASSEGggvtvITSEdWLA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 317 QPKT-GTEMApgffSEVRIVrigGGVDEIVANGEEGELIVAASDSAFvGYLNQPQATAE-KLQDGWYRTSDVAVWTPEGT 394
Cdd:PRK08276 313 HPGSvGKAVL----GEVRIL---DEDGNELPPGEIGTVYFEMDGYPF-EYHNDPEKTAAaRNPHGWVTVGDVGYLDEDGY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 395 VRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLS---ADALDTFCRsSELA 471
Cdd:PRK08276 385 LYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGdalAAELIAWLR-GRLA 463
|
490 500
....*....|....*....|....*..
1T5D_X 472 DFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:PRK08276 464 HYKCPRSIDFEDELPRTPTGKLYKRRL 490
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
1-501 |
7.97e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 165.59 E-value: 7.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 1 MQTVNEMLRRAATRAPDHCALAVpaRGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAV 80
Cdd:PRK06710 23 IQPLHKYVEQMASRYPEKKALHF--LGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 81 PALLNPRLKSAELA-ELIKRGemtAAVIAVGRQVADAIFQSGSGARII-FLGDLVRDGEPYSYG---PPIEDPQRE---- 151
Cdd:PRK06710 101 VVQTNPLYTERELEyQLHDSG---AKVILCLDLVFPRVTNVQSATKIEhVIVTRIADFLPFPKNllyPFVQKKQSNlvvk 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 152 -----------------------PAQP----AFIFYTSGTTGLPKAAIIPQRAAESRVLfMSTQ--VGLRHGRHnVVLGL 202
Cdd:PRK06710 178 vsesetihlwnsvekevntgvevPCDPendlALLQYTGGTTGFPKGVMLTHKNLVSNTL-MGVQwlYNCKEGEE-VVLGV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 203 MPLYHVVGFFAVLVAALALDGTYVVVEEFRPVDALQLVQQEQVTSLFATPTHLDALAAAAAHagSSLKLDSLRHVTFAGA 282
Cdd:PRK06710 256 LPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLL--KEYDISSIRACISGSA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 283 TMPDAVLETVHQHLPGEKVNIYGTTEA---MNSLYMRQPKT-GTEMAPGFFSEVRIVRIGGGvdEIVANGEEGELIVAAS 358
Cdd:PRK06710 334 PLPVEVQEKFETVTGGKLVEGYGLTESspvTHSNFLWEKRVpGSIGVPWPDTEAMIMSLETG--EALPPGEIGEIVVKGP 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 359 dSAFVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQ 438
Cdd:PRK06710 412 -QIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDP 490
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
1T5D_X 439 RWGQSVTACVVPRLGETLSADALDTFCRSSeLADFKRPKRYFILDQLPKNALNKVLRRQLVQQ 501
Cdd:PRK06710 491 YRGETVKAFVVLKEGTECSEEELNQFARKY-LAAYKVPKVYEFRDELPKTTVGKILRRVLIEE 552
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
16-498 |
1.74e-44 |
|
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: 162.83 E-value: 1.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 16 PDhcALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAE 95
Cdd:cd12114 1 PD--ATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 96 LIKRGEMTAAVI-AVGRQVADAIFQsgsgariiflgDLVRDGEPYSYGPPIEDPQREPAQPAFIFYTSGTTGLPKAAIIP 174
Cdd:cd12114 79 ILADAGARLVLTdGPDAQLDVAVFD-----------VLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMIS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 175 QRAAESRVLFMSTQVGLrhGRHNVVLGLMPLYH---VVGFFAVLVAAlaldGTYVVVEEFRPVDA---LQLVQQEQVTSL 248
Cdd:cd12114 148 HRAALNTILDINRRFAV--GPDDRVLALSSLSFdlsVYDIFGALSAG----ATLVLPDEARRRDPahwAELIERHGVTLW 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 249 FATPTHLDALAAAAAHAGSslKLDSLRHVTFAGATMPDAVLETVHQHLPG-EKVNIYGTTEA-MNSLYMRQPKTGTEMAP 326
Cdd:cd12114 222 NSVPALLEMLLDVLEAAQA--LLPSLRLVLLSGDWIPLDLPARLRALAPDaRLISLGGATEAsIWSIYHPIDEVPPDWRS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 327 ---GFFSEVRIVRIgggVDEI---VANGEEGELIVAASDSAfVGYLNQPQATAEK---LQDG--WYRTSDVAVWTPEGTV 395
Cdd:cd12114 300 ipyGRPLANQRYRV---LDPRgrdCPDWVPGELWIGGRGVA-LGYLGDPELTAARfvtHPDGerLYRTGDLGRYRPDGTL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 396 RILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLaDQRWGQSVTACVVPRL-GETLSADALDTFcRSSELADFK 474
Cdd:cd12114 376 EFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDNdGTPIAPDALRAF-LAQTLPAYM 453
|
490 500
....*....|....*....|....
1T5D_X 475 RPKRYFILDQLPKNALNKVLRRQL 498
Cdd:cd12114 454 IPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
2-498 |
1.13e-43 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 162.23 E-value: 1.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 2 QTVNEMLRRAATRAPDhcALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVP 81
Cdd:PRK06155 21 RTLPAMLARQAERYPD--RPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 82 ALLNPRLKSAELAELIKRGEmtAAVIAVGRQVADAIfqsgsgaRIIFLGDLVR------DGEP-------YSYGPPIEDP 148
Cdd:PRK06155 99 VPINTALRGPQLEHILRNSG--ARLLVVEAALLAAL-------EAADPGDLPLpavwllDAPAsvsvpagWSTAPLPPLD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 149 QR------EPAQPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGLRHGrhNVVLGLMPLYHVVGFfAVLVAALALD 222
Cdd:PRK06155 170 APapaaavQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGAD--DVLYTTLPLFHTNAL-NAFFQALLAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 223 GTYVVVEEF---RPVDALQLVQQ-------EQVTSLFATPThldalaaaaahaGSSLKLDSLRhVTFAGATmPDAVLETV 292
Cdd:PRK06155 247 ATYVLEPRFsasGFWPAVRRHGAtvtyllgAMVSILLSQPA------------RESDRAHRVR-VALGPGV-PAALHAAF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 293 HQHLPGEKVNIYGTTEAMNSLY--MRQPKTGT--EMAPGFfsEVRIVRIGggvDEIVANGEEGELIVAASDS-AFV-GYL 366
Cdd:PRK06155 313 RERFGVDLLDGYGSTETNFVIAvtHGSQRPGSmgRLAPGF--EARVVDEH---DQELPDGEPGELLLRADEPfAFAtGYF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 367 NQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTA 446
Cdd:PRK06155 388 GMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMA 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
1T5D_X 447 CVVPRLGETLSADALDTFCRsSELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:PRK06155 468 AVVLRDGTALEPVALVRHCE-PRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
30-450 |
1.54e-43 |
|
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: 159.68 E-value: 1.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 30 LTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELikrgemtaaviav 109
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYI------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 110 grqVADaifqsgSGARIIFLGDlvrdgepysygppiedpqrePAQPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQv 189
Cdd:cd05907 73 ---LND------SEAKALFVED--------------------PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAER- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 190 gLRHGRHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFRPV-DALQLVQQeqvTSLFATPTH-LDALAAAAAHAGS 267
Cdd:cd05907 123 -LPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLlDDLSEVRP---TVFLAVPRVwEKVYAAIKVKAVP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 268 SLK--------LDSLRHVTFAGATMPDAVLE-------TVHQhlpgekvnIYGTTE-----AMNSLymRQPKTGTEMAPG 327
Cdd:cd05907 199 GLKrklfdlavGGRLRFAASGGAPLPAELLHffralgiPVYE--------GYGLTEtsavvTLNPP--GDNRIGTVGKPL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 328 FFSEVRIvrigggvdeivanGEEGElIVAASDSAFVGYLNQPQATAE-KLQDGWYRTSDVAVWTPEGTVRILGRVDDMII 406
Cdd:cd05907 269 PGVEVRI-------------ADDGE-ILVRGPNVMLGYYKNPEATAEaLDADGWLHTGDLGEIDEDGFLHITGRKKDLII 334
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
1T5D_X 407 -SGGENIHPSEIERVLGTAPGVTEVVVIGlaDQRwgQSVTACVVP 450
Cdd:cd05907 335 tSGGKNISPEPIENALKASPLISQAVVIG--DGR--PFLVALIVP 375
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
27-487 |
1.15e-42 |
|
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: 158.26 E-value: 1.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 27 GLRLTHAELRARVEAVAARLHaDGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNprlKSAELaelikrGEMTAAV 106
Cdd:cd05909 5 GTSLTYRKLLTGAIALARKLA-KMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLN---YTAGL------RELRACI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 107 IAVGRQVA------------DAIFQSGSGARIIFLGDL---------VRDGEPYSYGPPIEDPQ-----REPAQPAFIFY 160
Cdd:cd05909 75 KLAGIKTVltskqfieklklHHLFDVEYDARIVYLEDLrakiskadkCKAFLAGKFPPKWLLRIfgvapVQPDDPAVILF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 161 TSGTTGLPKAAIIPQRAAESRVLFMSTQVGLRhgRHNVVLGLMPLYHVVGFFAVLVAALaLDGTYVVVeEFRPVDALQ-- 238
Cdd:cd05909 155 TSGSEGLPKGVVLSHKNLLANVEQITAIFDPN--PEDVVFGALPFFHSFGLTGCLWLPL-LSGIKVVF-HPNPLDYKKip 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 239 -LVQQEQVTSLFATPTHLDALAAAAahagSSLKLDSLRHVtFAGAtmpDAVLETVHQhLPGEKVNI-----YGTTE---- 308
Cdd:cd05909 231 eLIYDKKATILLGTPTFLRGYARAA----HPEDFSSLRLV-VAGA---EKLKDTLRQ-EFQEKFGIrilegYGTTEcspv 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 309 -AMNSLYM-RQPKTGTEMAPGFfsEVRIVRIGGGVDeiVANGEEGELIVAASdSAFVGYLNQPQATAEKLQDGWYRTSDV 386
Cdd:cd05909 302 iSVNTPQSpNKEGTVGRPLPGM--EVKIVSVETHEE--VPIGEGGLLLVRGP-NVMLGYLNEPELTSFAFGDGWYDTGDI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 387 AVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTA-PGVTEVVVIGLADQRWGQSVTACVVPrlgETLSADALDTFC 465
Cdd:cd05909 377 GKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTT---TDTDPSSLNDIL 453
|
490 500
....*....|....*....|..
1T5D_X 466 RSSELADFKRPKRYFILDQLPK 487
Cdd:cd05909 454 KNAGISNLAKPSYIHQVEEIPL 475
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
2-450 |
4.69e-42 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 158.34 E-value: 4.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 2 QTVNEMLRRAATRAPDHCALAVPARG--LRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGA 79
Cdd:COG1022 11 DTLPDLLRRRAARFPDRVALREKEDGiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 80 VPALLNPRLKSAELAELIKRGEMTAAVIAVGRQVA------------DAIFQ-----SGSGARIIFLGDLVRDGEPYSYG 142
Cdd:COG1022 91 VTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDkllevrdelpslRHIVVldprgLRDDPRLLSLDELLALGREVADP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 143 PPIEDP--QREPAQPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGLRHGrhNVVLGLMPLYHVVGFFaVLVAALA 220
Cdd:COG1022 171 AELEARraAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPG--DRTLSFLPLAHVFERT-VSYYALA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 221 LDGTYVVVEEFRPV-DALQLVQ------------------QEQVTS-------LF--ATPTHLDALAAAAAHAGSSLkLD 272
Cdd:COG1022 248 AGATVAFAESPDTLaEDLREVKptfmlavprvwekvyagiQAKAEEagglkrkLFrwALAVGRRYARARLAGKSPSL-LL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 273 SLRH------------------VTFA---GATMPDAVLE-------TVHQhlpgekvnIYGTTE-----AMNSLymRQPK 319
Cdd:COG1022 327 RLKHaladklvfsklrealggrLRFAvsgGAALGPELARffralgiPVLE--------GYGLTEtspviTVNRP--GDNR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 320 TGT--EMAPGffSEVRIvrigggvdeivanGEEGELIVAaSDSAFVGYLNQPQATAEKL-QDGWYRTSDVAVWTPEGTVR 396
Cdd:COG1022 397 IGTvgPPLPG--VEVKI-------------AEDGEILVR-GPNVMKGYYKNPEATAEAFdADGWLHTGDIGELDEDGFLR 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
1T5D_X 397 ILGRVDDMII-SGGENIHPSEIERVLGTAPGVTEVVVIGlaDQRwgQSVTACVVP 450
Cdd:COG1022 461 ITGRKKDLIVtSGGKNVAPQPIENALKASPLIEQAVVVG--DGR--PFLAALIVP 511
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
20-502 |
1.24e-41 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 154.64 E-value: 1.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 20 ALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIkr 99
Cdd:PRK09029 19 AIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEELL-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 100 gemtaaviavgRQVADAIFQSGSGARIIFLGDLVRDGEPYSYGPPIEDPQRepaqPAFIFYTSGTTGLPKAAIIPQRA-- 177
Cdd:PRK09029 97 -----------PSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVAWQPQR----LATMTLTSGSTGLPKAAVHTAQAhl 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 178 --AESRVLFMstqvglRHGRHNVVLGLMPLYHVVGFfAVLVAALALDGTYVVVEEFRPVDALQlvqqeQVT--SLFATpt 253
Cdd:PRK09029 162 asAEGVLSLM------PFTAQDSWLLSLPLFHVSGQ-GIVWRWLYAGATLVVRDKQPLEQALA-----GCThaSLVPT-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 254 hldalaaaaahagsSLK--LD------SLRHVTFAGATMPdavLETVHQhlpGEKVNI-----YGtteamnslyMrqpkt 320
Cdd:PRK09029 228 --------------QLWrlLDnrseplSLKAVLLGGAAIP---VELTEQ---AEQQGIrcwcgYG---------L----- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 321 gTEMApgffSEVRIVRIGG--GVDEIVANGE----EGELIVAASDSAfVGYLNQPQATAEKLQDGWYRTSDVAVWTpEGT 394
Cdd:PRK09029 274 -TEMA----STVCAKRADGlaGVGSPLPGREvklvDGEIWLRGASLA-LGYWRQGQLVPLVNDEGWFATRDRGEWQ-NGE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 395 VRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLsaDALDTFCrSSELADFK 474
Cdd:PRK09029 347 LTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESDSEAAV--VNLAEWL-QDKLARFQ 423
|
490 500
....*....|....*....|....*...
1T5D_X 475 RPKRYFILDQLPKNALNKVLRRQLVQQV 502
Cdd:PRK09029 424 QPVAYYLLPPELKNGGIKISRQALKEWV 451
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
11-499 |
3.15e-41 |
|
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: 154.07 E-value: 3.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 11 AATRAPDHCALAVPARGLRLTH----AELRARVEAvaarlhADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNP 86
Cdd:cd05929 1 LEARDLDRAQVFHQRRLLLLDVysiaLNRNARAAA------AEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 87 RLKSAElaelikrgemTAAVIAVGRQVADAIFQSGSGARIIFLGDLV-RDGEPysyGPPIEDPqrepAQPAFIFYTSGTT 165
Cdd:cd05929 75 RAPRAE----------ACAIIEIKAAALVCGLFTGGGALDGLEDYEAaEGGSP---ETPIEDE----AAGWKMLYSGGTT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 166 GLPKAaIIPQRAAESRVLF--MSTQVGLRHGRHNVVLGLMPLYHVVGFFAVLVAaLALDGTYVVVEEFRPVDALQLVQQE 243
Cdd:cd05929 138 GRPKG-IKRGLPGGPPDNDtlMAAALGFGPGADSVYLSPAPLYHAAPFRWSMTA-LFMGGTLVLMEKFDPEEFLRLIERY 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 244 QVTSLFATPTHLDALAAAAAHAGSSLKLDSLRHVTFAGATMPDAVLETVhQHLPGEKV-NIYGTTEAMNSLYMRqpktGT 322
Cdd:cd05929 216 RVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQW-IDWGGPIIwEYYGGTEGQGLTIIN----GE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 323 EMA--PG-----FFSEVRIVrigGGVDEIVANGEEGELIVAASDSafVGYLNQPQATAEKL-QDGWYRTSDVAVWTPEGT 394
Cdd:cd05929 291 EWLthPGsvgraVLGKVHIL---DEDGNEVPPGEIGEVYFANGPG--FEYTNDPEKTAAARnEGGWSTLGDVGYLDEDGY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 395 VRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGE---TLSADALDTFCRSSeLA 471
Cdd:cd05929 366 LYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGAdagTALAEELIAFLRDR-LS 444
|
490 500
....*....|....*....|....*...
1T5D_X 472 DFKRPKRYFILDQLPKNALNKVLRRQLV 499
Cdd:cd05929 445 RYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
6-498 |
3.65e-41 |
|
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: 153.24 E-value: 3.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 6 EMLRRAATRAPDHCALAVPARglRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLN 85
Cdd:cd12115 3 DLVEAQAARTPDAIALVCGDE--SLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 86 PRLKSAELAELIKRgemtaaviavgrqvadaifqsgSGARIIFLgdlvrdgepysygppiedpqrEPAQPAFIFYTSGTT 165
Cdd:cd12115 81 PAYPPERLRFILED----------------------AQARLVLT---------------------DPDDLAYVIYTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 166 GLPKAAIIPQRAAESRVLFMSTQVGLRHGRHnvVLGLMPLYHVVGFFAvLVAALALDGTYVVVEefrpvDALQLVQ---Q 242
Cdd:cd12115 118 GRPKGVAIEHRNAAAFLQWAAAAFSAEELAG--VLASTSICFDLSVFE-LFGPLATGGKVVLAD-----NVLALPDlpaA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 243 EQVTSLFATPTHLDalaaaaahagSSLKLD----SLRHVTFAGATMPDAVLETVHQHLPGEKV-NIYGTTEAmnSLYmrq 317
Cdd:cd12115 190 AEVTLINTVPSAAA----------ELLRHDalpaSVRVVNLAGEPLPRDLVQRLYARLQVERVvNLYGPSED--TTY--- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 318 pKTGTEMAPGFFSEVRIVR-IGGGVDEI-------VANGEEGELIVAASDSAfVGYLNQPQATAEK-LQDGW------YR 382
Cdd:cd12115 255 -STVAPVPPGASGEVSIGRpLANTQAYVldralqpVPLGVPGELYIGGAGVA-RGYLGRPGLTAERfLPDPFgpgarlYR 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 383 TSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALD 462
Cdd:cd12115 333 TGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLR 412
|
490 500 510
....*....|....*....|....*....|....*.
1T5D_X 463 TFCRsSELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:cd12115 413 RHLG-TRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
6-498 |
5.14e-41 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 154.83 E-value: 5.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 6 EMLRRAATRAPDHcalavPA---RGLRLTHAELRARVEAVAARLHAD-GLRPQQRVAVVAPNSADVVIAILALHRLGAVP 81
Cdd:PRK08974 27 DMFEQAVARYADQ-----PAfinMGEVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNLLQYPIALFGILRAGMIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 82 ALLNPRLKSAELAELIKRGEMTAAVIA--VGRQVADAIFQSGSGARIIF-LGDLVRDG---------------------- 136
Cdd:PRK08974 102 VNVNPLYTPRELEHQLNDSGAKAIVIVsnFAHTLEKVVFKTPVKHVILTrMGDQLSTAkgtlvnfvvkyikrlvpkyhlp 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 137 ------EPYSYGPPIE--DPQREPAQPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVG--LRHGRHNVVLGLmPLY 206
Cdd:PRK08974 182 daisfrSALHKGRRMQyvKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGplLHPGKELVVTAL-PLY 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 207 HVvgfFAVLVAAL---ALDGTYVVVEEFRPVDAL-QLVQQEQVTSLFATPTHLDALAAAAAHagSSLKLDSLRHVTFAGA 282
Cdd:PRK08974 261 HI---FALTVNCLlfiELGGQNLLITNPRDIPGFvKELKKYPFTAITGVNTLFNALLNNEEF--QELDFSSLKLSVGGGM 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 283 TMPDAVLETVHQHLPGEKVNIYGTTEAMNSL----YMRQPKTGTEMAPGFFSEVRIVRIGGGVdeiVANGEEGELIVAAs 358
Cdd:PRK08974 336 AVQQAVAERWVKLTGQYLLEGYGLTECSPLVsvnpYDLDYYSGSIGLPVPSTEIKLVDDDGNE---VPPGEPGELWVKG- 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 359 DSAFVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQ 438
Cdd:PRK08974 412 PQVMLGYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSE 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 439 RWGQSVTACVVPRlGETLSADALDTFCRsSELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:PRK08974 492 VSGEAVKIFVVKK-DPSLTEEELITHCR-RHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
16-498 |
3.54e-40 |
|
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: 150.60 E-value: 3.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 16 PDHCALAVpaRGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAE 95
Cdd:cd17649 1 PDAVALVF--GDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 96 LIKrgemtaaviavgrqvadaifqsGSGARIIFlgdlvrdgepysygppiedpQREPAQPAFIFYTSGTTGLPKAAIIPQ 175
Cdd:cd17649 79 MLE----------------------DSGAGLLL--------------------THHPRQLAYVIYTSGSTGTPKGVAVSH 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 176 RA------AESRVLFMSTQvglrhgrhNVVLGLMPLyHVVGFFAVLVAALaLDGTYVVV---EEFRPVDAL-QLVQQEQV 245
Cdd:cd17649 117 GPlaahcqATAERYGLTPG--------DRELQFASF-NFDGAHEQLLPPL-ICGACVVLrpdELWASADELaEMVRELGV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 246 TSLFATPTHLDALAAAAAHAGSSLKLdSLRHVTFAGATMPdavLETVHQHLPGEK--VNIYGTTEAMNSLYMRQPKTGTE 323
Cdd:cd17649 187 TVLDLPPAYLQQLAEEADRTGDGRPP-SLRLYIFGGEALS---PELLRRWLKAPVrlFNAYGPTEATVTPLVWKCEAGAA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 324 MAP-----GFFSEVRIVRIGGGVDEIVANGEEGELIVAASDSAfVGYLNQPQATAEK-LQDG-------WYRTSDVAVWT 390
Cdd:cd17649 263 RAGasmpiGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLA-RGYLGRPELTAERfVPDPfgapgsrLYRTGDLARWR 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 391 PEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVtACVVPRLGETLSAD--ALDTFCRSS 468
Cdd:cd17649 342 DDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLV-AYVVLRAAAAQPELraQLRTALRAS 420
|
490 500 510
....*....|....*....|....*....|
1T5D_X 469 eLADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:cd17649 421 -LPDYMVPAHLVFLARLPLTPNGKLDRKAL 449
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
8-498 |
9.55e-40 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 151.71 E-value: 9.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 8 LRRAATRAPDHCALAVPARglRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPR 87
Cdd:PLN03102 20 LKRASECYPNRTSIIYGKT--RFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 88 LKSAELAELIKRGEmtAAVIAVGRQVADAI---------FQSGSGARIIFLGDLVRDGEPYS----YGPPIEDPQREPAQ 154
Cdd:PLN03102 98 LDATSIAAILRHAK--PKILFVDRSFEPLArevlhllssEDSNLNLPVIFIHEIDFPKRPSSeeldYECLIQRGEPTPSL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 155 PAFIF------------YTSGTTGLPKAAIIPQRAAESRVLfmSTQVGLRHGRHNVVLGLMPLYHVVGF-FAVLVAALAl 221
Cdd:PLN03102 176 VARMFriqdehdpislnYTSGTTADPKGVVISHRGAYLSTL--SAIIGWEMGTCPVYLWTLPMFHCNGWtFTWGTAARG- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 222 dGTYVVVEEFRPVDALQLVQQEQVTSLFATPTHLDALAAaaahaGSSLKLD---SLRHVTFAGATMPDAVLETVhQHLPG 298
Cdd:PLN03102 253 -GTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLK-----GNSLDLSprsGPVHVLTGGSPPPAALVKKV-QRLGF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 299 EKVNIYGTTEAMNSL--------YMRQPKTgTEMApgfFSEVRIVRIGGGVDEIVANGEE-----------GELIVAASd 359
Cdd:PLN03102 326 QVMHAYGLTEATGPVlfcewqdeWNRLPEN-QQME---LKARQGVSILGLADVDVKNKETqesvprdgktmGEIVIKGS- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 360 SAFVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQR 439
Cdd:PLN03102 401 SIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPT 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1T5D_X 440 WGQSVTACVVPRLGETLSADALDTF----------CRSSeLADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:PLN03102 481 WGETPCAFVVLEKGETTKEDRVDKLvtrerdlieyCREN-LPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
20-498 |
1.10e-39 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 149.75 E-value: 1.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 20 ALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELaELIKR 99
Cdd:cd12116 3 ATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRL-RYILE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 100 GEMTAAVIAvgrqvadaifQSGSGARIIFLGDLVRDGEPYSYGPPIE-DPQREPAQPAFIFYTSGTTGLPKAAIIPQRAA 178
Cdd:cd12116 82 DAEPALVLT----------DDALPDRLPAGLPVLLLALAAAAAAPAApRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 179 ESRVLFMSTQVGLRHGRHnvVLGLMPlyhvVGF-FAVLVAALAL--DGTYVVVEEFRPVDALQLVQ---QEQVTSLFATP 252
Cdd:cd12116 152 VNFLHSMRERLGLGPGDR--LLAVTT----YAFdISLLELLLPLlaGARVVIAPRETQRDPEALARlieAHSITVMQATP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 253 ThldalaaaaahaGSSLKLDS----LRHVT-FAGATMPDAVLETVHQHLPGEKVNIYGTTEAmnSLYmrqpKTGTEMAPG 327
Cdd:cd12116 226 A------------TWRMLLDAgwqgRAGLTaLCGGEALPPDLAARLLSRVGSLWNLYGPTET--TIW----STAARVTAA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 328 ffseVRIVRIGGGVD-----------EIVANGEEGELIVAaSDSAFVGYLNQPQATAEKLQDG--------WYRTSDVAV 388
Cdd:cd12116 288 ----AGPIPIGRPLAntqvyvldaalRPVPPGVPGELYIG-GDGVAQGYLGRPALTAERFVPDpfagpgsrLYRTGDLVR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 389 WTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIgLADQRWGQSVTACVVPRLGETLSADALDTFCRSS 468
Cdd:cd12116 363 RRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVV-VREDGGDRRLVAYVVLKAGAAPDAAALRAHLRAT 441
|
490 500 510
....*....|....*....|....*....|
1T5D_X 469 eLADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:cd12116 442 -LPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
20-498 |
4.01e-39 |
|
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: 147.40 E-value: 4.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 20 ALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELikr 99
Cdd:cd17652 3 APAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYM--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 100 gemtaaviavgrqVADAifqsgsGARIIFlgdlvrdgepysygppiedpqREPAQPAFIFYTSGTTGLPKAAIIPQRAAE 179
Cdd:cd17652 80 -------------LADA------RPALLL---------------------TTPDNLAYVIYTSGSTGRPKGVVVTHRGLA 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 180 SrvlFMSTQV-GLRHGRHNVVLGlmplYHVVGF---FAVLVAALALDGTYVVV--EEFRPVDAL-QLVQQEQVTSLFATP 252
Cdd:cd17652 120 N---LAAAQIaAFDVGPGSRVLQ----FASPSFdasVWELLMALLAGATLVLApaEELLPGEPLaDLLREHRITHVTLPP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 253 THLDALaaaaahagSSLKLDSLRHVTFAGATMPdavLETVHQHLPGEK-VNIYGTTEAMNSLYMRQPKTGTEMAPgffse 331
Cdd:cd17652 193 AALAAL--------PPDDLPDLRTLVVAGEACP---AELVDRWAPGRRmINAYGPTETTVCATMAGPLPGGGVPP----- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 332 vrivrIGGGVD-----------EIVANGEEGELIVAASDSAfVGYLNQPQATAEK-LQDGW-------YRTSDVAVWTPE 392
Cdd:cd17652 257 -----IGRPVPgtrvyvldarlRPVPPGVPGELYIAGAGLA-RGYLNRPGLTAERfVADPFgapgsrmYRTGDLARWRAD 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 393 GTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCRSSeLAD 472
Cdd:cd17652 331 GQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAER-LPG 409
|
490 500
....*....|....*....|....*.
1T5D_X 473 FKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:cd17652 410 YMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
6-500 |
7.23e-39 |
|
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: 146.69 E-value: 7.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 6 EMLRRAATRAPDhcALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGA--VPal 83
Cdd:cd17653 1 DAFERIAAAHPD--AVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAayVP-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 84 LNPRLKSAELaelikrgemtaaviavgrqvaDAIFQsGSGARIIFLGDLVRDgepysygppiedpqrepaqPAFIFYTSG 163
Cdd:cd17653 77 LDAKLPSARI---------------------QAILR-TSGATLLLTTDSPDD-------------------LAYIIFTSG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 164 TTGLPKAAIIPQRAAESRVLFMSTQVGLRHG-RHNVVLGlmplyhvVGFFA---VLVAALALDGTYVVVEefrPVDALQL 239
Cdd:cd17653 116 STGIPKGVMVPHRGVLNYVSQPPARLDVGPGsRVAQVLS-------IAFDAcigEIFSTLCNGGTLVLAD---PSDPFAH 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 240 VQQEqVTSLFATPTHLdalaaaaahagSSLK---LDSLRHVTFAGATMPDAVLETvhqHLPG-EKVNIYGTTE-----AM 310
Cdd:cd17653 186 VART-VDALMSTPSIL-----------STLSpqdFPNLKTIFLGGEAVPPSLLDR---WSPGrRLYNAYGPTEctissTM 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 311 NSLYMRQPKTGTEMAPGffSEVRIVRIGggvDEIVANGEEGELIVAASDSAfVGYLNQPQATAEK-----LQDGW--YRT 383
Cdd:cd17653 251 TELLPGQPVTIGKPIPN--STCYILDAD---LQPVPEGVVGEICISGVQVA-RGYLGNPALTASKfvpdpFWPGSrmYRT 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 384 SDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIER-VLGTAPGVTEVVVIGLADQrwgqsVTACVVPrlgETLSADALD 462
Cdd:cd17653 325 GDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEvVLQSQPEVTQAAAIVVNGR-----LVAFVTP---ETVDVDGLR 396
|
490 500 510
....*....|....*....|....*....|....*...
1T5D_X 463 TFCRSSeLADFKRPKRYFILDQLPKNALNKVLRRQLVQ 500
Cdd:cd17653 397 SELAKH-LPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
2-498 |
1.11e-37 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 145.73 E-value: 1.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 2 QTVNEMLRRAATRAPDHCALAvpARGLRLTHAELRARVEAVAARL--HADgLRPQQRVAVVAPNSADVVIAILALHRLGA 79
Cdd:PRK12492 24 KSVVEVFERSCKKFADRPAFS--NLGVTLSYAELERHSAAFAAYLqqHTD-LVPGDRIAVQMPNVLQYPIAVFGALRAGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 80 VPALLNPRLKSAELAELIKRGEMTAAVI--AVGRQVADAIFQSGSGARI-IFLGDLVrdgePYSYG-------------- 142
Cdd:PRK12492 101 IVVNTNPLYTAREMRHQFKDSGARALVYlnMFGKLVQEVLPDTGIEYLIeAKMGDLL----PAAKGwlvntvvdkvkkmv 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 143 PPIEDPQ------------REPAQP--------AFIFYTSGTTGLPKAAIIPQR---AAESRVLFMSTQVG------LRH 193
Cdd:PRK12492 177 PAYHLPQavpfkqalrqgrGLSLKPvpvglddiAVLQYTGGTTGLAKGAMLTHGnlvANMLQVRACLSQLGpdgqplMKE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 194 GRHnVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFRPVDA-LQLVQQEQVTSLFATPTHLDALAAAAAHagSSLKLD 272
Cdd:PRK12492 257 GQE-VMIAPLPLYHIYAFTANCMCMMVSGNHNVLITNPRDIPGfIKELGKWRFSALLGLNTLFVALMDHPGF--KDLDFS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 273 SLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTE----AMNSLYMRQPKTGTEMAPGFFSEVRIVRIGGGVdeiVANG 348
Cdd:PRK12492 334 ALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTEtspvASTNPYGELARLGTVGIPVPGTALKVIDDDGNE---LPLG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 349 EEGELIVAASdSAFVGYLNQPQATAEKLQ-DGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGV 427
Cdd:PRK12492 411 ERGELCIKGP-QVMKGYWQQPEATAEALDaEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKV 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1T5D_X 428 TEVVVIGLADQRWGQSVTACVVPRLGeTLSADALDTFCRSSeLADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:PRK12492 490 ANCAAIGVPDERSGEAVKLFVVARDP-GLSVEELKAYCKEN-FTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
37-499 |
1.42e-37 |
|
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: 143.73 E-value: 1.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 37 ARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPAL----LNPRLKSAELAELI--KRGEMTAAVIAVG 110
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLvfvpLNPTLKESVLRYLVadAGGRIVLADAGAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 111 RQVADAIFQSGSGARIIFLGDLVRDGEPYSYGPPiedpqrEPAQPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVG 190
Cdd:cd05922 81 DRLRDALPASPDPGTVLDADGIRAARASAPAHEV------SHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 191 LRhgRHNVVLGLMPLYHVVGFfAVLVAALALDGTYVVVEEFRPVDAL-QLVQQEQVTSLFATPTHLDALAAAAAhagSSL 269
Cdd:cd05922 155 IT--ADDRALTVLPLSYDYGL-SVLNTHLLRGATLVLTNDGVLDDAFwEDLREHGATGLAGVPSTYAMLTRLGF---DPA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 270 KLDSLRHVTFAGATMPDAVLETVHQHLPGEKVNI-YGTTEAM-NSLYM------RQPKTGTEMAPGffSEVRIVRIGGGv 341
Cdd:cd05922 229 KLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVmYGQTEATrRMTYLpperilEKPGSIGLAIPG--GEFEILDDDGT- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 342 deIVANGEEGElIVAASDSAFVGYLNQPQA-TAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERV 420
Cdd:cd05922 306 --PTPPGEPGE-IVHRGPNVMKGYWNDPPYrRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAA 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1T5D_X 421 LGTAPGVTEVVVIGLADQRwGQSVTACVVPRLGETLSaDALDTFcrSSELADFKRPKRYFILDQLPKNALNKVLRRQLV 499
Cdd:cd05922 383 ARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKIDPK-DVLRSL--AERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
16-498 |
1.53e-37 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 144.98 E-value: 1.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 16 PDHCALAVPARGLRLTHAELRARVEAVAARLHAD-GLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPrlkSAELA 94
Cdd:PLN02574 53 NGDTALIDSSTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNP---SSSLG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 95 ELIKRGEMTAAVIA------VGR---------QVADAI-FQSGSGARIIFLGDLVRDGEPYSyGPPIEdpQREPAQpafI 158
Cdd:PLN02574 130 EIKKRVVDCSVGLAftspenVEKlsplgvpviGVPENYdFDSKRIEFPKFYELIKEDFDFVP-KPVIK--QDDVAA---I 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 159 FYTSGTTGLPKAAIIPQR----AAESRVLFMSTQVGlRHGRHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFRPV 234
Cdd:PLN02574 204 MYSSGTTGASKGVVLTHRnliaMVELFVRFEASQYE-YPGSDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRFDAS 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 235 DALQLVQQEQVTSLFATPTHLDALAAAAAHAGSSLkLDSLRHVTFAGATMPDAVLETVHQHLPG-EKVNIYGTTEA---- 309
Cdd:PLN02574 283 DMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEV-LKSLKQVSCGAAPLSGKFIQDFVQTLPHvDFIQGYGMTEStavg 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 310 ---MNSLYMRQPKTGTEMAPGFfsEVRIVRIGGGvdEIVANGEEGELIVAASdSAFVGYLNQPQATAEKL-QDGWYRTSD 385
Cdd:PLN02574 362 trgFNTEKLSKYSSVGLLAPNM--QAKVVDWSTG--CLLPPGNCGELWIQGP-GVMKGYLNNPKATQSTIdKDGWLRTGD 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 386 VAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFC 465
Cdd:PLN02574 437 IAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYV 516
|
490 500 510
....*....|....*....|....*....|...
1T5D_X 466 rSSELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:PLN02574 517 -AKQVAPYKKVRKVVFVQSIPKSPAGKILRREL 548
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
2-498 |
1.58e-37 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 147.50 E-value: 1.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 2 QTVNEMLRRAATRAPDHCALAvpARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVP 81
Cdd:PRK10252 458 TTLSALVAQQAAKTPDAPALA--DARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAW 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 82 ALLNPRLKSAELAeLIKRGEMTAAVIAVGRQVADaifqsgsgariiFLGdlVRDGEPYSYGPPIEDPQ------REPAQP 155
Cdd:PRK10252 536 LPLDTGYPDDRLK-MMLEDARPSLLITTADQLPR------------FAD--VPDLTSLCYNAPLAPQGaaplqlSQPHHT 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 156 AFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGLRHGrhNVVLGLMPLYHVVG---FFAVLVAalaldGTYVVV---E 229
Cdd:PRK10252 601 AYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTAD--DVVLQKTPCSFDVSvweFFWPFIA-----GAKLVMaepE 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 230 EFR-PVDALQLVQQEQVTSLFATPTHLDALAAAAAHAGSSLKLDSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTE 308
Cdd:PRK10252 674 AHRdPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTE 753
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 309 AM--NSLYmrqPKTGTEMAPGFFSEVRI--------VRIGGGVDEIVANGEEGELIVAASDSAfVGYLNQPQATAEKLQD 378
Cdd:PRK10252 754 AAvdVSWY---PAFGEELAAVRGSSVPIgypvwntgLRILDARMRPVPPGVAGDLYLTGIQLA-QGYLGRPDLTASRFIA 829
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 379 G-------WYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVV----VIGLADQRWGQS--VT 445
Cdd:PRK10252 830 DpfapgerMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVthacVINQAAATGGDArqLV 909
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
1T5D_X 446 ACVVPRLGETLSADALDTFCRsSELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:PRK10252 910 GYLVSQSGLPLDTSALQAQLR-ERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
155-495 |
2.90e-37 |
|
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: 139.46 E-value: 2.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 155 PAFIFYTSGTTGLPKAAIipqRAAESRVLFMSTQVGLRHG-RHNVVLGLMPLYHVVGFFAvLVAALALDGTYVVVEEFRP 233
Cdd:cd17633 2 PFYIGFTSGTTGLPKAYY---RSERSWIESFVCNEDLFNIsGEDAILAPGPLSHSLFLYG-AISALYLGGTFIGQRKFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 234 VDALQLVQQEQVTSLFATPTHLDALAAAAAHAgsslklDSLRHVTFAGATMPDAVLETVHQHLP-GEKVNIYGTTEA--- 309
Cdd:cd17633 78 KSWIRKINQYNATVIYLVPTMLQALARTLEPE------SKIKSIFSSGQKLFESTKKKLKNIFPkANLIEFYGTSELsfi 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 310 MNSLYMRQPKTGTEMAPgfFSEVRIvRIgggvdEIVANGEEGELIVAaSDSAFVGYLNQPQATAeklqDGWYRTSDVAVW 389
Cdd:cd17633 152 TYNFNQESRPPNSVGRP--FPNVEI-EI-----RNADGGEIGKIFVK-SEMVFSGYVRGGFSNP----DGWMSVGDIGYV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 390 TPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVprlGETLSADALDTFCRsSE 469
Cdd:cd17633 219 DEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS---GDKLTYKQLKRFLK-QK 294
|
330 340
....*....|....*....|....*.
1T5D_X 470 LADFKRPKRYFILDQLPKNALNKVLR 495
Cdd:cd17633 295 LSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
2-498 |
5.84e-37 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 142.90 E-value: 5.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 2 QTVNEMLRRAATRAPDHCALAVPARG---LRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLG 78
Cdd:PRK08008 7 QHLRQMWDDLADVYGHKTALIFESSGgvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 79 AVPALLNPRLKSAELAELIKRGEMTAAVIA-----VGRQVADaifQSGSGARIIFLgdlVRDGEPYSYGppIEDPQREPA 153
Cdd:PRK08008 87 AIMVPINARLLREESAWILQNSQASLLVTSaqfypMYRQIQQ---EDATPLRHICL---TRVALPADDG--VSSFTQLKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 154 Q---------------PAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGLRhgRHNVVLGLMPLYHVVGFFAVLVAA 218
Cdd:PRK08008 159 QqpatlcyapplstddTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALR--DDDVYLTVMPAFHIDCQCTAAMAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 219 LALDGTYVVVEEFRPVDALQLVQQEQVTSLFATPTHLDALAAAAAHAGSslKLDSLRHVTFAgATMPDAVLETVHQHLPG 298
Cdd:PRK08008 237 FSAGATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLMVQPPSAND--RQHCLREVMFY-LNLSDQEKDAFEERFGV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 299 EKVNIYGTTEAMNSLY-------MRQPKTGTemaPGFFSEVRIVRIGGGVdeiVANGEEGELIV--AASDSAFVGYLNQP 369
Cdd:PRK08008 314 RLLTSYGMTETIVGIIgdrpgdkRRWPSIGR---PGFCYEAEIRDDHNRP---LPAGEIGEICIkgVPGKTIFKEYYLDP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 370 QATAEKLQ-DGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACV 448
Cdd:PRK08008 388 KATAKVLEaDGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFV 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
1T5D_X 449 VPRLGETLSADALDTFCrSSELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:PRK08008 468 VLNEGETLSEEEFFAFC-EQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
2-498 |
1.05e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 142.59 E-value: 1.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 2 QTVNEMLRRAATRAPDHCALAvpARGLRLTHAELRARVEAVAARL-HADGLRPQQRVAVVAPNSADVVIAILALHRLGAV 80
Cdd:PRK05677 24 PNIQAVLKQSCQRFADKPAFS--NLGKTLTYGELYKLSGAFAAWLqQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 81 PALLNPRLKS---------------------AELAE---------------------LIKRGEMTAAVIAVGRQV-ADAI 117
Cdd:PRK05677 102 VVNTNPLYTAremehqfndsgakalvclanmAHLAEkvlpktgvkhvivtevadmlpPLKRLLINAVVKHVKKMVpAYHL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 118 FQSgsgariIFLGDLVRDGEpysyGPPIEDPQREPAQPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVG--LRHGR 195
Cdd:PRK05677 182 PQA------VKFNDALAKGA----GQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGsnLNEGC 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 196 HnVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFRPVDA-LQLVQQEQVTSLFATPTHLDALAAAAAHAgsslKLD-S 273
Cdd:PRK05677 252 E-ILIAPLPLYHIYAFTFHCMAMMLIGNHNILISNPRDLPAmVKELGKWKFSGFVGLNTLFVALCNNEAFR----KLDfS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 274 LRHVTFAGA-TMPDAVLETVHQHLPGEKVNIYGTTEA-----MNSLYMRQPKTGTEMAPGffsevRIVRIGGGVDEIVAN 347
Cdd:PRK05677 327 ALKLTLSGGmALQLATAERWKEVTGCAICEGYGMTETspvvsVNPSQAIQVGTIGIPVPS-----TLCKVIDDDGNELPL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 348 GEEGELIVAASdSAFVGYLNQPQATAEKL-QDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPG 426
Cdd:PRK05677 402 GEVGELCVKGP-QVMKGYWQRPEATDEILdSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPG 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1T5D_X 427 VTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCRsSELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:PRK05677 481 VLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMR-ANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
1-501 |
3.33e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 140.97 E-value: 3.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 1 MQTVNEMLRRaatRAPDHcALAVPARGLRLTHAELRARVEAVAARLhaDGLRPQQR---VAVVAPNSADVVIAILALHRL 77
Cdd:PRK07867 4 APTVAELLLP---LAEDD-DRGLYFEDSFTSWREHIRGSAARAAAL--RARLDPTRpphVGVLLDNTPEFSLLLGAAALS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 78 GAVPALLNPRLKSAELAELIKRGEmtAAVIAVGRQVADAIFQSGSGARIIflgdlVRDGEPYSY---GPPIEDPQREPAQ 154
Cdd:PRK07867 78 GIVPVGLNPTRRGAALARDIAHAD--CQLVLTESAHAELLDGLDPGVRVI-----NVDSPAWADelaAHRDAEPPFRVAD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 155 PAFIF---YTSGTTGLPKAAIIPQRAAESRVLFMSTQVGLrhGRHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEF 231
Cdd:PRK07867 151 PDDLFmliFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGL--GPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRKF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 232 RPVDALQLVQQEQVTS----------LFATPTHLDALAaaaahagsslklDSLRHVTFAGATMPDavLETVHQHLPGEKV 301
Cdd:PRK07867 229 SASGFLPDVRRYGATYanyvgkplsyVLATPERPDDAD------------NPLRIVYGNEGAPGD--IARFARRFGCVVV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 302 NIYGTTEAMNSLY------------------MRQPKTGTEMAPGFFSEVRIVrigggvdeivaNGEE--GELIVAASDSA 361
Cdd:PRK07867 295 DGFGSTEGGVAITrtpdtppgalgplppgvaIVDPDTGTECPPAEDADGRLL-----------NADEaiGELVNTAGPGG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 362 FVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWG 441
Cdd:PRK07867 364 FEGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVG 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
1T5D_X 442 QSVTACVVPRLGETLSADALDTFCRS-SELADFKRPKRYFILDQLPKNALNKVLRRQLVQQ 501
Cdd:PRK07867 444 DQVMAALVLAPGAKFDPDAFAEFLAAqPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAE 504
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
8-498 |
5.72e-36 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 140.75 E-value: 5.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 8 LRRAATRAPDHCAlaVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPR 87
Cdd:PLN02479 26 LERAAVVHPTRKS--VVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 88 LKSAELAELIkrGEMTAAVIAVGRQ-----------VADAIFQSGSGARIIFLGDLVRDGEPYSYG---PPIE------- 146
Cdd:PLN02479 104 LNAPTIAFLL--EHSKSEVVMVDQEfftlaeealkiLAEKKKSSFKPPLLIVIGDPTCDPKSLQYAlgkGAIEyekflet 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 147 -DPQREPAQPA------FIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGLRHGRhnVVLGLMPLYHVVGF-FAVLVAA 218
Cdd:PLN02479 182 gDPEFAWKPPAdewqsiALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGA--VYLWTLPMFHCNGWcFTWTLAA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 219 LAldGTYVVVEEFRPVDALQLVQQEQVTSLFATPTHLDALAAAAAHAgSSLKLDSLRHVTFAGATMPDAVLETVHQHlpG 298
Cdd:PLN02479 260 LC--GTNICLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSE-TILPLPRVVHVMTAGAAPPPSVLFAMSEK--G 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 299 EKV-NIYGTTEAMNslymrqPKTGTEMAPGFFS-----EVRI-----VRIGG--GVD--------EIVANGEEGELIVAA 357
Cdd:PLN02479 335 FRVtHTYGLSETYG------PSTVCAWKPEWDSlppeeQARLnarqgVRYIGleGLDvvdtktmkPVPADGKTMGEIVMR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 358 SDSAFVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLAD 437
Cdd:PLN02479 409 GNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPD 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1T5D_X 438 QRWGQSVTACVVPRLG-----ETLSADALDTFCRsSELADFKRPKRyFILDQLPKNALNKVLRRQL 498
Cdd:PLN02479 489 ERWGESPCAFVTLKPGvdksdEAALAEDIMKFCR-ERLPAYWVPKS-VVFGPLPKTATGKIQKHVL 552
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
6-495 |
6.36e-36 |
|
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: 140.32 E-value: 6.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 6 EMLRRAATRAPDHCALA-VPARGLR--LTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAV-- 80
Cdd:cd05970 21 DVVDAMAKEYPDKLALVwCDDAGEEriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIai 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 81 --PALLNP-----RLKSAELAELIKRGEMTaaviaVGRQVADAIFQSGSGARIIFLGDLVRDG------EPYSYGPPIED 147
Cdd:cd05970 101 paTHQLTAkdivyRIESADIKMIVAIAEDN-----IPEEIEKAAPECPSKPKLVWVGDPVPEGwidfrkLIKNASPDFER 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 148 PQREPAQ----PAFIFYTSGTTGLPKAAiipqraaesrvlfmstqvglrhgRHNVvlgLMPLYHVV----------GFFA 213
Cdd:cd05970 176 PTANSYPcgedILLVYFSSGTTGMPKMV-----------------------EHDF---TYPLGHIVtakywqnvreGGLH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 214 VLVAALA-------------LDGTYVVV---EEFRPVDALQLVQQEQVTSLFATPTHLDALAAAAAhagSSLKLDSLRHV 277
Cdd:cd05970 230 LTVADTGwgkavwgkiygqwIAGAAVFVydyDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDL---SRYDLSSLRYC 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 278 TFAGATMPDAVLETVHQHLPGEKVNIYGTTE---AMNSLYMRQPKTGT--EMAPGFfsEVRIVRIGGgvdEIVANGEEGE 352
Cdd:cd05970 307 TTAGEALNPEVFNTFKEKTGIKLMEGFGQTEttlTIATFPWMEPKPGSmgKPAPGY--EIDLIDREG---RSCEAGEEGE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 353 LIVAASDSA----FVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVT 428
Cdd:cd05970 382 IVIRTSKGKpvglFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVL 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1T5D_X 429 EVVVIGLADQRWGQSVTACVVP----RLGETLSADALDTFCRSSelADFKRPKRYFILDQLPKNALNKVLR 495
Cdd:cd05970 462 ECAVTGVPDPIRGQVVKATIVLakgyEPSEELKKELQDHVKKVT--APYKYPRIVEFVDELPKTISGKIRR 530
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
30-495 |
1.04e-35 |
|
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: 138.03 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 30 LTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLnprlksaelaelikrgeMTA-AVIA 108
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPL-----------------FTAfGPKA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 109 VGRQVAdaifqsGSGARIIFLGDLVRDgepysygppiedpqREPAQPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQ 188
Cdd:cd05973 64 IEHRLR------TSGARLVVTDAANRH--------------KLDSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 189 VGLR--------------HGRHNVVLGLMPLYHVVGFFAvlvAALALDGTYVVVEEFrpvdalqlvqqeQVTSLFATPTH 254
Cdd:cd05973 124 VDLRpedsfwnaadpgwaYGLYYAITGPLALGHPTILLE---GGFSVESTWRVIERL------------GVTNLAGSPTA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 255 LDALAAAAAHAGSSLKLdSLRHVTFAGATMPDAVLE--------TVHQHlpgekvniYGTTE---AMNSLY-----MRQP 318
Cdd:cd05973 189 YRLLMAAGAEVPARPKG-RLRRVSSAGEPLTPEVIRwfdaalgvPIHDH--------YGQTElgmVLANHHalehpVHAG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 319 KTGTEMaPGFfsevRIVRIGGGVDEiVANGEEGELIVAASDSA---FVGYLNQPQATAEklqDGWYRTSDVAVWTPEGTV 395
Cdd:cd05973 260 SAGRAM-PGW----RVAVLDDDGDE-LGPGEPGRLAIDIANSPlmwFRGYQLPDTPAID---GGYYLTGDTVEFDPDGSF 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 396 RILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLS---ADALDTFCRsSELAD 472
Cdd:cd05973 331 SFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTpalADELQLHVK-KRLSA 409
|
490 500
....*....|....*....|...
1T5D_X 473 FKRPKRYFILDQLPKNALNKVLR 495
Cdd:cd05973 410 HAYPRTIHFVDELPKTPSGKIQR 432
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
157-487 |
1.10e-35 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 136.36 E-value: 1.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 157 FIFYTSGTTGLPKAAI-----IPQRAAESR-----VLFMSTQVGLRHGRHN--VVLGLMPLYHVVGFFAVlvAALALDGT 224
Cdd:cd05924 7 YILYTGGTTGMPKGVMwrqedIFRMLMGGAdfgtgEFTPSEDAHKAAAAAAgtVMFPAPPLMHGTGSWTA--FGGLLGGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 225 YVVV--EEFRPVDALQLVQQEQVTSLFATPTHLDALAAAAAHAGSSLKLDSLRHVTFAGATMPDAVLETVHQHLPGEK-V 301
Cdd:cd05924 85 TVVLpdDRFDPEEVWRTIEKHKVTSMTIVGDAMARPLIDALRDAGPYDLSSLFAISSGGALLSPEVKQGLLELVPNITlV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 302 NIYGTTEAMNslymrqpkTGTEMAPGFFSEVRI-VRIGGG---VDE---IVANGEEGELIVAASDSAFVGYLNQPQATAE 374
Cdd:cd05924 165 DAFGSSETGF--------TGSGHSAGSGPETGPfTRANPDtvvLDDdgrVVPPGSGGVGWIARRGHIPLGYYGDEAKTAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 375 --KLQDG--WYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVP 450
Cdd:cd05924 237 tfPEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQL 316
|
330 340 350
....*....|....*....|....*....|....*..
1T5D_X 451 RLGETLSADALDTFCRsSELADFKRPKRYFILDQLPK 487
Cdd:cd05924 317 REGAGVDLEELREHCR-TRIARYKLPKQVVFVDEIER 352
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
1-501 |
2.33e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 138.62 E-value: 2.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 1 MQTVNEMLRraaTRAPDHcALAVPARGLRLTHAEL--RARVEAVAARLHADGLRPQQrVAVVAPNSADVVIAILALHRLG 78
Cdd:PRK13388 2 RDTIAQLLR---DRAGDD-TIAVRYGDRTWTWREVlaEAAARAAALIALADPDRPLH-VGVLLGNTPEMLFWLAAAALGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 79 AVPALLNPRLKSAELAELIKRGEMTAAVI-AVGRQVADAIfqSGSGARIiflgdLVRDGEPYS---YGPPIEDPQRE--P 152
Cdd:PRK13388 77 YVLVGLNTTRRGAALAADIRRADCQLLVTdAEHRPLLDGL--DLPGVRV-----LDVDTPAYAelvAAAGALTPHREvdA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 153 AQPAFIFYTSGTTGLPKAAIIPQraaeSRVLFMSTQVGLRHG--RHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEE 230
Cdd:PRK13388 150 MDPFMLIFTSGTTGAPKAVRCSH----GRLAFAGRALTERFGltRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 231 FRPVDALQLVQQEQVT----------SLFATPTHLDALAaaaahagsslklDSLRHVTFAGATMPDavLETVHQHLPGEK 300
Cdd:PRK13388 226 FSASGFLDDVRRYGATyfnyvgkplaYILATPERPDDAD------------NPLRVAFGNEASPRD--IAEFSRRFGCQV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 301 VNIYGTTE------------------AMNSLYMRQPKTGTEMAPGFFSEvrivrigggvDEIVANGEE--GELIVAASDS 360
Cdd:PRK13388 292 EDGYGSSEgavivvrepgtppgsigrGAPGVAIYNPETLTECAVARFDA----------HGALLNADEaiGELVNTAGAG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 361 AFVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRW 440
Cdd:PRK13388 362 FFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERV 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
1T5D_X 441 GQSVTACVVPRLGETLSADALDTFCRSSE-LADFKRPKRYFILDQLPKNALNKVLRRQLVQQ 501
Cdd:PRK13388 442 GDQVMAALVLRDGATFDPDAFAAFLAAQPdLGTKAWPRYVRIAADLPSTATNKVLKRELIAQ 503
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
4-498 |
2.98e-35 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 140.86 E-value: 2.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 4 VNEMLRRAATRAPDhcALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPAL 83
Cdd:PRK12316 2005 VHQRIAEQAARAPE--AIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVP 2082
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 84 LNPRLKSAELAELIkrGEMTAAVIAVGRQVADAIFQSGSGARIiflgDLVRDGEPYSYgpPIEDPQRE--PAQPAFIFYT 161
Cdd:PRK12316 2083 LDPNYPAERLAYML--EDSGAALLLTQRHLLERLPLPAGVARL----PLDRDAEWADY--PDTAPAVQlaGENLAYVIYT 2154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 162 SGTTGLPKAAIIPQRAAESRVLFMSTQVGLRHGrhNVVLGLMPlYHVVGFFAVLVAALaLDGTYVVVEEFRPVDALQL-- 239
Cdd:PRK12316 2155 SGSTGLPKGVAVSHGALVAHCQAAGERYELSPA--DCELQFMS-FSFDGAHEQWFHPL-LNGARVLIRDDELWDPEQLyd 2230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 240 -VQQEQVTSLFATPTHLDALAAAAAHAGSSLkldSLRHVTFAGATMPDAVLETVHQHLPGEK-VNIYGTTEAMNSLYM-- 315
Cdd:PRK12316 2231 eMERHGVTILDFPPVYLQQLAEHAERDGRPP---AVRVYCFGGEAVPAASLRLAWEALRPVYlFNGYGPTEAVVTPLLwk 2307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 316 --RQPKTGTEMAP-GFFSEVRIVRIGGGVDEIVANGEEGELIVAASDSAfVGYLNQPQATAEK-LQDGW-------YRTS 384
Cdd:PRK12316 2308 crPQDPCGAAYVPiGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLA-RGYLNRPGLTAERfVPDPFsasgerlYRTG 2386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 385 DVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLaDQRWGQSVTACVVPRLGETLSADALDTF 464
Cdd:PRK12316 2387 DLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAAEDLLAELRAW 2465
|
490 500 510
....*....|....*....|....*....|....
1T5D_X 465 CRSSeLADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:PRK12316 2466 LAAR-LPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
7-498 |
4.11e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 137.82 E-value: 4.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 7 MLRRAATRAPDHCALaVPARGlRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNP 86
Cdd:PRK13383 40 LLAVTAARWPGRTAI-IDDDG-ALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPIST 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 87 RLKSAELAELIKRGEMTaaVIAVGRQVADAIfqSGSGARIIFLGDLVRDGEPYSYGPPIEDPQRepaqpaFIFYTSGTTG 166
Cdd:PRK13383 118 EFRSDALAAALRAHHIS--TVVADNEFAERI--AGADDAVAVIDPATAGAEESGGRPAVAAPGR------IVLLTSGTTG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 167 LPKAaiIPQRAAESRVLFMSTQV----GLRHGRHNVVLglMPLYHVVGFfAVLVAALALDGTYVVVEEFRPVDALQLVQQ 242
Cdd:PRK13383 188 KPKG--VPRAPQLRSAVGVWVTIldrtRLRTGSRISVA--MPMFHGLGL-GMLMLTIALGGTVLTHRHFDAEAALAQASL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 243 EQVTSLFATPTHLDALAAAAAHAGSSLKLDSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTE------AMNSLYMR 316
Cdd:PRK13383 263 HRADAFTAVPVVLARILELPPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEvgigalATPADLRD 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 317 QPKTGTEMAPGffSEVRIV-RIGGGVDEIVAngeeGELIVAasdsafvGYLNQPQAT---AEKLQDGWYRTSDVAVWTPE 392
Cdd:PRK13383 343 APETVGKPVAG--CPVRILdRNNRPVGPRVT----GRIFVG-------GELAGTRYTdggGKAVVDGMTSTGDMGYLDNA 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 393 GTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCRsSELAD 472
Cdd:PRK13383 410 GRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLK-DRVSR 488
|
490 500
....*....|....*....|....*.
1T5D_X 473 FKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:PRK13383 489 FEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
16-498 |
1.03e-34 |
|
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: 135.29 E-value: 1.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 16 PDHCALAVPARglRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAE 95
Cdd:cd17650 1 PDAIAVSDATR--QLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 96 LIKRgemtaaviavgrqvadaifqsgSGARIIFLgdlvrdgepysygppiedpqrEPAQPAFIFYTSGTTGLPKAAIIPQ 175
Cdd:cd17650 79 MLED----------------------SGAKLLLT---------------------QPEDLAYVIYTSGTTGKPKGVMVEH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 176 RAAESRVLFMSTQVGLrhGRHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEE---FRPVDALQLVQQEQVTSLFATP 252
Cdd:cd17650 116 RNVAHAAHAWRREYEL--DSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDevkLDPAALYDLILKSRITLMESTP 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 253 THLDALAAAAAHAGssLKLDSLRhVTFAGATMPDA-----VLETVHQHLpgEKVNIYGTTEA-MNSLYMrqpktgtEMAP 326
Cdd:cd17650 194 ALIRPVMAYVYRNG--LDLSAMR-LLIVGSDGCKAqdfktLAARFGQGM--RIINSYGVTEAtIDSTYY-------EEGR 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 327 GFFSEVRIVRIGGGV-----------DEIVANGEEGELIVAASDSAfVGYLNQPQATAEKLQDG-------WYRTSDVAV 388
Cdd:cd17650 262 DPLGDSANVPIGRPLpntamyvlderLQPQPVGVAGELYIGGAGVA-RGYLNRPELTAERFVENpfapgerMYRTGDLAR 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 389 WTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRlgETLSADALDTFCrSS 468
Cdd:cd17650 341 WRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAA--ATLNTAELRAFL-AK 417
|
490 500 510
....*....|....*....|....*....|
1T5D_X 469 ELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:cd17650 418 ELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
12-498 |
1.08e-34 |
|
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: 135.92 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 12 ATRAPDHCALAVPARglRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPrlksA 91
Cdd:cd17655 7 AEKTPDHTAVVFEDQ--TLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDP----D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 92 ELAELIKrgemtaaVIAVGRQVADAIFQSGSGARIIFLGDLVRDGEPYSYGPPIED--PQREPAQPAFIFYTSGTTGLPK 169
Cdd:cd17655 81 YPEERIQ-------YILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENlePVSKSDDLAYVIYTSGSTGKPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 170 AAIIPQRaaesrvlfmstqvglrhGRHNVVLGLMPLYHV-----VGFFAVLV---------AALALDGTYVVV--EEFRP 233
Cdd:cd17655 154 GVMIEHR-----------------GVVNLVEWANKVIYQgehlrVALFASISfdasvteifASLLSGNTLYIVrkETVLD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 234 VDAL-QLVQQEQVTSLFATPTHLDALAAAAAHAGSSLKldslrHVTFAGATMPdAVLETVHQHLPGEKV---NIYGTTE- 308
Cdd:cd17655 217 GQALtQYIRQNRITIIDLTPAHLKLLDAADDSEGLSLK-----HLIVGGEALS-TELAKKIIELFGTNPtitNAYGPTEt 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 309 ---AMNSLYMRQPKTGTEM---APGFFSEVRIVRIGGgvdEIVANGEEGELIVAAsDSAFVGYLNQPQATAEK-LQDGW- 380
Cdd:cd17655 291 tvdASIYQYEPETDQQVSVpigKPLGNTRIYILDQYG---RPQPVGVAGELYIGG-EGVARGYLNRPELTAEKfVDDPFv 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 381 -----YRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRlgET 455
Cdd:cd17655 367 pgermYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSE--KE 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....
1T5D_X 456 LSADALDTFCrSSELADFKRPKrYFI-LDQLPKNALNKVLRRQL 498
Cdd:cd17655 445 LPVAQLREFL-ARELPDYMIPS-YFIkLDEIPLTPNGKVDRKAL 486
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
4-498 |
5.39e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 137.21 E-value: 5.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 4 VNEMLRRAATRAPDhcALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPAL 83
Cdd:PRK12467 1576 VHQLIEDQAAATPE--AVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVP 1653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 84 LNPRLKSAELAELIKrgEMTAAVIAVGRQVADAiFQSGSGARIIFLgdlvRDGEPYSYGPPIEDPQREPA--QPAFIFYT 161
Cdd:PRK12467 1654 LDPEYPRERLAYMIE--DSGIELLLTQSHLQAR-LPLPDGLRSLVL----DQEDDWLEGYSDSNPAVNLApqNLAYVIYT 1726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 162 SGTTGLPKAAIIPQRAAESRVLFMSTQVGLRHGrhNVVLGLMPL---YHVVGFFAVLvaalaLDGTYVVVEEF----RPV 234
Cdd:PRK12467 1727 SGSTGRPKGAGNRHGALVNRLCATQEAYQLSAA--DVVLQFTSFafdVSVWELFWPL-----INGARLVIAPPgahrDPE 1799
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 235 DALQLVQQEQVTSLFATPTHLDALAAAAAHAGSSLkldSLRHVTFAGATMPDAVLETVHQHLPGEK-VNIYGTTEAMNSL 313
Cdd:PRK12467 1800 QLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPL---SLRRVVCGGEALEVEALRPWLERLPDTGlFNLYGPTETAVDV 1876
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 314 YMRQPKTGTEmapgffSEVRIVRIGGGVDEI-----------VANGEEGELIVAASDSAfVGYLNQPQATAEKL------ 376
Cdd:PRK12467 1877 THWTCRRKDL------EGRDSVPIGQPIANLstyildaslnpVPIGVAGELYLGGVGLA-RGYLNRPALTAERFvadpfg 1949
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 377 -QDG-WYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGlADQRWGQSVTACVVPRLGE 454
Cdd:PRK12467 1950 tVGSrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIA-QDGANGKQLVAYVVPTDPG 2028
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
1T5D_X 455 TLSADALDTFCRS-------SELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:PRK12467 2029 LVDDDEAQVALRAilknhlkASLPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
12-498 |
1.80e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 132.83 E-value: 1.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 12 ATRAPDHCALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSA 91
Cdd:PRK13390 7 AQIAPDRPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 92 ELAELIkrGEMTAAVIAVGRQVADAIFQSGS--------GARIIFLGDLvrDGEPYSYGPPIEDpqrepaQP--AFIFYT 161
Cdd:PRK13390 87 EADYIV--GDSGARVLVASAALDGLAAKVGAdlplrlsfGGEIDGFGSF--EAALAGAGPRLTE------QPcgAVMLYS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 162 SGTTGLPKA--AIIPQRAAE---------SRVLFMSTQvglrhgrHNVVLGLMPLYHVVGF-FAVLVAALAldGTYVVVE 229
Cdd:PRK13390 157 SGTTGFPKGiqPDLPGRDVDapgdpivaiARAFYDISE-------SDIYYSSAPIYHAAPLrWCSMVHALG--GTVVLAK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 230 EFRPVDALQLVQQEQVTSLFATPTHLDALAAAAAHAGSSLKLDSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTEA 309
Cdd:PRK13390 228 RFDAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 310 MNSLYMRQPKTGTEMAPGFFSEVRIVRIGGGVDEIVANGEEGElIVAASDSAFVGYLNQPQATAEKLQDG---WYRTSDV 386
Cdd:PRK13390 308 HGMTFIDSPDWLAHPGSVGRSVLGDLHICDDDGNELPAGRIGT-VYFERDRLPFRYLNDPEKTAAAQHPAhpfWTTVGDL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 387 AVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLG----ETLSADALD 462
Cdd:PRK13390 387 GSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGirgsDELARELID 466
|
490 500 510
....*....|....*....|....*....|....*.
1T5D_X 463 tFCRsSELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:PRK13390 467 -YTR-SRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
29-434 |
4.96e-33 |
|
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: 130.55 E-value: 4.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 29 RLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLksaelaelikRGEMTAAVIA 108
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNL----------RGESLAHCLN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 109 VgrqvadaifqsgSGARIIFlgdlvrdgepysygppiedpqrepAQPAFIFYTSGTTGLPKAAIIPQRaaesRVLFMSTQ 188
Cdd:cd05940 73 V------------SSAKHLV------------------------VDAALYIYTSGTTGLPKAAIISHR----RAWRGGAF 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 189 VG--LRHGRHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFRPVDALQLVQQEQVTS----------LFATPTHLD 256
Cdd:cd05940 113 FAgsGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATIfqyigelcryLLNQPPKPT 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 257 ALA-AAAAHAGSSLKLDSLRHVT--FAGATmpdaVLEtvhqhlpgekvnIYGTTEAMNSLYMRQPKTGT---------EM 324
Cdd:cd05940 193 ERKhKVRMIFGNGLRPDIWEEFKerFGVPR----IAE------------FYAATEGNSGFINFFGKPGAigrnpsllrKV 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 325 APGFFSEV-----RIVRIGGGVDEIVANGEEGELIVAASD-SAFVGYLNQPQATAEKLQ------DGWYRTSDVAVWTPE 392
Cdd:cd05940 257 APLALVKYdlesgEPIRDAEGRCIKVPRGEPGLLISRINPlEPFDGYTDPAATEKKILRdvfkkgDAWFNTGDLMRLDGE 336
|
410 420 430 440
....*....|....*....|....*....|....*....|..
1T5D_X 393 GTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIG 434
Cdd:cd05940 337 GFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYG 378
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
2-504 |
7.64e-33 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 133.75 E-value: 7.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 2 QTVNEMLRRAATRAPDHCALAVPARglRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVP 81
Cdd:PRK12467 512 DCVHQLIEAQARQHPERPALVFGEQ--VLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAY 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 82 ALLNPRLKSAELAELIkrgEMTAAVIAVGRQVADAIFQSGSGARIIFLGDLVRDGEPYSYGPPieDPQREPAQPAFIFYT 161
Cdd:PRK12467 590 VPLDPEYPQDRLAYML---DDSGVRLLLTQSHLLAQLPVPAGLRSLCLDEPADLLCGYSGHNP--EVALDPDNLAYVIYT 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 162 SGTTGLPKAAIIPQRAAESRVLFMSTQVGLrhGRHNVVLGLMPlYHVVGFFAVLVAALALDGTYVVVEE---FRPVDALQ 238
Cdd:PRK12467 665 SGSTGQPKGVAISHGALANYVCVIAERLQL--AADDSMLMVST-FAFDLGVTELFGALASGATLHLLPPdcaRDAEAFAA 741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 239 LVQQEQVTSLFATPTHLDALAAAAAHAGSSlkldSLRHVTFAGATMPDAVLETVHQHLPGEKV-NIYGTTEA-MNSLYMR 316
Cdd:PRK12467 742 LMADQGVTVLKIVPSHLQALLQASRVALPR----PQRALVCGGEALQVDLLARVRALGPGARLiNHYGPTETtVGVSTYE 817
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 317 QPKTGTEMAPGFFS---EVRIVRIGGGVDEIVANGEEGELIVAASDSAFvGYLNQPQATAEKL------QDG--WYRTSD 385
Cdd:PRK12467 818 LSDEERDFGNVPIGqplANLGLYILDHYLNPVPVGVVGELYIGGAGLAR-GYHRRPALTAERFvpdpfgADGgrLYRTGD 896
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 386 VAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACV--VPRLGETLSA--DAL 461
Cdd:PRK12467 897 LARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVpaAVADGAEHQAtrDEL 976
|
490 500 510 520
....*....|....*....|....*....|....*....|...
1T5D_X 462 DTFCRSSeLADFKRPKRYFILDQLPKNALNKVLRRQLVQQVSS 504
Cdd:PRK12467 977 KAQLRQV-LPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDAS 1018
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
8-428 |
2.08e-32 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 130.40 E-value: 2.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 8 LRRAATRAPDHCALAVP--------ARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGA 79
Cdd:PRK09274 12 LPRAAQERPDQLAVAVPggrgadgkLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 80 VPALLNPRLKSAELAELIKRGEmTAAVIAVGR-QVADAIFQSGSGARI-------------IFLGDLVRDGEPYSYGPPI 145
Cdd:PRK09274 92 VPVLVDPGMGIKNLKQCLAEAQ-PDAFIGIPKaHLARRLFGWGKPSVRrlvtvggrllwggTTLATLLRDGAAAPFPMAD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 146 EDPQrepaQPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGLRHGrhNVVLGLMPLyhvvgfFAVLVAALaldGTY 225
Cdd:PRK09274 171 LAPD----DMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPG--EIDLPTFPL------FALFGPAL---GMT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 226 VVVEEF---RPVDA-----LQLVQQEQVTSLFATPTHLDALAAAAAHAGssLKLDSLRHVTFAGATMPDAVLETVHQHLP 297
Cdd:PRK09274 236 SVIPDMdptRPATVdpaklFAAIERYGVTNLFGSPALLERLGRYGEANG--IKLPSLRRVISAGAPVPIAVIERFRAMLP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 298 --GEKVNIYGTTEAM--NSLYMRQPKTGTEMA-------------PGffSEVRIVRIGGGV------DEIVANGEEGELI 354
Cdd:PRK09274 314 pdAEILTPYGATEALpiSSIESREILFATRAAtdngagicvgrpvDG--VEVRIIAISDAPipewddALRLATGEIGEIV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 355 VA---ASDSafvgYLNQPQATAE-KLQDG----WYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPG 426
Cdd:PRK09274 392 VAgpmVTRS----YYNRPEATRLaKIPDGqgdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPG 467
|
..
1T5D_X 427 VT 428
Cdd:PRK09274 468 VK 469
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
12-498 |
4.98e-32 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 128.94 E-value: 4.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 12 ATRAPDHCALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSA 91
Cdd:PLN02246 33 LSEFSDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 92 ELAELIKRGemTAAVIAVGRQVADAI--FQSGSGARIIFLGDLVRDGEPYSY-----GPPIEDPQREPAQPAFIFYTSGT 164
Cdd:PLN02246 113 EIAKQAKAS--GAKLIITQSCYVDKLkgLAEDDGVTVVTIDDPPEGCLHFSEltqadENELPEVEISPDDVVALPYSSGT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 165 TGLPKAAIIPQRaaeSRVLFMSTQV-----GLRHGRHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFRPVDALQL 239
Cdd:PLN02246 191 TGLPKGVMLTHK---GLVTSVAQQVdgenpNLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPKFEIGALLEL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 240 VQQEQVT-SLFATPTHLDALAAAAAHagsSLKLDSLRHVTFAGATMPDAVLETVHQHLPGEKVNI-YGTTEAMNSLYMRQ 317
Cdd:PLN02246 268 IQRHKVTiAPFVPPIVLAIAKSPVVE---KYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLGQgYGMTEAGPVLAMCL 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 318 --PKTGTEMAPGFF------SEVRIVRIGGGVDeiVANGEEGElIVAASDSAFVGYLNQPQATAEKL-QDGWYRTSDVAV 388
Cdd:PLN02246 345 afAKEPFPVKSGSCgtvvrnAELKIVDPETGAS--LPRNQPGE-ICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGY 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 389 WTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCrSS 468
Cdd:PLN02246 422 IDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFV-AK 500
|
490 500 510
....*....|....*....|....*....|
1T5D_X 469 ELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:PLN02246 501 QVVFYKRIHKVFFVDSIPKAPSGKILRKDL 530
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
27-498 |
1.31e-31 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 127.83 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 27 GLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIKRGEMTAAV 106
Cdd:PRK07059 46 GKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 107 I----------AVGRQVADAIFQSGSGARIIFLGDLV--------------------------RDGEPYSYGPPiedpQR 150
Cdd:PRK07059 126 VlenfattvqqVLAKTAVKHVVVASMGDLLGFKGHIVnfvvrrvkkmvpawslpghvrfndalAEGARQTFKPV----KL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 151 EPAQPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMST--QVGLRHGRH----NVVLGLmPLYHVvgfFAVLVAAL---AL 221
Cdd:PRK07059 202 GPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAwlQPAFEKKPRpdqlNFVCAL-PLYHI---FALTVCGLlgmRT 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 222 DGTYVVVEEFRPVDAL-QLVQQEQVTSLFATPTHLDALAAAAAHAgsslKLD--SLRHVTFAGATMPDAVLETVHQHLPG 298
Cdd:PRK07059 278 GGRNILIPNPRDIPGFiKELKKYQVHIFPAVNTLYNALLNNPDFD----KLDfsKLIVANGGGMAVQRPVAERWLEMTGC 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 299 EKVNIYGTTEAMNSLYMRQPK----TGTEMAPGFFSEVRIvRIGGGVDeiVANGEEGElIVAASDSAFVGYLNQPQATAE 374
Cdd:PRK07059 354 PITEGYGLSETSPVATCNPVDatefSGTIGLPLPSTEVSI-RDDDGND--LPLGEPGE-ICIRGPQVMAGYWNRPDETAK 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 375 KL-QDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVpRLG 453
Cdd:PRK07059 430 VMtADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVV-KKD 508
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
1T5D_X 454 ETLSADALDTFCRsSELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:PRK07059 509 PALTEEDVKAFCK-ERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
30-498 |
1.44e-31 |
|
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: 126.46 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 30 LTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIKRGEmtAAVIAV 109
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSE--AKVLIT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 110 GRQVADaifqsgsgariiflgdlvrdgepysygppiedpQREPAQPAFIFYTSGTTGLPKAAIIPQRAAESRVLfmstqv 189
Cdd:cd05969 79 TEELYE---------------------------------RTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYF------ 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 190 glrHGRHnvVLGLMP---LYH------VVGFFAVLVAALALDGTYVVVE-EFRPVDALQLVQQEQVTSLFATPTHLDALA 259
Cdd:cd05969 120 ---TGKY--VLDLHPddiYWCtadpgwVTGTVYGIWAPWLNGVTNVVYEgRFDAESWYGIIERVKVTVWYTAPTAIRMLM 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 260 AAAAHAGSSLKLDSLRHVTFAGATM-PDAVLEtvhqhlpGEKV------NIYGTTEA---MNSLYMRQPKTGTEMA---P 326
Cdd:cd05969 195 KEGDELARKYDLSSLRFIHSVGEPLnPEAIRW-------GMEVfgvpihDTWWQTETgsiMIANYPCMPIKPGSMGkplP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 327 GFfsEVRIVRIGGgvDEIVAnGEEGELIVAAS-DSAFVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMI 405
Cdd:cd05969 268 GV--KAAVVDENG--NELPP-GTKGILALKPGwPSMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDII 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 406 ISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSaDALD----TFCRsSELADFKRPKRYFI 481
Cdd:cd05969 343 KTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPS-DELKeeiiNFVR-QKLGAHVAPREIEF 420
|
490
....*....|....*..
1T5D_X 482 LDQLPKNALNKVLRRQL 498
Cdd:cd05969 421 VDNLPKTRSGKIMRRVL 437
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
4-498 |
2.47e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 129.31 E-value: 2.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 4 VNEMLRRAATRAPDHCALAVPARglRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPAL 83
Cdd:PRK12316 513 VHRLFEEQVERTPEAPALAFGEE--TLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVP 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 84 LNPRLKSAELAELIkrgEMTAAVIAVGRQVADAIFQSGSGARIIFLGDLVRDGEPYSYGPPieDPQREPAQPAFIFYTSG 163
Cdd:PRK12316 591 LDPEYPAERLAYML---EDSGVQLLLSQSHLGRKLPLAAGVQVLDLDRPAAWLEGYSEENP--GTELNPENLAYVIYTSG 665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 164 TTGLPKAAIIPQRAAESRVLFMSTQVGLrhGRHNVVLGLMPLYHVVGFFAVLVaALALDGTYVVV---EEFRPVDALQLV 240
Cdd:PRK12316 666 STGKPKGAGNRHRALSNRLCWMQQAYGL--GVGDTVLQKTPFSFDVSVWEFFW-PLMSGARLVVAapgDHRDPAKLVELI 742
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 241 QQEQVTSLFATPTHLDALAAAAAHAgsslKLDSLRHVTFAGATMPDAVLETVHQHLP-GEKVNIYGTTEA-MNSLYMRQP 318
Cdd:PRK12316 743 NREGVDTLHFVPSMLQAFLQDEDVA----SCTSLRRIVCSGEALPADAQEQVFAKLPqAGLYNLYGPTEAaIDVTHWTCV 818
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 319 KTGTEMAPgffsevrIVR-IGGGVDEI-------VANGEEGELIVAASDSAfVGYLNQPQATAEK-----LQDG--WYRT 383
Cdd:PRK12316 819 EEGGDSVP-------IGRpIANLACYIldanlepVPVGVLGELYLAGRGLA-RGYHGRPGLTAERfvpspFVAGerMYRT 890
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 384 SDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLAdqrwGQSVTACVVPRLGETLSADALDT 463
Cdd:PRK12316 891 GDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVLESEGGDWREALKA 966
|
490 500 510
....*....|....*....|....*....|....*
1T5D_X 464 FCRSSeLADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:PRK12316 967 HLAAS-LPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
29-498 |
5.60e-31 |
|
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: 126.66 E-value: 5.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 29 RLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIKRGE----MTA 104
Cdd:cd05967 82 TYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKpkliVTA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 105 AV-IAVGRQV------ADAIFQSGS-GARIIFL------GDLVRDGEPYSYGPPIEDPQR------EPAQPAFIFYTSGT 164
Cdd:cd05967 162 SCgIEPGKVVpykpllDKALELSGHkPHHVLVLnrpqvpADLTKPGRDLDWSELLAKAEPvdcvpvAATDPLYILYTSGT 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 165 TGLPKAAIIPQRA-AESRVLFMSTQVGLRHGrhNVVLGLMPLYHVVGFFAVLVAALaLDGTYVVVEEFRPV---DALQ-- 238
Cdd:cd05967 242 TGKPKGVVRDNGGhAVALNWSMRNIYGIKPG--DVWWAASDVGWVVGHSYIVYGPL-LHGATTVLYEGKPVgtpDPGAfw 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 239 -LVQQEQVTSLFATPTH--LDALAAAAAHAGSSLKLDSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTE-----AM 310
Cdd:cd05967 319 rVIEKYQVNALFTAPTAirAIRKEDPDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTEtgwpiTA 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 311 N--SLYMRQPKTGTEMAPGFFSEVRIVRIGGgvdEIVANGEEGELIVA------------ASDSAFV-GYLNQpqataek 375
Cdd:cd05967 399 NpvGLEPLPIKAGSPGKPVPGYQVQVLDEDG---EPVGPNELGNIVIKlplppgclltlwKNDERFKkLYLSK------- 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 376 lQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGET 455
Cdd:cd05967 469 -FPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVK 547
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
1T5D_X 456 LSADALDTFCRS---SELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:cd05967 548 ITAEELEKELVAlvrEQIGPVAAFRLVIFVKRLPKTRSGKILRRTL 593
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
2-428 |
6.16e-31 |
|
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: 125.86 E-value: 6.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 2 QTVNEMLRRAATRAPDHCALAVPARG--LRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGA 79
Cdd:cd05906 10 RTLLELLLRAAERGPTKGITYIDADGseEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 80 VPALLNP----RLKSAELAELIKRGEM-TAAVIAVGRQVADAIFQSGSGARIIFLGDLVRDGEPySYGPPIEDPQREPAQ 154
Cdd:cd05906 90 VPAPLTVpptyDEPNARLRKLRHIWQLlGSPVVLTDAELVAEFAGLETLSGLPGIRVLSIEELL-DTAADHDLPQSRPDD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 155 PAFIFYTSGTTGLPKAAIIPQRAAESRVLfmSTQVGLRHGRHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVV--EEF- 231
Cdd:cd05906 169 LALLMLTSGSTGFPKAVPLTHRNILARSA--GKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVHVptEEIl 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 232 -RPVDALQLVQQEQVTSLFAtPTHLDALAAAAAHAGSSLK--LDSLRHVTFAG----ATMPDAVLETVHQH-LPGEKVN- 302
Cdd:cd05906 247 aDPLRWLDLIDRYRVTITWA-PNFAFALLNDLLEEIEDGTwdLSSLRYLVNAGeavvAKTIRRLLRLLEPYgLPPDAIRp 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 303 IYGTTEAMN----SLYMRQPKTGTEMA--------PGFfsEVRIVRIGGGVdeiVANGEEGELIVAAsDSAFVGYLNQPQ 370
Cdd:cd05906 326 AFGMTETCSgviySRSFPTYDHSQALEfvslgrpiPGV--SMRIVDDEGQL---LPEGEVGRLQVRG-PVVTKGYYNNPE 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
1T5D_X 371 ATAEKLQ-DGWYRTSDVAvWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVT 428
Cdd:cd05906 400 ANAEAFTeDGWFRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVE 457
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
16-498 |
8.04e-31 |
|
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: 124.43 E-value: 8.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 16 PDHcaLAVPARGLRLTHAELRARVEAVAARLHADG-LRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELA 94
Cdd:cd17648 1 PDR--VAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 95 ELIkrgemtaaviavgrqvadaifqSGSGARIIFlgdlvrdgepysygppiedpqREPAQPAFIFYTSGTTGLPKAAIIP 174
Cdd:cd17648 79 FIL----------------------EDTGARVVI---------------------TNSTDLAYAIYTSGTTGKPKGVLVE 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 175 QRAAESRVLFMSTQVGLRHGRHNVVLGLMPlyHVVGFFAVLVAALALDGTYVVV--EEFRPV-DAL-QLVQQEQVTSLFA 250
Cdd:cd17648 116 HGSVVNLRTSLSERYFGRDNGDEAVLFFSN--YVFDFFVEQMTLALLNGQKLVVppDEMRFDpDRFyAYINREKVTYLSG 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 251 TPTHLDALAAAaahagsslKLDSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTE----AMNSLYMRQPKTgtEMAP 326
Cdd:cd17648 194 TPSVLQQYDLA--------RLPHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTEttvtNHKRFFPGDQRF--DKSL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 327 GFfsEVRIVR--IGGGVDEIVANGEEGELIVAAsDSAFVGYLNQPQATAEKL-----------QDG----WYRTSDVAVW 389
Cdd:cd17648 264 GR--PVRNTKcyVLNDAMKRVPVGAVGELYLGG-DGVARGYLNRPELTAERFlpnpfqteqerARGrnarLYKTGDLVRW 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 390 TPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIG--LADQRWGQSVTACVVPRLGE--TLSADALDTFC 465
Cdd:cd17648 341 LPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAkeDASQAQSRIQKYLVGYYLPEpgHVPESDLLSFL 420
|
490 500 510
....*....|....*....|....*....|...
1T5D_X 466 RSSeLADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:cd17648 421 RAK-LPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
3-504 |
1.20e-30 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 125.09 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 3 TVNEMLRRAATRAPDHCALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPA 82
Cdd:PLN02330 29 TLPDFVLQDAELYADKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 83 LLNPrlkSAELAELIKRGEMTAAVIAVgrqVADAIFQS--GSGARIIFLGDlVRDGEPYSYGPPIEDPQREPAQPAF--- 157
Cdd:PLN02330 109 GANP---TALESEIKKQAEAAGAKLIV---TNDTNYGKvkGLGLPVIVLGE-EKIEGAVNWKELLEAADRAGDTSDNeei 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 158 -------IFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGLRHGRHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEE 230
Cdd:PLN02330 182 lqtdlcaLPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMIGQVVTLGLIPFFHIYGITGICCATLRNKGKVVVMSR 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 231 FRPVDALQLVQQEQVTSLFATPTHLDALAAAAAHAGSSLKLDSLRHVTFAGATMPDAVLETVHQHLPGEKVN-IYGTTE- 308
Cdd:PLN02330 262 FELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLQAIMTAAAPLAPELLTAFEAKFPGVQVQeAYGLTEh 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 309 AMNSLYMRQPKTGTEMAP----GFFS---EVRIVRIGGGVDeiVANGEEGELIVAaSDSAFVGYLNQPQATAEKL-QDGW 380
Cdd:PLN02330 342 SCITLTHGDPEKGHGIAKknsvGFILpnlEVKFIDPDTGRS--LPKNTPGELCVR-SQCVMQGYYNNKEETDRTIdEDGW 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 381 YRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADA 460
Cdd:PLN02330 419 LHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEED 498
|
490 500 510 520
....*....|....*....|....*....|....*....|....
1T5D_X 461 LDTFCrSSELADFKRPKRYFILDQLPKNALNKVLRRQLVQQVSS 504
Cdd:PLN02330 499 ILNFV-AANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLS 541
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
353-500 |
1.64e-30 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 123.57 E-value: 1.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 353 LIVAASDSAFVGYLNQPQATAEKLQdgwyrTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVV 432
Cdd:PRK07445 303 NITIQAQSLALGYYPQILDSQGIFE-----TDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCV 377
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1T5D_X 433 IGLADQRWGQSVTACVVPRLGETlSADALDTfCRSSELADFKRPKRYFILDQLPKNALNKVLRRQLVQ 500
Cdd:PRK07445 378 LGLPDPHWGEVVTAIYVPKDPSI-SLEELKT-AIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
3-498 |
5.61e-30 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 123.19 E-value: 5.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 3 TVNEMLRRAATRAPDHCALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPA 82
Cdd:PRK05857 15 TVLDRVFEQARQQPEAIALRRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 83 LLNPRLKSAELAELIKRGEMTAAVIAVGRQVADAIFQSGSGARIIFLGDLVRDGEPYSYGPPIEDPQREPA----QPAFI 158
Cdd:PRK05857 95 MADGNLPIAAIERFCQITDPAAALVAPGSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNADqgseDPLAM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 159 FYTSGTTGLPKAAIIPQRAaesrvlFMSTQVGLRHGRHNVV--------LGLMPLYHVVGFFAVLVAALalDGTYVVVEE 230
Cdd:PRK05857 175 IFTSGTTGEPKAVLLANRT------FFAVPDILQKEGLNWVtwvvgettYSPLPATHIGGLWWILTCLM--HGGLCVTGG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 231 FRPVDALQLVQQEQVTSLFATPTHLDALAAAAAHAGSSLKldSLRHVTFAGATMPDAVLETVhQHLPGEKVNIYGTTEA- 309
Cdd:PRK05857 247 ENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVP--SLRLVGYGGSRAIAADVRFI-EATGVRTAQVYGLSETg 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 310 -------MNSLYMRQPKTGTEMAPGFFSEVRIVRIGGGvDEIVANGEE----GELIVAaSDSAFVGYLNQPQATAEKLQD 378
Cdd:PRK05857 324 ctalclpTDDGSIVKIEAGAVGRPYPGVDVYLAATDGI-GPTAPGAGPsasfGTLWIK-SPANMLGYWNNPERTAEVLID 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 379 GWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVP-------- 450
Cdd:PRK05857 402 GWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVAsaeldesa 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
1T5D_X 451 --RLGETLSAdaldTFCRSSElaDFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:PRK05857 482 arALKHTIAA----RFRRESE--PMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
27-498 |
5.72e-30 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 123.06 E-value: 5.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 27 GLRLTHAELRARVEAVAARLHAD-GLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELA-ELIKRGEMTA 104
Cdd:PRK08751 48 GKTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKhQLIDSGASVL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 105 AVI-----AVGRQVADA----IFQSGSGARIIF---------------------LGDLVRDGEPYSYG-----PPIedpQ 149
Cdd:PRK08751 128 VVIdnfgtTVQQVIADTpvkqVITTGLGDMLGFpkaalvnfvvkyvkklvpeyrINGAIRFREALALGrkhsmPTL---Q 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 150 REPAQPAFIFYTSGTTGLPKAAIIPQRAAESRVL----FMSTQVGLRHGrHNVVLGLMPLYHVVGFFAVLVAALALDGTY 225
Cdd:PRK08751 205 IEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQqahqWLAGTGKLEEG-CEVVITALPLYHIFALTANGLVFMKIGGCN 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 226 VVVEEfrPVDALQLVQQEQVTSLFATPTHLDALAAAAAHAG-SSLKLDSLRHVTFAGATMPDAVLETVHQHLPGEKVNIY 304
Cdd:PRK08751 284 HLISN--PRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGfDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAY 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 305 GTTEA-----MNSLYMrQPKTGTEMAPGFFSEVRIVRIGGgvdEIVANGEEGELIVAASdSAFVGYLNQPQATAEKLQ-D 378
Cdd:PRK08751 362 GLTETspaacINPLTL-KEYNGSIGLPIPSTDACIKDDAG---TVLAIGEIGELCIKGP-QVMKGYWKRPEETAKVMDaD 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 379 GWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRlGETLSA 458
Cdd:PRK08751 437 GWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKK-DPALTA 515
|
490 500 510 520
....*....|....*....|....*....|....*....|
1T5D_X 459 DALDTFCRSSeLADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:PRK08751 516 EDVKAHARAN-LTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
4-500 |
5.89e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 121.99 E-value: 5.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 4 VNEMLRRAATRAPDhcALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPAL 83
Cdd:PRK12316 4553 VHQLVAERARMTPD--AVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVP 4630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 84 LNPRLKSAELAELIkrGEMTAAVIAVGRQVADAIfQSGSGARIIFLGdlvRDGEPYSYgpPIEDPQR--EPAQPAFIFYT 161
Cdd:PRK12316 4631 LDPEYPRERLAYMM--EDSGAALLLTQSHLLQRL-PIPDGLASLALD---RDEDWEGF--PAHDPAVrlHPDNLAYVIYT 4702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 162 SGTTGLPKAAIIPQRAAESRVLFMSTQVGLrhGRHNVVLGLMPLY---HVVGFFAVLVAalaldGTYVVV---EEFRPVD 235
Cdd:PRK12316 4703 SGSTGRPKGVAVSHGSLVNHLHATGERYEL--TPDDRVLQFMSFSfdgSHEGLYHPLIN-----GASVVIrddSLWDPER 4775
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 236 ALQLVQQEQVTSLFATPTHLDALAAAAAHAGsslKLDSLRHVTFAGATMPDAVLETVHQHLPGEKV-NIYGTTEAMNSLY 314
Cdd:PRK12316 4776 LYAEIHEHRVTVLVFPPVYLQQLAEHAERDG---EPPSLRVYCFGGEAVAQASYDLAWRALKPVYLfNGYGPTETTVTVL 4852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 315 MRQPKTGTEMAPgffSEVRIVRIGGGVD--------EIVANGEEGELIVAASDSAfVGYLNQPQATAEKL-------QDG 379
Cdd:PRK12316 4853 LWKARDGDACGA---AYMPIGTPLGNRSgyvldgqlNPLPVGVAGELYLGGEGVA-RGYLERPALTAERFvpdpfgaPGG 4928
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 380 -WYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGlADQRWGQSVTACVVPRLGETLSA 458
Cdd:PRK12316 4929 rLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIA-QEGAVGKQLVGYVVPQDPALADA 5007
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
1T5D_X 459 DALDTFCRSS-------ELADFKRPKRYFILDQLPKNALNKVLRRQLVQ 500
Cdd:PRK12316 5008 DEAQAELRDElkaalreRLPEYMVPAHLVFLARMPLTPNGKLDRKALPQ 5056
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
31-495 |
9.75e-29 |
|
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: 118.69 E-value: 9.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 31 THAELRARVEAVAARLHAD-GLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIKRgemtaaviav 109
Cdd:cd05937 7 TYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKL---------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 110 grqvadaifqsgSGARIIFLgdlvrdgepysygppiedpqrEPAQPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQV 189
Cdd:cd05937 77 ------------SGSRFVIV---------------------DPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 190 GLRHGrhNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFRPVDALQLVQQEQVT----------SLFATPTHLDAla 259
Cdd:cd05937 124 NLKNG--DRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATiiqyvgelcrYLLSTPPSPYD-- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 260 aaaahagsslKLDSLRhVTFAGATMPDaVLETVHQHLPGEKV-NIYGTTEAMNSLYMRQPKTGTEMAPGFFSEVR----- 333
Cdd:cd05937 200 ----------RDHKVR-VAWGNGLRPD-IWERFRERFNVPEIgEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRrwkfe 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 334 ----IVRIGGGVDEI-----------VANGEEGELIV---AASDSAFVGYLNQPQATAEKL-------QDGWYRTSDVAV 388
Cdd:cd05937 268 nqvvLVKMDPETDDPirdpktgfcvrAPVGEPGEMLGrvpFKNREAFQGYLHNEDATESKLvrdvfrkGDIYFRTGDLLR 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 389 WTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLA----DQRWGqsvtaCVVPRLGEtlsADALDTF 464
Cdd:cd05937 348 QDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKvpghDGRAG-----CAAITLEE---SSAVPTE 419
|
490 500 510
....*....|....*....|....*....|.
1T5D_X 465 CRSSELADFKRpkryfilDQLPKNALNKVLR 495
Cdd:cd05937 420 FTKSLLASLAR-------KNLPSYAVPLFLR 443
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
4-498 |
1.74e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 120.65 E-value: 1.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 4 VNEMLRRAATRAPDHCALAVPARglRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPAL 83
Cdd:PRK12467 3097 VHQLIEAQVARTPEAPALVFGDQ--QLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVP 3174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 84 LNPRLKSAELAELIKRGEMtaAVIAVGRQVADAIFQSGSGARIiflgdLVRDGEPYSYGPPIEDPQREPAQPAFIFYTSG 163
Cdd:PRK12467 3175 LDPEYPRERLAYMIEDSGV--KLLLTQAHLLEQLPAPAGDTAL-----TLDRLDLNGYSENNPSTRVMGENLAYVIYTSG 3247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 164 TTGLPKAAIIPQRAAESRVLFMSTQVGLrhGRHNVVLGLMPLYH---VVGFFAVLVAalaldGTYVVVEEFRPVDALQLV 240
Cdd:PRK12467 3248 STGKPKGVGVRHGALANHLCWIAEAYEL--DANDRVLLFMSFSFdgaQERFLWTLIC-----GGCLVVRDNDLWDPEELW 3320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 241 QQ---EQVTSLFATPTHLDALAAAaahaGSSLKLDSLRHVTFAGATMPDAVLETVHQHLPGEKV-NIYGTTEAMNSLYMR 316
Cdd:PRK12467 3321 QAihaHRISIACFPPAYLQQFAED----AGGADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLtNGYGPTEAVVTVTLW 3396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 317 qpKTGTEMAPGFFSEVRIVRIGG-------GVDEIVANGEEGELIVAASDSAfVGYLNQPQATAEK-LQDGW-------Y 381
Cdd:PRK12467 3397 --KCGGDAVCEAPYAPIGRPVAGrsiyvldGQLNPVPVGVAGELYIGGVGLA-RGYHQRPSLTAERfVADPFsgsggrlY 3473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 382 RTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLaDQRWGQSVTACVVPrlgETLSADAL 461
Cdd:PRK12467 3474 RTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVP---ADPQGDWR 3549
|
490 500 510
....*....|....*....|....*....|....*....
1T5D_X 462 DTFCR--SSELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:PRK12467 3550 ETLRDhlAASLPDYMVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
156-498 |
2.01e-28 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 116.04 E-value: 2.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 156 AFIFYTSGTTGLPKAAiiPQRAAESRVLFMSTQVGLRHGRHNVVLGLMPLYHVVGFFAVLVAALAlDGTYVVV---EEFR 232
Cdd:cd05944 5 AAYFHTGGTTGTPKLA--QHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLA-SGAHVVLagpAGYR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 233 PVDALQ----LVQQEQVTSLFATPTHLDALAAAAAHAGSSlkldSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTE 308
Cdd:cd05944 82 NPGLFDnfwkLVERYRITSLSTVPTVYAALLQVPVNADIS----SLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 309 AmNSLYMRQPKtGTEMAPGF------FSEVRIVRIGGGVDEI--VANGEEGELIVAASDsAFVGYLNQPQATAEKLQDGW 380
Cdd:cd05944 158 A-TCLVAVNPP-DGPKRPGSvglrlpYARVRIKVLDGVGRLLrdCAPDEVGEICVAGPG-VFGGYLYTEGNKNAFVADGW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 381 YRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADA 460
Cdd:cd05944 235 LNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEE 314
|
330 340 350
....*....|....*....|....*....|....*...
1T5D_X 461 LDTFCRSSELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:cd05944 315 LLAWARDHVPERAAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
155-495 |
3.83e-28 |
|
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: 114.67 E-value: 3.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 155 PAFIFYTSGTTGLPKAAIIpqraaESRVLFMSTQVGLRHGRH----NVVLGLMPLYHVVGFFAVLVAALAlDGTYVVVEE 230
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLL-----ANKTFFAVPDILQKEGLNwvvgDVTYLPLPATHIGGLWWILTCLIH-GGLCVTGGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 231 FRPVDAL-QLVQQEQVTSLFATPTHLDALAAAAAHAGSSLKldSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTEA 309
Cdd:cd17635 77 NTTYKSLfKILTTNAVTTTCLVPTLLSKLVSELKSANATVP--SLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSET 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 310 MNSLYMRQPKTGTEMA------PGffSEVRIVRIGGGVdeiVANGEEGElIVAASDSAFVGYLNQPQATAEKLQDGWYRT 383
Cdd:cd17635 155 GTALCLPTDDDSIEINavgrpyPG--VDVYLAATDGIA---GPSASFGT-IWIKSPANMLGYWNNPERTAEVLIDGWVNT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 384 SDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPR--LGETLSADAL 461
Cdd:cd17635 229 GDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASaeLDENAIRALK 308
|
330 340 350
....*....|....*....|....*....|....
1T5D_X 462 DTFCRSSELadFKRPKRYFILDQLPKNALNKVLR 495
Cdd:cd17635 309 HTIRRELEP--YARPSTIVIVTDIPRTQSGKVKR 340
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
6-504 |
4.31e-28 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 117.40 E-value: 4.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 6 EMLRRAAtrAPDHCALAVPARglRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVP--AL 83
Cdd:PRK10946 29 DILTRHA--ASDAIAVICGER--QFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVAPvnAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 84 LNPRlkSAELAELIKrgEMTAAVIAVGRQ---VADAIF------QSGSGARIIFLGD---------LVRDGEPYSYGPPI 145
Cdd:PRK10946 105 FSHQ--RSELNAYAS--QIEPALLIADRQhalFSDDDFlntlvaEHSSLRVVLLLNDdgehslddaINHPAEDFTATPSP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 146 EDpqrepaQPAFIFYTSGTTGLPKaaIIPQ----------RAAESrvlfmstqvgLRHGRHNVVLGLMPLYHVV-----G 210
Cdd:PRK10946 181 AD------EVAFFQLSGGSTGTPK--LIPRthndyyysvrRSVEI----------CGFTPQTRYLCALPAAHNYpmsspG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 211 FFAVLVAAlaldGTYVVVEEFRPVDALQLVQQEQVTSLFATPTHLDALAAAAAHAGSSLKLDSLRHVTFAGATMPDAVLE 290
Cdd:PRK10946 243 ALGVFLAG----GTVVLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKLLQVGGARLSETLAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 291 TVHQHLPGEKVNIYGTTEAMNSlYMRQPKT--------GTEMAPGffSEVRIVRIGGgvdEIVANGEEGELIVAASDSaF 362
Cdd:PRK10946 319 RIPAELGCQLQQVFGMAEGLVN-YTRLDDSderifttqGRPMSPD--DEVWVADADG---NPLPQGEVGRLMTRGPYT-F 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 363 VGYLNQPQATAEKL-QDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWG 441
Cdd:PRK10946 392 RGYYKSPQHNASAFdANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMG 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
1T5D_X 442 QSVTACVVPRlgETLSADALDTFCRSSELADFKRPKRYFILDQLPKNALNKVLRRQLVQQVSS 504
Cdd:PRK10946 472 EKSCAFLVVK--EPLKAVQLRRFLREQGIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLAS 532
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
30-501 |
4.90e-28 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 118.21 E-value: 4.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 30 LTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAeLIKRGEMTAAVIAV 109
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHA-LAARNTEPALVVTS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 110 GrQVADAiFQSGSgarIIFLGDLVRDG---EPYSYGPPIEDPQrepaqpAFIFYTSGTTGLPKAAIIPQRAAESRVLFMS 186
Cdd:PRK06060 110 D-ALRDR-FQPSR---VAEAAELMSEAarvAPGGYEPMGGDAL------AYATYTSGTTGPPKAAIHRHADPLTFVDAMC 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 187 TQvGLRHGRHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEefRPVDA---LQLVQQEQVTSLFATPTHLDALAAAAa 263
Cdd:PRK06060 179 RK-ALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINS--APVTPeaaAILSARFGPSVLYGVPNFFARVIDSC- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 264 hagSSLKLDSLRHVTFAGATMPDAVLETVHQH------LPGEKVNIYGTTEAMNSLYMRQPKTGTEMAPGFfsEVRIVRI 337
Cdd:PRK06060 255 ---SPDSFRSLRCVVSAGEALELGLAERLMEFfggipiLDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPY--EIRVVAP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 338 GGGVdeiVANGEEGELIVAASDSAfVGYLNQPQATAEklQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEI 417
Cdd:PRK06060 330 DGTT---AGPGVEGDLWVRGPAIA-KGYWNRPDSPVA--NEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 418 ERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCRS--SELADFKRPKRYFILDQLPKNALNKVLR 495
Cdd:PRK06060 404 ERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGllNRLSAFKVPHRFAVVDRLPRTPNGKLVR 483
|
....*.
1T5D_X 496 RQLVQQ 501
Cdd:PRK06060 484 GALRKQ 489
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
10-476 |
7.13e-28 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 117.28 E-value: 7.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 10 RAATRAPDHCALAvpARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLK 89
Cdd:PRK08279 45 EAAARHPDRPALL--FEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 90 SAELAELIkrGEMTAAVIAVGRQVADAIFQSGS---GARIIFLGDLVRDGEP--------YSYGPPIEDPQREPA----Q 154
Cdd:PRK08279 123 GAVLAHSL--NLVDAKHLIVGEELVEAFEEARAdlaRPPRLWVAGGDTLDDPegyedlaaAAAGAPTTNPASRSGvtakD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 155 PAFIFYTSGTTGLPKAAIIPQRaaesRVLFMSTQVG--LRHGRHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFr 232
Cdd:PRK08279 201 TAFYIYTSGTTGLPKAAVMSHM----RWLKAMGGFGglLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKF- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 233 pvDALQL---VQQEQVTS----------LFATPTHldalaaaaahagsslKLDSLRHVTFA-GATMPDAVLETVHQHLPG 298
Cdd:PRK08279 276 --SASRFwddVRRYRATAfqyigelcryLLNQPPK---------------PTDRDHRLRLMiGNGLRPDIWDEFQQRFGI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 299 EKV-NIYGTTEAMNSLY--MRQPKTGTEMAPGFFSEVRIVRIGGGVDEIVAN----------GEEGELIVAASDSA-FVG 364
Cdd:PRK08279 339 PRIlEFYAASEGNVGFInvFNFDGTVGRVPLWLAHPYAIVKYDVDTGEPVRDadgrcikvkpGEVGLLIGRITDRGpFDG 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 365 YlNQPQATAEKL-----QDG--WYRTSDVavwtpegtVRILG--------RVDDMIISGGENIHPSEIERVLGTAPGVTE 429
Cdd:PRK08279 419 Y-TDPEASEKKIlrdvfKKGdaWFNTGDL--------MRDDGfghaqfvdRLGDTFRWKGENVATTEVENALSGFPGVEE 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
1T5D_X 430 VVVIGL----ADQRWGQsvtACVVPRLGETLSADALDTFCRsSELADFKRP 476
Cdd:PRK08279 490 AVVYGVevpgTDGRAGM---AAIVLADGAEFDLAALAAHLY-ERLPAYAVP 536
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
9-461 |
7.55e-28 |
|
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: 116.95 E-value: 7.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 9 RRAATRaPDHCALAV----PARGLRLTHAELRARVEAVAARLHADGlRPQQRVAVVAPNSADVVIAILALHRLG--AVPA 82
Cdd:cd05931 1 RRAAAR-PDRPAYTFlddeGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGaiAVPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 83 LL-NPRLKSAELAELIKRGEMTAAVIAVGRQVA---DAIFQSGSGARIIFLGDLVRDGEpysyGPPIEDPQREPAQPAFI 158
Cdd:cd05931 79 PPpTPGRHAERLAAILADAGPRVVLTTAAALAAvraFAASRPAAGTPRLLVVDLLPDTS----AADWPPPSPDPDDIAYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 159 FYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGLRHGRhnVVLGLMPLYHVVGFFAVLVAALALdGTYVVV---EEF--RP 233
Cdd:cd05931 155 QYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGD--VVVSWLPLYHDMGLIGGLLTPLYS-GGPSVLmspAAFlrRP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 234 VDALQLVQQEQVTSLFAtPT--HLDALAAAAAHAGSSLKLDSLRhVTFAGATMPDAvlETVHQ--------------HLP 297
Cdd:cd05931 232 LRWLRLISRYRATISAA-PNfaYDLCVRRVRDEDLEGLDLSSWR-VALNGAEPVRP--ATLRRfaeafapfgfrpeaFRP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 298 GekvniYGTTEAmnSLYM---------------------------RQPKTGTEMA----PGFFSEVRIVRIGGGvdEIVA 346
Cdd:cd05931 308 S-----YGLAEA--TLFVsggppgtgpvvlrvdrdalagravavaADDPAARELVscgrPLPDQEVRIVDPETG--RELP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 347 NGEEGElIVAASDSAFVGYLNQPQATAEKLQ-------DGWYRTSDVAVWTpEGTVRILGRVDDMIISGGENIHPSEIER 419
Cdd:cd05931 379 DGEVGE-IWVRGPSVASGYWGRPEATAETFGalaatdeGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGRNHYPQDIEA 456
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
1T5D_X 420 VLGTAPGV---TEVVVIGLADQRWGQSVTACVVPRLGETLSADAL 461
Cdd:cd05931 457 TAEEAHPAlrpGCVAAFSVPDDGEERLVVVAEVERGADPADLAAI 501
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
4-504 |
1.37e-27 |
|
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: 115.33 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 4 VNEMLRRAATRAPDHCALAVPARglRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPAL 83
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDG--SLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 84 LNPRLKSAELAELIKRgemtaaviavgrqvadaifqsgSGARIIFLGDlvrdgepysygppiedpqrePAQPAFIFYTSG 163
Cdd:cd05918 79 LDPSHPLQRLQEILQD----------------------TGAKVVLTSS--------------------PSDAAYVIFTSG 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 164 TTGLPKAAIIPQRAAESRVLFMSTQVGL-RHGRhnvvlglmplyhVVGF----FAV----LVAALALDGTYVVVEEFRPV 234
Cdd:cd05918 117 STGKPKGVVIEHRALSTSALAHGRALGLtSESR------------VLQFasytFDVsileIFTTLAAGGCLCIPSEEDRL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 235 DALQLVQQE-QVTSLFATPTHldalaaaaahaGSSLKLD---SLRHVTFAGATMPDAVLETVHQHLpgEKVNIYGTTEA- 309
Cdd:cd05918 185 NDLAGFINRlRVTWAFLTPSV-----------ARLLDPEdvpSLRTLVLGGEALTQSDVDTWADRV--RLINAYGPAECt 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 310 MNSLyMRQPKTGTEmapgffseVRIvrIGGGV------------DEIVANGEEGEL-----IVAAsdsafvGYLNQPQAT 372
Cdd:cd05918 252 IAAT-VSPVVPSTD--------PRN--IGRPLgatcwvvdpdnhDRLVPIGAVGELliegpILAR------GYLNDPEKT 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 373 AEKLQDG--W------------YRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGL--- 435
Cdd:cd05918 315 AAAFIEDpaWlkqegsgrgrrlYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVvkp 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 436 ADQRWGQSVTACVVPRLGETLSADALDTFCRSSE----------------LADFKRPKRYFILDQLPKNALNKVLRRQLV 499
Cdd:cd05918 395 KDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDefralvaelrsklrqrLPSYMVPSVFLPLSHLPLTASGKIDRRALR 474
|
....*
1T5D_X 500 QQVSS 504
Cdd:cd05918 475 ELAES 479
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
31-494 |
2.69e-27 |
|
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: 115.37 E-value: 2.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 31 THAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAV---------PALLNPRLKSAELAELIKRGE 101
Cdd:cd17634 86 SYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVhsvifggfaPEAVAGRIIDSSSRLLITADG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 102 MTAA--VIAVGRQVADAIFQSGSGARIIFLGDlvRDGEPYSY--------------GPPIEDPQR-EPAQPAFIFYTSGT 164
Cdd:cd17634 166 GVRAgrSVPLKKNVDDALNPNVTSVEHVIVLK--RTGSDIDWqegrdlwwrdliakASPEHQPEAmNAEDPLFILYTSGT 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 165 TGLPKAAI-----IPQRAAESrvlfmstqvgLRH----GRHNVVLGLMPLYHVVGFFAVLVAALALDGTyVVVEEFRPV- 234
Cdd:cd17634 244 TGKPKGVLhttggYLVYAATT----------MKYvfdyGPGDIYWCTADVGWVTGHSYLLYGPLACGAT-TLLYEGVPNw 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 235 ---DAL-QLVQQEQVTSLFATPTHLDALAAAAAHAGSSLKLDSLRHVTFAGATMPDAVLETVHQHLPGEK---VNIYGTT 307
Cdd:cd17634 313 ptpARMwQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKcpvVDTWWQT 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 308 EAMNSLYMRQP-----KTGTEMAPGFFSEVRIVRIGGgvdEIVANGEEGELIVAAS----DSAFVGYLNQPQATAEKLQD 378
Cdd:cd17634 393 ETGGFMITPLPgaielKAGSATRPVFGVQPAVVDNEG---HPQPGGTEGNLVITDPwpgqTRTLFGDHERFEQTYFSTFK 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 379 GWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLS- 457
Cdd:cd17634 470 GMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSp 549
|
490 500 510
....*....|....*....|....*....|....*....
1T5D_X 458 --ADALDTFCRsSELADFKRPKRYFILDQLPKNALNKVL 494
Cdd:cd17634 550 elYAELRNWVR-KEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
2-498 |
1.21e-26 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 114.88 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 2 QTVNEMLRRAATRAPDHCALAvpARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVP 81
Cdd:PRK05691 1131 AWLPELLNEQARQTPERIALV--WDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAY 1208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 82 ALLNPRLKSAELAELIkrGEMTAAVIAVGRQVADAIFQSgSGARIIFLGDLVRDGEPYSygPPIEDPQREpaQPAFIFYT 161
Cdd:PRK05691 1209 VPLDPDYPAERLAYML--ADSGVELLLTQSHLLERLPQA-EGVSAIALDSLHLDSWPSQ--APGLHLHGD--NLAYVIYT 1281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 162 SGTTGLPKAAIIPQRAAESRVLFMSTQVGLRHGrhNVVLGLMPLYHVVG----FFAVLVAA---LALDGtyvvvEEFRPV 234
Cdd:PRK05691 1282 SGSTGQPKGVGNTHAALAERLQWMQATYALDDS--DVLMQKAPISFDVSvwecFWPLITGCrlvLAGPG-----EHRDPQ 1354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 235 DALQLVQQEQVTSLFATPTHLDALAAAAAHAGSSlkldSLRHVTFAGATMPDAVLETVHQHLPGEKV-NIYGTTE-AMNS 312
Cdd:PRK05691 1355 RIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACT----SLRRLFSGGEALPAELRNRVLQRLPQVQLhNRYGPTEtAINV 1430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 313 LYMRQPKTGTEMAPgffsevrIVRIGGGVD--------EIVANGEEGELIVAASDSAfVGYLNQPQATAEKL------QD 378
Cdd:PRK05691 1431 THWQCQAEDGERSP-------IGRPLGNVLcrvldaelNLLPPGVAGELCIGGAGLA-RGYLGRPALTAERFvpdplgED 1502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 379 G--WYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIgLADQRWGQSVTACVVPRLGETL 456
Cdd:PRK05691 1503 GarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-VREGAAGAQLVGYYTGEAGQEA 1581
|
490 500 510 520
....*....|....*....|....*....|....*....|..
1T5D_X 457 SADALDTfCRSSELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:PRK05691 1582 EAERLKA-ALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
2-500 |
1.59e-26 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 112.62 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 2 QTVNEMLRRAATR---APDHCALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLG 78
Cdd:cd17642 14 GTAGEQLHKAMKRyasVPGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 79 AVPALLNPRLKSAELAELIKRGEMTaaVIAVGRQVADAIFQSGSGARI---IFLGDLVRD------------------GE 137
Cdd:cd17642 94 VGVAPTNDIYNERELDHSLNISKPT--IVFCSKKGLQKVLNVQKKLKIiktIIILDSKEDykgyqclytfitqnlppgFN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 138 PYSYGPPIEDPQRepaQPAFIFYTSGTTGLPKAAIIPQRAAESRvlfMSTQ----VGLRHGRHNVVLGLMPLYHVVGFFA 213
Cdd:cd17642 172 EYDFKPPSFDRDE---QVALIMNSSGSTGLPKGVQLTHKNIVAR---FSHArdpiFGNQIIPDTAILTVIPFHHGFGMFT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 214 VLvAALALDGTYVVVEEFRPVDALQLVQQEQVTSLFATPTHLDALAAAAAHagSSLKLDSLRHVTFAGATMPDAVLETVH 293
Cdd:cd17642 246 TL-GYLICGFRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLV--DKYDLSNLHEIASGGAPLSKEVGEAVA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 294 Q--HLPGEKVNiYGTTEAMNSLYMR-----QPKTGTEMAPGFfsEVRIVRIGGGvdEIVANGEEGELIVAAsDSAFVGYL 366
Cdd:cd17642 323 KrfKLPGIRQG-YGLTETTSAILITpegddKPGAVGKVVPFF--YAKVVDLDTG--KTLGPNERGELCVKG-PMIMKGYV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 367 NQPQATAEKL-QDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVT 445
Cdd:cd17642 397 NNPEATKALIdKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPA 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
1T5D_X 446 ACVVPRLGETLSADALDTFCrSSELADFKRPKRYFI-LDQLPKNALNKVLRRQLVQ 500
Cdd:cd17642 477 AVVVLEAGKTMTEKEVMDYV-ASQVSTAKRLRGGVKfVDEVPKGLTGKIDRRKIRE 531
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
29-501 |
1.67e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 112.88 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 29 RLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIKRGE------- 101
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEdryvlfd 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 102 -----MTAAVIA----VGRQVA--DAIFQSGSGARIIFLGDLVrDGEPYSYGPPIEDPQrepaQPAFIFYTSGTTGLPKA 170
Cdd:PRK07008 119 ltflpLVDALAPqcpnVKGWVAmtDAAHLPAGSTPLLCYETLV-GAQDGDYDWPRFDEN----QASSLCYTSGTTGNPKG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 171 AIIPQR--------AAESRVLFMSTQvglrhgrhNVVLGLMPLYHVVGFFavLVAALALDGTYVVVeefrPVDAL----- 237
Cdd:PRK07008 194 ALYSHRstvlhaygAALPDAMGLSAR--------DAVLPVVPMFHVNAWG--LPYSAPLTGAKLVL----PGPDLdgksl 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 238 -QLVQQEQVTSLFATPTHLDALAAAAAHAGssLKLDSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTEaMNSLYMR 316
Cdd:PRK07008 260 yELIEAERVTFSAGVPTVWLGLLNHMREAG--LRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTE-MSPLGTL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 317 QPKTGTEMAPGFFSEVRIV----RIGGGVD-EIV-ANGEE--------GELIVAAS---DSAFVGylnqpqaTAEKLQDG 379
Cdd:PRK07008 337 CKLKWKHSQLPLDEQRKLLekqgRVIYGVDmKIVgDDGRElpwdgkafGDLQVRGPwviDRYFRG-------DASPLVDG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 380 WYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSAD 459
Cdd:PRK07008 410 WFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTRE 489
|
490 500 510 520
....*....|....*....|....*....|....*....|..
1T5D_X 460 ALDTFcRSSELADFKRPKRYFILDQLPKNALNKVLRRQLVQQ 501
Cdd:PRK07008 490 ELLAF-YEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQ 530
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
28-434 |
3.61e-26 |
|
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: 111.41 E-value: 3.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 28 LRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIKRGEmtAAVI 107
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSE--SKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 108 AVGRQVADAIFQSGSGARII----FLGDLVRDGEPYS-----YGPPIEDPQREPAQPAFIFYTSGTTGLPKAAIIPQRAa 178
Cdd:cd05932 83 FVGKLDDWKAMAPGVPEGLIsislPPPSAANCQYQWDdliaqHPPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGS- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 179 esrvLFMSTQVGLRH---GRHNVVLGLMPLYHVVGFFAVLVAALaLDGTYVVVEEfrPVDA-LQLVQQEQVTSLFATPTH 254
Cdd:cd05932 162 ----FAWAAQAGIEHigtEENDRMLSYLPLAHVTERVFVEGGSL-YGGVLVAFAE--SLDTfVEDVQRARPTLFFSVPRL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 255 LDALAAAAAHAGSSLKLD--------------------SLRHVTFAG---ATMPDAVLETVHQhLPGEKVNIYGTTEAMN 311
Cdd:cd05932 235 WTKFQQGVQDKIPQQKLNlllkipvvnslvkrkvlkglGLDQCRLAGcgsAPVPPALLEWYRS-LGLNILEAYGMTENFA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 312 SLYMRQP---KTGTEMAPGFFSEVRIvrigggvdeivanGEEGELIVAaSDSAFVGYLNQPQATAEKL-QDGWYRTSDVA 387
Cdd:cd05932 314 YSHLNYPgrdKIGTVGNAGPGVEVRI-------------SEDGEILVR-SPALMMGYYKDPEATAEAFtADGFLRTGDKG 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
1T5D_X 388 VWTPEGTVRILGRVDDMI-ISGGENIHPSEIERVLGTAPGVTEVVVIG 434
Cdd:cd05932 380 ELDADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
28-498 |
3.83e-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: 111.01 E-value: 3.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 28 LRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIKRGEMTAavi 107
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 108 avgrqvadaifqsgsgariiFLGDLVRDgepysygppiedpqrepaQPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMST 187
Cdd:cd05910 78 --------------------FIGIPKAD------------------EPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQ 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 188 QVGLRHGrhNVVLGLMPLyhvvgfFAVLVAALALDGTYVVVEEFRPVDA-----LQLVQQEQVTSLFATPTHLDALAAAA 262
Cdd:cd05910 120 LYGIRPG--EVDLATFPL------FALFGPALGLTSVIPDMDPTRPARAdpqklVGAIRQYGVSIVFGSPALLERVARYC 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 263 AHAGssLKLDSLRHVTFAGATMPDAVLETVHQHLPGEK--VNIYGTTEAM--NSLYMRQPKTGTEMAPGFFS-------- 330
Cdd:cd05910 192 AQHG--ITLPSLRRVLSAGAPVPIALAARLRKMLSDEAeiLTPYGATEALpvSSIGSRELLATTTAATSGGAgtcvgrpi 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 331 ---EVRIVRI-GGGVDEI-----VANGEEGELIVAA---SDSafvgYLNQPQATA-EKLQDG----WYRTSDVAVWTPEG 393
Cdd:cd05910 270 pgvRVRIIEIdDEPIAEWddtleLPRGEIGEITVTGptvTPT----YVNRPVATAlAKIDDNsegfWHRMGDLGYLDDEG 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 394 TVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLAdQRWGQSVTACVVPRLGETLSADALDTFCR--SSELA 471
Cdd:cd05910 346 RLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVG-KPGCQLPVLCVEPLPGTITPRARLEQELRalAKDYP 424
|
490 500 510
....*....|....*....|....*....|.
1T5D_X 472 DFKRPKRYFILDQLP----KNAlnKVLRRQL 498
Cdd:cd05910 425 HTQRIGRFLIHPSFPvdirHNA--KIFREKL 453
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
29-459 |
5.71e-26 |
|
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: 111.59 E-value: 5.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 29 RLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGA----------VPALLN------PRL---- 88
Cdd:cd05943 98 EVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAiwsscspdfgVPGVLDrfgqiePKVlfav 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 89 -----------KSAELAELIKRGEMTAAVIAVGRQVADAIFQSGSGARIIFLGDLVRDGEpysyGPPIEDPQREPAQPAF 157
Cdd:cd05943 178 daytyngkrhdVREKVAELVKGLPSLLAVVVVPYTVAAGQPDLSKIAKALTLEDFLATGA----AGELEFEPLPFDHPLY 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 158 IFYTSGTTGLPKA------AIIPQRAAESRVlfmstQVGLRHGrhNVVL-----GLMpLYHvvgffaVLVAALALDGTYV 226
Cdd:cd05943 254 ILYSSGTTGLPKCivhgagGTLLQHLKEHIL-----HCDLRPG--DRLFyyttcGWM-MWN------WLVSGLAVGATIV 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 227 VVEE--FRPVDA--LQLVQQEQVTSLFATPTHLDALAAAAAHAGSSLKLDSLRHVTFAGATMPDAVLETVHQHLpGEKV- 301
Cdd:cd05943 320 LYDGspFYPDTNalWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHI-KPDVl 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 302 --NIYGTTEaMNSLYMRQPKTgtemAPGFFSEVRIVRIGGGVDeiVAN-------GEEGEL-IVAASDSAFVGYLNQPQA 371
Cdd:cd05943 399 laSISGGTD-IISCFVGGNPL----LPVYRGEIQCRGLGMAVE--AFDeegkpvwGEKGELvCTKPFPSMPVGFWNDPDG 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 372 TaeKLQD-------GWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSV 444
Cdd:cd05943 472 S--RYRAayfakypGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERV 549
|
490
....*....|....*
1T5D_X 445 TACVVPRLGETLSAD 459
Cdd:cd05943 550 ILFVKLREGVELDDE 564
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
142-504 |
9.26e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 108.21 E-value: 9.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 142 GPPIEDPQrepaqpAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGlrhGRHNVVLGlMPLYHVVGFfAVLVAALaL 221
Cdd:PRK07824 30 GEPIDDDV------ALVVATSGTTGTPKGAMLTAAALTASADATHDRLG---GPGQWLLA-LPAHHIAGL-QVLVRSV-I 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 222 DGTYVVV----EEFRPVD----ALQLVQQEQVTSLfaTPTHLDALAAAAAHAGSSLKLDSlrhVTFAGATMPDAVLETVH 293
Cdd:PRK07824 98 AGSEPVEldvsAGFDPTAlpraVAELGGGRRYTSL--VPMQLAKALDDPAATAALAELDA---VLVGGGPAPAPVLDAAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 294 QhLPGEKVNIYGTTE-AMNSLYMRQPKTGTEmapgffsevriVRIGGGVDEIvangeeGELIVAAsdsafvGYLNQPQ-- 370
Cdd:PRK07824 173 A-AGINVVRTYGMSEtSGGCVYDGVPLDGVR-----------VRVEDGRIAL------GGPTLAK------GYRNPVDpd 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 371 ATAEKlqdGWYRTSDVAVWTpEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVP 450
Cdd:PRK07824 229 PFAEP---GWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVG 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
1T5D_X 451 RLGETLSADALDTFCrSSELADFKRPKRYFILDQLPKNALNKVLRRQLVQQVSS 504
Cdd:PRK07824 305 DGGPAPTLEALRAHV-ARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRFAG 357
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
4-498 |
9.94e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 111.97 E-value: 9.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 4 VNEMLRRAATRAPDhcALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPAL 83
Cdd:PRK12316 3059 VHRLFEEQVERTPD--AVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVP 3136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 84 LNPRLKSAELAELIKrgemTAAVIAVGRQVADAIFQSGSGARIiflgDLVRDGEPYSYGPPieDPQREPAQPAFIFYTSG 163
Cdd:PRK12316 3137 LDPEYPEERLAYMLE----DSGAQLLLSQSHLRLPLAQGVQVL----DLDRGDENYAEANP--AIRTMPENLAYVIYTSG 3206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 164 TTGLPKAAIIPQRAAESRVLFMSTQVGLrhGRHNVVLGLMPlYHVVGFFAVLVAALAlDGTYVVVEEFRPVDALQLVQQE 243
Cdd:PRK12316 3207 STGKPKGVGIRHSALSNHLCWMQQAYGL--GVGDRVLQFTT-FSFDVFVEELFWPLM-SGARVVLAGPEDWRDPALLVEL 3282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 244 QVTSLFATPTHLDALAAAAAHAGSSLKLDSLRHVTFAGATMPDAVLETVHQHLPgeKVNIYGTTEAMNSLYMRQPKTGTE 323
Cdd:PRK12316 3283 INSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLP--LYNLYGPTEATITVTHWQCVEEGK 3360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 324 MAPGFFSEV--RIVRIGGGVDEIVANGEEGELIVAASDSAfVGYLNQPQATAEKLQ-------DGWYRTSDVAVWTPEGT 394
Cdd:PRK12316 3361 DAVPIGRPIanRACYILDGSLEPVPVGALGELYLGGEGLA-RGYHNRPGLTAERFVpdpfvpgERLYRTGDLARYRADGV 3439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 395 VRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLAdqrwGQSVTACVVPRLGETLSADALDTFCRSSeLADFK 474
Cdd:PRK12316 3440 IEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVD----GRQLVAYVVPEDEAGDLREALKAHLKAS-LPEYM 3514
|
490 500
....*....|....*....|....
1T5D_X 475 RPKRYFILDQLPKNALNKVLRRQL 498
Cdd:PRK12316 3515 VPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
29-450 |
2.70e-25 |
|
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: 108.60 E-value: 2.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 29 RLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPAllnPRLKSAELAELIKrgemtaavia 108
Cdd:cd17640 5 RITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDV---VRGSDSSVEELLY---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 109 vgrqvadaIFQSgSGARIIFLgdlvrdgepysygppiedpQREPAQPAFIFYTSGTTGLPKAAIIPQRAAESRV----LF 184
Cdd:cd17640 72 --------ILNH-SESVALVV-------------------ENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIrslsDI 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 185 MSTQVGLRhgrhnvVLGLMPLYH----VVGFFAVLVAALALDGTYVVVEE----FRPV---------DALQLVQQEQVTS 247
Cdd:cd17640 124 VPPQPGDR------FLSILPIWHsyerSAEYFIFACGCSQAYTSIRTLKDdlkrVKPHyivsvprlwESLYSGIQKQVSK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 248 LFATpthldalaaAAAHAGSSLKLDSLRHVTFAGATMPDAVlETVHQHLPGEKVNIYGTTEAMNSLYMRQ---PKTGTEM 324
Cdd:cd17640 198 SSPI---------KQFLFLFFLSGGIFKFGISGGGALPPHV-DTFFEAIGIEVLNGYGLTETSPVVSARRlkcNVRGSVG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 325 APGFFSEVRIVRIGGGvdEIVANGEEGELIVAaSDSAFVGYLNQPQATAEKL-QDGWYRTSDVAVWTPEGTVRILGRVDD 403
Cdd:cd17640 268 RPLPGTEIKIVDPEGN--VVLPPGEKGIVWVR-GPQVMKGYYKNPEATSKVLdSDGWFNTGDLGWLTCGGELVLTGRAKD 344
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
1T5D_X 404 MII-SGGENIHPSEIERVLGTAPGVTEVVVIGlADQRwgqSVTACVVP 450
Cdd:cd17640 345 TIVlSNGENVEPQPIEEALMRSPFIEQIMVVG-QDQK---RLGALIVP 388
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
5-498 |
6.24e-25 |
|
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: 107.26 E-value: 6.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 5 NEMLRRAATRAPDHcaLAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALL 84
Cdd:cd17645 1 HQLFEEQVERTPDH--VAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 85 NPRLKSAELAELIkrgemtaaviavgrqvADaifqsgSGARIIFlgdlvrdgepysygppiedpqREPAQPAFIFYTSGT 164
Cdd:cd17645 79 DPDYPGERIAYML----------------AD------SSAKILL---------------------TNPDDLAYVIYTSGS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 165 TGLPKAAIIPQRAAESRVLFMSTQVGLRHGRHNVVlglmplYHVVGF-------FAVLVAALALdgtYVVVEEFR-PVDA 236
Cdd:cd17645 116 TGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLV------YASFSFdasaweiFPHLTAGAAL---HVVPSERRlDLDA 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 237 L-QLVQQEQVTSLFaTPTHLDALAaaaahagSSLKLDSLRHVTFAGATMPDAVLEtvhqhlPGEKVNIYGTTE--AMNSL 313
Cdd:cd17645 187 LnDYFNQEGITISF-LPTGAAEQF-------MQLDNQSLRVLLTGGDKLKKIERK------GYKLVNNYGPTEntVVATS 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 314 YMRQPKTGTEMAPGFFSEVRIVRIGGGVdEIVANGEEGELIVAASDSAfVGYLNQPQATAEKL-------QDGWYRTSDV 386
Cdd:cd17645 253 FEIDKPYANIPIGKPIDNTRVYILDEAL-QLQPIGVAGELCIAGEGLA-RGYLNRPELTAEKFivhpfvpGERMYRTGDL 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 387 AVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRlgETLSADALDTFCR 466
Cdd:cd17645 331 AKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAP--EEIPHEELREWLK 408
|
490 500 510
....*....|....*....|....*....|..
1T5D_X 467 SSeLADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:cd17645 409 ND-LPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
27-433 |
2.00e-24 |
|
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: 105.99 E-value: 2.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 27 GLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIKRGEmtaav 106
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSE----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 107 iavgrqvadaifqsgsgARIIFLGDlvrdgepysygppiedpqrePAQPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMS 186
Cdd:cd05914 80 -----------------AKAIFVSD--------------------EDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 187 TQVGLRHGrhNVVLGLMPLYHVVGFFAVLVAALALdGTYVVVEEFRPVDALQLVQQEQVTSLFATPTH-----LDALAAA 261
Cdd:cd05914 123 EVVLLGKG--DKILSILPLHHIYPLTFTLLLPLLN-GAHVVFLDKIPSAKIIALAFAQVTPTLGVPVPlviekIFKMDII 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 262 AAHAGSSLKL--------DSLRHVTF----------------AGATMPDAVLETVHQhlPGEKVNI-YGTTEAMNSLYMR 316
Cdd:cd05914 200 PKLTLKKFKFklakkinnRKIRKLAFkkvheafggnikefviGGAKINPDVEEFLRT--IGFPYTIgYGMTETAPIISYS 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 317 QPKTGTEMAPGFFSEVRIVRIgggvDEIVANGEEGELIVAAsDSAFVGYLNQPQATAEKL-QDGWYRTSDVAVWTPEGTV 395
Cdd:cd05914 278 PPNRIRLGSAGKVIDGVEVRI----DSPDPATGEGEIIVRG-PNVMKGYYKNPEATAEAFdKDGWFHTGDLGKIDAEGYL 352
|
410 420 430
....*....|....*....|....*....|....*....
1T5D_X 396 RILGRVDDMIISG-GENIHPSEIERVLGTAPGVTEVVVI 433
Cdd:cd05914 353 YIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVLESLVV 391
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
16-498 |
5.11e-24 |
|
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: 104.86 E-value: 5.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 16 PDHCALAVPARglRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAE 95
Cdd:cd17656 2 PDAVAVVFENQ--KLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 96 LIKrgEMTAAVIAVGRQVADAIFQSGSGARIIFLGDLVRDGEPYSYGPPIEDPqrepaqpAFIFYTSGTTGLPKAAIIPQ 175
Cdd:cd17656 80 IML--DSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSDDL-------LYIIYTSGTTGKPKGVQLEH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 176 RAAESRVLFMSTQVGLRHGrHNVVLGLMPLYHVVgfFAVLVAALALDGT-YVVVEEF-RPVDAL-QLVQQEQVTSLFaTP 252
Cdd:cd17656 151 KNMVNLLHFEREKTNINFS-DKVLQFATCSFDVC--YQEIFSTLLSGGTlYIIREETkRDVEQLfDLVKRHNIEVVF-LP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 253 THLDALAAAAAHAGSSLkLDSLRHVTFAGA--TMPDAVLETVHQHlpgeKV---NIYGTTEA-MNSLYMRQPKT-GTEMA 325
Cdd:cd17656 227 VAFLKFIFSEREFINRF-PTCVKHIITAGEqlVITNEFKEMLHEH----NVhlhNHYGPSEThVVTTYTINPEAeIPELP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 326 PgffsevrIVRIGGGVDEIVAN--------GEEGELIVAASDSAfVGYLNQPQATAEKL-------QDGWYRTSDVAVWT 390
Cdd:cd17656 302 P-------IGKPISNTWIYILDqeqqlqpqGIVGELYISGASVA-RGYLNRQELTAEKFfpdpfdpNERMYRTGDLARYL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 391 PEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRlgETLSADALDTFCrSSEL 470
Cdd:cd17656 374 PDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVME--QELNISQLREYL-AKQL 450
|
490 500
....*....|....*....|....*...
1T5D_X 471 ADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:cd17656 451 PEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
29-499 |
2.42e-23 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 103.49 E-value: 2.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 29 RLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPAL---------LNPRLKSAE------- 92
Cdd:PRK10524 84 TYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVvfggfashsLAARIDDAKpvlivsa 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 93 ---------------LAELIKRGEMT-AAVIAVGRQVADAIFQSG-----SGARIIFLGDLVrdgepysygpPIEdpQRE 151
Cdd:PRK10524 164 dagsrggkvvpykplLDEAIALAQHKpRHVLLVDRGLAPMARVAGrdvdyATLRAQHLGARV----------PVE--WLE 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 152 PAQPAFIFYTSGTTGLPK-------------AA----IIPQRAAEsrVLFMSTQVGLrhgrhnvvlglmplyhVVG---- 210
Cdd:PRK10524 232 SNEPSYILYTSGTTGKPKgvqrdtggyavalATsmdtIFGGKAGE--TFFCASDIGW----------------VVGhsyi 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 211 FFAVLVAALAldgtyVVVEEFRPV--DA---LQLVQQEQVTSLFATPTHLDALAAAAAHAGSSLKLDSLRHVTFAGATMP 285
Cdd:PRK10524 294 VYAPLLAGMA-----TIMYEGLPTrpDAgiwWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLD 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 286 DAVLETVHQHLPGEKVNIYGTTE-------AMNSLYMRQPKTGTEMAPGFFSEVRIVRIGGGvdEIVANGEEGELIVAA- 357
Cdd:PRK10524 369 EPTASWISEALGVPVIDNYWQTEtgwpilaIARGVEDRPTRLGSPGVPMYGYNVKLLNEVTG--EPCGPNEKGVLVIEGp 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 358 -----------SDSAFV----GYLNQPQataeklqdgwYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLG 422
Cdd:PRK10524 447 lppgcmqtvwgDDDRFVktywSLFGRQV----------YSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESIS 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 423 TAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLsADALDTFCRSSE--------LADFKRPKRYFILDQLPKNALNKVL 494
Cdd:PRK10524 517 SHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSL-ADREARLALEKEimalvdsqLGAVARPARVWFVSALPKTRSGKLL 595
|
....*
1T5D_X 495 RRQLV 499
Cdd:PRK10524 596 RRAIQ 600
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
29-501 |
2.97e-23 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 102.91 E-value: 2.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 29 RLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIKRGEMTAAV-- 106
Cdd:PRK06018 39 RTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVItd 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 107 ---IAVGRQVADAIfqsGSGARIIFLGDLVRDGEPY-----SYGPPIEDPQREPAQPAF-------IFYTSGTTGLPKAA 171
Cdd:PRK06018 119 ltfVPILEKIADKL---PSVERYVVLTDAAHMPQTTlknavAYEEWIAEADGDFAWKTFdentaagMCYTSGTTGDPKGV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 172 IIPQRaaeSRVL--FMSTQVG-LRHGRHNVVLGLMPLYHV----VGFFAVLVAA------LALDGTYVvveefrpvdaLQ 238
Cdd:PRK06018 196 LYSHR---SNVLhaLMANNGDaLGTSAADTMLPVVPLFHAnswgIAFSAPSMGTklvmpgAKLDGASV----------YE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 239 LVQQEQVTSLFATPTHLDALAAAAAHAGssLKLDSLRHVTFAGATMPDAVLETVHQhLPGEKVNIYGTTEA--MNSLYMR 316
Cdd:PRK06018 263 LLDTEKVTFTAGVPTVWLMLLQYMEKEG--LKLPHLKMVVCGGSAMPRSMIKAFED-MGVEVRHAWGMTEMspLGTLAAL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 317 QPK----TG--------TEMAPGFFSEVRIVRIGGgvDEIVANGEE-GELIV--AASDSAFVGylnqpqATAEKL-QDGW 380
Cdd:PRK06018 340 KPPfsklPGdarldvlqKQGYPPFGVEMKITDDAG--KELPWDGKTfGRLKVrgPAVAAAYYR------VDGEILdDDGF 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 381 YRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADA 460
Cdd:PRK06018 412 FDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREE 491
|
490 500 510 520
....*....|....*....|....*....|....*....|.
1T5D_X 461 LDTFCrSSELADFKRPKRYFILDQLPKNALNKVLRRQLVQQ 501
Cdd:PRK06018 492 ILKYM-DGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQ 531
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
3-498 |
4.17e-23 |
|
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: 102.13 E-value: 4.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 3 TVNEMLRRAATRAPDhcALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPA 82
Cdd:cd17644 1 CIHQLFEEQVERTPD--AVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 83 LLNPRLKSAELAelikrgemtaaVIAVGRQVADAIFQsgsgariiflgdlvrdgepysygppiedpqrePAQPAFIFYTS 162
Cdd:cd17644 79 PLDPNYPQERLT-----------YILEDAQISVLLTQ--------------------------------PENLAYVIYTS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 163 GTTGLPKAAIIPQRAAesrvlfmstqVGLRHGRHNVVlGLMPLYHVVGF--FAVLVAA-----LALDGTYVVV--EEFRP 233
Cdd:cd17644 116 GSTGKPKGVMIEHQSL----------VNLSHGLIKEY-GITSSDRVLQFasIAFDVAAeeiyvTLLSGATLVLrpEEMRS 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 234 --VDALQLVQQEQVTSLFATPTHLDALAAAAAHAGSSLkLDSLRHVTFAG-ATMPDAV--LETVHQHLPgEKVNIYGTTE 308
Cdd:cd17644 185 slEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDL-PSSLRLVIVGGeAVQPELVrqWQKNVGNFI-QLINVYGPTE 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 309 AMNSLYMRQPKTGTEMApgfFSEVRIVRIGGGV-----DE---IVANGEEGELIVAASDSAfVGYLNQPQATAEK-LQDG 379
Cdd:cd17644 263 ATIAATVCRLTQLTERN---ITSVPIGRPIANTqvyilDEnlqPVPVGVPGELHIGGVGLA-RGYLNRPELTAEKfISHP 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 380 W--------YRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPR 451
Cdd:cd17644 339 FnsseserlYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPH 418
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
1T5D_X 452 LGETLSADALDTFCrSSELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:cd17644 419 YEESPSTVELRQFL-KAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
1-487 |
6.29e-23 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 103.08 E-value: 6.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 1 MQTVNEMLRRAATRAPDHCALAvPARGLRLTHAELRARVEAVAARLhADGLRPQQRVAVVAPNSADVVIAILALHRLGAV 80
Cdd:PRK08633 614 LPPLAEAWIDTAKRNWSRLAVA-DSTGGELSYGKALTGALALARLL-KRELKDEENVGILLPPSVAGALANLALLLAGKV 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 81 PALLNPRLKSAELAELIKRGEMTaaVIAVGRQVAD------AIFQSGSGARIIFLGDL---VRDGE-----------PYS 140
Cdd:PRK08633 692 PVNLNYTASEAALKSAIEQAQIK--TVITSRKFLEklknkgFDLELPENVKVIYLEDLkakISKVDkltallaarllPAR 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 141 YGPPIEDPQREPAQPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGLRhgRHNVVLGLMPLYHVVGFFAVLVAALa 220
Cdd:PRK08633 770 LLKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLR--NDDVILSSLPFFHSFGLTVTLWLPL- 846
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 221 LDGTYVVVEEfRPVDAL---QLVQQEQVTSLFATPTHLDALAAAAAHagSSLKLDSLRHVTfAGA-TMPDAVLETVHqhl 296
Cdd:PRK08633 847 LEGIKVVYHP-DPTDALgiaKLVAKHRATILLGTPTFLRLYLRNKKL--HPLMFASLRLVV-AGAeKLKPEVADAFE--- 919
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 297 pgEKVNI-----YGTTE-----AMN------SLYMRQP--KTGT-EMA-PGFfsevrIVRIgggVD----EIVANGEEGE 352
Cdd:PRK08633 920 --EKFGIrilegYGATEtspvaSVNlpdvlaADFKRQTgsKEGSvGMPlPGV-----AVRI---VDpetfEELPPGEDGL 989
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 353 LIVAASDsAFVGYLNQPQATAEKLQD----GWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVT 428
Cdd:PRK08633 990 ILIGGPQ-VMKGYLGDPEKTAEVIKDidgiGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGE 1068
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
1T5D_X 429 EVV--VIGLADQRWGQSVtaCVVPRLGETlSADALDTFCRSSELADFKRPKRYFILDQLPK 487
Cdd:PRK08633 1069 EVVfaVTAVPDEKKGEKL--VVLHTCGAE-DVEELKRAIKESGLPNLWKPSRYFKVEALPL 1126
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
1-496 |
9.45e-23 |
|
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: 101.80 E-value: 9.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 1 MQTVNEMLRRAATRAPDHCALAVPA-RGL--RLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRL 77
Cdd:cd05968 60 MNIVEQLLDKWLADTRTRPALRWEGeDGTsrTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 78 GAV---------PALLNPRLKSAELAELI------KRG---EMTAAVIAVGRQ---VADAIFQSGSGAriiflGDLVRDG 136
Cdd:cd05968 140 GGIvvpifsgfgKEAAATRLQDAEAKALItadgftRRGrevNLKEEADKACAQcptVEKVVVVRHLGN-----DFTPAKG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 137 EPYSY-----GPPIEDPQREPAQPAFIFYTSGTTGLPKAAI-----IPQRAAESrvlfMSTQVGLRHGrhNVVLGLMPLY 206
Cdd:cd05968 215 RDLSYdeekeTAGDGAERTESEDPLMIIYTSGTTGKPKGTVhvhagFPLKAAQD----MYFQFDLKPG--DLLTWFTDLG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 207 HVVGFFAVLvAALALDGTYVVVE---EFRPVDAL-QLVQQEQVTSLFATPTHLDALAAAAAHAGSSLKLDSLRHVTFAGA 282
Cdd:cd05968 289 WMMGPWLIF-GGLILGATMVLYDgapDHPKADRLwRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 283 TM-PDAVLETVHQHLPGEK--VNIYGtteamnslymrqpktGTEMAPGFFSEVRIVRIGG--------GVDEIV------ 345
Cdd:cd05968 368 PWnPEPWNWLFETVGKGRNpiINYSG---------------GTEISGGILGNVLIKPIKPssfngpvpGMKADVldesgk 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 346 -ANGEEGELIVAAsdsAFVG-----------YLNqpqATAEKLQDGWYRtSDVAVWTPEGTVRILGRVDDMIISGGENIH 413
Cdd:cd05968 433 pARPEVGELVLLA---PWPGmtrgfwrdedrYLE---TYWSRFDNVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVG 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 414 PSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLS---ADALDTFCrSSELADFKRPKRYFILDQLPKNAL 490
Cdd:cd05968 506 PAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTealAEELMERV-ADELGKPLSPERILFVKDLPKTRN 584
|
....*.
1T5D_X 491 NKVLRR 496
Cdd:cd05968 585 AKVMRR 590
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
9-498 |
2.40e-22 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 100.35 E-value: 2.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 9 RRAATRAPDHCAL--AVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVpalLNP 86
Cdd:PRK04319 51 RHADGGRKDKVALryLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAI---VGP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 87 rLKSAELAELIK-RGEMTAAVIAV------GRQVADAIfqsgSGARIIFL-GDLVRDGEPY----------SYGPPIEDP 148
Cdd:PRK04319 128 -LFEAFMEEAVRdRLEDSEAKVLIttpallERKPADDL----PSLKHVLLvGEDVEEGPGTldfnalmeqaSDEFDIEWT 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 149 QREpaQPAFIFYTSGTTGLPKAAIIPQRAAesrvlfmstqvgLRH---GRhnVVLGLMP--LYH-------VVGFFAVLV 216
Cdd:PRK04319 203 DRE--DGAILHYTSGSTGKPKGVLHVHNAM------------LQHyqtGK--YVLDLHEddVYWctadpgwVTGTSYGIF 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 217 AALALDGTYVVVE-EFRPVDALQLVQQEQVTSLFATPTHLDALAAAAAHAGSSLKLDSLRHVTFAGATM-PDAVLEtvhq 294
Cdd:PRK04319 267 APWLNGATNVIDGgRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDLSSLRHILSVGEPLnPEVVRW---- 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 295 hlpGEKV---NIYGT---TEA---MNSLY---------MRQPKTGTEMApgffsevrIVRIGGgvDEIVANgEEGEL-IV 355
Cdd:PRK04319 343 ---GMKVfglPIHDNwwmTETggiMIANYpamdikpgsMGKPLPGIEAA--------IVDDQG--NELPPN-RMGNLaIK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 356 AASDSAFVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGL 435
Cdd:PRK04319 409 KGWPSMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGK 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1T5D_X 436 ADQRWGQSVTACVVPRLGETLSaDALdtfcrSSELADFKR--------PKRYFILDQLPKNALNKVLRRQL 498
Cdd:PRK04319 489 PDPVRGEIIKAFVALRPGYEPS-EEL-----KEEIRGFVKkglgahaaPREIEFKDKLPKTRSGKIMRRVL 553
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
30-502 |
3.19e-21 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 96.78 E-value: 3.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 30 LTHAELRARVEAVAARLHAD-GLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLN----------------------- 85
Cdd:PRK05620 39 TTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNkqlmndqivhiinhaedevivad 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 86 PRLKSaELAELIKRGEMTAAVIAVGRQVAD-AIFQSGSGARIIFLGDLVrDGEPYSYgppiEDPQREPAQPAFIFYTSGT 164
Cdd:PRK05620 119 PRLAE-QLGEILKECPCVRAVVFIGPSDADsAAAHMPEGIKVYSYEALL-DGRSTVY----DWPELDETTAAAICYSTGT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 165 TGLPKAAIIPQRAA--ESRVLFMSTQVGLRHGRhnVVLGLMPLYHVVGFfAVLVAALaLDGTYVVVEEfRPVDALQLVQQ 242
Cdd:PRK05620 193 TGAPKGVVYSHRSLylQSLSLRTTDSLAVTHGE--SFLCCVPIYHVLSW-GVPLAAF-MSGTPLVFPG-PDLSAPTLAKI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 243 EQVTS---LFATPTHLDALAAAAAHagSSLKLDSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTEAMNSLYMRQPK 319
Cdd:PRK05620 268 IATAMprvAHGVPTLWIQLMVHYLK--NPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPP 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 320 TGT--------EMAPGFFS---EVRIVRIGGGVDEIVANgeEGEL-----IVAAS------------DSAFVGYlNQPQA 371
Cdd:PRK05620 346 SGVsgearwayRVSQGRFPaslEYRIVNDGQVMESTDRN--EGEIqvrgnWVTASyyhspteegggaASTFRGE-DVEDA 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 372 TAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQ-----SVTA 446
Cdd:PRK05620 423 NDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGErplavTVLA 502
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
1T5D_X 447 CVVPRLGETlsADALDTFCRsSELADFKRPKRYFILDQLPKNALNKVLRRQLVQQV 502
Cdd:PRK05620 503 PGIEPTRET--AERLRDQLR-DRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHL 555
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
30-498 |
8.14e-21 |
|
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: 94.56 E-value: 8.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 30 LTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIKRGEmtaAVIAV 109
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGG---AVYAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 110 GRQVADAifqsgsgariiflgdlvrdgepysygppiedpqrepAQPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQV 189
Cdd:cd05974 78 VDENTHA------------------------------------DDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWI 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 190 GLRHGrhNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEE--FRPVDALQLVQQEQVTSLFATPTHLDALAAAAAhagS 267
Cdd:cd05974 122 GLKPG--DVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYarFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDL---A 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 268 SLKLdSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTE--AMNSLYMRQP-KTGT--EMAPGFFSEVrivrigggVD 342
Cdd:cd05974 197 SFDV-KLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTEttALVGNSPGQPvKAGSmgRPLPGYRVAL--------LD 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 343 EIVANGEEGELIVAASDSAFVG----YLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIE 418
Cdd:cd05974 268 PDGAPATEGEVALDLGDTRPVGlmkgYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 419 RVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLG-ETLSADALDTFCRSSE-LADFKRPKRYFILdQLPKNALNKVLRR 496
Cdd:cd05974 348 SVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGyEPSPETALEIFRFSRErLAPYKRIRRLEFA-ELPKTISGKIRRV 426
|
..
1T5D_X 497 QL 498
Cdd:cd05974 427 EL 428
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
2-486 |
8.59e-21 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 96.19 E-value: 8.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 2 QTVNEMLRRAATR-APDHCALAVPARGlRLTHAELRARvEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAV 80
Cdd:PRK06814 631 RTLFEALIEAAKIhGFKKLAVEDPVNG-PLTYRKLLTG-AFVLGRKLKKNTPPGENVGVMLPNANGAAVTFFALQSAGRV 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 81 PALLN-----PRLKSAELAELIKRGEMTAAVIAVGRqVADAIFQSGSGARIIFLGDLVR--------DGEPYSYGPPIED 147
Cdd:PRK06814 709 PAMINfsagiANILSACKAAQVKTVLTSRAFIEKAR-LGPLIEALEFGIRIIYLEDVRAqigladkiKGLLAGRFPLVYF 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 148 PQREPAQPAFIFYTSGTTGLPKAAIIPQRA-------AESRVLFmstqvglrhGRHNVVLGLMPLYHVVGFFAVLVAALa 220
Cdd:PRK06814 788 CNRDPDDPAVILFTSGSEGTPKGVVLSHRNllanraqVAARIDF---------SPEDKVFNALPVFHSFGLTGGLVLPL- 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 221 LDGT----------YVVVEEfrpvdalqLVQQEQVTSLFATPThldaLAAAAAHAGSSLKLDSLRHVtFAGAtmpDAVLE 290
Cdd:PRK06814 858 LSGVkvflypsplhYRIIPE--------LIYDTNATILFGTDT----FLNGYARYAHPYDFRSLRYV-FAGA---EKVKE 921
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 291 TVHQhLPGEKVNI-----YGTTEAMNSLYMRQP---KTGT--EMAPGFFSEVRIVRiggGVDeivangEEGELIVAAsDS 360
Cdd:PRK06814 922 ETRQ-TWMEKFGIrilegYGVTETAPVIALNTPmhnKAGTvgRLLPGIEYRLEPVP---GID------EGGRLFVRG-PN 990
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 361 AFVGYLN-QPQATAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQR 439
Cdd:PRK06814 991 VMLGYLRaENPGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDAR 1070
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
1T5D_X 440 WGQSVTACVVprlGETLSADALDTFCRSSELADFKRPKRYFILDQLP 486
Cdd:PRK06814 1071 KGERIILLTT---ASDATRAAFLAHAKAAGASELMVPAEIITIDEIP 1114
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
154-501 |
2.90e-20 |
|
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: 93.68 E-value: 2.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 154 QPAFIFYTSGTTGLPKAAIIPQRAAeSRVLFMSTQVGLRHGRHNVVLGLMPLYHVVGFFAVLVAALALdGTYVVVEE--- 230
Cdd:cd05928 175 EPMAIYFTSGTTGSPKMAEHSHSSL-GLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQ-GACVFVHHlpr 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 231 FRPVDALQLVQQEQVTSLFATPTHLDALAAAAAhagSSLKLDSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTEAM 310
Cdd:cd05928 253 FDPLVILKTLSSYPITTFCGAPTVYRMLVQQDL---SSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETG 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 311 nsLYMRQPKtGTEMAPGFFS------EVRIVRIGGGVdeiVANGEEGELIVAASD----SAFVGYLNQPQATAEKLQDGW 380
Cdd:cd05928 330 --LICANFK-GMKIKPGSMGkasppyDVQIIDDNGNV---LPPGTEGDIGIRVKPirpfGLFSGYVDNPEKTAATIRGDF 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 381 YRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVV---PRLG---E 454
Cdd:cd05928 404 YLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVlapQFLShdpE 483
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
1T5D_X 455 TLSADaLDTFCRSSElADFKRPKRYFILDQLPKNALNKVLRRQLVQQ 501
Cdd:cd05928 484 QLTKE-LQQHVKSVT-APYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
27-501 |
2.93e-20 |
|
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: 93.26 E-value: 2.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 27 GLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIKRgemtaav 106
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITV------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 107 iavgrqvadaifqsgSGAR-IIFlgDLVRDGEPYSYGPPIEDPQREPAQPAFIFYTSGTTGLPKAAIIpqraAESRVLFM 185
Cdd:cd05939 74 ---------------SKAKaLIF--NLLDPLLTQSSTEPPSQDDVNFRDKLFYIYTSGTTGLPKAAVI----VHSRYYRI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 186 STQV--GLRHGRHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFRP-----------VDALQLVqQEQVTSLFATP 252
Cdd:cd05939 133 AAGAyyAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSAsnfwddcvkynCTIVQYI-GEICRYLLAQP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 253 THLdalaaaaahagsslklDSLRH---VTFAGATMPDAVLETVHQ-HLP--GEkvnIYGTTEAMNSLYMRQPKTGtemAP 326
Cdd:cd05939 212 PSE----------------EEQKHnvrLAVGNGLRPQIWEQFVRRfGIPqiGE---FYGATEGNSSLVNIDNHVG---AC 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 327 GFFS-------EVRIVRIGGGVDEIV----------ANGEEGELI--VAASD--SAFVGYLNQpQATAEKLQ-------D 378
Cdd:cd05939 270 GFNSrilpsvyPIRLIKVDEDTGELIrdsdglcipcQPGEPGLLVgkIIQNDplRRFDGYVNE-GATNKKIArdvfkkgD 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 379 GWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGL-ADQRWGQSVTACVVPRLGETls 457
Cdd:cd05939 349 SAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVeVPGVEGRAGMAAIVDPERKV-- 426
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
1T5D_X 458 adALDTFCRS--SELADFKRPKRYFILDQLPKNALNKVLRRQLVQQ 501
Cdd:cd05939 427 --DLDRFSAVlaKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKE 470
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
30-461 |
1.84e-19 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 91.61 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 30 LTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALL----NPRLKSAELAELikRGEMT-- 103
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLplpmGFGGRESYIAQL--RGMLAsa 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 104 -AAVIAVGRQVADAIFQSGSGARIIFLGDLVRDGEPysYGPPIEDPQREPAQPAFIFYTSGTTGLPKAAIIPQRAAesrv 182
Cdd:PRK09192 128 qPAAIITPDELLPWVNEATHGNPLLHVLSHAWFKAL--PEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRAL---- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 183 lfMSTQVGLRHGRHNVVLG-----LMPLYH---VVGFF-AVLVAALALDgtYVVVEEF--RPVDALQLVQQEQVTSLFAt 251
Cdd:PRK09192 202 --MANLRAISHDGLKVRPGdrcvsWLPFYHdmgLVGFLlTPVATQLSVD--YLPTRDFarRPLQWLDLISRNRGTISYS- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 252 PTHLDALAAAAAHAGSSLKLD-SLRHVTFAGATM--PDaVLETVHQHL------PGEKVNIYGTTEAMNSLYMRQPKTG- 321
Cdd:PRK09192 277 PPFGYELCARRVNSKDLAELDlSCWRVAGIGADMirPD-VLHQFAEAFapagfdDKAFMPSYGLAEATLAVSFSPLGSGi 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 322 ------------TEMAPGFFSEVR----IVRIGGGVD--EIVANGEEGEL--------IVAASDSAFVGYLNQPQATAEK 375
Cdd:PRK09192 356 vveevdrdrleyQGKAVAPGAETRrvrtFVNCGKALPghEIEIRNEAGMPlpervvghICVRGPSLMSGYFRDEESQDVL 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 376 LQDGWYRTSDVAvWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVT--EVVVIGLaDQRWGQSVTACVVPRLG 453
Cdd:PRK09192 436 AADGWLDTGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSI-AQENGEKIVLLVQCRIS 513
|
....*...
1T5D_X 454 ETLSADAL 461
Cdd:PRK09192 514 DEERRGQL 521
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1-427 |
2.31e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 91.21 E-value: 2.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 1 MQTVNEMLRRAATRAPDHCALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAV 80
Cdd:PRK07768 1 MSRFTEKMYANARTSPRGMVTGEPDAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 81 PALLN---PRLKSAELAELIKR--GEMTAAVIAVGRQVADAIFQ-SGSGARIIFLGDLVRdgepysyGPPIEDPQREPAQ 154
Cdd:PRK07768 81 LTMLHqptPRTDLAVWAEDTLRviGMIGAKAVVVGEPFLAAAPVlEEKGIRVLTVADLLA-------ADPIDPVETGEDD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 155 PAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGLRHGrHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVeefRPV 234
Cdd:PRK07768 154 LALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVE-TDVMVSWLPLFHDMGMVGFLTVPMYFGAELVKV---TPM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 235 DALQ--LVQQEQVTSLFATPTHL-------DALAAAAAHAGSSLKLDSLRhVTFAGATMPD-AVLETV------HQHLPG 298
Cdd:PRK07768 230 DFLRdpLLWAELISKYRGTMTAApnfayalLARRLRRQAKPGAFDLSSLR-FALNGAEPIDpADVEDLldagarFGLRPE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 299 EKVNIYGTTEAMNSLYMRQPKTG---TEMAPGFFSEV------------RIVRIGGGVD--EIVANGEEGEL-------- 353
Cdd:PRK07768 309 AILPAYGMAEATLAVSFSPCGAGlvvDEVDADLLAALrravpatkgntrRLATLGPPLPglEVRVVDEDGQVlpprgvgv 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1T5D_X 354 IVAASDSAFVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGV 427
Cdd:PRK07768 389 IELRGESVTPGYLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGV 462
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
4-494 |
4.80e-19 |
|
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: 90.21 E-value: 4.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 4 VNEMLRRAATRAPDHCALAVPARGLR------------------LTHAELRARVEAVAARLHADG-LRPQQRVAVVAPNS 64
Cdd:cd17632 24 LAQIIATVMTGYADRPALGQRATELVtdpatgrttlrllprfetITYAELWERVGAVAAAHDPEQpVRPGDFVAVLGFTS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 65 ADVVIAILALHRLGAVPALLN----------------PRLKSAELAELIKRGEMTAAVIAVGRQV-----------ADAI 117
Cdd:cd17632 104 PDYATVDLALTRLGAVSVPLQagasaaqlapilaetePRLLAVSAEHLDLAVEAVLEGGTPPRLVvfdhrpevdahRAAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 118 FQS-----GSGARIIFLGDLVRDGEPYSYGPPI-EDPQREPaqPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGL 191
Cdd:cd17632 184 ESArerlaAVGIPVTTLTLIAVRGRDLPPAPLFrPEPDDDP--LALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 192 RHgRHNVVLGLMPLYHVVGfFAVLVAALALDGT-YVVVE-----------EFRPVDAL------QLVQQEQVTSLFATPT 253
Cdd:cd17632 262 RP-PASITLNFMPMSHIAG-RISLYGTLARGGTaYFAAAsdmstlfddlaLVRPTELFlvprvcDMLFQRYQAELDRRSV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 254 HLDALAAAAAHAGSSLKlDSLRHVTFAGATMPDAVLET-----VHQHLPGEKVNIYGTTEA----MNSLYMRQPKTGTEM 324
Cdd:cd17632 340 AGADAETLAERVKAELR-ERVLGGRLLAAVCGSAPLSAemkafMESLLDLDLHDGYGSTEAgaviLDGVIVRPPVLDYKL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 325 AP----GFFSEVRivrigggvdeivaNGEEGELIVaASDSAFVGYLNQPQATAEKL-QDGWYRTSDV-AVWTPEGTVRIL 398
Cdd:cd17632 419 VDvpelGYFRTDR-------------PHPRGELLV-KTDTLFPGYYKRPEVTAEVFdEDGFYRTGDVmAELGPDRLVYVD 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 399 GRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWgqsVTACVVP-----------RLGETLsADALDTFCRS 467
Cdd:cd17632 485 RRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNSERAY---LLAVVVPtqdalagedtaRLRAAL-AESLQRIARE 560
|
570 580
....*....|....*....|....*..
1T5D_X 468 SELADFKRPkRYFILDQLPKNALNKVL 494
Cdd:cd17632 561 AGLQSYEIP-RDFLIETEPFTIANGLL 586
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
2-498 |
6.96e-19 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 90.61 E-value: 6.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 2 QTVNEMLRRAATRAPDhcALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVP 81
Cdd:PRK05691 2188 QTLHGLFAAQAARTPQ--APALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAY 2265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 82 ALLNPRLKSAELAELIKRGEMtaAVIAVGRQVADAIFQSGSG-ARIIFLGDLVR-DGEPYSYGPPIEDPQREpaqpAFIF 159
Cdd:PRK05691 2266 VPLDPEYPLERLHYMIEDSGI--GLLLSDRALFEALGELPAGvARWCLEDDAAAlAAYSDAPLPFLSLPQHQ----AYLI 2339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 160 YTSGTTGLPKAAIIPQRAaesrvLFMSTQVGLRHgrhnvvLGLMP-----LYHVVGFFAV---LVAALaLDGTYVVVEEF 231
Cdd:PRK05691 2340 YTSGSTGKPKGVVVSHGE-----IAMHCQAVIER------FGMRAddcelHFYSINFDAAserLLVPL-LCGARVVLRAQ 2407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 232 RPVDA---LQLVQQEQVTSLFATPTHLDALAAAAAHAGSSLkldSLRHVTFAGATMPDAVLETVHQHL-PGEKVNIYGTT 307
Cdd:PRK05691 2408 GQWGAeeiCQLIREQQVSILGFTPSYGSQLAQWLAGQGEQL---PVRMCITGGEALTGEHLQRIRQAFaPQLFFNAYGPT 2484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 308 EA----MNSLYMRQPKTGTEMAPgfFSEVRIVRIGGGVDE---IVANGEEGELIVAASDSAfVGYLNQPQATAEKL---- 376
Cdd:PRK05691 2485 ETvvmpLACLAPEQLEEGAASVP--IGRVVGARVAYILDAdlaLVPQGATGELYVGGAGLA-QGYHDRPGLTAERFvadp 2561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 377 --QDG--WYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSV--TACVVP 450
Cdd:PRK05691 2562 faADGgrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAgyLVSAVA 2641
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
1T5D_X 451 RLGETLSA---DALDTFCRsSELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:PRK05691 2642 GQDDEAQAalrEALKAHLK-QQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
28-498 |
1.20e-18 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 88.64 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 28 LRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIKRGEMTAAVI 107
Cdd:cd05915 23 HRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 108 avgrqvaDAIFQSGSGARIIFLGDLVRDGEPYSYGPPIED------PQREPAQPA------FIFYTSGTTGLPKAAIIPQ 175
Cdd:cd05915 103 -------DPNLLPLVEAIRGELKTVQHFVVMDEKAPEGYLayeealGEEADPVRVperaacGMAYTTGTTGLPKGVVYSH 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 176 RAAESRVLFMSTQVGLRHGRHNVVLGLMPLYHVVGFFAVLVAAlALDGTYVVVEEFRPVDAL-QLVQQEQVTSLFATPTH 254
Cdd:cd05915 176 RALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAAT-LVGAKQVLPGPRLDPASLvELFDGEGVTFTAGVPTV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 255 LDALAAAAAHAGSSLKLDSlrHVTFAGATMPDAVLETvhQHLPGEKVNI-YGTTEAMN----SLYMRQPKTGTEMAP--- 326
Cdd:cd05915 255 WLALADYLESTGHRLKTLR--RLVVGGSAAPRSLIAR--FERMGVEVRQgYGLTETSPvvvqNFVKSHLESLSEEEKltl 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 327 ------GFFSEVRIVrIGGGVDEIVANGEEGELIVAASDSAFVGYLNQPQAT-AEKLQDGWYRTSDVAVWTPEGTVRILG 399
Cdd:cd05915 331 kaktglPIPLVRLRV-ADEEGRPVPKDGKALGEVQLKGPWITGGYYGNEEATrSALTPDGFFRTGDIAVWDEEGYVEIKD 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 400 RVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDtFCRsSELADFKR-PKR 478
Cdd:cd05915 410 RLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTPEELNE-HLL-KAGFAKWQlPDA 487
|
490 500
....*....|....*....|
1T5D_X 479 YFILDQLPKNALNKVLRRQL 498
Cdd:cd05915 488 YVFAEEIPRTSAGKFLKRAL 507
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
26-434 |
1.48e-17 |
|
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: 85.42 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 26 RGLRLTHAELRARVEAVAARLHAD-GLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAE--------- 95
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHcfrccgakv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 96 LIKRGEMTAAVIAVG---RQVADAIFQSGSGAR---IIFLGDLVRDGepySYGPPIEDPQREPA--QPAFIFYTSGTTGL 167
Cdd:cd05938 82 LVVAPELQEAVEEVLpalRADGVSVWYLSHTSNtegVISLLDKVDAA---SDEPVPASLRAHVTikSPALYIYTSGTTGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 168 PKAAIIPQRaaesRVLFMSTQVGLRHGR-HNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFrpvDALQL---VQQE 243
Cdd:cd05938 159 PKAARISHL----RVLQCSGFLSLCGVTaDDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKF---SASQFwddCRKH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 244 QVT----------SLFATP-THLDALAAAAAHAGSSLKLDSLRhvTFAGATMPDAVLETvhqhlpgekvniYGTTEA--- 309
Cdd:cd05938 232 NVTviqyigellrYLCNQPqSPNDRDHKVRLAIGNGLRADVWR--EFLRRFGPIRIREF------------YGSTEGnig 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 310 -MNslYmrqpkTGTEMAPG--------FFSEVRI---------VRIGGGVDEIVANGEEGeLIVA--ASDSAFVGYLNQP 369
Cdd:cd05938 298 fFN--Y-----TGKIGAVGrvsylyklLFPFELIkfdvekeepVRDAQGFCIPVAKGEPG-LLVAkiTQQSPFLGYAGDK 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1T5D_X 370 QATAEKL-------QDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIG 434
Cdd:cd05938 370 EQTEKKLlrdvfkkGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYG 441
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
14-461 |
1.93e-17 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 85.23 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 14 RAPDHcaLAVPARG-----LRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAV-------- 80
Cdd:PRK03584 96 RRDDR--PAIIFRGedgprRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIwsscspdf 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 81 --PALL------NPRL---------------KSAELAELIKRGEMTAAVIAVGRQVADAIFqsGSGARIIFLGDLVRDGE 137
Cdd:PRK03584 174 gvQGVLdrfgqiEPKVliavdgyryggkafdRRAKVAELRAALPSLEHVVVVPYLGPAAAA--AALPGALLWEDFLAPAE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 138 PysygPPIEDPQREPAQPAFIFYTSGTTGLPKAaiIPQRA------------------AESRVLFMSTqvglrhgrhnvv 199
Cdd:PRK03584 252 A----AELEFEPVPFDHPLWILYSSGTTGLPKC--IVHGHggillehlkelglhcdlgPGDRFFWYTT------------ 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 200 LGLMplyhvvgFFAVLVAALALDGTYVVVE--EFRP-VDAL-QLVQQEQVTSLFATPTHLDALAAAAAHAGSSLKLDSLR 275
Cdd:PRK03584 314 CGWM-------MWNWLVSGLLVGATLVLYDgsPFYPdPNVLwDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALR 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 276 HVTFAGATMPDAVLETVHQHLpGEKV---NIYGtteamnslymrqpktGTEMAPGFFSEVRI--VRIGG------GVDEI 344
Cdd:PRK03584 387 TIGSTGSPLPPEGFDWVYEHV-KADVwlaSISG---------------GTDICSCFVGGNPLlpVYRGEiqcrglGMAVE 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 345 VAN-------GEEGELIVAASDSAF-VGYLNQPqataeklqDG-WYRTS------------DVAVWTPEGTVRILGRVDD 403
Cdd:PRK03584 451 AWDedgrpvvGEVGELVCTKPFPSMpLGFWNDP--------DGsRYRDAyfdtfpgvwrhgDWIEITEHGGVVIYGRSDA 522
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
1T5D_X 404 MIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSaDAL 461
Cdd:PRK03584 523 TLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLD-DAL 579
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
24-498 |
2.22e-17 |
|
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: 84.92 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 24 PARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAV---------PALLNPRLKSAELA 94
Cdd:cd05966 79 PDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVhsvvfagfsAESLADRINDAQCK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 95 ELI-----KRGEMT--------AA---------VIAVGRQVADAIFQSGsgaRIIFLGDLVRDGEPYSYGPPI--EDPqr 150
Cdd:cd05966 159 LVItadggYRGGKViplkeivdEAlekcpsvekVLVVKRTGGEVPMTEG---RDLWWHDLMAKQSPECEPEWMdsEDP-- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 151 epaqpAFIFYTSGTTGLPK------AAIIPQRAAESR---------VLFMSTQVGLRHGRHNVVLGlmPLyhvvgffavl 215
Cdd:cd05966 234 -----LFILYTSGSTGKPKgvvhttGGYLLYAATTFKyvfdyhpddIYWCTADIGWITGHSYIVYG--PL---------- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 216 vaalaLDGTYVVVEEFRPV--DA---LQLVQQEQVTSLFATPTHLDALAAAAAHAGSSLKLDSLRhvtfagatmpdaVLE 290
Cdd:cd05966 297 -----ANGATTVMFEGTPTypDPgryWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLR------------VLG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 291 TV------------HQHLPGEKVNIYGT---TE---AMNSlymrqPKTG-TEMAPG-----FFS-EVRIVRIGGGVdeiV 345
Cdd:cd05966 360 SVgepinpeawmwyYEVIGKERCPIVDTwwqTEtggIMIT-----PLPGaTPLKPGsatrpFFGiEPAILDEEGNE---V 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 346 ANGEEGELIVAAS-DSAFVGYLNQPQA---TAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVL 421
Cdd:cd05966 432 EGEVEGYLVIKRPwPGMARTIYGDHERyedTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESAL 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 422 GTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSaDALDT---FCRSSELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:cd05966 512 VAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPS-DELRKelrKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRIL 590
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
21-498 |
7.29e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 84.45 E-value: 7.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 21 LAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIKRG 100
Cdd:PRK05691 3737 IAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELS 3816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 101 EM-----TAAVIAVGRQVADAIfqSGSGARIIFLGDLVRDGEPYSYGPPIEDpqrEPAQPAFIFYTSGTTGLPKAAIIPQ 175
Cdd:PRK05691 3817 RTpvlvcSAACREQARALLDEL--GCANRPRLLVWEEVQAGEVASHNPGIYS---GPDNLAYVIYTSGSTGLPKGVMVEQ 3891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 176 RAAESRVLFMSTQVGLrhGRHNVVLGLMPLYHVVGFFAVLVAALaLDGTYVVVEE---FRPVDALQLVQQEQVTSLFATP 252
Cdd:PRK05691 3892 RGMLNNQLSKVPYLAL--SEADVIAQTASQSFDISVWQFLAAPL-FGARVEIVPNaiaHDPQGLLAHVQAQGITVLESVP 3968
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 253 THLDALAAAAAHAgsslkLDSLRHVTFAGATMPDAVLETVHQHLPGEK-VNIYGTTEAMNSL-YMR---QPKTGTEMAPG 327
Cdd:PRK05691 3969 SLIQGMLAEDRQA-----LDGLRWMLPTGEAMPPELARQWLQRYPQIGlVNAYGPAECSDDVaFFRvdlASTRGSYLPIG 4043
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 328 FFSEVRIVRIGGGVDEIVANGEEGELIVAASDSAfVGYLNQPQATA------------EKLqdgwYRTSDVAVWTPEGTV 395
Cdd:PRK05691 4044 SPTDNNRLYLLDEALELVPLGAVGELCVAGTGVG-RGYVGDPLRTAlafvphpfgapgERL----YRTGDLARRRSDGVL 4118
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 396 RILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVViGLADQRWGQSVTACVVPRLGETLSADALDTFCR--SSELADF 473
Cdd:PRK05691 4119 EYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAV-AVQEGVNGKHLVGYLVPHQTVLAQGALLERIKQrlRAELPDY 4197
|
490 500
....*....|....*....|....*
1T5D_X 474 KRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:PRK05691 4198 MVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
30-450 |
5.66e-16 |
|
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: 80.34 E-value: 5.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 30 LTHAELRARVEAVAARLHADGLR--PQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIKRGEMTAAVI 107
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 108 AvgrqvadaifqsgSGARIIFLGDLVRDGEPYsygpPIEDPQREPAQPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMST 187
Cdd:cd05927 86 D-------------AGVKVYSLEEFEKLGKKN----KVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 188 QVGlRHGRHN---VVLGLMPLYHV---------------VGFFAVLVAAL-----ALDGTYVVVEE---FRPVDALQLVQ 241
Cdd:cd05927 149 ILE-ILNKINptdVYISYLPLAHIfervvealflyhgakIGFYSGDIRLLlddikALKPTVFPGVPrvlNRIYDKIFNKV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 242 QEQVT---SLFATPTHLDALAAAAAHAGSSLKLDSL-------------RHVTFAGATMPDAVLETVHQHLPGEKVNIYG 305
Cdd:cd05927 228 QAKGPlkrKLFNFALNYKLAELRSGVVRASPFWDKLvfnkikqalggnvRLMLTGSAPLSPEVLEFLRVALGCPVLEGYG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 306 TTE--AMNSL-YMRQPKTGTEMAPGFFSEVRIVriggGVDEI--VANGE--EGELIVAASdSAFVGYLNQPQATAEKL-Q 377
Cdd:cd05927 308 QTEctAGATLtLPGDTSVGHVGGPLPCAEVKLV----DVPEMnyDAKDPnpRGEVCIRGP-NVFSGYYKDPEKTAEALdE 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1T5D_X 378 DGWYRTSDVAVWTPEGTVRILGRVDDMI-ISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWgqsVTACVVP 450
Cdd:cd05927 383 DGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIENIYARSPFVAQIFVYGDSLKSF---LVAIVVP 453
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
150-498 |
6.14e-16 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 79.82 E-value: 6.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 150 REPAQPAFIFYTSGTTGLPKAAIIPQRA-----AESRVLFMSTQvglrhgrHNVVLGLMPLY---HVVGFF-AVLVAALA 220
Cdd:cd17654 115 RTDECLAYVIHTSGTTGTPKIVAVPHKCilpniQHFRSLFNITS-------EDILFLTSPLTfdpSVVEIFlSLSSGATL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 221 LDG-TYVVVEEFRPVDAlqLVQQEQVTSLFATPTHLDALAAAAAHAGSSLKLDSLRHVTFAGATMP-DAVLETVHQHLPG 298
Cdd:cd17654 188 LIVpTSVKVLPSKLADI--LFKRHRITVLQATPTLFRRFGSQSIKSTVLSATSSLRVLALGGEPFPsLVILSSWRGKGNR 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 299 EKV-NIYGTTEAMN-SLYMRQPKTGTEMAPGFFSEVRIVRigggVDEIVANGEEGELIVAASDSAFV--GYLNQPQATae 374
Cdd:cd17654 266 TRIfNIYGITEVSCwALAYKVPEEDSPVQLGSPLLGTVIE----VRDQNGSEGTGQVFLGGLNRVCIldDEVTVPKGT-- 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 375 klqdgWYRTSDVaVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIgLADQrwgQSVTACVVPRLGE 454
Cdd:cd17654 340 -----MRATGDF-VTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVT-LSDQ---QRLIAFIVGESSS 409
|
330 340 350 360
....*....|....*....|....*....|....*....|....
1T5D_X 455 TLSADALDTFCRSSEladfKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:cd17654 410 SRIHKELQLTLLSSH----AIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
12-502 |
9.69e-16 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 79.55 E-value: 9.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 12 ATRAPDhcALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGA--VP-ALLNPrl 88
Cdd:PRK04813 12 AQTQPD--FPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHayIPvDVSSP-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 89 ksAELAELIKRGEMTAAVIAVGRQVADAifqsgSGARIIFLGDLVRDGEPYsyGPPIEDPQREPAQPAFIFYTSGTTGLP 168
Cdd:PRK04813 88 --AERIEMIIEVAKPSLIIATEELPLEI-----LGIPVITLDELKDIFATG--NPYDFDHAVKGDDNYYIIFTSGTTGKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 169 KAAIIPQRAAESRVLFMSTQVGLrhGRHNVVLG---------LMPLYhvvgffavlvAALALDGTYVVVEE---FRPVDA 236
Cdd:PRK04813 159 KGVQISHDNLVSFTNWMLEDFAL--PEGPQFLNqapysfdlsVMDLY----------PTLASGGTLVALPKdmtANFKQL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 237 LQLVQQEQVTSLFATPTHLDALAAAAAHAGSslKLDSLRHVTFAGATMPDAVLETVHQHLPGEKV-NIYGTTEA------ 309
Cdd:PRK04813 227 FETLPQLPINVWVSTPSFADMCLLDPSFNEE--HLPNLTHFLFCGEELPHKTAKKLLERFPSATIyNTYGPTEAtvavts 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 310 ----------MNSLYMRQPKTGTEmapgffseVRIVRIGGgvdEIVANGEEGELIVAAsDSAFVGYLNQPQATAE--KLQ 377
Cdd:PRK04813 305 ieitdemldqYKRLPIGYAKPDSP--------LLIIDEEG---TKLPDGEQGEIVISG-PSVSKGYLNNPEKTAEafFTF 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 378 DGW--YRTSDVAVwTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGET 455
Cdd:PRK04813 373 DGQpaYHTGDAGY-LEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDF 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
1T5D_X 456 LSADALDTFCR---SSELADFKRPKRYFILDQLPKNALNKVLRRQLVQQV 502
Cdd:PRK04813 452 EREFELTKAIKkelKERLMEYMIPRKFIYRDSLPLTPNGKIDRKALIEEV 501
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
31-434 |
1.37e-15 |
|
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: 79.39 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 31 THAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIKRGEMTAAVIAVG 110
Cdd:cd17641 13 TWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAEDE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 111 RQVaDAIFQSGSG--------------------ARIIFLGDLVRDGEPYSYGPP----IEDPQREPAQPAFIFYTSGTTG 166
Cdd:cd17641 93 EQV-DKLLEIADRipsvryviycdprgmrkyddPRLISFEDVVALGRALDRRDPglyeREVAAGKGEDVAVLCTTSGTTG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 167 LPKAAIIPQRAaesrvlFMSTQVGLRH----GRHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEfrPVDALQLVQQ 242
Cdd:cd17641 172 KPKLAMLSHGN------FLGHCAAYLAadplGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIVNFPEE--PETMMEDLRE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 243 EQVTSLFATP--------------------------------THLDALAAAAAHAGSSLKLDS----------------- 273
Cdd:cd17641 244 IGPTFVLLPPrvwegiaadvrarmmdatpfkrfmfelgmklgLRALDRGKRGRPVSLWLRLASwladallfrplrdrlgf 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 274 --LRHVTFAGATM-PDavletVHQHLPGEKVNI---YGTTEaMNSLYMRQPK-------TGTEMaPGffSEVRIVriggg 340
Cdd:cd17641 324 srLRSAATGGAALgPD-----TFRFFHAIGVPLkqlYGQTE-LAGAYTVHRDgdvdpdtVGVPF-PG--TEVRID----- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 341 vdeivangEEGElIVAASDSAFVGYLNQPQATAE-KLQDGWYRTSDVAVWTPEGTVRILGRVDD-MIISGGENIHPSEIE 418
Cdd:cd17641 390 --------EVGE-ILVRSPGVFVGYYKNPEATAEdFDEDGWLHTGDAGYFKENGHLVVIDRAKDvGTTSDGTRFSPQFIE 460
|
490
....*....|....*.
1T5D_X 419 RVLGTAPGVTEVVVIG 434
Cdd:cd17641 461 NKLKFSPYIAEAVVLG 476
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
31-498 |
5.15e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 77.00 E-value: 5.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 31 THAELRARVEAVAARLH-ADglRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAelaelikrgemTAAVIAV 109
Cdd:PRK08308 10 SKSDFDLRLQRYEEMEQfQE--AAGNRFAVCLKDPFDIITLVFFLKEKGASVLPIHPDTPKE-----------AAIRMAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 110 GRQVADAIFQSGSgariIFLGDLvrdgEPYSYGPPiedpqrepaqpAFIFYTSGTTGLPK------AAIipQRAAESRVL 183
Cdd:PRK08308 77 RAGCHGLLYGESD----FTKLEA----VNYLAEEP-----------SLLQYSSGTTGEPKlirrswTEI--DREIEAYNE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 184 FMSTQVGLrhgrhnVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFRPVDALQLVQQEQVTSLFATPTHLDALaaaaa 263
Cdd:PRK08308 136 ALNCEQDE------TPIVACPVTHSYGLICGVLAALTRGSKPVIITNKNPKFALNILRNTPQHILYAVPLMLHIL----- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 264 haGSSLKLDSLRH-VTFAGATMPDAVLETVH---QHLpgekVNIYGTTEAMNSLYMRQPKTGTEM-APgffseVRIVRIG 338
Cdd:PRK08308 205 --GRLLPGTFQFHaVMTSGTPLPEAWFYKLRertTYM----MQQYGCSEAGCVSICPDMKSHLDLgNP-----LPHVSVS 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 339 GGVDEivanGEEGELIVAASDSAFvgylnqpqataeklqdgwyRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIE 418
Cdd:PRK08308 274 AGSDE----NAPEEIVVKMGDKEI-------------------FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVE 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 419 RVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRlgETLSADALDTFCRsSELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:PRK08308 331 DVMLRLPGVQEAVVYRGKDPVAGERVKAKVISH--EEIDPVQLREWCI-QHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
416-492 |
7.21e-15 |
|
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: 69.50 E-value: 7.21e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1T5D_X 416 EIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCRsSELADFKRPKRYFILDQLPKNALNK 492
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVR-EELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
8-437 |
2.31e-13 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 72.11 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 8 LRRAATRAPDHCALAVPARGLRLTH--AELRARVEAVAARLHADGlrPQQRVAVVAPNSADVVIAIL-ALHRLGAVPALL 84
Cdd:PRK05851 8 LSDAMTASGRDLVVLDRESGLWRRHpwPEVHGRAENVAARLLDRD--RPGAVGLVGEPTVELVAAIQgAWLAGAAVSILP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 85 NPRlksaelaelikRGemtaaviAVGRQVADAIFQ--SGSGARIIF-LGDLVRDGEPYSYGPPIED-------------P 148
Cdd:PRK05851 86 GPV-----------RG-------ADDGRWADATLTrfAGIGVRTVLsHGSHLERLRAVDSSVTVHDlataahtnrsaslT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 149 QREPAQPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGLRHGrHNVVLGLMPLYHVVGFFAVLVAALALDGTYVV- 227
Cdd:PRK05851 148 PPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAA-TDVGCSWLPLYHDMGLAFLLTAALAGAPLWLAp 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 228 -----VEEFRPVDALQlvqqEQVTSLFATPTHLDALAAAAAHAGSSLKLDSLRHVTFAGATMPDAVLETVHQHL------ 296
Cdd:PRK05851 227 ttafsASPFRWLSWLS----DSRATLTAAPNFAYNLIGKYARRVSDVDLGALRVALNGGEPVDCDGFERFATAMapfgfd 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 297 PGEKVNIYGTTEAMNSLYMRQPKTGTEMA--------------------PGFfsEVRIVRIGGGVDeiVANGEEGELIVA 356
Cdd:PRK05851 303 AGAAAPSYGLAESTCAVTVPVPGIGLRVDevttddgsgarrhavlgnpiPGM--EVRISPGDGAAG--VAGREIGEIEIR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 357 ASdSAFVGYLNQPQATAeklqDGWYRTSDVAVWTPEGTVrILGRVDDMIISGGENIHPSEIERVLGTAPGVTE--VVVIG 434
Cdd:PRK05851 379 GA-SMMSGYLGQAPIDP----DDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVREgaVVAVG 452
|
...
1T5D_X 435 LAD 437
Cdd:PRK05851 453 TGE 455
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
30-450 |
1.65e-12 |
|
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: 69.55 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 30 LTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLksaelaelikrGEmtaaviav 109
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATL-----------GE-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 110 grqvaDAIFQS--GSGARIIFLgdlvrDGEPysygppiEDPqrepaqpAFIFYTSGTTGLPKAAIIPQRAAESRVLFMST 187
Cdd:cd17639 67 -----DALIHSlnETECSAIFT-----DGKP-------DDL-------ACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 188 QVGLRHGRHNVVLGLMPLYHVVGFFAVLVAALA------------LDGTYVV----VEEFRP------------------ 233
Cdd:cd17639 123 RVPELLGPDDRYLAYLPLAHIFELAAENVCLYRggtigygsprtlTDKSKRGckgdLTEFKPtlmvgvpaiwdtirkgvl 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 234 --VDALQLVQQeqvtSLFATpthldalaaaaahaGSSLKLDSLRHvtfaGATMP---DAVLETVHQHLPG---------- 298
Cdd:cd17639 203 akLNPMGGLKR----TLFWT--------------AYQSKLKALKE----GPGTPlldELVFKKVRAALGGrlrymlsgga 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 299 -------EKVNI--------YGTTE---AMNSLYMRQPKTGTEMAPGFFSEVRIVRIGGGVDEIVANGEEGELIVAASdS 360
Cdd:cd17639 261 plsadtqEFLNIvlcpviqgYGLTEtcaGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDKPPPRGEILIRGP-N 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 361 AFVGYLNQPQATAEKL-QDGWYRTSDVAVWTPEGTVRILGRVDDMI-ISGGENIHPSEIERVLGTAPGVTEVVVigLADQ 438
Cdd:cd17639 340 VFKGYYKNPEKTKEAFdGDGWFHTGDIGEFHPDGTLKIIDRKKDLVkLQNGEYIALEKLESIYRSNPLVNNICV--YADP 417
|
490
....*....|..
1T5D_X 439 RwGQSVTACVVP 450
Cdd:cd17639 418 D-KSYPVAIVVP 428
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
31-496 |
3.71e-12 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 68.69 E-value: 3.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 31 THAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILAL--HRLGAVP--------------------------- 81
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACaaHSLICVPlydtlgpgavdyivdhaeidfvfvqdk 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 82 ---ALLNPRLKSAelaeliKRGEMTAAVIAVGRQVADAIFQSGSgariiflgdlvrdgEPYSYGPPIEDPQREPAQP--- 155
Cdd:PLN02430 158 kikELLEPDCKSA------KRLKAIVSFTSVTEEESDKASQIGV--------------KTYSWIDFLHMGKENPSETnpp 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 156 -----AFIFYTSGTTGLPKAAIIPQRAAESRV----LFMStQVGLRHGRHNVVLGLMPLYHV---------------VGF 211
Cdd:PLN02430 218 kpldiCTIMYTSGTSGDPKGVVLTHEAVATFVrgvdLFME-QFEDKMTHDDVYLSFLPLAHIldrmieeyffrkgasVGY 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 212 FAVLVAAL-----ALDGTYVV----------------VEEFRPV-----DAL---QLVQQEQ-VTSLFATPTHLDAL-AA 260
Cdd:PLN02430 297 YHGDLNALrddlmELKPTLLAgvprvferihegiqkaLQELNPRrrlifNALykyKLAWMNRgYSHKKASPMADFLAfRK 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 261 AAAHAGSSLKLdslrhVTFAGATMPDAVLETVHQHLPGEKVNIYGTTEAMNSLYMRQPK----TGTEMAPGFFSEVRIVR 336
Cdd:PLN02430 377 VKAKLGGRLRL-----LISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDemcmLGTVGAPAVYNELRLEE 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 337 IGGGVDEIVANGEEGELIVAASdSAFVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMI-ISGGENIHPS 415
Cdd:PLN02430 452 VPEMGYDPLGEPPRGEICVRGK-CLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALE 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 416 EIERVLGTAPGVTEVVVIGladQRWGQSVTACVVPRLGETLSADALDTFCRS-SELADFKRPKRYfILDQLPKNALNKVL 494
Cdd:PLN02430 531 YLENVYGQNPIVEDIWVYG---DSFKSMLVAVVVPNEENTNKWAKDNGFTGSfEELCSLPELKEH-ILSELKSTAEKNKL 606
|
..
1T5D_X 495 RR 496
Cdd:PLN02430 607 RG 608
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
3-435 |
3.87e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 68.53 E-value: 3.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 3 TVNEMLRRAATRAPDHCALA---VPARGLR-LTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLG 78
Cdd:PRK12582 50 SIPHLLAKWAAEAPDRPWLAqrePGHGQWRkVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 79 aVPA----------------------LLNPRLKSAELAELIKRGEMTAAVIAVGRQVADAifqSGSGARIIFLGDLVRdg 136
Cdd:PRK12582 130 -VPAapvspayslmshdhaklkhlfdLVKPRVVFAQSGAPFARALAALDLLDVTVVHVTG---PGEGIASIAFADLAA-- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 137 epysyGPPIED-----PQREPAQPAFIFYTSGTTGLPKAAIIPQRA-AESRVLFMSTQVGLRHGRHNVVLGLMPLYHVVG 210
Cdd:PRK12582 204 -----TPPTAAvaaaiAAITPDTVAKYLFTSGSTGMPKAVINTQRMmCANIAMQEQLRPREPDPPPPVSLDWMPWNHTMG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 211 FFAVLVAALALDGTYvVVEEFRPVDALqlvQQEQVTSLF-ATPTHLDALAAAAAHAGSSLKLD---------SLRHVTFA 280
Cdd:PRK12582 279 GNANFNGLLWGGGTL-YIDDGKPLPGM---FEETIRNLReISPTVYGNVPAGYAMLAEAMEKDdalrrsffkNLRLMAYG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 281 GATMPDAVLETVHQH---LPGEKVNI---YGTTEAmnslymrQP-KTGTEMAPGffsevRIVRIG---GGVD-EIVANGE 349
Cdd:PRK12582 355 GATLSDDLYERMQALavrTTGHRIPFytgYGATET-------APtTTGTHWDTE-----RVGLIGlplPGVElKLAPVGD 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 350 EGELIVAAsDSAFVGYLNQPQATAEKL-QDGWYRTSDVAVWT----PEGTVRILGRV-DDMIISGGENIHPSE--IERVL 421
Cdd:PRK12582 423 KYEVRVKG-PNVTPGYHKDPELTAAAFdEEGFYRLGDAARFVdpddPEKGLIFDGRVaEDFKLSTGTWVSVGTlrPDAVA 501
|
490
....*....|....
1T5D_X 422 GTAPGVTEVVVIGL 435
Cdd:PRK12582 502 ACSPVIHDAVVAGQ 515
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
8-452 |
5.36e-12 |
|
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: 68.23 E-value: 5.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 8 LRRAATRAPDHCALAV--PARGLR-LTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALL 84
Cdd:cd05921 1 LAHWARQAPDRTWLAEreGNGGWRrVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 85 NPR--LKSAELA------ELIKRGEMTAAVIAVGRQVADAIFQSGSgaRIIFLGDLVRDGEPYSYGPPIEDPQREPAQPA 156
Cdd:cd05921 81 SPAysLMSQDLAklkhlfELLKPGLVFAQDAAPFARALAAIFPLGT--PLVVSRNAVAGRGAISFAELAATPPTAAVDAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 157 F----------IFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGLRHGRHNVVLGLMPLYHVVGFFAVLVAALALDGTYv 226
Cdd:cd05921 159 FaavgpdtvakFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPPVLVDWLPWNHTFGGNHNFNLVLYNGGTL- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 227 VVEEFRPVDAL--QLVQ--QEQVTSLFATPTHLDALAAAAAHAGSSLK---LDSLRHVTFAGATMPDAVLETVHQ---HL 296
Cdd:cd05921 238 YIDDGKPMPGGfeETLRnlREISPTVYFNVPAGWEMLVAALEKDEALRrrfFKRLKLMFYAGAGLSQDVWDRLQAlavAT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 297 PGEKVNI---YGTTE-AMNSLYMRQPKTGTEM----APGffSEVRIVRIGGGVdEIVANGEEgeliVAAsdsafvGYLNQ 368
Cdd:cd05921 318 VGERIPMmagLGATEtAPTATFTHWPTERSGLiglpAPG--TELKLVPSGGKY-EVRVKGPN----VTP------GYWRQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 369 PQATAEKL-QDGWYRTSDVAVWT-PEGTVRIL---GRV-DDMIISGGENIH--PSEIERVLGTAPGVTEVVVIGLAdqrw 440
Cdd:cd05921 385 PELTAQAFdEEGFYCLGDAAKLAdPDDPAKGLvfdGRVaEDFKLASGTWVSvgPLRARAVAACAPLVHDAVVAGED---- 460
|
490
....*....|..
1T5D_X 441 GQSVTACVVPRL 452
Cdd:cd05921 461 RAEVGALVFPDL 472
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
158-428 |
9.80e-12 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 66.71 E-value: 9.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 158 IFYTSGTTGLPKaaIIP------QRAAE--SRVLFMStqvGLRHGrhNVVLgLMPLYHV-VGFFAVLVAALALdGTYVVV 228
Cdd:COG1541 88 IHASSGTTGKPT--VVGytrkdlDRWAElfARSLRAA---GVRPG--DRVQ-NAFGYGLfTGGLGLHYGAERL-GATVIP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 229 ------EEfrpvdALQLVQQEQVTSLFATPTHLDALAAAAAHAGSSLKLDSLRHVTFAGATMPDAVLETVHQHLPGEKVN 302
Cdd:COG1541 159 agggntER-----QLRLMQDFGPTVLVGTPSYLLYLAEVAEEEGIDPRDLSLKKGIFGGEPWSEEMRKEIEERWGIKAYD 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 303 IYGTTEamnslymrqpktgteMAPGFFSE---------------VRIVRIGGGvdEIVANGEEGELIVaasdsafvgyln 367
Cdd:COG1541 234 IYGLTE---------------VGPGVAYEceaqdglhiwedhflVEIIDPETG--EPVPEGEEGELVV------------ 284
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1T5D_X 368 qpqaTAekLQDGW-----YRTSDVAVWTPE----GT-----VRILGRVDDMIISGGENIHPSEIERVLGTAPGVT 428
Cdd:COG1541 285 ----TT--LTKEAmplirYRTGDLTRLLPEpcpcGRthpriGRILGRADDMLIIRGVNVFPSQIEEVLLRIPEVG 353
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
124-428 |
2.23e-11 |
|
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: 65.72 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 124 ARIIFL--GDLvRDGEPYsygPPIEDPQRepaQPAFIFYTSGTTGLPKAAIIPQR------AAESRVLFMSTqvglrhGR 195
Cdd:cd05913 54 RKLPFTtkEDL-RDNYPF---GLFAVPRE---KVVRIHASSGTTGKPTVVGYTKNdldvwaELVARCLDAAG------VT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 196 HNVVLGLMPLYHV-VGFFAVLVAALALdGTYVVveefrPVDA------LQLVQQEQVTSLFATPTHLDALAAAAAHAGSS 268
Cdd:cd05913 121 PGDRVQNAYGYGLfTGGLGFHYGAERL-GALVI-----PAGGgnterqLQLIKDFGPTVLCCTPSYALYLAEEAEEEGID 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 269 LKLDSLRHVTFAGATMPDAVLETVHQHLPGEKVNIYGTTEAMNslymrqPKTGTEMA----PGFFSEVRIVRIgggVD-- 342
Cdd:cd05913 195 PRELSLKVGIFGAEPWTEEMRKRIERRLGIKAYDIYGLTEIIG------PGVAFECEekdgLHIWEDHFIPEI---IDpe 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 343 --EIVANGEEGELIVAAsdsafvgylnqpqATAEKLQDGWYRTSDVAVWTPE----GTV-----RILGRVDDMIISGGEN 411
Cdd:cd05913 266 tgEPVPPGEVGELVFTT-------------LTKEAMPLIRYRTRDITRLLPGpcpcGRThrridRITGRSDDMLIIRGVN 332
|
330
....*....|....*..
1T5D_X 412 IHPSEIERVLGTAPGVT 428
Cdd:cd05913 333 VFPSQIEDVLLKIPGLG 349
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
145-439 |
4.97e-11 |
|
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: 65.07 E-value: 4.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 145 IEDPQRePAQPAFIFYTSGTTGLPKAAIIPQ-------RAAESRVLFMSTQVGlrhgrHNVVLGLMPLYHVVG-----FF 212
Cdd:cd05933 143 IISSQK-PNQCCTLIYTSGTTGMPKGVMLSHdnitwtaKAASQHMDLRPATVG-----QESVVSYLPLSHIAAqildiWL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 213 AVLVAAL-------ALDGTYV-VVEEFRPVDALQLVQ-----QEQVTSLFATPTH-----------LDALAAAAAHAGSS 268
Cdd:cd05933 217 PIKVGGQvyfaqpdALKGTLVkTLREVRPTAFMGVPRvwekiQEKMKAVGAKSGTlkrkiaswakgVGLETNLKLMGGES 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 269 --------------------LKLDSLRHVTFAGATMPDavlETVHQHLpgeKVNI-----YGTTEAMNSLYMRQPKTgte 323
Cdd:cd05933 297 psplfyrlakklvfkkvrkaLGLDRCQKFFTGAAPISR---ETLEFFL---SLNIpimelYGMSETSGPHTISNPQA--- 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 324 mapgffseVRIVRIGGGV-------DEIVANGEeGELIVAASdSAFVGYLNQPQATAEKL-QDGWYRTSDVAVWTPEGTV 395
Cdd:cd05933 368 --------YRLLSCGKALpgcktkiHNPDADGI-GEICFWGR-HVFMGYLNMEDKTEEAIdEDGWLHSGDLGKLDEDGFL 437
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
1T5D_X 396 RILGRVDDMII-SGGENIHPSEIERVLGTA-PGVTEVVVIGlaDQR 439
Cdd:cd05933 438 YITGRIKELIItAGGENVPPVPIEDAVKKElPIISNAMLIG--DKR 481
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
2-421 |
2.29e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 63.65 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 2 QTVNEMLRRAATRAPDHCALAV----PARGLRLTHAELRARVEAVAARLHADGlRPQQRVAVVAPNSADVVIAILALHRL 77
Cdd:PRK05691 9 LTLVQALQRRAAQTPDRLALRFladdPGEGVVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 78 G--AVPAL---LNPRLKSAELAELIKRGEmtAAVIAVGRQVADAIFQSGSGARIIFLGDLVRDGEPYSYGPPIEDPQREP 152
Cdd:PRK05691 88 GviAVPAYppeSARRHHQERLLSIIADAE--PRLLLTVADLRDSLLQMEELAAANAPELLCVDTLDPALAEAWQEPALQP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 153 AQPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGLRHGRHNVVLGLMPLYHVVGFFAVLVAALaLDGTYVVVEE-- 230
Cdd:PRK05691 166 DDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPDDVIVSWLPLYHDMGLIGGLLQPI-FSGVPCVLMSpa 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 231 ---FRPVDALQLVQQEQVTsLFATPTHLDALAAAAAHAGSSLKLD-SLRHVTFAGAT-MPDAVLETVHQHL------PGE 299
Cdd:PRK05691 245 yflERPLRWLEAISEYGGT-ISGGPDFAYRLCSERVSESALERLDlSRWRVAYSGSEpIRQDSLERFAEKFaacgfdPDS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 300 KVNIYGTTEAmnSLYMRQPKTGTEMA---------------PGFFS------------EVRIVRIGGGvdEIVANGEEGE 352
Cdd:PRK05691 324 FFASYGLAEA--TLFVSGGRRGQGIPaleldaealarnraePGTGSvlmscgrsqpghAVLIVDPQSL--EVLGDNRVGE 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1T5D_X 353 lIVAASDSAFVGYLNQPQATAEKL--QDG--WYRTSDVAvWTPEGTVRILGRVDDMIISGGENIHPSEIERVL 421
Cdd:PRK05691 400 -IWASGPSIAHGYWRNPEASAKTFveHDGrtWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTV 470
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
30-457 |
4.43e-10 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 61.76 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 30 LTHAELRARVEAVAARLHAdglRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIKRGEMTAAVIAv 109
Cdd:PRK06334 46 LSYNQVRKAVIALATKVSK---YPDQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTS- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 110 gRQVADAIFQS-GSG----ARIIFLGDL---------VRDG----EPYSYGPPIED-PQREPAQPAFIFYTSGTTGLPKA 170
Cdd:PRK06334 122 -KQLMQHLAQThGEDaeypFSLIYMEEVrkelsfwekCRIGiymsIPFEWLMRWFGvSDKDPEDVAVILFTSGTEKLPKG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 171 A-------IIPQRAAesrVLFMSTQvglrhgRHNVVLGLMPLYHVVGFFAVLVAALaLDGTYVVV--EEFRPVDALQLVQ 241
Cdd:PRK06334 201 VplthanlLANQRAC---LKFFSPK------EDDVMMSFLPPFHAYGFNSCTLFPL-LSGVPVVFayNPLYPKKIVEMID 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 242 QEQVTSLFATPTHLDALAAAAAHAGSSlkLDSLRHVTFAGATMPDAVLETVHQHLPGEKVNI-YGTTE-----AMNSlyM 315
Cdd:PRK06334 271 EAKVTFLGSTPVFFDYILKTAKKQESC--LPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQgYGTTEcspviTINT--V 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 316 RQPKTGTEMA-PGFFSEVRIVRIGGGVDeiVANGEEGeLIVAASDSAFVGYL-NQP-QATAEKLQDGWYRTSDVAVWTPE 392
Cdd:PRK06334 347 NSPKHESCVGmPIRGMDVLIVSEETKVP--VSSGETG-LVLTRGTSLFSGYLgEDFgQGFVELGGETWYVTGDLGYVDRH 423
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1T5D_X 393 GTVRILGRVDDMIISGGENIHPSEIERVL------GTAPGVTEVVVIGLAdqrwGQSVTACVVPRLGETLS 457
Cdd:PRK06334 424 GELFLKGRLSRFVKIGAEMVSLEALESILmegfgqNAADHAGPLVVCGLP----GEKVRLCLFTTFPTSIS 490
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
30-219 |
1.26e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 60.51 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 30 LTHAELRARVEAVAARLHADGlRPQQRVAVVAPNSADVVIAILALHRLG--AVPaLLNP-------RLKsAELAELIKRG 100
Cdd:PRK07769 56 LTWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLIAFFGALYAGriAVP-LFDPaepghvgRLH-AVLDDCTPSA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 101 EMTAAVIAVGrqvADAIFQSGSGA---RIIFLgDLVRDGEPYSYGPPieDPQREPAqpAFIFYTSGTTGLPKAAIIPQRA 177
Cdd:PRK07769 133 ILTTTDSAEG---VRKFFRARPAKerpRVIAV-DAVPDEVGATWVPP--EANEDTI--AYLQYTSGSTRIPAGVQITHLN 204
|
170 180 190 200
....*....|....*....|....*....|....*....|..
1T5D_X 178 AESRVLFMSTQVGLRHGRHNVvlGLMPLYHVVGFFAVLVAAL 219
Cdd:PRK07769 205 LPTNVLQVIDALEGQEGDRGV--SWLPFFHDMGLITVLLPAL 244
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
304-495 |
1.29e-09 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 60.63 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 304 YGTTEA----MNSLYMRQPKTGTEMAPGFFSEVRIVRIGGGVDEIVANGEEGElIVAASDSAFVGYLNQPQATAEKLQDG 379
Cdd:PLN02861 415 YGLTEScggcFTSIANVFSMVGTVGVPMTTIEARLESVPEMGYDALSDVPRGE-ICLRGNTLFSGYHKRQDLTEEVLIDG 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 380 WYRTSDVAVWTPEGTVRILGRVDDMI-ISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWgqsVTACVVPrlgetlSA 458
Cdd:PLN02861 494 WFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESF---LVAVVVP------DR 564
|
170 180 190 200
....*....|....*....|....*....|....*....|...
1T5D_X 459 DALDTFCRSSELA-DFKR----PK-RYFILDQLPKNALNKVLR 495
Cdd:PLN02861 565 QALEDWAANNNKTgDFKSlcknLKaRKYILDELNSTGKKLQLR 607
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
2-435 |
1.83e-09 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 59.89 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 2 QTVNEMLRRAATRAPDHCALAvpARG-----LRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSAD-VVIAILALH 75
Cdd:PRK08180 39 RRLTDRLVHWAQEAPDRVFLA--ERGadggwRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEhALLALAAMY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 76 rLGAVPALLNP--RLKSAELAELikR---GEMTAAVIAV--GRQVADAIFQSG-SGARIIFLGDLVRDGEPYSYGPPIED 147
Cdd:PRK08180 117 -AGVPYAPVSPaySLVSQDFGKL--RhvlELLTPGLVFAddGAAFARALAAVVpADVEVVAVRGAVPGRAATPFAALLAT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 148 PQREPAQPAF----------IFYTSGTTGLPKAAIIPQRaaesrvlfM--STQVGLR------HGRHNVVLGLMPLYHVV 209
Cdd:PRK08180 194 PPTAAVDAAHaavgpdtiakFLFTSGSTGLPKAVINTHR--------MlcANQQMLAqtfpflAEEPPVLVDWLPWNHTF 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 210 GFFAVLVAALALDGTYVVvEEFRPVDA-----LQLVQQEQVTSLFATPTHLDALAAAaahagssLKLDS---------LR 275
Cdd:PRK08180 266 GGNHNLGIVLYNGGTLYI-DDGKPTPGgfdetLRNLREISPTVYFNVPKGWEMLVPA-------LERDAalrrrffsrLK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 276 HVTFAGATMPDAVLETVH----QHLpGEKVNI---YGTTEAMNS-LYMRQPKTGTEM----APGffSEVRIVRIGGGVdE 343
Cdd:PRK08180 338 LLFYAGAALSQDVWDRLDrvaeATC-GERIRMmtgLGMTETAPSaTFTTGPLSRAGNiglpAPG--CEVKLVPVGGKL-E 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 344 IVANGeegelivaasDSAFVGYLNQPQATAEKL-QDGWYRTSDVAVWT----PEGTVRILGRV-DDMIISGGE--NIHPS 415
Cdd:PRK08180 414 VRVKG----------PNVTPGYWRAPELTAEAFdEEGYYRSGDAVRFVdpadPERGLMFDGRIaEDFKLSSGTwvSVGPL 483
|
490 500
....*....|....*....|
1T5D_X 416 EIERVLGTAPGVTEVVVIGL 435
Cdd:PRK08180 484 RARAVSAGAPLVQDVVITGH 503
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
362-401 |
1.02e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 57.68 E-value: 1.02e-08
10 20 30 40
....*....|....*....|....*....|....*....|.
1T5D_X 362 FVGYLNQPQATAEKL-QDGWYRTSDVAVWTPEGTVRILGRV 401
Cdd:PTZ00216 518 FKGYYKQEELTREVLdEDGWFHTGDVGSIAANGTLRIIGRV 558
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
24-498 |
1.27e-08 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 57.60 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 24 PARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIK--RGE 101
Cdd:PLN02654 115 PGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVdcKPK 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 102 MTAAVIAVGRqvadaifqsgsGARIIFLGDLV---------------------------RDGEPYSYGPPI--ED----- 147
Cdd:PLN02654 195 VVITCNAVKR-----------GPKTINLKDIVdaaldesakngvsvgicltyenqlamkREDTKWQEGRDVwwQDvvpny 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 148 PQREPAQ------PAFIFYTSGTTGLPK------------AAIIPQRAAE---SRVLFMSTQVGLRHGRHNVVLGLMply 206
Cdd:PLN02654 264 PTKCEVEwvdaedPLFLLYTSGSTGKPKgvlhttggymvyTATTFKYAFDykpTDVYWCTADCGWITGHSYVTYGPM--- 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 207 hvvgffavlvaalaLDGTYVVVEEFRPV--DA---LQLVQQEQVTSLFATPTHLDALAAAAAHAGSSLKLDSLRhvtfag 281
Cdd:PLN02654 341 --------------LNGATVLVFEGAPNypDSgrcWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLR------ 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 282 atmpdaVLETVhqhlpGEKVN---------IYGTTEAMNSLYMRQPKTGTEM----------APG-----FFSEVRIVri 337
Cdd:PLN02654 401 ------VLGSV-----GEPINpsawrwffnVVGDSRCPISDTWWQTETGGFMitplpgawpqKPGsatfpFFGVQPVI-- 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 338 gggVDEivaNGEE------GELIVAAS-DSAF---VGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIIS 407
Cdd:PLN02654 468 ---VDE---KGKEiegecsGYLCVKKSwPGAFrtlYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINV 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 408 GGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCRS--SELADFKRPKRYFILDQL 485
Cdd:PLN02654 542 SGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLILTvrNQIGAFAAPDKIHWAPGL 621
|
570
....*....|...
1T5D_X 486 PKNALNKVLRRQL 498
Cdd:PLN02654 622 PKTRSGKIMRRIL 634
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
335-504 |
1.97e-08 |
|
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: 56.73 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 335 VRIGGGVDEIVANGEEGElIVAASDSAFVGYLNQPQATAEKL-QDGWYRTSDVAvWTPEGTVRILGRVDDMIISGGENIH 413
Cdd:cd05908 325 IRICDEDNKILPDGYIGH-IQIRGKNVTPGYYNNPEATAKVFtDDGWLKTGDLG-FIRNGRLVITGREKDIIFVNGQNVY 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 414 PSEIERVLGTAPGVT--EVVVIGLADQRWGQSVTACVVprlgetLSADALDTFCR-----SSELADFK--RPKRYFILDQ 484
Cdd:cd05908 403 PHDIERIAEELEGVElgRVVACGVNNSNTRNEEIFCFI------EHRKSEDDFYPlgkkiKKHLNKRGgwQINEVLPIRR 476
|
170 180
....*....|....*....|
1T5D_X 485 LPKNALNKVLRRQLVQQVSS 504
Cdd:cd05908 477 IPKTTSGKVKRYELAQRYQS 496
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
26-220 |
8.06e-08 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 54.75 E-value: 8.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 26 RGLRLTHAELRARVEAVAARL--HAdglRPQQRVAVVAPNSADVVIAILALHRLG--AVPaLLNPRLKS-AELAELIKRg 100
Cdd:PRK12476 65 CAVELTWTQLGVRLRAVGARLqqVA---GPGDRVAILAPQGIDYVAGFFAAIKAGtiAVP-LFAPELPGhAERLDTALR- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 101 EMTAAVIAVGRQVADAIFQsgsgariiFLGDLVRDGEPY---------SYGPPIEDPQREPAQPAFIFYTSGTTGLPKAA 171
Cdd:PRK12476 140 DAEPTVVLTTTAAAEAVEG--------FLRNLPRLRRPRviaidaipdSAGESFVPVELDTDDVSHLQYTSGSTRPPVGV 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
1T5D_X 172 IIPQRAAESRVLFMSTQVG-LRHGRHNVvlGLMPLYHVVGFFAVLVAALA 220
Cdd:PRK12476 212 EITHRAVGTNLVQMILSIDlLDRNTHGV--SWLPLYHDMGLSMIGFPAVY 259
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
131-434 |
3.26e-07 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 53.10 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 131 DLVRDGEPYSYGPPIedpqREPAQPAFIFYTSGTTGLPKAAIIPQRAA---ESRVLFMSTQVGLRHGRHNVVLGLMPLYH 207
Cdd:PLN02614 205 EFLKLGEGKQYDLPI----KKKSDICTIMYTSGTTGDPKGVMISNESIvtlIAGVIRLLKSANAALTVKDVYLSYLPLAH 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 208 V---------------VGFFAVLVAALALDgtyvvVEEFRPVD--ALQLVQQEQVTSLFATPTHLDALAAAAAHAGSSLK 270
Cdd:PLN02614 281 IfdrvieecfiqhgaaIGFWRGDVKLLIED-----LGELKPTIfcAVPRVLDRVYSGLQKKLSDGGFLKKFVFDSAFSYK 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 271 LDSLR----HVTfAGATMPDAVLETVHQHLpGEKVNI---------------------------YGTTEAMNSLYMRQPK 319
Cdd:PLN02614 356 FGNMKkgqsHVE-ASPLCDKLVFNKVKQGL-GGNVRIilsgaaplashvesflrvvacchvlqgYGLTESCAGTFVSLPD 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 320 T----GTEMAPGFFSEVRIVRIGGGVDEIVANGEEGELIVAASdSAFVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTV 395
Cdd:PLN02614 434 EldmlGTVGPPVPNVDIRLESVPEMEYDALASTPRGEICIRGK-TLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSM 512
|
330 340 350 360
....*....|....*....|....*....|....*....|
1T5D_X 396 RILGRVDDMI-ISGGENIHPSEIERVLGTAPGVTEVVVIG 434
Cdd:PLN02614 513 KIIDRKKNIFkLSQGEYVAVENIENIYGEVQAVDSVWVYG 552
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
379-498 |
5.38e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 52.07 E-value: 5.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 379 GWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLS- 457
Cdd:PRK00174 483 GMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSd 562
|
90 100 110 120
....*....|....*....|....*....|....*....|...
1T5D_X 458 --ADALDTFCRsSELADFKRPKRYFILDQLPKNALNKVLRRQL 498
Cdd:PRK00174 563 elRKELRNWVR-KEIGPIAKPDVIQFAPGLPKTRSGKIMRRIL 604
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
301-451 |
5.84e-07 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 52.13 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 301 VNIYGTTEAMNSL-YMRQPKTGTEmaPGFFSEVRIVRIGG----GVDEIVAN----------GEEGELIVAASDSAfVGY 365
Cdd:cd17647 253 VNMYGTTETQRAVsYFEVPSRSSD--PTFLKNLKDVMPAGrgmlNVQLLVVNrndrtqicgiGEVGEIYVRAGGLA-EGY 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 366 LNQPQATAEKLQDGW-----------------------------YRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSE 416
Cdd:cd17647 330 RGLPELNKEKFVNNWfvepdhwnyldkdnnepwrqfwlgprdrlYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGE 409
|
170 180 190
....*....|....*....|....*....|....*
1T5D_X 417 IERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPR 451
Cdd:cd17647 410 IDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPR 444
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
301-464 |
2.10e-06 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 50.45 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 301 VNIYGTTEAMNSL-YMRQPKTGTEmaPGFFSEVRIVRIGG----GVDEIVAN----------GEEGELIVAASDSAfVGY 365
Cdd:TIGR03443 559 VNMYGTTETQRAVsYFEIPSRSSD--STFLKNLKDVMPAGkgmkNVQLLVVNrndrtqtcgvGEVGEIYVRAGGLA-EGY 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 366 LNQPQATAEKLQDGW-----------------------------YRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSE 416
Cdd:TIGR03443 636 LGLPELNAEKFVNNWfvdpshwidldkennkperefwlgprdrlYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGE 715
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
1T5D_X 417 IERVLGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGetlsADALDTF 464
Cdd:TIGR03443 716 IDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVPQDK----SDELEEF 759
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
155-502 |
3.16e-06 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 49.43 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 155 PAFIFYTSGTTGLPKAA----IIPQRAAESRVLFMSTQVGlrhgrhNVVLGLMPLYHVVGffAVLVAALALDGTYVVVEE 230
Cdd:PLN03051 121 VTNILFSSGTTGEPKAIpwthLSPLRCASDGWAHMDIQPG------DVVCWPTNLGWMMG--PWLLYSAFLNGATLALYG 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 231 FRPV--DALQLVQQEQVTSLFATPTHLDALAAAAAHAGSSLKLDSLRHVTFAG-ATMPDAVLETVHQHLPGEKVNIY-GT 306
Cdd:PLN03051 193 GAPLgrGFGKFVQDAGVTVLGLVPSIVKAWRHTGAFAMEGLDWSKLRVFASTGeASAVDDVLWLSSVRGYYKPVIEYcGG 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 307 TEaMNSLYMrqpkTGTEMAPGFFSEVRIVRIGGGVDEIVANGEE--------GE-----LIVAASDSAF------VGYLN 367
Cdd:PLN03051 273 TE-LASGYI----SSTLLQPQAPGAFSTASLGTRFVLLNDNGVPypddqpcvGEvalapPMLGASDRLLnadhdkVYYKG 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 368 QPQATAEKLQdgWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTA-PGVTEVVVIGLADQRWGQSVTA 446
Cdd:PLN03051 348 MPMYGSKGMP--LRRHGDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACDRAvAGIAETAAVGVAPPDGGPELLV 425
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
1T5D_X 447 CVVPR--LGETLSA---DALDTFCR---SSELADFKRPKRYFILDQLPKNALNKVLRRQLVQQV 502
Cdd:PLN03051 426 IFLVLgeEKKGFDQarpEALQKKFQeaiQTNLNPLFKVSRVKIVPELPRNASNKLLRRVLRDQL 489
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
31-246 |
4.73e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 49.33 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 31 THAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPrlkSAELAELIKRGEMTAAV---- 106
Cdd:PRK07868 474 TYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLMPP---DTDLAAAVRLGGVTEIItdpt 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 107 -IAVGRQVADAIFQSGSGARiiflgdlvRDGEPYSYGPPIEDPQREPAQ---P-------------AFI-FYTSGTTGLP 168
Cdd:PRK07868 551 nLEAARQLPGRVLVLGGGES--------RDLDLPDDADVIDMEKIDPDAvelPgwyrpnpglardlAFIaFSTAGGELVA 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1T5D_X 169 KaAIIPQRAAESRvlfMSTQVGLRHGRHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFRPVDALQLVQQEQVT 246
Cdd:PRK07868 623 K-QITNYRWALSA---FGTASAAALDRRDTVYCLTPLHHESGLLVSLGGAVVGGSRIALSRGLDPDRFVQEVRQYGVT 696
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
29-503 |
7.46e-05 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 45.46 E-value: 7.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 29 RLTHAELRARVEAVAARLHADGLRPQQRVAVVAPNSADVVIAILALHRLGAV---------PALLNPRLKSAE-----LA 94
Cdd:PLN03052 208 RMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVvvsiadsfaPSEIATRLKISKakaifTQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 95 ELIKRGEMTaavIAVGRQVADA-------IFQSGSGARI-IFLGDLVRDgEPYSYGPPIEDPQREPA--QP--AF--IFY 160
Cdd:PLN03052 288 DVIVRGGKS---IPLYSRVVEAkapkaivLPADGKSVRVkLREGDMSWD-DFLARANGLRRPDEYKAveQPveAFtnILF 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 161 TSGTTGLPKA----AIIPQRAAESRVLFMSTQVGlrhgrhNVV-----LGLMPLYHVVgfFAVLV--AALAL-DGTyvvv 228
Cdd:PLN03052 364 SSGTTGEPKAipwtQLTPLRAAADAWAHLDIRKG------DIVcwptnLGWMMGPWLV--YASLLngATLALyNGS---- 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 229 eefrPVDA--LQLVQQEQVTSLFATPTHLDALAAAAAHAGssLKLDSLRHVTFAG-ATMPDAVLETVHQHLPGEKVNIYG 305
Cdd:PLN03052 432 ----PLGRgfAKFVQDAKVTMLGTVPSIVKTWKNTNCMAG--LDWSSIRCFGSTGeASSVDDYLWLMSRAGYKPIIEYCG 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 306 TTEaMNSLYMrqpkTGTEMAPGFFSEVRIVRIGGGV-----------DEIVANGEEG--ELIVAASDSAF------VGYL 366
Cdd:PLN03052 506 GTE-LGGGFV----TGSLLQPQAFAAFSTPAMGCKLfilddsgnpypDDAPCTGELAlfPLMFGASSTLLnadhykVYFK 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 367 NQPQATAEKLQdgwyRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTA-PGVTEVVVIGLADQRWG--QS 443
Cdd:PLN03052 581 GMPVFNGKILR----RHGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCNAAdESVLETAAIGVPPPGGGpeQL 656
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
1T5D_X 444 VTACVVPRL-GETLSADALDTFCRS---SELADFKRPKRYFILDQLPKNALNKVLRRQLVQQVS 503
Cdd:PLN03052 657 VIAAVLKDPpGSNPDLNELKKIFNSaiqKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQQLA 720
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
30-96 |
1.01e-04 |
|
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: 45.03 E-value: 1.01e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1T5D_X 30 LTHAELRARVEAVAARL-HADGLRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAEL 96
Cdd:cd05905 15 LTWGKLLSRAEKIAAVLqKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFL 82
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
351-434 |
2.85e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 43.55 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 351 GELIVAASdSAFVGYLNQPQATAEKL-QDGWYRTSDVAVWTPEGTVRILGRVDDMI-ISGGENIHPSEIERVLGTAPGVT 428
Cdd:PLN02736 459 GEICVRGP-IIFKGYYKDEVQTREVIdEDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYAKCKFVA 537
|
....*.
1T5D_X 429 EVVVIG 434
Cdd:PLN02736 538 QCFVYG 543
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
151-495 |
1.23e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 41.65 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 151 EPAQPAFIFYTSGTTGLPKAAIipqRAAESRVlfmstqVGLRHG-----RHNVVLGLMPLYHV--VGFFAVLVAALALDG 223
Cdd:PTZ00237 252 ESSHPLYILYTSGTTGNSKAVV---RSNGPHL------VGLKYYwrsiiEKDIPTVVFSHSSIgwVSFHGFLYGSLSLGN 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 224 TYVVVE------EFRPVDALQLVQQEQVTSLFATPTHLDALAAA---AAHAGSSLKLDSLRHVTFAGATMPDAVLETVHQ 294
Cdd:PTZ00237 323 TFVMFEggiiknKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTdpeATIIRSKYDLSNLKEIWCGGEVIEESIPEYIEN 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 295 HLPGEKVNIYGTTE----------AMNSLYMRQPKTGTEMAPGFFSEVRIVRiggGVDEIvanGEEGELIVAASDSAFVG 364
Cdd:PTZ00237 403 KLKIKSSRGYGQTEigitylycygHINIPYNATGVPSIFIKPSILSEDGKEL---NVNEI---GEVAFKLPMPPSFATTF 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 365 YLNQpqataEKLQD------GWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQ 438
Cdd:PTZ00237 477 YKND-----EKFKQlfskfpGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDP 551
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
1T5D_X 439 RWGQSVTACVVprLGETLSADALD--------TFCRSSELADFKRPKRYFILDQLPKNALNKVLR 495
Cdd:PTZ00237 552 DCYNVPIGLLV--LKQDQSNQSIDlnklkneiNNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
52-486 |
1.61e-03 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 41.23 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 52 RPQQRVAVVAPNSADVVIAILALHRLGAVPALLN-----PRLKSAELAELIKrgemtaaVIAVGRQVADA-----IFQSG 121
Cdd:PRK08043 253 VEGERIGLMLPNATISAAVIFGASLRRRIPAMMNytagvKGLTSAITAAEIK-------TIFTSRQFLDKgklwhLPEQL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 122 SGARIIFLGDLVRDGEP--------YSYGPPIEDPQREPAQPAFIFYTSGTTGLPKAAIIPQRAAESRV----------- 182
Cdd:PRK08043 326 TQVRWVYLEDLKDDVTTadklwifaHLLMPRLAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVeqiktiadftp 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 183 --LFMSTqvglrhgrhnvvlglMPLYHVVGFFAVLVAALaLDGT----------YVVVEEfrpvdalqLVQQEQVTSLFA 250
Cdd:PRK08043 406 ndRFMSA---------------LPLFHSFGLTVGLFTPL-LTGAevflypsplhYRIVPE--------LVYDRNCTVLFG 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 251 TPThldaLAAAAAHAGSSLKLDSLRHVTfAGAtmpDAVLETVHQhLPGEKVNI-----YGTTE-----AMNSLYMRQPKT 320
Cdd:PRK08043 462 TST----FLGNYARFANPYDFARLRYVV-AGA---EKLQESTKQ-LWQDKFGLrilegYGVTEcapvvSINVPMAAKPGT 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 321 GTEMAPGFfsEVRIVRI-----GGGVDEIVANGEEGELIVAASdsafvGYLNQPQATAEK--LQDGWYRTSDVAVWTPEG 393
Cdd:PRK08043 533 VGRILPGM--DARLLSVpgieqGGRLQLKGPNIMNGYLRVEKP-----GVLEVPTAENARgeMERGWYDTGDIVRFDEQG 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 394 TVRILGRVDDMIISGGENIHPSEIERV-LGTAPGVTEVVVIGlADQRWGQsvtACVVPRLGETLSADALDTFCRSSELAD 472
Cdd:PRK08043 606 FVQIQGRAKRFAKIAGEMVSLEMVEQLaLGVSPDKQHATAIK-SDASKGE---ALVLFTTDSELTREKLQQYAREHGVPE 681
|
490
....*....|....
1T5D_X 473 FKRPKRYFILDQLP 486
Cdd:PRK08043 682 LAVPRDIRYLKQLP 695
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
330-418 |
2.96e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 40.31 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1T5D_X 330 SEVRIV----RI---GGGVDEIVANGEEgeliVAAsdsafvGYLNQPQATAEKLQ-----------DG-WYRTSDVAVWT 390
Cdd:PRK05850 379 PTVRIVdpdtCIecpAGTVGEIWVHGDN----VAA------GYWQKPEETERTFGatlvdpspgtpEGpWLRTGDLGFIS 448
|
90 100
....*....|....*....|....*...
1T5D_X 391 pEGTVRILGRVDDMIISGGENIHPSEIE 418
Cdd:PRK05850 449 -EGELFIVGRIKDLLIVDGRNHYPDDIE 475
|
|
| |
