|
Name |
Accession |
Description |
Interval |
E-value |
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
18-507 |
0e+00 |
|
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: 687.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 18 PSRRALAVPGK-VDLSHAALDALVDAAAARLAADaGVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFE 96
Cdd:cd05926 1 PDAPALVVPGStPALTYADLAELVDDLARQLAAL-GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 97 FYLSDSGARLLITNPEGNVAAQAAASKLGLAHTTASLKDAAGQVH-----LAGFPASAAAAAKDFANDPSDVALFLHTSG 171
Cdd:cd05926 80 FYLADLGSKLVLTPKGELGPASRAASKLGLAILELALDVGVLIRApsaesLSNLLADKKNAKSEGVPLPDDLALILHTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 172 TTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTLPAagRFSASTFWADMRGA 251
Cdd:cd05926 160 TTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPP--RFSASTFWPDVRDY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 252 GATWYTAVPTIHQIIIDRHTSKPEAEYPALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEASHLMTSNPLPEdGAR 331
Cdd:cd05926 238 NATWYTAVPTIHQILLNRPEPNPESPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNPLPP-GPR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 332 KAGSVGRAVGQEMAILDEEGRRVEAGKSGEVCVRGANVTSGYKGNPEAN-EAAFRFGWFHTGDIGVVDEEGYLRLVGRIK 410
Cdd:cd05926 317 KPGSVGKPVGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANaEAAFKDGWFRTGDLGYLDADGYLFLTGRIK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 411 ELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIAD 490
Cdd:cd05926 397 ELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHLAAFKVPKKVYFVD 476
|
490
....*....|....*..
gi 1002261995 491 ELPKTATGKIQRRIVAQ 507
Cdd:cd05926 477 ELPKTATGKIQRRKVAE 493
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
52-509 |
9.95e-149 |
|
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: 433.47 E-value: 9.95e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITnpegnvaaqaaasklglahtta 131
Cdd:COG0318 45 GVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT---------------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 slkdaagqvhlagfpasaaaaakdfandpsdvALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPL 211
Cdd:COG0318 103 --------------------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 FHVHGLLCGLLASLASGASVTLPAagRFSASTFWADMRGAGATWYTAVPTIHQIIIdRHTSKPEAEYPALRFIRSCSASL 291
Cdd:COG0318 151 FHVFGLTVGLLAPLLAGATLVLLP--RFDPERVLELIERERVTVLFGVPTMLARLL-RHPEFARYDLSSLRLVVSGGAPL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 292 APAIMEKLEAAFGAPVVEAYAMTEASHLMTSNPlPEDGARKAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVCVRGANVT 370
Cdd:COG0318 228 PPELLERFEERFGVRIVEGYGLTETSPVVTVNP-EDPGERRPGSVGRPLpGVEVRIVDEDGRELPPGEVGEIVVRGPNVM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 371 SGYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGE 450
Cdd:COG0318 307 KGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGE 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002261995 451 EINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRRIVAQHF 509
Cdd:COG0318 387 RVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERY 445
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
2-509 |
8.56e-134 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 398.49 E-value: 8.56e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 2 ETPTLTTLLKAAVATFPSRRALAVPG-KVDLSHAALDALVDAAAARLAADaGVLPGHVVALAFPNTVELVIMFLAVIRAR 80
Cdd:PRK05852 14 FGPRIADLVEVAATRLPEAPALVVTAdRIAISYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAASRAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 81 AVAAPLNPAYTQEEFEFYLSDSGARLLITNPEG-NVAAQAAASKLGLAHTTASLKDAAG---QVHLAGFPASAAAAAKDF 156
Cdd:PRK05852 93 LVVVPLDPALPIAEQRVRSQAAGARVVLIDADGpHDRAEPTTRWWPLTVNVGGDSGPSGgtlSVHLDAATEPTPATSTPE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 157 ANDPSDvALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTLPAA 236
Cdd:PRK05852 173 GLRPDD-AMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPAR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 237 GRFSASTFWADMRGAGATWYTAVPTIHQIIIDR-HTSKPEAEYPALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTE 315
Cdd:PRK05852 252 GRFSAHTFWDDIKAVGATWYTAVPTIHQILLERaATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 316 ASHLMTSNPLP-----EDGARKAGSVGRAVGQEMAILDEEGRRVEAGKSGEVCVRGANVTSGYKGNPEANEAAFRFGWFH 390
Cdd:PRK05852 332 ATHQVTTTQIEgigqtENPVVSTGLVGRSTGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWLR 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 391 TGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEEEVL 470
Cdd:PRK05852 412 TGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELV 491
|
490 500 510
....*....|....*....|....*....|....*....
gi 1002261995 471 AYCRRNLAAFKVPKKVYIADELPKTATGKIQRRIVAQHF 509
Cdd:PRK05852 492 QFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQF 530
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
52-503 |
1.29e-133 |
|
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: 395.39 E-value: 1.29e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNpegnvaaqaaaskLGLAHTTA 131
Cdd:cd05936 45 GVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIVA-------------VSFTDLLA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 SLKDAAGQVhlagfpasaaaaakdfANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVY--RLTEADATVIVL 209
Cdd:cd05936 112 AGAPLGERV----------------ALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLedLLEGDDVVLAAL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 210 PLFHVHGLLCGLLASLASGASVTL-PaagRFSASTFWADMRGAGATWYTAVPTIHqIIIDRHTSKPEAEYPALRFIRSCS 288
Cdd:cd05936 176 PLFHVFGLTVALLLPLALGATIVLiP---RFRPIGVLKEIRKHRVTIFPGVPTMY-IALLNAPEFKKRDFSSLRLCISGG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 289 ASLAPAIMEKLEAAFGAPVVEAYAMTEASHLMTSNPLpeDGARKAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVCVRGA 367
Cdd:cd05936 252 APLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPL--DGPRKPGSIGIPLpGTEVKIVDDDGEELPPGEVGELWVRGP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 368 NVTSGYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAK 447
Cdd:cd05936 330 QVMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPY 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002261995 448 YGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:cd05936 410 SGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRR 465
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
162-501 |
3.28e-126 |
|
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: 371.62 E-value: 3.28e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 162 DVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVhGLLCGLLASLASGASVTLPaaGRFSA 241
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLL--PKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 242 STFWADMRGAGATWYTAVPTIHQIIIDrHTSKPEAEYPALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEASHLMT 321
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLK-APESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 322 SNPlPEDGARKAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVCVRGANVTSGYKGNPEANEAAFRFGWFHTGDIGVVDEE 400
Cdd:cd04433 157 TGP-PDDDARKPGSVGRPVpGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDED 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 401 GYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAF 480
Cdd:cd04433 236 GYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAPY 315
|
330 340
....*....|....*....|.
gi 1002261995 481 KVPKKVYIADELPKTATGKIQ 501
Cdd:cd04433 316 KVPRRVVFVDALPRTASGKID 336
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
52-503 |
6.58e-111 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 339.08 E-value: 6.58e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEGNVAAQAAASKLGLAHTT- 130
Cdd:PRK06187 52 GVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVi 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 131 ----ASLKDAAGQVH-LAGFPASAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADAT 205
Cdd:PRK06187 132 vegdGPAAPLAPEVGeYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVY 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 206 VIVLPLFHVHGLLCGLLAsLASGASVTLPaaGRFSASTFWADMRGAGATWYTAVPTIHQIIIdRHTSKPEAEYPALRFIR 285
Cdd:PRK06187 212 LVIVPMFHVHAWGLPYLA-LMAGAKQVIP--RRFDPENLLDLIETERVTFFFAVPTIWQMLL-KAPRAYFVDFSSLRLVI 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 286 SCSASLAPAIMEKLEAAFGAPVVEAYAMTEASHLMTSNPLPE---DGARKAGSVGRAV-GQEMAILDEEGRRVEA-GKS- 359
Cdd:PRK06187 288 YGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVLPPEDqlpGQWTKRRSAGRPLpGVEARIVDDDGDELPPdGGEv 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 360 GEVCVRGANVTSGYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAV 439
Cdd:PRK06187 368 GEIIVRGPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVA 447
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002261995 440 AFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:PRK06187 448 VIGVPDEKWGERPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKR 511
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
52-502 |
3.20e-110 |
|
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: 334.58 E-value: 3.20e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLItnpegnvaaqaaasklglahtta 131
Cdd:cd17631 41 GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF----------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 slkdaagqvhlagfpasaaaaakdfandpSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPL 211
Cdd:cd17631 98 -----------------------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 FHVHGLLCGLLASLASGASVTLPAagRFSASTFWADMRGAGATWYTAVPTIHQIIIdRHTSKPEAEYPALRFIRSCSASL 291
Cdd:cd17631 149 FHIGGLGVFTLPTLLRGGTVVILR--KFDPETVLDLIERHRVTSFFLVPTMIQALL-QHPRFATTDLSSLRAVIYGGAPM 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 292 APAIMEKLEAaFGAPVVEAYAMTEASHLMTSNPlPEDGARKAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVCVRGANVT 370
Cdd:cd17631 226 PERLLRALQA-RGVKFVQGYGMTETSPGVTFLS-PEDHRRKLGSAGRPVfFVEVRIVDPDGREVPPGEVGEIVVRGPHVM 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 371 SGYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGE 450
Cdd:cd17631 304 AGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGE 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1002261995 451 EINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQR 502
Cdd:cd17631 384 AVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
52-503 |
2.11e-107 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 329.94 E-value: 2.11e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITnpEGNVAAQAAASKLGLAH--- 128
Cdd:PRK07656 51 GIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFV--LGLFLGVDYSATTRLPAleh 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 129 ----TTASLKDAAGQVHLAGFPASAAAAAKDFAN-DPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEAD 203
Cdd:PRK07656 129 vvicETEEDDPHTEKMKTFTDFLAAGDPAERAPEvDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 204 ATVIVLPLFHVHGLLCGLLASLASGASVtLPAAgRFSASTFWADMRGAGATWYTAVPTIHQIIIDrHTSKPEAEYPALRF 283
Cdd:PRK07656 209 RYLAANPFFHVFGYKAGVNAPLMRGATI-LPLP-VFDPDEVFRLIETERITVLPGPPTMYNSLLQ-HPDRSAEDLSSLRL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 284 IRSCSASLAPAIMEKLEAAFGAPVV-EAYAMTEASHLMTSNPLPEDGARKAGSVGRA-VGQEMAILDEEGRRVEAGKSGE 361
Cdd:PRK07656 286 AVTGAASMPVALLERFESELGVDIVlTGYGLSEASGVTTFNRLDDDRKTVAGTIGTAiAGVENKIVNELGEEVPVGEVGE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 362 VCVRGANVTSGYKGNPEANEAAFRF-GWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVA 440
Cdd:PRK07656 366 LLVRGPNVMKGYYDDPEATAAAIDAdGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAV 445
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002261995 441 FGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:PRK07656 446 IGVPDERLGEVGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKR 508
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
52-507 |
1.01e-105 |
|
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: 323.09 E-value: 1.01e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLItnpegnvaaqaaasklglahtta 131
Cdd:cd05941 33 KDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL----------------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 slkdaagqvhlagfpasaaaaakdfandpsDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPL 211
Cdd:cd05941 90 ------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 FHVHGLLCGLLASLASGASVTLpaAGRFSASTFWADMRGAGATWYTAVPTIHQIII---DRHTSKPEAEYPA----LRFI 284
Cdd:cd05941 140 HHVHGLVNALLCPLFAGASVEF--LPKFDPKEVAISRLMPSITVFMGVPTIYTRLLqyyEAHFTDPQFARAAaaerLRLM 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 285 RSCSASLAPAIMEKLEAAFGAPVVEAYAMTEAShLMTSNPLpeDGARKAGSVGRAV-GQEMAILDEEGRR-VEAGKSGEV 362
Cdd:cd05941 218 VSGSAALPVPTLEEWEAITGHTLLERYGMTEIG-MALSNPL--DGERRPGTVGMPLpGVQARIVDEETGEpLPRGEVGEI 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 363 CVRGANVTSGYKGNPEANEAAFRF-GWFHTGDIGVVDEEGYLRLVGRIK-ELINRGGEKISPIEVDSVLLGHPAIAQAVA 440
Cdd:cd05941 295 QVRGPSVFKEYWNKPEATKEEFTDdGWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAV 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002261995 441 FGVPDAKYGEEINCAVIPREGV-SLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRRIVAQ 507
Cdd:cd05941 375 IGVPDPDWGERVVAVVVLRAGAaALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
52-503 |
5.45e-104 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 318.08 E-value: 5.45e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITnpegnvaaqaaasklglahtta 131
Cdd:cd05934 24 GIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV---------------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 slkdaagqvhlagfpasaaaaakdfandpsDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPL 211
Cdd:cd05934 82 ------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 FHVHGLLCGLLASLASGASVTLpaAGRFSASTFWADMRGAGATWYTAVPTIHQIIIdrhtSKPEAEYPALRFIRSCSASL 291
Cdd:cd05934 132 FHINAQAVSVLAALSVGATLVL--LPRFSASRFWSDVRRYGATVTNYLGAMLSYLL----AQPPSPDDRAHRLRAAYGAP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 292 APA-IMEKLEAAFGAPVVEAYAMTEASHLMTSnplPEDGARKAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVCVRGAN- 368
Cdd:cd05934 206 NPPeLHEEFEERFGVRLLEGYGMTETIVGVIG---PRDEPRRPGSIGRPApGYEVRIVDDDGQELPAGEPGELVIRGLRg 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 369 --VTSGYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDA 446
Cdd:cd05934 283 wgFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDE 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1002261995 447 KYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:cd05934 363 VGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKA 419
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
52-416 |
9.43e-95 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 294.22 E-value: 9.43e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNP----EGNVAAQAAASKLGLA 127
Cdd:pfam00501 42 GVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLITDDalklEELLEALGKLEVVKLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 128 HTTASLKDAAGQVHLAGFPASAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVY----RLTEAD 203
Cdd:pfam00501 122 LVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 204 ATVIVLPLFHVHGLLCGLLASLASGASVTLPA-AGRFSASTFWADMRGAGATWYTAVPTIHQIIIdRHTSKPEAEYPALR 282
Cdd:pfam00501 202 RVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPgFPALDPAALLELIERYKVTVLYGVPTLLNMLL-EAGAPKRALLSSLR 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 283 FIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEASHLMTSNPLPEDGARKAGSVGRAV-GQEMAILDEE-GRRVEAGKSG 360
Cdd:pfam00501 281 LVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEDLRSLGSVGRPLpGTEVKIVDDEtGEPVPPGEPG 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1002261995 361 EVCVRGANVTSGYKGNPEANEAAF-RFGWFHTGDIGVVDEEGYLRLVGRIKELINRG 416
Cdd:pfam00501 361 ELCVRGPGVMKGYLNDPELTAEAFdEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
52-501 |
6.29e-89 |
|
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: 281.41 E-value: 6.29e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEGNVAAQAAASKLG----LA 127
Cdd:cd05911 31 GLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDPDGLEKVKEAAKELGpkdkII 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 128 HTTASLKDAAGQVHLAGFPASAAAAA--KDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTE--AD 203
Cdd:cd05911 111 VLDDKPDGVLSIEDLLSPTLGEEDEDlpPPLKDGKDDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGNDgsND 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 204 ATVIVLPLFHVHGLLCgLLASLASGASV-TLPaagRFSASTFWADMRGAGATWYTAVPTIHQIIIdRHTSKPEAEYPALR 282
Cdd:cd05911 191 VILGFLPLYHIYGLFT-TLASLLNGATViIMP---KFDSELFLDLIEKYKITFLYLVPPIAAALA-KSPLLDKYDLSSLR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 283 FIRSCSASLAPAIMEKLEAAFG-APVVEAYAMTEASHLMTSNPlpeDGARKAGSVGRAV-GQEMAILDEEGRRVEA-GKS 359
Cdd:cd05911 266 VILSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNP---DGDDKPGSVGRLLpNVEAKIVDDDGKDSLGpNEP 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 360 GEVCVRGANVTSGYKGNPEANEAAFRF-GWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQA 438
Cdd:cd05911 343 GEICVRGPQVMKGYYNNPEATKETFDEdGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADA 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002261995 439 VAFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFK-VPKKVYIADELPKTATGKIQ 501
Cdd:cd05911 423 AVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYKqLRGGVVFVDEIPKSASGKIL 486
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
160-502 |
6.40e-89 |
|
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: 276.85 E-value: 6.40e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 160 PSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTLPAAGrF 239
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSPS-F 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 240 SASTFWADMRGAGATWYTAVPTIHQIIIDrHTSKPEAEYPALRFIRSCSASLAPAIMEKLEAAFGAP-VVEAYAMTEASH 318
Cdd:cd05917 80 DPLAVLEAIEKEKCTALHGVPTMFIAELE-HPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKdVTIAYGMTETSP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 319 LMTsNPLPEDGA-RKAGSVGRAVG-QEMAILDEEGRRV-EAGKSGEVCVRGANVTSGYKGNPEA-NEAAFRFGWFHTGDI 394
Cdd:cd05917 159 VST-QTRTDDSIeKRVNTVGRIMPhTEAKIVDPEGGIVpPVGVPGELCIRGYSVMKGYWNDPEKtAEAIDGDGWLHTGDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 395 GVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCR 474
Cdd:cd05917 238 AVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKAYCK 317
|
330 340
....*....|....*....|....*...
gi 1002261995 475 RNLAAFKVPKKVYIADELPKTATGKIQR 502
Cdd:cd05917 318 GKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
4-505 |
9.49e-88 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 280.73 E-value: 9.49e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 4 PTLTTLLKAAVATFPSRRALAVPGK----VDLSHAALDALVDAAAArlaadaGVLPGHVVALAFPNTVELVIMFLAVIRA 79
Cdd:PRK05605 32 TTLVDLYDNAVARFGDRPALDFFGAtttyAELGKQVRRAAAGLRAL------GVRPGDRVAIVLPNCPQHIVAFYAVLRL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 80 RAVAAPLNPAYTQEEFEFYLSDSGARLLI---------------TNPEGNVA-----AQAAASKLGLAHTTASLKDAAGQ 139
Cdd:PRK05605 106 GAVVVEHNPLYTAHELEHPFEDHGARVAIvwdkvaptverlrrtTPLETIVSvnmiaAMPLLQRLALRLPIPALRKARAA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 140 VH------------LAGFPASAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRA-VYRLTEADATV 206
Cdd:PRK05605 186 LTgpapgtvpwetlVDAAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAwVPGLGDGPERV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 207 I-VLPLFHVHGL-LCGLLASLASGASVTLPaagRFSASTFWADMRGAGATWYTAVPTIHQIIIDrhtsKPEAEYPALRFI 284
Cdd:PRK05605 266 LaALPMFHAYGLtLCLTLAVSIGGELVLLP---APDIDLILDAMKKHPPTWLPGVPPLYEKIAE----AAEERGVDLSGV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 285 R---SCSASLAPAIMEKLEAAFGAPVVEAYAMTEASHLMTSNPLPEDgaRKAGSVGRAV-GQEMAILDEE--GRRVEAGK 358
Cdd:PRK05605 339 RnafSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPIIVGNPMSDD--RRPGYVGVPFpDTEVRIVDPEdpDETMPDGE 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 359 SGEVCVRGANVTSGYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQA 438
Cdd:PRK05605 417 EGELLVRGPQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDA 496
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002261995 439 VAFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRRIV 505
Cdd:PRK05605 497 AVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREV 563
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
52-503 |
5.64e-87 |
|
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: 276.81 E-value: 5.64e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEGnvaaqaaASKLGLAHTTA 131
Cdd:cd05904 53 GGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAEL-------AEKLASLALPV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 SLKDAA---GQVHLAGFPASAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEA--DATV 206
Cdd:cd05904 126 VLLDSAefdSLSFSDLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDseDVFL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 207 IVLPLFHVHGLLCGLLASLASGAsvTLPAAGRFSASTFWADMRGAGATWYTAVPTI------HQIIIDRHTSKpeaeypa 280
Cdd:cd05904 206 CVLPMFHIYGLSSFALGLLRLGA--TVVVMPRFDLEELLAAIERYKVTHLPVVPPIvlalvkSPIVDKYDLSS------- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 281 LRFIRSCSASLAPAIMEKLEAAF-GAPVVEAYAMTEASHLMTSNPLPEDGARKAGSVGRAV-GQEMAILD-EEGRRVEAG 357
Cdd:cd05904 277 LRQIMSGAAPLGKELIEAFRAKFpNVDLGQGYGMTESTGVVAMCFAPEKDRAKYGSVGRLVpNVEAKIVDpETGESLPPN 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 358 KSGEVCVRGANVTSGYKGNPEANEAAFRF-GWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIA 436
Cdd:cd05904 357 QTGELWIRGPSIMKGYLNNPEATAATIDKeGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEIL 436
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002261995 437 QAVAFGVPDAKYGeEINCA-VIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:cd05904 437 DAAVIPYPDEEAG-EVPMAfVVRKPGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRK 503
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
161-503 |
2.29e-84 |
|
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: 266.91 E-value: 2.29e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 161 SDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLCgLLASLASGASVTLpaAGRFS 240
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSI-LMRSVIYGMTVYL--VDKFD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 241 ASTFWADMRGAGATWYTAVPTIHQIIIDRHtskPEAEYPALRFIRSCSASLAPAIMEKLEAaFGAPVVEAYAMTE-ASHL 319
Cdd:cd05912 154 AEQVLHLINSGKVTIISVVPTMLQRLLEIL---GEGYPNNLRCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTEtCSQI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 320 MTSNPlpEDGARKAGSVGRAV-GQEMAILDEEGRrveAGKSGEVCVRGANVTSGYKGNPEANEAAFRFGWFHTGDIGVVD 398
Cdd:cd05912 230 VTLSP--EDALNKIGSAGKPLfPVELKIEDDGQP---PYEVGEILLKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLD 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 399 EEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGeEINCAVIPREGvSLGEEEVLAYCRRNLA 478
Cdd:cd05912 305 EEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWG-QVPVAFVVSER-PISEEELIAYCSEKLA 382
|
330 340
....*....|....*....|....*
gi 1002261995 479 AFKVPKKVYIADELPKTATGKIQRR 503
Cdd:cd05912 383 KYKVPKKIYFVDELPRTASGKLLRH 407
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
52-507 |
3.83e-83 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 266.73 E-value: 3.83e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEGNVAAQAAASKLGLAHTTa 131
Cdd:PRK06839 49 NVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVI- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 SLKDAAGqvhlagfpasAAAAAKDFANDPSDVALFL--HTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVL 209
Cdd:PRK06839 128 SITSLKE----------IEDRKIDNFVEKNESASFIicYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 210 PLFHVHGLLCGLLASLASGASVTLPaaGRFSASTFWADMRGAGATWYTAVPTIHQIIIDrhtsKPEAEYPALRFIRSCSA 289
Cdd:PRK06839 198 PLFHIGGIGLFAFPTLFAGGVIIVP--RKFEPTKALSMIEKHKVTVVMGVPTIHQALIN----CSKFETTNLQSVRWFYN 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 290 SLAPAIMEkLEAAF---GAPVVEAYAMTEASH--LMTSNplpEDGARKAGSVGRAVG-QEMAILDEEGRRVEAGKSGEVC 363
Cdd:PRK06839 272 GGAPCPEE-LMREFidrGFLFGQGFGMTETSPtvFMLSE---EDARRKVGSIGKPVLfCDYELIDENKNKVEVGEVGELL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 364 VRGANVTSGYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGV 443
Cdd:PRK06839 348 IRGPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGR 427
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002261995 444 PDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRRIVAQ 507
Cdd:PRK06839 428 QHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVN 491
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
52-503 |
1.01e-81 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 263.72 E-value: 1.01e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEGNVAAQAAASKLGLAHTTA 131
Cdd:PRK08316 57 GLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLIL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 SLK-----DAAGQVHLAGFPASAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATV 206
Cdd:PRK08316 137 SLVlggreAPGGWLDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 207 IVLPLFHVHGLLCGLLASLASGASVTL---PAAGRFSAStfwadMRGAGATWYTAVPTIhQIIIDRHtskPEAEYPALRF 283
Cdd:PRK08316 217 HALPLYHCAQLDVFLGPYLYVGATNVIldaPDPELILRT-----IEAERITSFFAPPTV-WISLLRH---PDFDTRDLSS 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 284 IRSC--SASLAP-AIMEKLEAAF-GAPVVEAYAMTEASHLMTSnpL-PEDGARKAGSVGRAV-GQEMAILDEEGRRVEAG 357
Cdd:PRK08316 288 LRKGyyGASIMPvEVLKELRERLpGLRFYNCYGQTEIAPLATV--LgPEEHLRRPGSAGRPVlNVETRVVDDDGNDVAPG 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 358 KSGEVCVRGANVTSGYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQ 437
Cdd:PRK08316 366 EVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAE 445
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002261995 438 AVAFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:PRK08316 446 VAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKR 511
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
52-505 |
2.05e-81 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 263.90 E-value: 2.05e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEG----------NVAAQAAA 121
Cdd:COG0365 60 GVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGlrggkvidlkEKVDEALE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 122 SKLGLAHT-----TASLKDAAGQVHLAGFPASAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRN-LAASVQNIRA 195
Cdd:COG0365 140 ELPSLEHVivvgrTGADVPMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKY 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 196 VYRLTEAD-----ATVivlplFHVHGLLCGLLASLASGASVTL-PAAGRF-SASTFWADMRGAGAT-WYTAvPT-IHQII 266
Cdd:COG0365 220 VLDLKPGDvfwctADI-----GWATGHSYIVYGPLLNGATVVLyEGRPDFpDPGRLWELIEKYGVTvFFTA-PTaIRALM 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 267 idRHTSKPEAEY--PALRFIrsCSA--SLAPAIMEKLEAAFGAPVVEAYAMTEASHLMTSNPLpeDGARKAGSVGRAV-G 341
Cdd:COG0365 294 --KAGDEPLKKYdlSSLRLL--GSAgePLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLP--GLPVKPGSMGKPVpG 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 342 QEMAILDEEGRRVEAGKSGEVCVRGAN--VTSGYKGNPEANEAAFR---FGWFHTGDIGVVDEEGYLRLVGRIKELINRG 416
Cdd:COG0365 368 YDVAVVDEDGNPVPPGEEGELVIKGPWpgMFRGYWNDPERYRETYFgrfPGWYRTGDGARRDEDGYFWILGRSDDVINVS 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 417 GEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEE---EVLAYCRRNLAAFKVPKKVYIADELP 493
Cdd:COG0365 448 GHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDElakELQAHVREELGPYAYPREIEFVDELP 527
|
490
....*....|..
gi 1002261995 494 KTATGKIQRRIV 505
Cdd:COG0365 528 KTRSGKIMRRLL 539
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
52-503 |
2.55e-81 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 261.44 E-value: 2.55e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEgnvaaqaaasklgLAHtta 131
Cdd:PRK03640 48 GVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDDD-------------FEA--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 slKDAAGQVHLAGFPASAAAAAKDFAN--DPSDVALFLHTSGTTSRPKGVPLTQRN----LAASVQNIRavyrLTEADAT 205
Cdd:PRK03640 112 --KLIPGISVKFAELMNGPKEEAEIQEefDLDEVATIMYTSGTTGKPKGVIQTYGNhwwsAVGSALNLG----LTEDDCW 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 206 VIVLPLFHVHGLlCGLLASLASGASVTLpaAGRFSASTFWADMRGAGATWYTAVPTIHQIIIDRHtskPEAEYPAlrFIR 285
Cdd:PRK03640 186 LAAVPIFHISGL-SILMRSVIYGMRVVL--VEKFDAEKINKLLQTGGVTIISVVSTMLQRLLERL---GEGTYPS--SFR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 286 SCSASLAPAIMEKLEAA--FGAPVVEAYAMTE-ASHLMTSNPlpEDGARKAGSVGRAV-GQEMAILDEeGRRVEAGKSGE 361
Cdd:PRK03640 258 CMLLGGGPAPKPLLEQCkeKGIPVYQSYGMTEtASQIVTLSP--EDALTKLGSAGKPLfPCELKIEKD-GVVVPPFEEGE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 362 VCVRGANVTSGYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAF 441
Cdd:PRK03640 335 IVVKGPNVTKGYLNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVV 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002261995 442 GVPDAKYGeEINCAVIPReGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:PRK03640 415 GVPDDKWG-QVPVAFVVK-SGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRH 474
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
52-509 |
2.30e-79 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 256.73 E-value: 2.30e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPegnvAAQAAASKLGLAHTTA 131
Cdd:PRK07514 49 GVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCDP----ANFAWLSKIAAAAGAP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 SLK--DAAGQVHLAGFPASAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVL 209
Cdd:PRK07514 125 HVEtlDADGTGSLLEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHAL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 210 PLFHVHGLLCGLLASLASGAS-VTLPaagRFSASTFWADMrgAGATWYTAVPTIHQIIIDRHTSKPEAEYPALRFIrSCS 288
Cdd:PRK07514 205 PIFHTHGLFVATNVALLAGASmIFLP---KFDPDAVLALM--PRATVMMGVPTFYTRLLQEPRLTREAAAHMRLFI-SGS 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 289 ASLAPAIMEKLEAAFGAPVVEAYAMTEASHLmTSNPLpeDGARKAGSVGRAV-GQEMAILD-EEGRRVEAGKSGEVCVRG 366
Cdd:PRK07514 279 APLLAETHREFQERTGHAILERYGMTETNMN-TSNPY--DGERRAGTVGFPLpGVSLRVTDpETGAELPPGEIGMIEVKG 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 367 ANVTSGYKGNPEANEAAFRF-GWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPD 445
Cdd:PRK07514 356 PNVFKGYWRMPEKTAEEFRAdGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPH 435
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002261995 446 AKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRRIVAQHF 509
Cdd:PRK07514 436 PDFGEGVTAVVVPKPGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQY 499
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
52-502 |
7.42e-79 |
|
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: 253.46 E-value: 7.42e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEGNVAAQAAasklglahtta 131
Cdd:cd05903 22 GVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPERFRQFDPAA----------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 slkdaagqvhlagfpasaaaaakdfanDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPL 211
Cdd:cd05903 91 ---------------------------MPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPM 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 FHVHGLLCGLLASLASGASVTLpaAGRFSASTFWADMRGAGATWYTAVPTIHQIIIdRHTSKPEAEYPALRFIRSCSASL 291
Cdd:cd05903 144 AHQTGFVYGFTLPLLLGAPVVL--QDIWDPDKALALMREHGVTFMMGATPFLTDLL-NAVEEAGEPLSRLRTFVCGGATV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 292 APAIMEKLEAAFGAPVVEAYAMTEASHLMTSNPLPEDGARkAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVCVRGANVT 370
Cdd:cd05903 221 PRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPEDRR-LYTDGRPLpGVEIKVVDDTGATLAPGVEGELLSRGPSVF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 371 SGYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGE 450
Cdd:cd05903 300 LGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGE 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1002261995 451 EINCAVIPREGVSLGEEEVLAYC-RRNLAAFKVPKKVYIADELPKTATGKIQR 502
Cdd:cd05903 380 RACAVVVTKSGALLTFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKVQK 432
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
52-501 |
2.24e-76 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 250.50 E-value: 2.24e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITN----------------PEgnv 115
Cdd:PRK08315 64 GIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAAdgfkdsdyvamlyelaPE--- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 116 AAQAAASKLGLA-------------------HTTASLKDAAGQVHLAGFPASAAAAakdfanDPSDVALFLHTSGTTSRP 176
Cdd:PRK08315 141 LATCEPGQLQSArlpelrrviflgdekhpgmLNFDELLALGRAVDDAELAARQATL------DPDDPINIQYTSGTTGFP 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 177 KGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTLPAAGrFSASTFWADMRGAGATWY 256
Cdd:PRK08315 215 KGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPLYHCFGMVLGNLACVTHGATMVYPGEG-FDPLATLAAVEEERCTAL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 257 TAVPT--IhqiiidrhtskpeAEYPALRFIRSCSASLAPAIMEkleaafGAP--------VVE---------AYAMTEAS 317
Cdd:PRK08315 294 YGVPTmfI-------------AELDHPDFARFDLSSLRTGIMA------GSPcpievmkrVIDkmhmsevtiAYGMTETS 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 318 HLMTSNPLPEDGARKAGSVGRAV-GQEMAILDEE-GRRVEAGKSGEVCVRGANVTSGYKGNPEA-NEAAFRFGWFHTGDI 394
Cdd:PRK08315 355 PVSTQTRTDDPLEKRVTTVGRALpHLEVKIVDPEtGETVPRGEQGELCTRGYSVMKGYWNDPEKtAEAIDADGWMHTGDL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 395 GVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEInCA-VIPREGVSLGEEEVLAYC 473
Cdd:PRK08315 435 AVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEV-CAwIILRPGATLTEEDVRDFC 513
|
490 500
....*....|....*....|....*...
gi 1002261995 474 RRNLAAFKVPKKVYIADELPKTATGKIQ 501
Cdd:PRK08315 514 RGKIAHYKIPRYIRFVDEFPMTVTGKIQ 541
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
167-502 |
2.52e-76 |
|
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: 243.72 E-value: 2.52e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 167 LHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTLPaagRFSASTFWA 246
Cdd:cd17637 6 IHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVME---KFDPAEALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 247 DMRGAGATWYTAVPTIHQIIIDRHTSKPeaeyPALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEASHLMTSNPLP 326
Cdd:cd17637 83 LIEEEKVTLMGSFPPILSNLLDAAEKSG----VDLSSLRHVLGLDAPETIQRFEETTGATFWSLYGQTETSGLVTLSPYR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 327 EdgarKAGSVGRAVG-QEMAILDEEGRRVEAGKSGEVCVRGANVTSGYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRL 405
Cdd:cd17637 159 E----RPGSAGRPGPlVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYLWY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 406 VGRI--KELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVP 483
Cdd:cd17637 235 AGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFVGSRIARYKKP 314
|
330
....*....|....*....
gi 1002261995 484 KKVYIADELPKTATGKIQR 502
Cdd:cd17637 315 RYVVFVEALPKTADGSIDR 333
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
1-502 |
2.43e-74 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 245.45 E-value: 2.43e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 1 METPTLTTLLKAAVATFPSRRALAV-PGKVDLSHAALDALVDAAAARLAADaGVLPGHVVALAFPNTVELVIMFLAVIRA 79
Cdd:PRK12583 15 LLTQTIGDAFDATVARFPDREALVVrHQALRYTWRQLADAVDRLARGLLAL-GVQPGDRVGIWAPNCAEWLLTQFATARI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 80 RAVAAPLNPAYTQEEFEFYLSDSGARLLITNPE----------GNVAAQAAASKLGlAHTTASLKDAAGQVHLAGFP--- 146
Cdd:PRK12583 94 GAILVNINPAYRASELEYALGQSGVRWVICADAfktsdyhamlQELLPGLAEGQPG-ALACERLPELRGVVSLAPAPppg 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 147 --------------ASAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLaasVQNIRAV---YRLTEADATVIVL 209
Cdd:PRK12583 173 flawhelqargetvSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNI---LNNGYFVaesLGLTEHDRLCVPV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 210 PLFHVHGLLCGLLASLASGASVTLPAAGrFSAStfwADMRGAGATWYTA---VPTIHQIIIDrHTSKPEAEYPALRFIRS 286
Cdd:PRK12583 250 PLYHCFGMVLANLGCMTVGACLVYPNEA-FDPL---ATLQAVEEERCTAlygVPTMFIAELD-HPQRGNFDLSSLRTGIM 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 287 CSASLAPAIMEKLEAAFGAPVVE-AYAMTEASHLMTSNPLPEDGARKAGSVGRAVG-QEMAILDEEGRRVEAGKSGEVCV 364
Cdd:PRK12583 325 AGAPCPIEVMRRVMDEMHMAEVQiAYGMTETSPVSLQTTAADDLERRVETVGRTQPhLEVKVVDPDGATVPRGEIGELCT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 365 RGANVTSGYKGNPEAN-EAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGV 443
Cdd:PRK12583 405 RGYSVMKGYWNNPEATaESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGV 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002261995 444 PDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQR 502
Cdd:PRK12583 485 PDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
52-504 |
2.74e-74 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 244.87 E-value: 2.74e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEGNVAAQAAASKLGLAHT-T 130
Cdd:PRK08314 57 GVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRHViV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 131 ASLKDA-----------------------AGQVHLAGFPASAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLA 187
Cdd:PRK08314 137 AQYSDYlpaepeiavpawlraepplqalaPGGVVAWKEALAAGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVM 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 188 ASVQNIRAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTL------PAAGRFsastfwadMRGAGATWYTAVPT 261
Cdd:PRK08314 217 ANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLmprwdrEAAARL--------IERYRVTHWTNIPT 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 262 IhqiIIDRHTSKPEAEY--PALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTE---ASHlmtSNPLpedGARKAGSV 336
Cdd:PRK08314 289 M---VVDFLASPGLAERdlSSLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTEtmaQTH---SNPP---DRPKLQCL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 337 GRAV-GQEMAILD-EEGRRVEAGKSGEVCVRGANVTSGYKGNPEANEAAF------RFgwFHTGDIGVVDEEGYLRLVGR 408
Cdd:PRK08314 360 GIPTfGVDARVIDpETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFieidgkRF--FRTGDLGRMDEEGYFFITDR 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 409 IKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREG--VSLGEEEVLAYCRRNLAAFKVPKKV 486
Cdd:PRK08314 438 LKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEarGKTTEEEIIAWAREHMAAYKYPRIV 517
|
490
....*....|....*...
gi 1002261995 487 YIADELPKTATGKIQRRI 504
Cdd:PRK08314 518 EFVDSLPKSGSGKILWRQ 535
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
52-503 |
1.41e-73 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 242.28 E-value: 1.41e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPE-----GNVAAQAAASKLGL 126
Cdd:PRK08008 58 GIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQfypmyRQIQQEDATPLRHI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 127 AHTTASLKDAAGQVHLAGFPASAAAAAKDFAN-DPSDVALFLHTSGTTSRPKGVPLTQRNLA-----ASVQNiravyRLT 200
Cdd:PRK08008 138 CLTRVALPADDGVSSFTQLKAQQPATLCYAPPlSTDDTAEILFTSGTTSRPKGVVITHYNLRfagyySAWQC-----ALR 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 201 EADATVIVLPLFHVHGLLCGLLASLASGAsvTLPAAGRFSASTFWADMRGAGATWYTAVPtihqIIIDRHTSKPEAEYPA 280
Cdd:PRK08008 213 DDDVYLTVMPAFHIDCQCTAAMAAFSAGA--TFVLLEKYSARAFWGQVCKYRATITECIP----MMIRTLMVQPPSANDR 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 281 LRFIRSCSASLAPAIMEKL--EAAFGAPVVEAYAMTEA-SHLMTSNPlpeDGARKAGSVGRA-VGQEMAILDEEGRRVEA 356
Cdd:PRK08008 287 QHCLREVMFYLNLSDQEKDafEERFGVRLLTSYGMTETiVGIIGDRP---GDKRRWPSIGRPgFCYEAEIRDDHNRPLPA 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 357 GKSGEVCVRGA---NVTSGYKGNPEANEAAFRF-GWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGH 432
Cdd:PRK08008 364 GEIGEICIKGVpgkTIFKEYYLDPKATAKVLEAdGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATH 443
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002261995 433 PAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:PRK08008 444 PKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKK 514
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
85-505 |
2.16e-73 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 241.87 E-value: 2.16e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 85 PLNPAYTQEEFEFYLSDSGARLLITN---PEGNVAAQAAASKLGLAHTTASLKDAAGQVHLAGFPASAAAAAKDFANDps 161
Cdd:PRK07470 86 PTNFRQTPDEVAYLAEASGARAMICHadfPEHAAAVRAASPDLTHVVAIGGARAGLDYEALVARHLGARVANAAVDHD-- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 162 DVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRA--VYRLTEADATVIVLPLFH---VHGLLcgllaSLASGASVTLPAA 236
Cdd:PRK07470 164 DPCWFFFTSGTTGRPKAAVLTHGQMAFVITNHLAdlMPGTTEQDASLVVAPLSHgagIHQLC-----QVARGAATVLLPS 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 237 GRFSASTFWADMRGAGATWYTAVPTIHQIIIDrHTSKPEAEYPALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEA 316
Cdd:PRK07470 239 ERFDPAEVWALVERHRVTNLFTVPTILKMLVE-HPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEV 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 317 SHLMTSNP----LPEDG-ARKAGSVGRA-VGQEMAILDEEGRRVEAGKSGEVCVRGANVTSGYKGNPEANEAAFRFGWFH 390
Cdd:PRK07470 318 TGNITVLPpalhDAEDGpDARIGTCGFErTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWFR 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 391 TGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGeEINCAV-IPREGVSLGEEEV 469
Cdd:PRK07470 398 TGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWG-EVGVAVcVARDGAPVDEAEL 476
|
410 420 430
....*....|....*....|....*....|....*.
gi 1002261995 470 LAYCRRNLAAFKVPKKVYIADELPKTATGKIQRRIV 505
Cdd:PRK07470 477 LAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
52-502 |
1.21e-72 |
|
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: 239.58 E-value: 1.21e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEgnvAAQAAASKLGLAHTTA 131
Cdd:cd05959 50 GVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGE---LAPVLAAALTKSEHTL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 SLKDA-------AGQVHLAGFPASAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQN-IRAVYRLTEAD 203
Cdd:cd05959 127 VVLIVsggagpeAGALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELyARNVLGIREDD 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 204 ATVIVLPLFHVHGLLCGLLASLASGASVTLpAAGRFSASTFWADMRGAGATWYTAVPTIHQIIIDRHTSkPEAEYPALRF 283
Cdd:cd05959 207 VCFSAAKLFFAYGLGNSLTFPLSVGATTVL-MPERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNL-PSRDLSSLRL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 284 IRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEASHLMTSNpLPedGARKAGSVGRAV-GQEMAILDEEGRRVEAGKSGEV 362
Cdd:cd05959 285 CVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSN-RP--GRVRYGTTGKPVpGYEVELRDEDGGDVADGEPGEL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 363 CVRGANVTSGYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFG 442
Cdd:cd05959 362 YVRGPSSATMYWNNRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVG 441
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002261995 443 VPDAKYGEEINCAVIPREGVSLGE---EEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQR 502
Cdd:cd05959 442 VEDEDGLTKPKAFVVLRPGYEDSEaleEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQR 504
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
159-503 |
1.63e-72 |
|
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: 239.45 E-value: 1.63e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 159 DPSDVALFLHTSGTTSRPKGVPLTQRNL---AASVQNIRAVYrLTEADATVIVLPLFHVHGLlcGL-LASLASGASVTLP 234
Cdd:cd12119 161 DENTAAAICYTSGTTGNPKGVVYSHRSLvlhAMAALLTDGLG-LSESDVVLPVVPMFHVNAW--GLpYAAAMVGAKLVLP 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 235 aaGRF-SASTFWADMRGAGATWYTAVPTIHQIIIDrHTSKPEAEYPALRFIRSCSASLAPAIMEKLEAAfGAPVVEAYAM 313
Cdd:cd12119 238 --GPYlDPASLAELIEREGVTFAAGVPTVWQGLLD-HLEANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGM 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 314 TEASHLMTSNPLP--------EDGARKAGSVGRAV-GQEMAILDEEGRRVEA-GKS-GEVCVRGANVTSGYKGNPEANEA 382
Cdd:cd12119 314 TETSPLGTVARPPsehsnlseDEQLALRAKQGRPVpGVELRIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKNDEESEA 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 383 AFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGV 462
Cdd:cd12119 394 LTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGA 473
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1002261995 463 SLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:cd12119 474 TVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKK 514
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
5-502 |
1.94e-72 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 239.66 E-value: 1.94e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 5 TLTTLLKAAVATFPSRrALAVPGKVDLSHAALDALVDAAAARLAADaGVLPGHVVALAFPNTVELVIMFLAVIRARAVAA 84
Cdd:PRK06155 22 TLPAMLARQAERYPDR-PLLVFGGTRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 85 PLNPAYTQEEFEFYLSDSGARLLITNPEGnVAAQAAASKLGLAHTTASLKDAAGQVHLAGFPASAAAAAKDFAND----- 159
Cdd:PRK06155 100 PINTALRGPQLEHILRNSGARLLVVEAAL-LAALEAADPGDLPLPAVWLLDAPASVSVPAGWSTAPLPPLDAPAPaaavq 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 160 PSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLlCGLLASLASGASVTLPAagRF 239
Cdd:PRK06155 179 PGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNAL-NAFFQALLAGATYVLEP--RF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 240 SASTFWADMRGAGATWYTAVPTIHQIIIDRHTSKPEAEYPaLRfiRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEASHL 319
Cdd:PRK06155 256 SASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHR-VR--VALGPGVPAALHAAFRERFGVDLLDGYGSTETNFV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 320 MTSNPlpedGARKAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVCVRGAN---VTSGYKGNPEANEAAFRFGWFHTGDIG 395
Cdd:PRK06155 333 IAVTH----GSQRPGSMGRLApGFEARVVDEHDQELPDGEPGELLLRADEpfaFATGYFGMPEKTVEAWRNLWFHTGDRV 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 396 VVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRR 475
Cdd:PRK06155 409 VRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEP 488
|
490 500
....*....|....*....|....*..
gi 1002261995 476 NLAAFKVPKKVYIADELPKTATGKIQR 502
Cdd:PRK06155 489 RLAYFAVPRYVEFVAALPKTENGKVQK 515
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
52-505 |
3.46e-72 |
|
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: 235.84 E-value: 3.46e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITnpegnvaaqaaasklglahtTA 131
Cdd:cd05935 22 GVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV--------------------GS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 SLKDaagqvhlagfpasaaaaakdfandpsdVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPL 211
Cdd:cd05935 82 ELDD---------------------------LALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 FHVHGLLCGLLASLASGASVTLpaAGRFSASTFWADMRGAGATWYTAVPTIhqiIIDRHTSKPEAEY--PALRFIRSCSA 289
Cdd:cd05935 135 FHVTGFVGSLNTAVYVGGTYVL--MARWDRETALELIEKYKVTFWTNIPTM---LVDLLATPEFKTRdlSSLKVLTGGGA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 290 SLAPAIMEKLEAAFGAPVVEAYAMTEASHLMTSNPLpedGARKAGSVGRAV-GQEMAILD-EEGRRVEAGKSGEVCVRGA 367
Cdd:cd05935 210 PMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPP---LRPKLQCLGIP*fGVDARVIDiETGRELPPNEVGEIVVRGP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 368 NVTSGYKGNPEANEAAF------RFgwFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAF 441
Cdd:cd05935 287 QIFKGYWNRPEETEESFieikgrRF--FRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVI 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002261995 442 GVPDAKYGEEINCAVIPREGV--SLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRRIV 505
Cdd:cd05935 365 SVPDERVGEEVKAFIVLRPEYrgKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
85-507 |
1.43e-71 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 235.65 E-value: 1.43e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 85 PLNPAYTQEEFEFYLSDSGARLLItnpegnvaAQAAASKLGLAHTTASLKDAAGQVHlagfpasaaaaakdFANDPSDVA 164
Cdd:PRK07787 74 PVPPDSGVAERRHILADSGAQAWL--------GPAPDDPAGLPHVPVRLHARSWHRY--------------PEPDPDAPA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 165 LFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTlpAAGRFSASTF 244
Cdd:PRK07787 132 LIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFV--HTGRPTPEAY 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 245 wADMRGAGATWYTAVPTI-HQIIIDrhTSKPEAEYPAlRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEAshLMTSN 323
Cdd:PRK07787 210 -AQALSEGGTLYFGVPTVwSRIAAD--PEAARALRGA-RLLVSGSAALPVPVFDRLAALTGHRPVERYGMTET--LITLS 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 324 PLPeDGARKAGSVGRAV-GQEMAILDEEGRRVEA-GKS-GEVCVRGANVTSGYKGNPEANEAAFRF-GWFHTGDIGVVDE 399
Cdd:PRK07787 284 TRA-DGERRPGWVGLPLaGVETRLVDEDGGPVPHdGETvGELQVRGPTLFDGYLNRPDATAAAFTAdGWFRTGDVAVVDP 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 400 EGYLRLVGRIK-ELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSlgEEEVLAYCRRNLA 478
Cdd:PRK07787 363 DGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVA--ADELIDFVAQQLS 440
|
410 420
....*....|....*....|....*....
gi 1002261995 479 AFKVPKKVYIADELPKTATGKIQRRIVAQ 507
Cdd:PRK07787 441 VHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
52-502 |
1.28e-70 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 237.16 E-value: 1.28e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLaVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLIT-NPE-GNVAAQAAASKLGLAHT 129
Cdd:PRK07529 79 GVGPGDVVAFLLPNLPETHFALW-GGEAAGIANPINPLLEPEQIAELLRAAGAKVLVTlGPFpGTDIWQKVAEVLAALPE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 130 TASLKDAAGQVHLAGFPASAAAAAKDFAND------------------------PSDVALFLHTSGTTSRPKGVPLTQRN 185
Cdd:PRK07529 158 LRTVVEVDLARYLPGPKRLAVPLIRRKAHArildfdaelarqpgdrlfsgrpigPDDVAAYFHTGGTTGMPKLAQHTHGN 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 186 LAASVQNIRAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTL--PAAGRFSA--STFWADMRGAGATWYTAVPT 261
Cdd:PRK07529 238 EVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLatPQGYRGPGviANFWKIVERYRINFLSGVPT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 262 IH----QIIIDRH--TSkpeaeypaLRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEASHLMTSNPLpeDGARKAGS 335
Cdd:PRK07529 318 VYaallQVPVDGHdiSS--------LRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPP--DGERRIGS 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 336 VG-RAVGQEM--AILDEEGRRV---EAGKSGEVCVRGANVTSGYKgNPEANEAAFRF-GWFHTGDIGVVDEEGYLRLVGR 408
Cdd:PRK07529 388 VGlRLPYQRVrvVILDDAGRYLrdcAVDEVGVLCIAGPNVFSGYL-EAAHNKGLWLEdGWLNTGDLGRIDADGYFWLTGR 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 409 IKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGeEINCA-VIPREGVSLGEEEVLAYCRRNL---AAfkVPK 484
Cdd:PRK07529 467 AKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAG-ELPVAyVQLKPGASATEAELLAFARDHIaerAA--VPK 543
|
490
....*....|....*...
gi 1002261995 485 KVYIADELPKTATGKIQR 502
Cdd:PRK07529 544 HVRILDALPKTAVGKIFK 561
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
52-507 |
5.49e-69 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 230.79 E-value: 5.49e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLI-------TNPEGNVaaqaaaskL 124
Cdd:PRK06087 70 GIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFaptlfkqTRPVDLI--------L 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 125 GLAHTTASLKDAAGQVHLAGFPASAAAAAKDFANDP---------SDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRA 195
Cdd:PRK06087 142 PLQNQLPQLQQIVGVDKLAPATSSLSLSQIIADYEPlttaitthgDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 196 VYRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTLpaAGRFSASTFWADMRGAGATWYT-AVPTIHQIIidRHTSKP 274
Cdd:PRK06087 222 RLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVL--LDIFTPDACLALLEQQRCTCMLgATPFIYDLL--NLLEKQ 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 275 EAEYPALRFIRsCSASLAPAIMEKLEAAFGAPVVEAYAMTEAS-HLMTsnPLPEDGARKAGSVGRAV-GQEMAILDEEGR 352
Cdd:PRK06087 298 PADLSALRFFL-CGGTTIPKKVARECQQRGIKLLSVYGSTESSpHAVV--NLDDPLSRFMHTDGYAAaGVEIKVVDEARK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 353 RVEAGKSGEVCVRGANVTSGYKGNPEA-NEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLG 431
Cdd:PRK06087 375 TLPPGCEGEEASRGPNVFMGYLDEPELtARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQ 454
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002261995 432 HPAIAQAVAFGVPDAKYGEEINCAVIPREGV-SLGEEEVLAY-CRRNLAAFKVPKKVYIADELPKTATGKIQRRIVAQ 507
Cdd:PRK06087 455 HPKIHDACVVAMPDERLGERSCAYVVLKAPHhSLTLEEVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
52-502 |
1.38e-68 |
|
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: 226.56 E-value: 1.38e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITnpegnvaaqaaASKLGLAHTTA 131
Cdd:TIGR01923 20 GIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLT-----------DSLLEEKDFQA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 slkDAAGQVHLAGFPASAAAAAKDFandpSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPL 211
Cdd:TIGR01923 89 ---DSLDRIEAAGRYETSLSASFNM----DQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWLLSLPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 FHVHGLlCGLLASLASGASVTLPAagRFSAstFWADMRGAGATWYTAVPTIHQIIIDRhTSKPEAeypaLRFIRsCSASL 291
Cdd:TIGR01923 162 YHISGL-SILFRWLIEGATLRIVD--KFNQ--LLEMIANERVTHISLVPTQLNRLLDE-GGHNEN----LRKIL-LGGSA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 292 APAIMEKLEAAFGAPVVEAYAMTEASHLMTSNPLPEDGARkaGSVGRAV-GQEMAIldeegRRVEAGKSGEVCVRGANVT 370
Cdd:TIGR01923 231 IPAPLIEEAQQYGLPIYLSYGMTETCSQVTTATPEMLHAR--PDVGRPLaGREIKI-----KVDNKEGHGEIMVKGANLM 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 371 SGYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGE 450
Cdd:TIGR01923 304 KGYLYQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQ 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1002261995 451 EINCAVIPREGVSlgEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQR 502
Cdd:TIGR01923 384 VPVAYIVSESDIS--QAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILR 433
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
52-505 |
1.87e-68 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 227.77 E-value: 1.87e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNpegnvAAQAAASKLGLAhtTA 131
Cdd:PRK09088 43 GCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGD-----DAVAAGRTDVED--LA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 SLKDAAGQVHLAGFPASaaaaakdfanDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPL 211
Cdd:PRK09088 116 AFIASADALEPADTPSI----------PPERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPM 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 FHVHGLLCGLLASLASGASVTLPAAGRFSASTFWADMRGAGATWYTAVPTIHQIIidrhTSKPEAEYPALRFIRSCSASL 291
Cdd:PRK09088 186 FHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLGDPALGITHYFCVPQMAQAF----RAQPGFDAAALRHLTALFTGG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 292 APAIMEKLEA--AFGAPVVEAYAMTEASHLMTSNPLPEDGARKAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVCVRGAN 368
Cdd:PRK09088 262 APHAAEDILGwlDDGIPMVDGFGMSEAGTVFGMSVDCDVIRAKAGAAGIPTpTVQTRVVDDQGNDCPAGVPGELLLRGPN 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 369 VTSGYKGNPEANEAAFRF-GWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAK 447
Cdd:PRK09088 342 LSPGYWRRPQATARAFTGdGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQ 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1002261995 448 YGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRRIV 505
Cdd:PRK09088 422 WGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
52-505 |
2.30e-68 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 228.72 E-value: 2.30e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEGNV--AAQAAASKLGLAHT 129
Cdd:PRK06188 58 GLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGISTLIVDPAPFVerALALLARVPSLKHV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 130 TaSLKDAAGQVHLAGFPASAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVL 209
Cdd:PRK06188 138 L-TLGPVPDGVDLLAAAAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 210 PLFHVHGLLcgLLASLASGASVTLPAAgrFSASTFWADMRGAGATWYTAVPTIHQIIIDrHTSKPEAEYPALRFIRSCSA 289
Cdd:PRK06188 217 PLSHAGGAF--FLPTLLRGGTVIVLAK--FDPAEVLRAIEEQRITATFLVPTMIYALLD-HPDLRTRDLSSLETVYYGAS 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 290 SLAPA-IMEKLEAaFGAPVVEAYAMTEA----SHLMTSNPLPEDGARkAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVC 363
Cdd:PRK06188 292 PMSPVrLAEAIER-FGPIFAQYYGQTEApmviTYLRKRDHDPDDPKR-LTSCGRPTpGLRVALLDEDGREVAQGEVGEIC 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 364 VRGANVTSGYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGV 443
Cdd:PRK06188 370 VRGPLVMDGYWNRPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGV 449
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002261995 444 PDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRRIV 505
Cdd:PRK06188 450 PDEKWGEAVTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
52-504 |
2.67e-68 |
|
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: 227.18 E-value: 2.67e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEGNVAAQAAASKlglahtta 131
Cdd:cd12118 50 GISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVDREFEYEDLLAEGD-------- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 slKDAAGQVhlagfpasaaaaakdfANDPSDVALFLHTSGTTSRPKGVPLTQRNLA-ASVQNI-------RAVYRLTead 203
Cdd:cd12118 122 --PDFEWIP----------------PADEWDPIALNYTSGTTGRPKGVVYHHRGAYlNALANIlewemkqHPVYLWT--- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 204 atvivLPLFHVHGLlCGLLASLASGA-SVTLPaagRFSASTFWADMRGAGATWYTAVPTIHQIIIDrhtSKPEAEYPALR 282
Cdd:cd12118 181 -----LPMFHCNGW-CFPWTVAAVGGtNVCLR---KVDAKAIYDLIEKHKVTHFCGAPTVLNMLAN---APPSDARPLPH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 283 FIRSCSASLAP--AIMEKLEAaFGAPVVEAYAMTEASHLMTSN---------PLPEDGARKA-GSVGRAVGQEMAILDEE 350
Cdd:cd12118 249 RVHVMTAGAPPpaAVLAKMEE-LGFDVTHVYGLTETYGPATVCawkpewdelPTEERARLKArQGVRYVGLEEVDVLDPE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 351 GRR-VEA-GKS-GEVCVRGANVTSGYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDS 427
Cdd:cd12118 328 TMKpVPRdGKTiGEIVFRGNIVMKGYLKNPEATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEG 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002261995 428 VLLGHPAIAQAVAFGVPDAKYGeEINCAVIP-REGVSLGEEEVLAYCRRNLAAFKVPKKVYIaDELPKTATGKIQRRI 504
Cdd:cd12118 408 VLYKHPAVLEAAVVARPDEKWG-EVPCAFVElKEGAKVTEEEIIAFCREHLAGFMVPKTVVF-GELPKTSTGKIQKFV 483
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
2-507 |
1.13e-66 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 225.30 E-value: 1.13e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 2 ETPTLTTLLKAAVATFPSRRALAVPGKvDLSHAALDALVDAAAARLAADaGVLPGHVVALAFPNTVELVIMFLAVIRARA 81
Cdd:PRK06710 22 DIQPLHKYVEQMASRYPEKKALHFLGK-DITFSVFHDKVKRFANYLQKL-GVEKGDRVAIMLPNCPQAVIGYYGTLLAGG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 82 VAAPLNPAYTQEEFEFYLSDSGARLLI----TNPEgnVAAQAAASKL----------------GLAHTTASLK------- 134
Cdd:PRK06710 100 IVVQTNPLYTERELEYQLHDSGAKVILcldlVFPR--VTNVQSATKIehvivtriadflpfpkNLLYPFVQKKqsnlvvk 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 135 -DAAGQVHLAGFPASAAAAAKDFANDP-SDVALFLHTSGTTSRPKGVPLTQRNLAA-SVQNIRAVYRLTEADATVI-VLP 210
Cdd:PRK06710 178 vSESETIHLWNSVEKEVNTGVEVPCDPeNDLALLQYTGGTTGFPKGVMLTHKNLVSnTLMGVQWLYNCKEGEEVVLgVLP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 211 LFHVHGLLCGLLASLASGASVTLpaAGRFSASTFWADMRGAGATWYTAVPTIHQIIIDRHTSKpEAEYPALRFIRSCSAS 290
Cdd:PRK06710 258 FFHVYGMTAVMNLSIMQGYKMVL--IPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLK-EYDISSIRACISGSAP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 291 LAPAIMEKLEAAFGAPVVEAYAMTEASHLMTSNPLPEDgaRKAGSVGRAV--GQEMAILDEEGRRVEAGKSGEVCVRGAN 368
Cdd:PRK06710 335 LPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEK--RVPGSIGVPWpdTEAMIMSLETGEALPPGEIGEIVVKGPQ 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 369 VTSGYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKY 448
Cdd:PRK06710 413 IMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYR 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002261995 449 GEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRRIVAQ 507
Cdd:PRK06710 493 GETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIE 551
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
5-503 |
1.45e-64 |
|
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: 218.86 E-value: 1.45e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 5 TLTTLLKAAVATFPSRRALaVPGKVDLSHAALDALVDAAAARLAADaGVLPGHVVALAFPNTVELVIMFLAVIRARAVaa 84
Cdd:COG1021 26 TLGDLLRRRAERHPDRIAV-VDGERRLSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFALFRAGAI-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 85 PLN--PAYTQEEFEFYLSDSGARLLIT--NPEG----NVAAQAAASKLGLAHTTAsLKDAAGQVHLAGFPASAAAAAKDF 156
Cdd:COG1021 102 PVFalPAHRRAEISHFAEQSEAVAYIIpdRHRGfdyrALARELQAEVPSLRHVLV-VGDAGEFTSLDALLAAPADLSEPR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 157 AnDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLC-GLLASLASGASVTLpa 235
Cdd:COG1021 181 P-DPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHNFPLSSpGVLGVLYAGGTVVL-- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 236 AGRFSASTFWADMRGAGATWYTAVPTIHQIIIDrHTSKPEAEYPALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTE 315
Cdd:COG1021 258 APDPSPDTAFPLIERERVTVTALVPPLALLWLD-AAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 316 AshLMTSNPLPEDGARKAGSVGRAV--GQEMAILDEEGRRVEAGKSGEVCVRGANVTSGYKGNPEANEAAF-RFGWFHTG 392
Cdd:COG1021 337 G--LVNYTRLDDPEEVILTTQGRPIspDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFtPDGFYRTG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 393 DIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEInCA-VIPReGVSLGEEEVLA 471
Cdd:COG1021 415 DLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERS-CAfVVPR-GEPLTLAELRR 492
|
490 500 510
....*....|....*....|....*....|...
gi 1002261995 472 YCR-RNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:COG1021 493 FLReRGLAAFKLPDRLEFVDALPLTAVGKIDKK 525
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
162-502 |
1.37e-63 |
|
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: 210.44 E-value: 1.37e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 162 DVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGASVtLPAAgRFSA 241
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATV-VPVA-VFDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 242 STFWADMRGAGATWYTAVPTIHQIIIDrHTSKPEAEYPALRFIRSCSASLAPAIMEKLEAAFG-APVVEAYAMTEASHLM 320
Cdd:cd17638 79 DAILEAIERERITVLPGPPTLFQSLLD-HPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGfETVLTAYGLTEAGVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 321 TSNPlPEDGARKAGSVGRAV-GQEMAILDEegrrveagksGEVCVRGANVTSGYKGNPEANEAAFRF-GWFHTGDIGVVD 398
Cdd:cd17638 158 MCRP-GDDAETVATTCGRACpGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDAdGWLHTGDVGELD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 399 EEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGeEINCA-VIPREGVSLGEEEVLAYCRRNL 477
Cdd:cd17638 227 ERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMG-EVGKAfVVARPGVTLTEEDVIAWCRERL 305
|
330 340
....*....|....*....|....*
gi 1002261995 478 AAFKVPKKVYIADELPKTATGKIQR 502
Cdd:cd17638 306 ANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
52-505 |
1.53e-63 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 215.13 E-value: 1.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEGNVAAQAAASKLGLahtta 131
Cdd:PRK06145 48 GIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDEEFDAIVALETPKIVI----- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 slkDAAGQVHLAGFPASAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPL 211
Cdd:PRK06145 123 ---DAAAQADSRRLAQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 FHVHGLLCGLLASLASGAsvTLPAAGRFSASTFWADM---RGAGAtWYTAVptihqiIIDRHTSKPEAEYPALRFIRSCS 288
Cdd:PRK06145 200 YHVGAFDLPGIAVLWVGG--TLRIHREFDPEAVLAAIerhRLTCA-WMAPV------MLSRVLTVPDRDRFDLDSLAWCI 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 289 A----SLAPAIMEKLEAAFGAPVVEAYAMTEAshlMTSNPLPEDGAR--KAGSVGRAVGQ-EMAILDEEGRRVEAGKSGE 361
Cdd:PRK06145 271 GggekTPESRIRDFTRVFTRARYIDAYGLTET---CSGDTLMEAGREieKIGSTGRALAHvEIRIADGAGRWLPPNMKGE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 362 VCVRGANVTSGYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAF 441
Cdd:PRK06145 348 ICMRGPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVI 427
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002261995 442 GVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRRIV 505
Cdd:PRK06145 428 GVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
2-503 |
1.74e-63 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 216.55 E-value: 1.74e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 2 ETPTLTTLLKAAVATFPSRRALAVPGKVdLSHAALDALVDAAAARLAADAGVLPGHVVALAFPNTVELVIMFLAVIRARA 81
Cdd:PRK05677 22 EYPNIQAVLKQSCQRFADKPAFSNLGKT-LTYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 82 VAAPLNPAYTQEEFEFYLSDSGARLLITnpEGNVA--AQAAASKLGLAHTTAS------------LKDAA---------- 137
Cdd:PRK05677 101 IVVNTNPLYTAREMEHQFNDSGAKALVC--LANMAhlAEKVLPKTGVKHVIVTevadmlpplkrlLINAVvkhvkkmvpa 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 138 ----GQVHLAGFPASAAAAAKDFAN-DPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVY--RLTEADATVIV-L 209
Cdd:PRK05677 179 yhlpQAVKFNDALAKGAGQPVTEANpQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMgsNLNEGCEILIApL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 210 PLFHVHGLLCGLLASLASGA-SVTLPAAGRFSAstFWADMRGAGATWYTAVPTIHQIIIDRHTSKpEAEYPALRFIRSCS 288
Cdd:PRK05677 259 PLYHIYAFTFHCMAMMLIGNhNILISNPRDLPA--MVKELGKWKFSGFVGLNTLFVALCNNEAFR-KLDFSALKLTLSGG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 289 ASLAPAIMEKLEAAFGAPVVEAYAMTEASHLMTSNPLpedGARKAGSVGRAVGQEMA-ILDEEGRRVEAGKSGEVCVRGA 367
Cdd:PRK05677 336 MALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPS---QAIQVGTIGIPVPSTLCkVIDDDGNELPLGEVGELCVKGP 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 368 NVTSGYKGNPEANEAAFRF-GWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDA 446
Cdd:PRK05677 413 QVMKGYWQRPEATDEILDSdGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDE 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1002261995 447 KYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:PRK05677 493 KSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRR 549
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
52-503 |
3.88e-63 |
|
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: 212.20 E-value: 3.88e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITnpegnvaaqaaasklglahtta 131
Cdd:cd05972 21 GLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT---------------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 slkdaagqvhlagfpasaaaaakdfanDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPL 211
Cdd:cd05972 79 ---------------------------DAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNIADP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 FHVHGLLCGLLASLASGASVTLPAAGRFSASTFWADMRGAGATWYTAVPTIHQIIIDRHTSkpEAEYPALRFIRSCSASL 291
Cdd:cd05972 132 GWAKGAWSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLS--SYKFSHLRLVVSAGEPL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 292 APAIMEKLEAAFGAPVVEAYAMTEaSHLMTSNPLPEDgaRKAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVCVRGANVT 370
Cdd:cd05972 210 NPEVIEWWRAATGLPIRDGYGQTE-TGLTVGNFPDMP--VKPGSMGRPTpGYDVAIIDDDGRELPPGEEGDIAIKLPPPG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 371 --SGYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKY 448
Cdd:cd05972 287 lfLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVR 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1002261995 449 GEEINCAVIPREGVSLGEE---EVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:cd05972 367 GEVVKAFVVLTSGYEPSEElaeELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRV 424
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
52-509 |
1.07e-62 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 215.35 E-value: 1.07e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLItnpegnVAAQAAASKL-GLAHTT 130
Cdd:COG1022 61 GVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLF------VEDQEQLDKLlEVRDEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 131 ASLK-----------DAAGQVHL-------AGFPASAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQN 192
Cdd:COG1022 135 PSLRhivvldprglrDDPRLLSLdellalgREVADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARA 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 193 IRAVYRLTEADATVIVLPLFHVHGLLCGLLAsLASGASVTLPAagrfSASTFWADMRGAGATWYTAVP----TIHQIIID 268
Cdd:COG1022 215 LLERLPLGPGDRTLSFLPLAHVFERTVSYYA-LAAGATVAFAE----SPDTLAEDLREVKPTFMLAVPrvweKVYAGIQA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 269 RHTSKP-------------------------------EAEYPA----------------LRFIRSCSASLAPAIMEKLEA 301
Cdd:COG1022 290 KAEEAGglkrklfrwalavgrryararlagkspslllRLKHALadklvfsklrealggrLRFAVSGGAALGPELARFFRA 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 302 AfGAPVVEAYAMTEASHLMTSNPlpeDGARKAGSVGRAV-GQEMAIldeegrrveaGKSGEVCVRGANVTSGYKGNPEAN 380
Cdd:COG1022 370 L-GIPVLEGYGLTETSPVITVNR---PGDNRIGTVGPPLpGVEVKI----------AEDGEILVRGPNVMKGYYKNPEAT 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 381 EAAF-RFGWFHTGDIGVVDEEGYLRLVGRIKELI-NRGGEKISPIEVDSVLLGHPAIAQAVAFG----------VPD--- 445
Cdd:COG1022 436 AEAFdADGWLHTGDIGELDEDGFLRITGRKKDLIvTSGGKNVAPQPIENALKASPLIEQAVVVGdgrpflaaliVPDfea 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 446 -AKYGEEINcavIPREGVS--LGEEEVLAY-------CRRNLAAFKVPKKVYIadeLPK---------TATGKIQRRIVA 506
Cdd:COG1022 516 lGEWAEENG---LPYTSYAelAQDPEVRALiqeevdrANAGLSRAEQIKRFRL---LPKeftiengelTPTLKLKRKVIL 589
|
...
gi 1002261995 507 QHF 509
Cdd:COG1022 590 EKY 592
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
85-506 |
1.41e-62 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 211.53 E-value: 1.41e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 85 PLNPAYTQEEFEFYLSDSGARLLITNPEGNVAAQAAASKLGLAHTTASLKDAAGQVHLAGFPAsaaaaakdfaNDPSDVA 164
Cdd:cd05922 51 PLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDALPASPDPGTVLDADGIRAARASAPAHE----------VSHEDLA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 165 LFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLlCGLLASLASGASVTLPAAGRFSAsTF 244
Cdd:cd05922 121 LLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGL-SVLNTHLLRGATLVLTNDGVLDD-AF 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 245 WADMRGAGATWYTAVPTIHQIIiDRHTSKPeAEYPALRFIRSCSASLAPAIMEKLEAAF-GAPVVEAYAMTEASHLMTSN 323
Cdd:cd05922 199 WEDLREHGATGLAGVPSTYAML-TRLGFDP-AKLPSLRYLTQAGGRLPQETIARLRELLpGAQVYVMYGQTEATRRMTYL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 324 PlPEDGARKAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVCVRGANVTSGYKGNPEANEAAFRFG-WFHTGDIGVVDEEG 401
Cdd:cd05922 277 P-PERILEKPGSIGLAIpGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGgVLHTGDLARRDEDG 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 402 YLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKyGEEINCAVIPREGVSLgeEEVLAYCRRNLAAFK 481
Cdd:cd05922 356 FLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKIDP--KDVLRSLAERLPPYK 432
|
410 420
....*....|....*....|....*
gi 1002261995 482 VPKKVYIADELPKTATGKIQRRIVA 506
Cdd:cd05922 433 VPATVRVVDELPLTASGKVDYAALR 457
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
52-505 |
4.98e-62 |
|
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: 209.67 E-value: 4.98e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEgnvaaqaaasklgLAHTTa 131
Cdd:cd05969 21 GVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE-------------LYERT- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 slkdaagqvhlagfpasaaaaakdfanDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPL 211
Cdd:cd05969 87 ---------------------------DPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYWCTADP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 FHVHGLLCGLLASLASGASVTLpAAGRFSASTFWADMRGAGAT-WYTAvPTIHQIIIdRHTSKPEAEY--PALRFIRSCS 288
Cdd:cd05969 140 GWVTGTVYGIWAPWLNGVTNVV-YEGRFDAESWYGIIERVKVTvWYTA-PTAIRMLM-KEGDELARKYdlSSLRFIHSVG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 289 ASLAPAIMEKLEAAFGAPVVEAYAMTEASHLMTSNPLPEDGarKAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVCVRGA 367
Cdd:cd05969 217 EPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYPCMPI--KPGSMGKPLpGVKAAVVDENGNELPPGTKGILALKPG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 368 --NVTSGYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPD 445
Cdd:cd05969 295 wpSMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPD 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002261995 446 AKYGEEINCAVIPREGVSLGEE---EVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRRIV 505
Cdd:cd05969 375 PLRGEIIKAFISLKEGFEPSDElkeEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVL 437
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
52-507 |
1.41e-61 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 211.07 E-value: 1.41e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITnPEGNVAAQAAASKLGLAHTTA 131
Cdd:PRK13295 76 GVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVV-PKTFRGFDHAAMARRLRPELP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 SLK-----DAAGQV----HLAG----FPASAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYR 198
Cdd:PRK13295 155 ALRhvvvvGGDGADsfeaLLITpaweQEPDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 199 LTEADATVIVLPLFHVHGLLCGLLASLASGASVTL-----PAagRFSAStfwadMRGAGATWYTA-VPTIHQIIidRHTS 272
Cdd:PRK13295 235 LGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLqdiwdPA--RAAEL-----IRTEGVTFTMAsTPFLTDLT--RAVK 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 273 KPEAEYPALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEAShLMTSNPLPEDGARKAGSVGRAV-GQEMAILDEEG 351
Cdd:PRK13295 306 ESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENG-AVTLTKLDDPDERASTTDGCPLpGVEVRVVDADG 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 352 RRVEAGKSGEVCVRGANVTSGYKGNPEANEAAFRfGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLG 431
Cdd:PRK13295 385 APLPAGQIGRLQVRGCSNFGGYLKRPQLNGTDAD-GWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYR 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 432 HPAIAQAVAFGVPDAKYGEEInCA-VIPREGVSLGEEEVLAYCRRN-LAAFKVPKKVYIADELPKTATGKIQ----RRIV 505
Cdd:PRK13295 464 HPAIAQVAIVAYPDERLGERA-CAfVVPRPGQSLDFEEMVEFLKAQkVAKQYIPERLVVRDALPRTPSGKIQkfrlREML 542
|
..
gi 1002261995 506 AQ 507
Cdd:PRK13295 543 RG 544
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
52-502 |
3.64e-61 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 207.31 E-value: 3.64e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEgnvaaqaaasklglahtta 131
Cdd:cd05919 31 GVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSAD------------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 slkdaagqvhlagfpasaaaaakdfandpsDVALFLHTSGTTSRPKGVPLTQRNLAASVQNI-RAVYRLTEADATVIVLP 210
Cdd:cd05919 92 ------------------------------DIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMaREALGLTPGDRVFSSAK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 211 LFHVHGLLCGLLASLASGASVTLpAAGRFSASTFWADMRGAGATWYTAVPTIHQIIIDRHTSKPEAeYPALRFIRSCSAS 290
Cdd:cd05919 142 MFFGYGLGNSLWFPLAVGASAVL-NPGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDA-LRSLRLCVSAGEA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 291 LAPAIMEKLEAAFGAPVVEAYAMTEASHLMTSNplpEDGARKAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVCVRGANV 369
Cdd:cd05919 220 LPRGLGERWMEHFGGPILDGIGATEVGHIFLSN---RPGAWRLGSTGRPVpGYEIRLVDEEGHTIPPGEEGDLLVRGPSA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 370 TSGYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYG 449
Cdd:cd05919 297 AVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGL 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002261995 450 EEINCAVIPREGVSLGE---EEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQR 502
Cdd:cd05919 377 SRLTAFVVLKSPAAPQEslaRDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQR 432
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
52-503 |
6.92e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 208.22 E-value: 6.92e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPE-GNVAAQAAA-SKLGLAHT 129
Cdd:PRK08276 32 GLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVSAAlADTAAELAAeLPAGVPLL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 130 TASLKDAAGqvhlagFPASAAAAAKDFANDPSDV---ALFLHTSGTTSRPKGV--PLTQRN-LAASVQNIRAVYRLTEAD 203
Cdd:PRK08276 112 LVVAGPVPG------FRSYEEALAAQPDTPIADEtagADMLYSSGTTGRPKGIkrPLPGLDpDEAPGMMLALLGFGMYGG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 204 ATVIVL---PLFHVHGLLCGLLASLASGASVTLPaagRFSASTFWADMRGAGATWYTAVPTIHQiiidRHTSKPE---AE 277
Cdd:PRK08276 186 PDSVYLspaPLYHTAPLRFGMSALALGGTVVVME---KFDAEEALALIERYRVTHSQLVPTMFV----RMLKLPEevrAR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 278 Y--PALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEASHLMTSNPlpEDGARKAGSVGRAVGQEMAILDEEGRRVE 355
Cdd:PRK08276 259 YdvSSLRVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSEGGGVTVITS--EDWLAHPGSVGKAVLGEVRILDEDGNELP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 356 AGKSGEVCVRGANVTSGYKGNPEANEAAFR-FGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPA 434
Cdd:PRK08276 337 PGEIGTVYFEMDGYPFEYHNDPEKTAAARNpHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPK 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002261995 435 IAQAVAFGVPDAKYGEEINCAVIPREGVSLGEE---EVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:PRK08276 417 VADVAVFGVPDEEMGERVKAVVQPADGADAGDAlaaELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKR 488
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
162-509 |
1.84e-60 |
|
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: 201.79 E-value: 1.84e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 162 DVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLCgLLASLASGASVTLPAAGRFSA 241
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAI-LVRSLLAGAELVLLERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 242 StfwaDMRGAGATWYTAVPTIHQIIIDRHtsKPEAEYPALRFIRSCSASLAPAIMEKLEAAfGAPVVEAYAMTE-ASHLM 320
Cdd:cd17630 80 E----DLAPPGVTHVSLVPTQLQRLLDSG--QGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTEtASQVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 321 TSNPlpedGARKAGSVGRAVgqemaildeEGRRVEAGKSGEVCVRGANVTSGYKGNPEANEAAFRfGWFHTGDIGVVDEE 400
Cdd:cd17630 153 TKRP----DGFGRGGVGVLL---------PGRELRIVEDGEIWVGGASLAMGYLRGQLVPEFNED-GWFTTKDLGELHAD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 401 GYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSlgEEEVLAYCRRNLAAF 480
Cdd:cd17630 219 GRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPAD--PAELRAWLKDKLARF 296
|
330 340
....*....|....*....|....*....
gi 1002261995 481 KVPKKVYIADELPKTATGKIQRRIVAQHF 509
Cdd:cd17630 297 KLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
160-500 |
1.91e-60 |
|
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: 203.10 E-value: 1.91e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 160 PSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTLPAAGRF 239
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 240 SAST----FWADMRGAGATWYTAVPTIHQIIIDRHTskpEAEYPALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTE 315
Cdd:cd05944 81 RNPGlfdnFWKLVERYRITSLSTVPTVYAALLQVPV---NADISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 316 ASHLMTSNPlpEDGARKAGSVGRAV---GQEMAILDEEG---RRVEAGKSGEVCVRGANVTSGYKGNPEANEAAFRFGWF 389
Cdd:cd05944 158 ATCLVAVNP--PDGPKRPGSVGLRLpyaRVRIKVLDGVGrllRDCAPDEVGEICVAGPGVFGGYLYTEGNKNAFVADGWL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 390 HTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGeEINCAVIP-REGVSLGEEE 468
Cdd:cd05944 236 NTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAG-ELPVAYVQlKPGAVVEEEE 314
|
330 340 350
....*....|....*....|....*....|....*
gi 1002261995 469 VLAYCRRNL---AAfkVPKKVYIADELPKTATGKI 500
Cdd:cd05944 315 LLAWARDHVperAA--VPKHIEVLEELPVTAVGKV 347
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
168-502 |
4.15e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 207.11 E-value: 4.15e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 168 HTSGTTSRPKGVPLTQRNLA-ASVQNI-------RAVYRLTeadatvivLPLFHVHGLLCGLLASLASGASVTLPaagRF 239
Cdd:PRK08162 189 YTSGTTGNPKGVVYHHRGAYlNALSNIlawgmpkHPVYLWT--------LPMFHCNGWCFPWTVAARAGTNVCLR---KV 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 240 SASTFWADMRGAGATWYTAVPTIHQIIID-RHTSKPEAEYPalrfIRSCSASLAP--AIMEKLEAAfGAPVVEAYAMTEA 316
Cdd:PRK08162 258 DPKLIFDLIREHGVTHYCGAPIVLSALINaPAEWRAGIDHP----VHAMVAGAAPpaAVIAKMEEI-GFDLTHVYGLTET 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 317 SHLMTSN---------PLPEDGARKAGSVGRAVGQE-MAILD-EEGRRVEA-GKS-GEVCVRGANVTSGYKGNPEANEAA 383
Cdd:PRK08162 333 YGPATVCawqpewdalPLDERAQLKARQGVRYPLQEgVTVLDpDTMQPVPAdGETiGEIMFRGNIVMKGYLKNPKATEEA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 384 FRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGeEINCAVIP-REGV 462
Cdd:PRK08162 413 FAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWG-EVPCAFVElKDGA 491
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1002261995 463 SLGEEEVLAYCRRNLAAFKVPKKVYIAdELPKTATGKIQR 502
Cdd:PRK08162 492 SATEEEIIAHCREHLAGFKVPKAVVFG-ELPKTSTGKIQK 530
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
55-503 |
1.59e-59 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 205.83 E-value: 1.59e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 55 PGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLI---------------TNPEGNVAAQA 119
Cdd:PRK12492 74 PGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVylnmfgklvqevlpdTGIEYLIEAKM 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 120 A----ASKLGLAHTTA-SLKDAAGQVHLAGFPASAAAAAKDFANDPS-------DVALFLHTSGTTSRPKGVPLTQRNLA 187
Cdd:PRK12492 154 GdllpAAKGWLVNTVVdKVKKMVPAYHLPQAVPFKQALRQGRGLSLKpvpvgldDIAVLQYTGGTTGLAKGAMLTHGNLV 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 188 ASVQNIRAVYRLTEADATVIV----------LPLFHVHGLLCGLLASLASGASVTLPAAGRfSASTFWADMRGAGATWYT 257
Cdd:PRK12492 234 ANMLQVRACLSQLGPDGQPLMkegqevmiapLPLYHIYAFTANCMCMMVSGNHNVLITNPR-DIPGFIKELGKWRFSALL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 258 AVPTIHQIIIDrHTSKPEAEYPALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEASHLMTSNPLPEDGarKAGSVG 337
Cdd:PRK12492 313 GLNTLFVALMD-HPGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELA--RLGTVG 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 338 RAV-GQEMAILDEEGRRVEAGKSGEVCVRGANVTSGYKGNPEANEAAFRF-GWFHTGDIGVVDEEGYLRLVGRIKELINR 415
Cdd:PRK12492 390 IPVpGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAeGWFKTGDIAVIDPDGFVRIVDRKKDLIIV 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 416 GGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGvSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKT 495
Cdd:PRK12492 470 SGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDP-GLSVEELKAYCKENFTGYKVPKHIVLRDSLPMT 548
|
....*...
gi 1002261995 496 ATGKIQRR 503
Cdd:PRK12492 549 PVGKILRR 556
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
52-505 |
3.63e-59 |
|
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: 202.06 E-value: 3.63e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNpegnvaaqaaasklglahtta 131
Cdd:cd05907 26 GVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE--------------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 slkdaagqvhlagfpasaaaaakdfanDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPL 211
Cdd:cd05907 85 ---------------------------DPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 FHVHGLLCGLLASLASGASVTLPaagrFSASTFWADMRGAGATWYTAVPTIHQIIID--RHTSKPE--------AEYPAL 281
Cdd:cd05907 138 AHVFERRAGLYVPLLAGARIYFA----SSAETLLDDLSEVRPTVFLAVPRVWEKVYAaiKVKAVPGlkrklfdlAVGGRL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 282 RFIRSCSASLAPAIMEKLEAAfGAPVVEAYAMTEASHLMTSNPLpedGARKAGSVGRAV-GQEMAILDEegrrveagksG 360
Cdd:cd05907 214 RFAASGGAPLPAELLHFFRAL-GIPVYEGYGLTETSAVVTLNPP---GDNRIGTVGKPLpGVEVRIADD----------G 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 361 EVCVRGANVTSGYKGNPEAN-EAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELI-NRGGEKISPIEVDSVLLGHPAIAQA 438
Cdd:cd05907 280 EILVRGPNVMLGYYKNPEATaEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQA 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 439 VAFG----------VPD----AKYGEEINCAVIPREGVsLGEEEVLAYCRR-------NLAAFKVPKKVYIADELP---- 493
Cdd:cd05907 360 VVIGdgrpflvaliVPDpealEAWAEEHGIAYTDVAEL-AANPAVRAEIEAaveaanaRLSRYEQIKKFLLLPEPFtien 438
|
490
....*....|....
gi 1002261995 494 --KTATGKIQRRIV 505
Cdd:cd05907 439 geLTPTLKLKRPVI 452
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
159-503 |
1.98e-58 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 202.98 E-value: 1.98e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 159 DPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYR--LTEADATVIV-LPLFHVHGLLCGLLASLASGASVTLPA 235
Cdd:PRK08974 204 VPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGplLHPGKELVVTaLPLYHIFALTVNCLLFIELGGQNLLIT 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 236 AGRfSASTFWADMRGAGATWYTAVPTIHQIIIDRHTSKpEAEYPALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTE 315
Cdd:PRK08974 284 NPR-DIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQ-ELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 316 ASHLMTSNPLpeDGARKAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVCVRGANVTSGYKGNPEANEAAFRFGWFHTGDI 394
Cdd:PRK08974 362 CSPLVSVNPY--DLDYYSGSIGLPVpSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVIKDGWLATGDI 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 395 GVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGvSLGEEEVLAYCR 474
Cdd:PRK08974 440 AVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDP-SLTEEELITHCR 518
|
330 340
....*....|....*....|....*....
gi 1002261995 475 RNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:PRK08974 519 RHLTGYKVPKLVEFRDELPKSNVGKILRR 547
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
5-503 |
3.54e-58 |
|
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: 200.25 E-value: 3.54e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 5 TLTTLLKAAVATFPSRRALaVPGKVDLSHAALDALVDAAAARLAADaGVLPGHVVALAFPNTVELVIMFLAVIRARAVAA 84
Cdd:cd05920 16 PLGDLLARSAARHPDRIAV-VDGDRRLTYRELDRRADRLAAGLRGL-GIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 85 PLNPAYTQEEFEFYLSDSGARLLITNPEgnvaaQAAASKLGLAHTTASlkdaagqvhlagfpasaaaaakdfanDPSDVA 164
Cdd:cd05920 94 LALPSHRRSELSAFCAHAEAVAYIVPDR-----HAGFDHRALARELAE--------------------------SIPEVA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 165 LFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLC-GLLASLASGASVTLpaAGRFSAST 243
Cdd:cd05920 143 LFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLACpGVLGTLLAGGRVVL--APDPSPDA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 244 FWADMRGAGATWYTAVPTIHQIIIDrHTSKPEAEYPALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEAshLMTSN 323
Cdd:cd05920 221 AFPLIEREGVTVTALVPALVSLWLD-AAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEG--LLNYT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 324 PLPEDGARKAGSVGRAV--GQEMAILDEEGRRVEAGKSGEVCVRGANVTSGYKGNPEANEAAFRF-GWFHTGDIGVVDEE 400
Cdd:cd05920 298 RLDDPDEVIIHTQGRPMspDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPdGFYRTGDLVRRTPD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 401 GYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEInCAVIPREGVSLGEEEVLAYCR-RNLAA 479
Cdd:cd05920 378 GYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERS-CAFVVLRDPPPSAAQLRRFLReRGLAA 456
|
490 500
....*....|....*....|....
gi 1002261995 480 FKVPKKVYIADELPKTATGKIQRR 503
Cdd:cd05920 457 YKLPDRIEFVDSLPLTAVGKIDKK 480
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
52-500 |
7.33e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 201.16 E-value: 7.33e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPE-GNVAAQAAASKLGLAHTT 130
Cdd:PRK07786 63 GVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAAlAPVATAVRDIVPLLSTVV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 131 ASLKDAAGQVHLAGFPASAAAAAKDFANDPSDV-ALFLHTSGTTSRPKGVPLTQRNLAA-SVQNIRAVYRLTEADATVIV 208
Cdd:PRK07786 143 VAGGSSDDSVLGYEDLLAEAGPAHAPVDIPNDSpALIMYTSGTTGRPKGAVLTHANLTGqAMTCLRTNGADINSDVGFVG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 209 LPLFHVHGLlCGLLASLASGASVTLPAAGRFSASTFWADMRGAGATWYTAVPTIHQIIIDRHTSKPEAEypALRFIRSCS 288
Cdd:PRK07786 223 VPLFHIAGI-GSMLPGLLLGAPTVIYPLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDL--ALRVLSWGA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 289 ASLAPAIMEKLEAAF-GAPVVEAYAMTEASHLmTSNPLPEDGARKAGSVGRAVGQ-EMAILDEEGRRVEAGKSGEVCVRG 366
Cdd:PRK07786 300 APASDTLLRQMAATFpEAQILAAFGQTEMSPV-TCMLLGEDAIRKLGSVGKVIPTvAARVVDENMNDVPVGEVGEIVYRA 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 367 ANVTSGYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDA 446
Cdd:PRK07786 379 PTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADE 458
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1002261995 447 KYGE-EINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKI 500
Cdd:PRK07786 459 KWGEvPVAVAAVRNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
52-502 |
5.95e-57 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 199.11 E-value: 5.95e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLIT--------------NPEGNVAA 117
Cdd:PRK06178 79 GVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLAldqlapvveqvraeTSLRHVIV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 118 QAAASKLGlAHTTASLKD--------AAGQVHLAGFPASAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNL--- 186
Cdd:PRK06178 159 TSLADVLP-AEPTLPLPDslraprlaAAGAIDLLPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMvyt 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 187 AASvqNIRAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTLPAagRFSASTFWADMRGAGATwYTAVPTIHQII 266
Cdd:PRK06178 238 AAA--AYAVAVVGGEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLA--RWDAVAFMAAVERYRVT-RTVMLVDNAVE 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 267 IDRHTSKPEAEYPALRFIRSCS--ASLAPAIMEKLEAAFGAPVVEA-YAMTEaSHlmTSNPLPE-------DGARKAGSV 336
Cdd:PRK06178 313 LMDHPRFAEYDLSSLRQVRVVSfvKKLNPDYRQRWRALTGSVLAEAaWGMTE-TH--TCDTFTAgfqdddfDLLSQPVFV 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 337 GRAV-GQEMAILDEE-GRRVEAGKSGEVCVRGANVTSGYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELIN 414
Cdd:PRK06178 390 GLPVpGTEFKICDFEtGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLK 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 415 RGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPkKVYIADELPK 494
Cdd:PRK06178 470 VNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVP-EIRIVDALPM 548
|
....*...
gi 1002261995 495 TATGKIQR 502
Cdd:PRK06178 549 TATGKVRK 556
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
52-503 |
1.11e-56 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 197.90 E-value: 1.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPegnvaaqAAASKL-GLAHTT 130
Cdd:PLN02246 71 GIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQS-------CYVDKLkGLAEDD 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 131 ASL-----KDAAGQVHLAGFPASAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASV-QNIRA----VYrLT 200
Cdd:PLN02246 144 GVTvvtidDPPEGCLHFSELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVaQQVDGenpnLY-FH 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 201 EADATVIVLPLFHVHGLLCGLLASLASGASVTLPAagRFSASTFWADMRGAGATWYTAVPTIHQIIIdrhtSKPEAEYPA 280
Cdd:PLN02246 223 SDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMP--KFEIGALLELIQRHKVTIAPFVPPIVLAIA----KSPVVEKYD 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 281 LRFIRSCSASLAPaiMEK-LEAAFGAPVVEA-----YAMTEASHLMT------SNPLPEdgarKAGSVGRAV-GQEMAIL 347
Cdd:PLN02246 297 LSSIRMVLSGAAP--LGKeLEDAFRAKLPNAvlgqgYGMTEAGPVLAmclafaKEPFPV----KSGSCGTVVrNAELKIV 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 348 D-EEGRRVEAGKSGEVCVRGANVTSGYKGNPEANEAAF-RFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEV 425
Cdd:PLN02246 371 DpETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAEL 450
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002261995 426 DSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:PLN02246 451 EALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRK 528
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
52-502 |
4.08e-55 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 192.75 E-value: 4.08e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEGNVAAQAAASKL-GLAHTT 130
Cdd:TIGR02262 51 GVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALLPVIKAALGKSpHLEHRV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 131 ASLKDAAGQVHLAGFPASAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNI-RAVYRLTEADATVIVL 209
Cdd:TIGR02262 131 VVGRPEAGEVQLAELLATESEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYaRNTLGIREDDVCFSAA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 210 PLFHVHGLLCGLLASLASGASVTLPAAgRFSASTFWADMRGAGATWYTAVPTIHQIIIDRHTSKPEAEYpALRFIRSCSA 289
Cdd:TIGR02262 211 KLFFAYGLGNALTFPMSVGATTVLMGE-RPTPDAVFDRLRRHQPTIFYGVPTLYAAMLADPNLPSEDQV-RLRLCTSAGE 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 290 SLAPAIMEKLEAAFGAPVVEAYAMTEASHLMTSNpLPedGARKAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVCVRGAN 368
Cdd:TIGR02262 289 ALPAEVGQRWQARFGVDIVDGIGSTEMLHIFLSN-LP--GDVRYGTSGKPVpGYRLRLVGDGGQDVADGEPGELLISGPS 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 369 VTSGYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKY 448
Cdd:TIGR02262 366 SATMYWNNRAKSRDTFQGEWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDG 445
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1002261995 449 GEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQR 502
Cdd:TIGR02262 446 LIKPKAFVVLRPGQTALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQR 499
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
52-502 |
1.01e-54 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 190.04 E-value: 1.01e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNpegnvAAQAaaSKLGlahtta 131
Cdd:cd05973 21 GVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD-----AANR--HKLD------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 slkdaagqvhlagfpasaaaaakdfandpSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPL 211
Cdd:cd05973 88 -----------------------------SDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAADP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 FHVHGLLCGLLASLASGASVTLPAAGrFSASTFWADMRGAGATWYTAVPTIHQIIIDRHTSKPEAEYPALRFIRSCSASL 291
Cdd:cd05973 139 GWAYGLYYAITGPLALGHPTILLEGG-FSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPKGRLRRVSSAGEPL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 292 APAIMEKLEAAFGAPVVEAYAMTEASHLMTSNPLPEDGARkAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVCVRGANVT 370
Cdd:cd05973 218 TPEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEHPVH-AGSAGRAMpGWRVAVLDDDGDELGPGEPGRLAIDIANSP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 371 ----SGYKGNPEAneaAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDA 446
Cdd:cd05973 297 lmwfRGYQLPDTP---AIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDP 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002261995 447 KYGEEINCAVIPREGVSLGEE---EVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQR 502
Cdd:cd05973 374 ERTEVVKAFVVLRGGHEGTPAladELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQR 432
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
52-503 |
1.41e-54 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 189.57 E-value: 1.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNpegnvaaqaaasklglahtta 131
Cdd:cd05971 27 GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTD--------------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 slkdaagqvhlagfpasaaaaakdfanDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPL 211
Cdd:cd05971 86 ---------------------------GSDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGDLYWTPA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 --FHVHGLLCGLLASLASGASVTLPAAGRFSASTFWADMRGAGATWYTAVPTIHQIIidRHTSKPEAEYP-ALRFIRSCS 288
Cdd:cd05971 139 dwAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMM--RQQGEQLKHAQvKLRAIATGG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 289 ASLAPAIMEKLEAAFGAPVVEAYAMTEASHLMTSNPLPedGARKAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVCVR-- 365
Cdd:cd05971 217 ESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNCSAL--FPIKPGSMGKPIpGHRVAIVDDNGTPLPPGEVGEIAVElp 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 366 GANVTSGYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPD 445
Cdd:cd05971 295 DPVAFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPD 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002261995 446 AKYGEEINCAVIPREGVSLGEE---EVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:cd05971 375 PIRGEIVKAFVVLNPGETPSDAlarEIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRR 435
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
2-503 |
1.53e-54 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 192.54 E-value: 1.53e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 2 ETPTLTTLLKAAVATFPSRRALAVPGKvDLSHAALDALVDAAAARLAADaGVLPGHVVALAFPNTVELVIMFLAVIRARA 81
Cdd:PRK07059 21 QYPSLADLLEESFRQYADRPAFICMGK-AITYGELDELSRALAAWLQSR-GLAKGARVAIMMPNVLQYPVAIAAVLRAGY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 82 VAAPLNPAYTQEEFEFYLSDSGARLLITNPEGNVAAQAAASKLGLAHT-TASLKDA------------------------ 136
Cdd:PRK07059 99 VVVNVNPLYTPRELEHQLKDSGAEAIVVLENFATTVQQVLAKTAVKHVvVASMGDLlgfkghivnfvvrrvkkmvpawsl 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 137 AGQVHLAGFPASAAAAAKDFAN-DPSDVALFLHTSGTTSRPKGVPLTQRNLAASV-------QNIRAVYRLTEADATVIV 208
Cdd:PRK07059 179 PGHVRFNDALAEGARQTFKPVKlGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqmeawlQPAFEKKPRPDQLNFVCA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 209 LPLFHVHGL-LCGLLASLASGASVTLPAAGRFSAstFWADMRGAGATWYTAVPTIHQIIIDrHTSKPEAEYPALRFIRSC 287
Cdd:PRK07059 259 LPLYHIFALtVCGLLGMRTGGRNILIPNPRDIPG--FIKELKKYQVHIFPAVNTLYNALLN-NPDFDKLDFSKLIVANGG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 288 SASLAPAIMEKLEAAFGAPVVEAYAMTEASHLMTSNPLpeDGARKAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVCVRG 366
Cdd:PRK07059 336 GMAVQRPVAERWLEMTGCPITEGYGLSETSPVATCNPV--DATEFSGTIGLPLpSTEVSIRDDDGNDLPLGEPGEICIRG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 367 ANVTSGYKGNP-EANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPD 445
Cdd:PRK07059 414 PQVMAGYWNRPdETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPD 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1002261995 446 AKYGEEINCAVIpREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:PRK07059 494 EHSGEAVKLFVV-KKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRR 550
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
52-510 |
1.58e-54 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 192.12 E-value: 1.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPegnvAAQAAASKLGLAHTTA 131
Cdd:PLN02330 76 GLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTND----TNYGKVKGLGLPVIVL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 SLKDAAGQVHLAGFPASAAAAAKDFAND---PSDVALFLHTSGTTSRPKGVPLTQRNLAA----SVQNIRAvyRLTEADA 204
Cdd:PLN02330 152 GEEKIEGAVNWKELLEAADRAGDTSDNEeilQTDLCALPFSSGTTGISKGVMLTHRNLVAnlcsSLFSVGP--EMIGQVV 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 205 TVIVLPLFHVHGLLCGLLASLASGASVTlpAAGRFSASTFWADMRGAGATWYTAVPTI------HQIIIDRHTSKPEaey 278
Cdd:PLN02330 230 TLGLIPFFHIYGITGICCATLRNKGKVV--VMSRFELRTFLNALITQEVSFAPIVPPIilnlvkNPIVEEFDLSKLK--- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 279 paLRFIRSCSASLAPAIMEKLEAAF-GAPVVEAYAMTEASHLMTSNPLPEDGA--RKAGSVGRAVGQ-EMAILD-EEGRR 353
Cdd:PLN02330 305 --LQAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEHSCITLTHGDPEKGHgiAKKNSVGFILPNlEVKFIDpDTGRS 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 354 VEAGKSGEVCVRGANVTSGYKGNPEANEAAF-RFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGH 432
Cdd:PLN02330 383 LPKNTPGELCVRSQCVMQGYYNNKEETDRTIdEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTH 462
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002261995 433 PAIAQAVAFGVPDAKYGE-EINCAVIPREGVSlGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRRIVAQHFV 510
Cdd:PLN02330 463 PSVEDAAVVPLPDEEAGEiPAACVVINPKAKE-SEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKML 540
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
169-503 |
1.88e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 192.06 E-value: 1.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 169 TSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLCGLLAsLASGASVTLPAagRFSASTFWADM 248
Cdd:PRK07788 215 TSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLA-MALGSTVVLRR--RFDPEATLEDI 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 249 RGAGATWYTAVPTIHQIIIDrHTSKPEAEY--PALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEASHLMTSNPlp 326
Cdd:PRK07788 292 AKHKATALVVVPVMLSRILD-LGPEVLAKYdtSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEVAFATIATP-- 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 327 EDGARKAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVCVRGANVTSGYKGNPEANEAAfrfGWFHTGDIGVVDEEGYLRL 405
Cdd:PRK07788 369 EDLAEAPGTVGRPPkGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGRDKQIID---GLLSSGDVGYFDEDGLLFV 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 406 VGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKK 485
Cdd:PRK07788 446 DGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPRD 525
|
330
....*....|....*...
gi 1002261995 486 VYIADELPKTATGKIQRR 503
Cdd:PRK07788 526 VVFLDELPRNPTGKVLKR 543
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
162-506 |
3.15e-54 |
|
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: 188.84 E-value: 3.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 162 DVALFLHTSGTTSRPKGVPLTQRNLAASVQNI-RAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGAS-VTLPAAgrf 239
Cdd:cd05958 98 DICILAFTSGTTGAPKATMHFHRDPLASADRYaVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASgVLLEEA--- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 240 SASTFWADMRGAGATWYTAVPTIHQIIIDrHTSKPEAEYPALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEASHL 319
Cdd:cd05958 175 TPDLLLSAIARYKPTVLFTAPTAYRAMLA-HPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHI 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 320 MTSNPlpEDGARkAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVCVRGAnvtSGYKGNPEANEA-AFRFGWFHTGDIGVV 397
Cdd:cd05958 254 FISAR--PGDAR-PGATGKPVpGYEAKVVDDEGNPVPDGTIGRLAVRGP---TGCRYLADKRQRtYVQGGWNITGDTYSR 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 398 DEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGE---EEVLAYCR 474
Cdd:cd05958 328 DPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPvlaRELQDHAK 407
|
330 340 350
....*....|....*....|....*....|..
gi 1002261995 475 RNLAAFKVPKKVYIADELPKTATGKIQRRIVA 506
Cdd:cd05958 408 AHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
52-503 |
1.38e-53 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 188.75 E-value: 1.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITN-----------PEG------- 113
Cdd:PRK12406 32 GVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHadllhglasalPAGvtvlsvp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 114 NVAAQAAASKLGLAHTTASlkdaAGQVHLAGFPASAAAAAKDFANDPSDValfLHTSGTTSRPKGV---PLTQRNLAASV 190
Cdd:PRK12406 112 TPPEIAAAYRISPALLTPP----AGAIDWEGWLAQQEPYDGPPVPQPQSM---IYTSGTTGHPKGVrraAPTPEQAAAAE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 191 QNIRAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTLPaagRFSASTFWADMRGAGATWYTAVPTIHqIIIDRH 270
Cdd:PRK12406 185 QMRALIYGLKPGIRALLTGPLYHSAPNAYGLRAGRLGGVLVLQP---RFDPEELLQLIERHRITHMHMVPTMF-IRLLKL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 271 TSKPEAEY--PALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEASHLMTSNPlpEDGARKAGSVGRAV-GQEMAIL 347
Cdd:PRK12406 261 PEEVRAKYdvSSLRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGAVTFATS--EDALSHPGTVGKAApGAELRFV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 348 DEEGRRVEAGKSGEVCVRGANVTS-GYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVD 426
Cdd:PRK12406 339 DEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIE 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002261995 427 SVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:PRK12406 419 AVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKR 495
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
4-503 |
1.86e-53 |
|
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: 188.10 E-value: 1.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 4 PTLTTLLKAAVATFPSRRALAVP-GKVDLSHAALDALVDAAAARLAADaGVLPGHVVALAFPNTVELVIMFLAVIRARAV 82
Cdd:cd05923 1 QTVFEMLRRAASRAPDACAIADPaRGLRLTYSELRARIEAVAARLHAR-GLRPGQRVAVVLPNSVEAVIALLALHRLGAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 83 AAPLNPAYTQEEFefylsdsgaRLLITNPEGNVAAQAAASKLGLAHTTASLKD-AAGQVHLAGFPASAAAAAKDFANDPS 161
Cdd:cd05923 80 PALINPRLKAAEL---------AELIERGEMTAAVIAVDAQVMDAIFQSGVRVlALSDLVGLGEPESAGPLIEDPPREPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 162 DVALFLHTSGTTSRPKGVPLTQRNLAASVQNI--RAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTLPAAgrF 239
Cdd:cd05923 151 QPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMstQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEE--F 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 240 SASTFWADMRGAGATWYTAVPTIHQIIIDRHTSKPEaEYPALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEAshl 319
Cdd:cd05923 229 DPADALKLIEQERVTSLFATPTHLDALAAAAEFAGL-KLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEA--- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 320 MTSNPLPedgARKAGSVGRA-VGQEMAILDEEGRRVEA---GKSGEVCV-RGANVT-SGYKGNPEANEAAFRFGWFHTGD 393
Cdd:cd05923 305 MNSLYMR---DARTGTEMRPgFFSEVRIVRIGGSPDEAlanGEEGELIVaAAADAAfTGYLNQPEATAKKLQDGWYRTGD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 394 IGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGvSLGEEEVLAYC 473
Cdd:cd05923 382 VGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG-TLSADELDQFC 460
|
490 500 510
....*....|....*....|....*....|.
gi 1002261995 474 RRN-LAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:cd05923 461 RASeLADFKRPRRYFFLDELPKNAMNKVLRR 491
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
165-498 |
6.93e-53 |
|
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: 182.12 E-value: 6.93e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 165 LFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTLPAAGRFSASTF 244
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFVRRVDAEEVLEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 245 WADMRGAGAtwYTAVPTIHQIIIDRHTSKPEAEypALRFIRSCS--ASLAPAIMEKLEAAFGApvveaYAMTEASHLMTS 322
Cdd:cd17636 84 IEAERCTHA--FLLPPTIDQIVELNADGLYDLS--SLRSSPAAPewNDMATVDTSPWGRKPGG-----YGQTEVMGLATF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 323 NPLPEDGARKAGSVGRAVgqEMAILDEEGRRVEAGKSGEVCVRGANVTSGYKGNPEANEAAFRFGWFHTGDIGVVDEEGY 402
Cdd:cd17636 155 AALGGGAIGGAGRPSPLV--QVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRGGWHHTNDLGRREPDGS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 403 LRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKV 482
Cdd:cd17636 233 LSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRARIASYKK 312
|
330
....*....|....*.
gi 1002261995 483 PKKVYIADELPKTATG 498
Cdd:cd17636 313 PKSVEFADALPRTAGG 328
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
159-500 |
1.25e-52 |
|
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: 185.61 E-value: 1.25e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 159 DPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTL---PA 235
Cdd:cd05909 145 QPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFhpnPL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 236 AGRFSASTfwadMRGAGATWYTAVPTIHQIIIDRhtSKPEaEYPALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTE 315
Cdd:cd05909 225 DYKKIPEL----IYDKKATILLGTPTFLRGYARA--AHPE-DFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 316 ASHLMTSNpLPEdGARKAGSVGRAV-GQEMAILDEEGR-RVEAGKSGEVCVRGANVTSGYKGNPEANEAAFRFGWFHTGD 393
Cdd:cd05909 298 CSPVISVN-TPQ-SPNKEGTVGRPLpGMEVKIVSVETHeEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGD 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 394 IGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVA-FGVPDAKYGEEINCAVIPREgvsLGEEEVLAY 472
Cdd:cd05909 376 IGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAvVSVPDGRKGEKIVLLTTTTD---TDPSSLNDI 452
|
330 340 350
....*....|....*....|....*....|..
gi 1002261995 473 CRR----NLAafkVPKKVYIADELPKTATGKI 500
Cdd:cd05909 453 LKNagisNLA---KPSYIHQVEEIPLLGTGKP 481
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
52-507 |
2.88e-52 |
|
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: 185.81 E-value: 2.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEGNVAAQAAASKLGLAHTTA 131
Cdd:cd17642 65 GLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIIKTII 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 SL---KDAAGQVHL-------AGFPASAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIR---AVYR 198
Cdd:cd17642 145 ILdskEDYKGYQCLytfitqnLPPGFNEYDFKPPSFDRDEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARdpiFGNQ 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 199 LTEADATVIVLPLFHVHGLLCgLLASLASGASVTLpaAGRFSASTFWADMRGAGATWYTAVPTIHqIIIDRHTSKPEAEY 278
Cdd:cd17642 225 IIPDTAILTVIPFHHGFGMFT-TLGYLICGFRVVL--MYKFEEELFLRSLQDYKVQSALLVPTLF-AFFAKSTLVDKYDL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 279 PALRFIRSCSASLAPAIMEKLEAAFGAPVV-EAYAMTEASHLMTSNPlpeDGARKAGSVGRAV-GQEMAILD-EEGRRVE 355
Cdd:cd17642 301 SNLHEIASGGAPLSKEVGEAVAKRFKLPGIrQGYGLTETTSAILITP---EGDDKPGAVGKVVpFFYAKVVDlDTGKTLG 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 356 AGKSGEVCVRGANVTSGYKGNPEANEAAF-RFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPA 434
Cdd:cd17642 378 PNERGELCVKGPMIMKGYVNNPEATKALIdKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPK 457
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002261995 435 IAQAVAFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNL-AAFKVPKKVYIADELPKTATGKIQRRIVAQ 507
Cdd:cd17642 458 IFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYVASQVsTAKRLRGGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
52-503 |
5.63e-52 |
|
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: 182.73 E-value: 5.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITnpegnvaaqaaasklglahtta 131
Cdd:cd05930 33 GVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLVLT---------------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 slkdaagqvhlagfpasaaaaakdfanDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATV-IVLP 210
Cdd:cd05930 91 ---------------------------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLqFTSF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 211 LFHVHglLCGLLASLASGAS-VTLPAAGRFSASTFWADMRGAGATWYTAVPTIHQIIIDrhtSKPEAEYPALRFIRSCSA 289
Cdd:cd05930 144 SFDVS--VWEIFGALLAGATlVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQ---ELELAALPSLRLVLVGGE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 290 SLAPAIMEKLEAAF-GAPVVEAYAMTEASHLMTSNPLPEDGARKAG-SVGRAV-GQEMAILDEEGRRVEAGKSGEVCVRG 366
Cdd:cd05930 219 ALPPDLVRRWRELLpGARLVNLYGPTEATVDATYYRVPPDDEEDGRvPIGRPIpNTRVYVLDENLRPVPPGVPGELYIGG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 367 ANVTSGYKGNPEANEAAFR----FGW---FHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAV 439
Cdd:cd05930 299 AGLARGYLNRPELTAERFVpnpfGPGermYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAA 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002261995 440 AFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:cd05930 379 VVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRK 442
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
52-502 |
3.09e-51 |
|
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: 181.49 E-value: 3.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNpegnvaaqaaasklglahtta 131
Cdd:cd05914 28 GVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS--------------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 slkdaagqvhlagfpasaaaaakdfanDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPL 211
Cdd:cd05914 87 ---------------------------DEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 FHVHGLLCGLLASLASGASVTL---PAAGRFSASTF------------WADMR-----------GAGATWYTAVPTIHQI 265
Cdd:cd05914 140 HHIYPLTFTLLLPLLNGAHVVFldkIPSAKIIALAFaqvtptlgvpvpLVIEKifkmdiipkltLKKFKFKLAKKINNRK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 266 IIDRHTSK-PEAEYPALRFIRSCSASLAPAIMEKLEAAfGAPVVEAYAMTEASHLMTSNPlpeDGARKAGSVGRAV-GQE 343
Cdd:cd05914 220 IRKLAFKKvHEAFGGNIKEFVIGGAKINPDVEEFLRTI-GFPYTIGYGMTETAPIISYSP---PNRIRLGSAGKVIdGVE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 344 MAILDEEGRRVEagksGEVCVRGANVTSGYKGNPEANEAAF-RFGWFHTGDIGVVDEEGYLRLVGRIKELINRG-GEKIS 421
Cdd:cd05914 296 VRIDSPDPATGE----GEIIVRGPNVMKGYYKNPEATAEAFdKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIY 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 422 PIEVDSVLLGHPAIA-----------QAVAFGVPDAKYGEEINcavIPREGVSLgEEEVLAYCRRNLAAFKVPKKVYI-A 489
Cdd:cd05914 372 PEEIEAKINNMPFVLeslvvvqekklVALAYIDPDFLDVKALK---QRNIIDAI-KWEVRDKVNQKVPNYKKISKVKIvK 447
|
490
....*....|...
gi 1002261995 490 DELPKTATGKIQR 502
Cdd:cd05914 448 EEFEKTPKGKIKR 460
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
168-516 |
4.76e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 182.60 E-value: 4.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 168 HTSGTTSRPKGVPLTQRN--LAASVQNIRAVYRLTEADATVIVLPLFHVHGLlcGLLASLA-SGASVTLPAAGRFSASTF 244
Cdd:PRK07008 183 YTSGTTGNPKGALYSHRStvLHAYGAALPDAMGLSARDAVLPVVPMFHVNAW--GLPYSAPlTGAKLVLPGPDLDGKSLY 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 245 WAdMRGAGATWYTAVPTIHQIIIDrHTSKPEAEYPALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEASHLMTS-- 322
Cdd:PRK07008 261 EL-IEAERVTFSAGVPTVWLGLLN-HMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLck 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 323 -----NPLPEDGARKA-GSVGRAV-GQEMAILDEEGRRVE-AGKS-GEVCVRGANVTSGYKGNpeaNEAAFRFGWFHTGD 393
Cdd:PRK07008 339 lkwkhSQLPLDEQRKLlEKQGRVIyGVDMKIVGDDGRELPwDGKAfGDLQVRGPWVIDRYFRG---DASPLVDGWFPTGD 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 394 IGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYC 473
Cdd:PRK07008 416 VATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELLAFY 495
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1002261995 474 RRNLAAFKVPKKVYIADELPKTATGKIQRRIVAQHFVVPVLPT 516
Cdd:PRK07008 496 EGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQFRDYVLPT 538
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
158-503 |
1.22e-50 |
|
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: 179.37 E-value: 1.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 158 NDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADaTVIVLPLFH----VHGLLCgllaSLASGASVTL 233
Cdd:cd05945 94 ADGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGD-VFLNQAPFSfdlsVMDLYP----ALASGATLVP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 234 --PAAGRFSASTFwADMRGAGATWYTAVPTIHQIIIDRHTSKPEaEYPALRFIRSCSASLAPAIMEKLEAAF-GAPVVEA 310
Cdd:cd05945 169 vpRDATADPKQLF-RFLAEHGITVWVSTPSFAAMCLLSPTFTPE-SLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNT 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 311 YAMTEASHLMTSNPLPEDGARKAGSV--GRAV-GQEMAILDEEGRRVEAGKSGEVCVRGANVTSGYKGNPEANEAAFRF- 386
Cdd:cd05945 247 YGPTEATVAVTYIEVTPEVLDGYDRLpiGYAKpGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPd 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 387 ---GWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVS 463
Cdd:cd05945 327 egqRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAE 406
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1002261995 464 LG-EEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:cd05945 407 AGlTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRK 447
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
159-503 |
3.54e-49 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 177.53 E-value: 3.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 159 DPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTLPAagR 238
Cdd:PRK13388 148 DAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPA--K 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 239 FSASTFWADMRGAGATWYTAVPTIHQIIIDRHTSKPEAEYPaLRFIRSCSASlaPAIMEKLEAAFGAPVVEAYAMTEASH 318
Cdd:PRK13388 226 FSASGFLDDVRRYGATYFNYVGKPLAYILATPERPDDADNP-LRVAFGNEAS--PRDIAEFSRRFGCQVEDGYGSSEGAV 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 319 LMTsnplPEDGArKAGSVGRAV----------GQE--MAILDEEGRRVEAGKS-GE-VCVRGANVTSGYKGNPEANEAAF 384
Cdd:PRK13388 303 IVV----REPGT-PPGSIGRGApgvaiynpetLTEcaVARFDAHGALLNADEAiGElVNTAGAGFFEGYYNNPEATAERM 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 385 RFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSL 464
Cdd:PRK13388 378 RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATF 457
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1002261995 465 GEEEVLAY--CRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:PRK13388 458 DPDAFAAFlaAQPDLGTKAWPRYVRIAADLPSTATNKVLKR 498
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
169-502 |
5.42e-49 |
|
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: 171.43 E-value: 5.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 169 TSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLcGLLASLASGASVTLpaAGRFSASTFWADM 248
Cdd:cd17633 8 TSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLY-GAISALYLGGTFIG--QRKFNPKSWIRKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 249 RGAGATWYTAVPT-IHQII-IDRHTSKpeaeypaLRFIRSCSASLAPAIMEKLEAAF-GAPVVEAYAMTEAShLMTSNpL 325
Cdd:cd17633 85 NQYNATVIYLVPTmLQALArTLEPESK-------IKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSELS-FITYN-F 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 326 PEDgARKAGSVGRAV-GQEMAILDEEGrrveaGKSGEVCVRGANVTSGYKGNPEANEAafrfGWFHTGDIGVVDEEGYLR 404
Cdd:cd17633 156 NQE-SRPPNSVGRPFpNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNPD----GWMSVGDIGYVDEEGYLY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 405 LVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGeEINCAVIprEGVSLGEEEVLAYCRRNLAAFKVPK 484
Cdd:cd17633 226 LVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFG-EIAVALY--SGDKLTYKQLKRFLKQKLSRYEIPK 302
|
330
....*....|....*...
gi 1002261995 485 KVYIADELPKTATGKIQR 502
Cdd:cd17633 303 KIIFVDSLPYTSSGKIAR 320
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
159-506 |
7.48e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 176.41 E-value: 7.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 159 DPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTLPAagR 238
Cdd:PRK07867 150 DPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRR--K 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 239 FSASTFWADMRGAGATWYTAVPTIHQIIIDRHTSKPEAEYPaLRFIRSCSAslAPAIMEKLEAAFGAPVVEAYAMTEASH 318
Cdd:PRK07867 228 FSASGFLPDVRRYGATYANYVGKPLSYVLATPERPDDADNP-LRIVYGNEG--APGDIARFARRFGCVVVDGFGSTEGGV 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 319 LMTSNPlpedgARKAGSVGRAVGQeMAILDEE-------------GRRVEAGKSGE-VCVRGANVTSGYKGNPEANEAAF 384
Cdd:PRK07867 305 AITRTP-----DTPPGALGPLPPG-VAIVDPDtgtecppaedadgRLLNADEAIGElVNTAGPGGFEGYYNDPEADAERM 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 385 RFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKI--SPIEvdSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGV 462
Cdd:PRK07867 379 RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLgtAPIE--RILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGA 456
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1002261995 463 SLGEEEVLAY--CRRNLAAFKVPKKVYIADELPKTATGKIQRRIVA 506
Cdd:PRK07867 457 KFDPDAFAEFlaAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLS 502
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
159-503 |
1.94e-48 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 175.84 E-value: 1.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 159 DPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQN----IRAVYRLTEADATVIV-LPLFHVHGLLCGLLASLASGASVTL 233
Cdd:PRK08751 206 EPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQahqwLAGTGKLEEGCEVVITaLPLYHIFALTANGLVFMKIGGCNHL 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 234 PAAGRfSASTFWADMRGAGATWYTAVPTIHQIIIDRhTSKPEAEYPALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAM 313
Cdd:PRK08751 286 ISNPR-DMPGFVKELKKTRFTAFTGVNTLFNGLLNT-PGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 314 TEASHLMTSNPLpeDGARKAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVCVRGANVTSGYKGNPEANEAAFRF-GWFHT 391
Cdd:PRK08751 364 TETSPAACINPL--TLKEYNGSIGLPIpSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDAdGWLHT 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 392 GDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINcAVIPREGVSLGEEEVLA 471
Cdd:PRK08751 442 GDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVK-VVIVKKDPALTAEDVKA 520
|
330 340 350
....*....|....*....|....*....|..
gi 1002261995 472 YCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:PRK08751 521 HARANLTGYKQPRIIEFRKELPKTNVGKILRR 552
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
52-503 |
1.22e-47 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 173.49 E-value: 1.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEgNVaaqaaaSKLG-LAHTT 130
Cdd:PLN02574 88 GVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPE-NV------EKLSpLGVPV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 131 ASLKDAagqVHLAGFPASAAAAAKDFANDPS----------DVALFLHTSGTTSRPKGVPLTQRNLAASVQN-IRAVYRL 199
Cdd:PLN02574 161 IGVPEN---YDFDSKRIEFPKFYELIKEDFDfvpkpvikqdDVAAIMYSSGTTGASKGVVLTHRNLIAMVELfVRFEASQ 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 200 TEADAT----VIVLPLFHVHGLLCGLLASLASGASVTLpaAGRFSASTFWADMRGAGATWYTAVPTIHQIIIdrHTSKPE 275
Cdd:PLN02574 238 YEYPGSdnvyLAALPMFHIYGLSLFVVGLLSLGSTIVV--MRRFDASDMVKVIDRFKVTHFPVVPPILMALT--KKAKGV 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 276 AEYPaLRFIRSCSASLAP----AIMEKLEAAFGAPVVEAYAMTEASHLMTSNpLPEDGARKAGSVGR-AVGQEMAILD-E 349
Cdd:PLN02574 314 CGEV-LKSLKQVSCGAAPlsgkFIQDFVQTLPHVDFIQGYGMTESTAVGTRG-FNTEKLSKYSSVGLlAPNMQAKVVDwS 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 350 EGRRVEAGKSGEVCVRGANVTSGYKGNPEANEA-AFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSV 428
Cdd:PLN02574 392 TGCLLPPGNCGELWIQGPGVMKGYLNNPKATQStIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAV 471
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002261995 429 LLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:PLN02574 472 LISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRR 546
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
168-518 |
3.33e-47 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 172.24 E-value: 3.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 168 HTSGTTSRPKGVPLTQRN--LAASVQNIRAVYRLTEADATVIVLPLFHVHGLlcGLLASL-ASGASVTLPAAgRFSASTF 244
Cdd:PRK06018 184 YTSGTTGDPKGVLYSHRSnvLHALMANNGDALGTSAADTMLPVVPLFHANSW--GIAFSApSMGTKLVMPGA-KLDGASV 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 245 WADMRGAGATWYTAVPTIHQIIIdRHTSKPEAEYPALRFIrSCSASLAPAIMEKLEAAFGAPVVEAYAMTEASHLMTSNP 324
Cdd:PRK06018 261 YELLDTEKVTFTAGVPTVWLMLL-QYMEKEGLKLPHLKMV-VCGGSAMPRSMIKAFEDMGVEVRHAWGMTEMSPLGTLAA 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 325 LPEDGARKAGSV--------GRA-VGQEMAILDEEGRRVEA-GKS-GEVCVRGANVTSGY-KGNPEANEAAfrfGWFHTG 392
Cdd:PRK06018 339 LKPPFSKLPGDArldvlqkqGYPpFGVEMKITDDAGKELPWdGKTfGRLKVRGPAVAAAYyRVDGEILDDD---GFFDTG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 393 DIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEEEVLAY 472
Cdd:PRK06018 416 DVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEILKY 495
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1002261995 473 CRRNLAAFKVPKKVYIADELPKTATGKIQRRIVAQHFVVPVLPTKA 518
Cdd:PRK06018 496 MDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQFKDYKLPTAA 541
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
54-509 |
3.40e-47 |
|
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: 172.04 E-value: 3.40e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 54 LPGHVVALAFPNTVELVIMFLAVIRARAVAAPL---NPAYTQEEFEFYLSDSGARLLITNPE------GNVAAQAAASKL 124
Cdd:cd05931 46 KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLpppTPGRHAERLAAILADAGPRVVLTTAAalaavrAFAASRPAAGTP 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 125 GLAHTTASLKDAAGQVHLAGFpasaaaaakdfanDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADA 204
Cdd:cd05931 126 RLLVVDLLPDTSAADWPPPSP-------------DPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 205 TVIVLPLFHVHGLLCGLLASLASGASVTLPAAGRFSASTF-WADMRGA-GATWyTAVPTI-HQIIIDRHTSKPEAEY--P 279
Cdd:cd05931 193 VVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAAFLRRPLrWLRLISRyRATI-SAAPNFaYDLCVRRVRDEDLEGLdlS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 280 ALRFIRSCSASLAPAIMEKLEAAFgAP-------VVEAYAMTEASHLMTSNPL-----------------------PEDG 329
Cdd:cd05931 272 SWRVALNGAEPVRPATLRRFAEAF-APfgfrpeaFRPSYGLAEATLFVSGGPPgtgpvvlrvdrdalagravavaaDDPA 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 330 ARKAGSVGRAV-GQEMAILDEEGRR-VEAGKSGEVCVRGANVTSGYKGNPEANEAAFRF-------GWFHTGDIGVVDeE 400
Cdd:cd05931 351 ARELVSCGRPLpDQEVRIVDPETGReLPDGEVGEIWVRGPSVASGYWGRPEATAETFGAlaatdegGWLRTGDLGFLH-D 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 401 GYLRLVGRIKELINRGGEKISP--IEvDSVLLGHPAI--AQAVAFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRRN 476
Cdd:cd05931 430 GELYITGRLKDLIIVRGRNHYPqdIE-ATAEEAHPALrpGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAA 508
|
490 500 510
....*....|....*....|....*....|....*..
gi 1002261995 477 LA-AFKV-PKKVYI--ADELPKTATGKIQRRIVAQHF 509
Cdd:cd05931 509 VArEHGVaPADVVLvrPGSIPRTSSGKIQRRACRAAY 545
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
52-500 |
1.16e-46 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 169.80 E-value: 1.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNP--EGNVAAQAAASKLGLAHt 129
Cdd:PRK13390 45 GLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVASAalDGLAAKVGADLPLRLSF- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 130 taslkdaAGQVHLAGFPASAAAAAKDFANDPSDVALFLHTSGTTSRPKGV--PLTQRNLAAS----VQNIRAVYRLTEAD 203
Cdd:PRK13390 124 -------GGEIDGFGSFEAALAGAGPRLTEQPCGAVMLYSSGTTGFPKGIqpDLPGRDVDAPgdpiVAIARAFYDISESD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 204 ATVIVLPLFHVHGL-LCGLLASLasGASVTLpaAGRFSASTFWADMRGAGATWYTAVPTIHQIIIDRHTS-KPEAEYPAL 281
Cdd:PRK13390 197 IYYSSAPIYHAAPLrWCSMVHAL--GGTVVL--AKRFDAQATLGHVERYRITVTQMVPTMFVRLLKLDADvRTRYDVSSL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 282 RFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEAsHLMTSNPLPeDGARKAGSVGRAVGQEMAILDEEGRRVEAGKSGE 361
Cdd:PRK13390 273 RAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEA-HGMTFIDSP-DWLAHPGSVGRSVLGDLHICDDDGNELPAGRIGT 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 362 VCVRGANVTSGYKGNPE----ANEAAFRFgWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQ 437
Cdd:PRK13390 351 VYFERDRLPFRYLNDPEktaaAQHPAHPF-WTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHD 429
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002261995 438 AVAFGVPDAKYGEEINCAVIPREGVSLGEE---EVLAYCRRNLAAFKVPKKVYIADELPKTATGKI 500
Cdd:PRK13390 430 VAVIGVPDPEMGEQVKAVIQLVEGIRGSDElarELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKL 495
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
162-508 |
4.64e-46 |
|
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: 168.83 E-value: 4.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 162 DVALFLHTSGTTSRPKGV------PLTQRNLAASVQNIRAVYR-LTEADATVIVLplfhVHGLLCGllaSLASGASVTLP 234
Cdd:cd05970 186 DILLVYFSSGTTGMPKMVehdftyPLGHIVTAKYWQNVREGGLhLTVADTGWGKA----VWGKIYG---QWIAGAAVFVY 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 235 AAGRFSASTFWADMRGAGATWYTAVPTIHQIIIDRHTSKpeAEYPALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMT 314
Cdd:cd05970 259 DYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSR--YDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQT 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 315 EASHLMTSNPLPEDgarKAGSVGR-AVGQEMAILDEEGRRVEAGKSGEVCVRGAN-----VTSGYKGNPEANEAAFRFGW 388
Cdd:cd05970 337 ETTLTIATFPWMEP---KPGSMGKpAPGYEIDLIDREGRSCEAGEEGEIVIRTSKgkpvgLFGGYYKDAEKTAEVWHDGY 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 389 FHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEE- 467
Cdd:cd05970 414 YHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEEl 493
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1002261995 468 --EVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRRIVAQH 508
Cdd:cd05970 494 kkELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRER 536
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
165-503 |
4.65e-46 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 168.78 E-value: 4.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 165 LFLHTSGTTSRPKGvplTQRNLAASVQNIRAVYRLTEADA---TVIVLPLFHVHGLLCGLLASLASGASVTlpaAGRFSA 241
Cdd:PRK13382 200 VILLTSGTTGTPKG---ARRSGPGGIGTLKAILDRTPWRAeepTVIVAPMFHAWGFSQLVLAASLACTIVT---RRRFDP 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 242 STFWADMRGAGATWYTAVPTIhqiiIDRHTSKPE-----AEYPALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEA 316
Cdd:PRK13382 274 EATLDLIDRHRATGLAVVPVM----FDRIMDLPAevrnrYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 317 SHLMTSNPlpEDGARKAGSVGR-AVGQEMAILDEEGRRVEAGKSGEVCVRGANVTSGYKGNPEANeaaFRFGWFHTGDIG 395
Cdd:PRK13382 350 GMIATATP--ADLRAAPDTAGRpAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSGSTKD---FHDGFMASGDVG 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 396 VVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRR 475
Cdd:PRK13382 425 YLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRD 504
|
330 340
....*....|....*....|....*...
gi 1002261995 476 NLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:PRK13382 505 NLANYKVPRDIVVLDELPRGATGKILRR 532
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
91-505 |
7.66e-46 |
|
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: 166.78 E-value: 7.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 91 TQEEFEFYLSDSGARLLITNPEGnvaaqAAASKLGLAHTTASLKDAAGQVHLAGFPASAAAAAKDFANDPSDVA---LFL 167
Cdd:cd05929 57 FAAAAAWKCGACPAYKSSRAPRA-----EACAIIEIKAAALVCGLFTGGGALDGLEDYEAAEGGSPETPIEDEAagwKML 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 168 HTSGTTSRPKGVpltQRNLAASVQNIRAV------YRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTLPaagRFSA 241
Cdd:cd05929 132 YSGGTTGRPKGI---KRGLPGGPPDNDTLmaaalgFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLME---KFDP 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 242 STFWADMRGAGATWYTAVPTIHQiiidRHTSKPEAEYPA-----LRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEA 316
Cdd:cd05929 206 EEFLRLIERYRVTFAQFVPTMFV----RLLKLPEAVRNAydlssLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEG 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 317 SHLMTSNPlpEDGARKAGSVGRAVGQEMAILDEEGRRVEAGKSGEVCVRGA---NVTSGYKGNPEANEAAfrfGWFHTGD 393
Cdd:cd05929 282 QGLTIING--EEWLTHPGSVGRAVLGKVHILDEDGNEVPPGEIGEVYFANGpgfEYTNDPEKTAAARNEG---GWSTLGD 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 394 IGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGE---EEVL 470
Cdd:cd05929 357 VGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTalaEELI 436
|
410 420 430
....*....|....*....|....*....|....*
gi 1002261995 471 AYCRRNLAAFKVPKKVYIADELPKTATGKIQRRIV 505
Cdd:cd05929 437 AFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
161-502 |
1.21e-45 |
|
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: 163.20 E-value: 1.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 161 SDVALFLHTSGTTSRPKGVPLTQRNLAASVQNI-RAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTlpAAGRF 239
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILqKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVT--GGENT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 240 SASTFWADMRGAGATWYTAVPTIHQIIIDRHTSKpEAEYPALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEAShl 319
Cdd:cd17635 79 TYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSA-NATVPSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETG-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 320 mTSNPLP-EDGARKAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVCVRGANVTSGYKGNPEANEAAFRFGWFHTGDIGVV 397
Cdd:cd17635 156 -TALCLPtDDDSIEINAVGRPYpGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLGER 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 398 DEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPR----EGVSLGEEEVLayc 473
Cdd:cd17635 235 REDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASaeldENAIRALKHTI--- 311
|
330 340
....*....|....*....|....*....
gi 1002261995 474 RRNLAAFKVPKKVYIADELPKTATGKIQR 502
Cdd:cd17635 312 RRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
52-509 |
2.51e-45 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 167.28 E-value: 2.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNpegnvaaqAAASKLGLAHTTA 131
Cdd:PLN02860 53 GLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTD--------ETCSSWYEELQND 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 SLKDAAGQVHLAGFPASAAAAAKDFAND------------------PSDVALFLHTSGTTSRPKGVPLTQRNLAA-SVQN 192
Cdd:PLN02860 125 RLPSLMWQVFLESPSSSVFIFLNSFLTTemlkqralgtteldyawaPDDAVLICFTSGTTGRPKGVTISHSALIVqSLAK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 193 IrAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTLPaagRFSASTFWADMRGAGATWYTAVPTIHQIIID-RHT 271
Cdd:PLN02860 205 I-AIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLP---KFDAKAALQAIKQHNVTSMITVPAMMADLISlTRK 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 272 SKPEAEYPALRFIRSCSASLAPAIMEKLEAAF-GAPVVEAYAMTEASHLMT------------SNPLPEDGARKAGSV-- 336
Cdd:PLN02860 281 SMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFpNAKLFSAYGMTEACSSLTfmtlhdptlespKQTLQTVNQTKSSSVhq 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 337 --GRAVGQ-----EMAILDEEGRRVeagksGEVCVRGANVTSGYKG-NPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGR 408
Cdd:PLN02860 361 pqGVCVGKpaphvELKIGLDESSRV-----GRILTRGPHVMLGYWGqNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGR 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 409 IKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREG--------------VSLGEEEVLAYCR 474
Cdd:PLN02860 436 SNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGwiwsdnekenakknLTLSSETLRHHCR 515
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1002261995 475 -RNLAAFKVPKKVYI-ADELPKTATGKIQR----RIVAQHF 509
Cdd:PLN02860 516 eKNLSRFKIPKLFVQwRKPFPLTTTGKIRRdevrREVLSHL 556
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
52-504 |
3.12e-45 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 166.99 E-value: 3.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEgnVAAQAAASKL-GLAH-- 128
Cdd:PRK04319 94 GVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPA--LLERKPADDLpSLKHvl 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 129 -TTASLKDAAGQVHLAGFPASAAAAAKDFANDPSDVALFLHTSGTTSRPKGV------PLTQRNLAASVQNIRA--VYRL 199
Cdd:PRK04319 172 lVGEDVEEGPGTLDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVlhvhnaMLQHYQTGKYVLDLHEddVYWC 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 200 TeADatvivlPLFhVHGLLCGLLASLASGASvTLPAAGRFSASTFWADMRGAGAT-WYTAvPTIHQIIIdRHTSKPEAEY 278
Cdd:PRK04319 252 T-AD------PGW-VTGTSYGIFAPWLNGAT-NVIDGGRFSPERWYRILEDYKVTvWYTA-PTAIRMLM-GAGDDLVKKY 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 279 --PALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEASHLMTSNPLPEDgaRKAGSVGRAV-GQEMAILDEEGRRVE 355
Cdd:PRK04319 321 dlSSLRHILSVGEPLNPEVVRWGMKVFGLPIHDNWWMTETGGIMIANYPAMD--IKPGSMGKPLpGIEAAIVDDQGNELP 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 356 AGKSGEVCVRGA--NVTSGYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHP 433
Cdd:PRK04319 399 PNRMGNLAIKKGwpSMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHP 478
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002261995 434 AIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEE---EVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRRI 504
Cdd:PRK04319 479 AVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEElkeEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRV 552
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
168-505 |
9.14e-45 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 165.79 E-value: 9.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 168 HTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTLPaagRFSASTFWAD 247
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNGWCFTWTLAALCGTNICLR---QVTAKAIYSA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 248 MRGAGATWYTAVPTIHQIIIDrhTSKPEAEYPALRFIRSCSASLAP-----AIMEKLeaafGAPVVEAYAMTEASHLMT- 321
Cdd:PLN02479 279 IANYGVTHFCAAPVVLNTIVN--APKSETILPLPRVVHVMTAGAAPppsvlFAMSEK----GFRVTHTYGLSETYGPSTv 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 322 --------SNPlPEDGARKAGSVG-RAVGQE-MAILD-EEGRRVEA-GKS-GEVCVRGANVTSGYKGNPEANEAAFRFGW 388
Cdd:PLN02479 353 cawkpewdSLP-PEEQARLNARQGvRYIGLEgLDVVDtKTMKPVPAdGKTmGEIVMRGNMVMKGYLKNPKANEEAFANGW 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 389 FHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEEE 468
Cdd:PLN02479 432 FHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEA 511
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1002261995 469 VLA-----YCRRNLAAFKVPKKVyIADELPKTATGKIQRRIV 505
Cdd:PLN02479 512 ALAedimkFCRERLPAYWVPKSV-VFGPLPKTATGKIQKHVL 552
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
52-440 |
1.63e-44 |
|
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: 161.66 E-value: 1.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEgnvaAQAAASKLGLAHTTA 131
Cdd:TIGR01733 21 GVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSA----LASRLAGLVLPVILL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 SlkdaagQVHLAGFPASAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADatviVLPL 211
Cdd:TIGR01733 97 D------PLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDD----RVLQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 FHVHGL---LCGLLASLASGAS-VTLPAAGRFSASTFWADMRGAGA-TWYTAVPTIHQIIIDRHtskpEAEYPALRFIRS 286
Cdd:TIGR01733 167 FASLSFdasVEEIFGALLAGATlVVPPEDEERDDAALLAALIAEHPvTVLNLTPSLLALLAAAL----PPALASLRLVIL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 287 CSASLAPAIMEKLEAAFG-APVVEAYAMTEASHLMTSNPLPEDGARKAGSV--GRAV-GQEMAILDEEGRRVEAGKSGEV 362
Cdd:TIGR01733 243 GGEALTPALVDRWRARGPgARLINLYGPTETTVWSTATLVDPDDAPRESPVpiGRPLaNTRLYVLDDDLRPVPVGVVGEL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 363 CVRGANVTSGYKGNPEANEAAF---------RFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHP 433
Cdd:TIGR01733 323 YIGGPGVARGYLNRPELTAERFvpdpfaggdGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHP 402
|
....*..
gi 1002261995 434 AIAQAVA 440
Cdd:TIGR01733 403 GVREAVV 409
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
85-503 |
9.29e-44 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 162.17 E-value: 9.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 85 PLNPAYTQEEFEFYLSDSGARLLITN-PEGNVAAQAAASKLGLAHTTASLKDAAGQvHLAGFPASAAAAAKDFANDPSDV 163
Cdd:PRK13391 78 CVNSHLTPAEAAYIVDDSGARALITSaAKLDVARALLKQCPGVRHRLVLDGDGELE-GFVGYAEAVAGLPATPIADESLG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 164 ALFLHTSGTTSRPKGV--------PLTQRNLAASVQNIravYRLTEADATVIVLPLFHVHGL-LCGLLASLasGASVTLp 234
Cdd:PRK13391 157 TDMLYSSGTTGRPKGIkrplpeqpPDTPLPLTAFLQRL---WGFRSDMVYLSPAPLYHSAPQrAVMLVIRL--GGTVIV- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 235 aAGRFSASTFWADMRGAGATWYTAVPTIhqiiIDRHTSKPEA-----EYPALRFIRSCSASLAPAIMEKLEAAFGAPVVE 309
Cdd:PRK13391 231 -MEHFDAEQYLALIEEYGVTHTQLVPTM----FSRMLKLPEEvrdkyDLSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 310 AYAMTEASHLMTSNPlpEDGARKAGSVGRAVGQEMAILDEEGRRVEAGKSGEVCVRGANVTSgYKGNPEANEAAF--RFG 387
Cdd:PRK13391 306 YYAATEGLGFTACDS--EEWLAHPGTVGRAMFGDLHILDDDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARhpDGT 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 388 WFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGE- 466
Cdd:PRK13391 383 WSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPa 462
|
410 420 430
....*....|....*....|....*....|....*....
gi 1002261995 467 --EEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:PRK13391 463 laAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKR 501
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
52-503 |
5.86e-43 |
|
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: 158.63 E-value: 5.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITnpegnvaaqaaasklglahtta 131
Cdd:cd17643 33 GVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLLLT---------------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 slkdaagqvhlagfpasaaaaakdfanDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVivlpL 211
Cdd:cd17643 91 ---------------------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWT----L 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 FH----------VHGllcgllaSLASGAS-VTLPAAGRFSASTFWADMRGAGATWYTAVPTIHQIIIDRHTSKPEAEyPA 280
Cdd:cd17643 140 FHsyafdfsvweIWG-------ALLHGGRlVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDP-LA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 281 LRFIRSCSASLAPAIMEKLEAAFGAP---VVEAYAMTEASHLMTSNPL-PEDGARKAGSV-GRAV-GQEMAILDEEGRRV 354
Cdd:cd17643 212 LRYVIFGGEALEAAMLRPWAGRFGLDrpqLVNMYGITETTVHVTFRPLdAADLPAAAASPiGRPLpGLRVYVLDADGRPV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 355 EAGKSGEVCVRGANVTSGYKGNPEanEAAFRFG----------WFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIE 424
Cdd:cd17643 292 PPGVVGELYVSGAGVARGYLGRPE--LTAERFVanpfggpgsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGE 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002261995 425 VDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:cd17643 370 IEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRA 448
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
52-503 |
1.55e-42 |
|
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: 158.21 E-value: 1.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPegnvAAQAAASKLGLAHTTA 131
Cdd:cd17646 44 GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLTTA----DLAARLPAGGDVALLG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 SLKDAAGQVHLAGFPAsaaaaakdfanDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPL 211
Cdd:cd17646 120 DEALAAPPATPPLVPP-----------RPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 -FHVHglLCGLLASLASGASVTLPAAGRFSASTFWAD-MRGAGATWYTAVPTIHQIIIDrhtsKPEAE-YPALRFIRSCS 288
Cdd:cd17646 189 sFDVS--VWELFWPLVAGARLVVARPGGHRDPAYLAAlIREHGVTTCHFVPSMLRVFLA----EPAAGsCASLRRVFCSG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 289 ASLAPAIMEKLEAAFGAPVVEAYAMTEASHLMTSNPLPEDGARKAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVCVRGA 367
Cdd:cd17646 263 EALPPELAARFLALPGAELHNLYGPTEAAIDVTHWPVRGPAETPSVPIGRPVpNTRLYVLDDALRPVPVGVPGELYLGGV 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 368 NVTSGYKGNPEANEAAFRFGWF-------HTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVA 440
Cdd:cd17646 343 QLARGYLGRPALTAERFVPDPFgpgsrmyRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVV 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002261995 441 FGVPDAKYGEEINCAVIPREG-VSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:cd17646 423 VARAAPAGAARLVGYVVPAAGaAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRA 486
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
59-502 |
4.16e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 156.86 E-value: 4.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 59 VALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNpegnvaaqaaasklglAHTTASLKDAAG 138
Cdd:PRK07638 53 IAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTE----------------RYKLNDLPDEEG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 139 QVHLA---GFPASAAAAAKDFANDPSDVALFL-HTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHV 214
Cdd:PRK07638 117 RVIEIdewKRMIEKYLPTYAPIENVQNAPFYMgFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 215 HgLLCGLLASLASGASVTLPAagRFSASTFWADMRGAGATWYTAVPTIhqiiidrhtskPEAEYPALRFIRS-----CSA 289
Cdd:PRK07638 197 L-FLYGAISTLYVGQTVHLMR--KFIPNQVLDKLETENISVMYTVPTM-----------LESLYKENRVIENkmkiiSSG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 290 SLAPAI-MEKLEAAFgaPVVEAYAMTEASHL-MTSNPLPEDGARKAGSVGRAVGQ-EMAILDEEGRRVEAGKSGEVCVRG 366
Cdd:PRK07638 263 AKWEAEaKEKIKNIF--PYAKLYEFYGASELsFVTALVDEESERRPNSVGRPFHNvQVRICNEAGEEVQKGEIGTVYVKS 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 367 ANVTSGYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDA 446
Cdd:PRK07638 341 PQFFMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDS 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002261995 447 KYGeEINCAVIprEGvSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQR 502
Cdd:PRK07638 421 YWG-EKPVAII--KG-SATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIAR 472
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
52-499 |
4.98e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 157.74 E-value: 4.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPE--GNVAAqaAASKLGLAHT 129
Cdd:PRK07798 49 GLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVYEREfaPRVAE--VLPRLPKLRT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 130 TASLKDAAGQ------VHLAGFPASAAAAAKDFANDPSDVaLFLHTSGTTSRPKGVPLTQRNL---------AASVQNIR 194
Cdd:PRK07798 127 LVVVEDGSGNdllpgaVDYEDALAAGSPERDFGERSPDDL-YLLYTGGTTGMPKGVMWRQEDIfrvllggrdFATGEPIE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 195 AVYRLTEADA------TVIVLPLFHVHGLLcGLLASLASGASVTLPAAGRFSASTFWADMRGAGATWYTAV------Pti 262
Cdd:PRK07798 206 DEEELAKRAAagpgmrRFPAPPLMHGAGQW-AAFAALFSGQTVVLLPDVRFDADEVWRTIEREKVNVITIVgdamarP-- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 263 hqiIIDRHTSKPEAEYPALRFIRSCSASLAPAIMEKLEAAF-GAPVVEAYAMTEASHLMTSnpLPEDGARKAGSVGRAVG 341
Cdd:PRK07798 283 ---LLDALEARGPYDLSSLFAIASGGALFSPSVKEALLELLpNVVLTDSIGSSETGFGGSG--TVAKGAVHTGGPRFTIG 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 342 QEMAILDEEGRRVEAGkSGEVCV--RGANVTSGYKGNPEANEAAFR-FG---WFHTGDIGVVDEEGYLRLVGRIKELINR 415
Cdd:PRK07798 358 PRTVVLDEDGNPVEPG-SGEIGWiaRRGHIPLGYYKDPEKTAETFPtIDgvrYAIPGDRARVEADGTITLLGRGSVCINT 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 416 GGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKT 495
Cdd:PRK07798 437 GGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRS 516
|
....
gi 1002261995 496 ATGK 499
Cdd:PRK07798 517 PAGK 520
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
52-502 |
6.13e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 157.60 E-value: 6.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLI----------------TNPEGNV 115
Cdd:PRK06164 56 GVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVvwpgfkgidfaailaaVPPDALP 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 116 AAQAAASKLGLAHTTASLKDAAGQVHLAGFPASAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRA 195
Cdd:PRK06164 136 PLRAIAVVDDAADATPAPAPGARVQLFALPDPAPPAAAGERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIAR 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 196 VYRLTEADATVIVLPLFHVHGLlCGLLASLASGAS-VTLPAagrFSASTFWADMRGAGATWYTAVPTIHQIIIDrhTSKP 274
Cdd:PRK06164 216 AYGYDPGAVLLAALPFCGVFGF-STLLGALAGGAPlVCEPV---FDAARTARALRRHRVTHTFGNDEMLRRILD--TAGE 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 275 EAEYPALRfiRSCSASLAPAIMEKLEAAF--GAPVVEAYAMTEASHLMTSNPLPEDGARKAGSVGRAV--GQEMAILD-E 349
Cdd:PRK06164 290 RADFPSAR--LFGFASFAPALGELAALARarGVPLTGLYGSSEVQALVALQPATDPVSVRIEGGGRPAspEARVRARDpQ 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 350 EGRRVEAGKSGEVCVRGANVTSGYKGNPEANEAAFRF-GWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSV 428
Cdd:PRK06164 368 DGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDdGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHA 447
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002261995 429 LLGHPAIAQAVAFGVPDAKYGEEInCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATG---KIQR 502
Cdd:PRK06164 448 LEALPGVAAAQVVGATRDGKTVPV-AFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQK 523
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
158-507 |
8.27e-42 |
|
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: 158.25 E-value: 8.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 158 NDPSDValfLHTSGTTSRPKGVpltQRN----LAASVQNIRAVYRL-------TEADATVIVLPLFHVHG-LLCGLLASL 225
Cdd:cd05967 230 TDPLYI---LYTSGTTGKPKGV---VRDngghAVALNWSMRNIYGIkpgdvwwAASDVGWVVGHSYIVYGpLLHGATTVL 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 226 ASGASVTLPAAGrfsasTFWADMRGAGATWYTAVPTIHQIIidrHTSKPEAEY------PALRFIRSCSASLAPAIMEKL 299
Cdd:cd05967 304 YEGKPVGTPDPG-----AFWRVIEKYQVNALFTAPTAIRAI---RKEDPDGKYikkydlSSLRTLFLAGERLDPPTLEWA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 300 EAAFGAPVVEAYAMTEASHLMTSNPLP-EDGARKAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVCVRGA---NVTSGYK 374
Cdd:cd05967 376 ENTLGVPVIDHWWQTETGWPITANPVGlEPLPIKAGSPGKPVpGYQVQVLDEDGEPVGPNELGNIVIKLPlppGCLLTLW 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 375 GNPEANEAAF--RF-GWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEE 451
Cdd:cd05967 456 KNDERFKKLYlsKFpGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQV 535
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 452 INCAVIPREGVSLGEE----EVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRRIVAQ 507
Cdd:cd05967 536 PLGLVVLKEGVKITAEelekELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRK 595
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
52-502 |
1.34e-40 |
|
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: 153.59 E-value: 1.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLS---------DSGarLLITNPEGnVAAQAAAS 122
Cdd:cd05906 60 GLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPNARLRklrhiwqllGSP--VVLTDAEL-VAEFAGLE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 123 KLGL-----AHTTASLKDAAGQVHLAGFpasaaaaakdfanDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVY 197
Cdd:cd05906 137 TLSGlpgirVLSIEELLDTAADHDLPQS-------------RPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHN 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 198 RLTEADATVIVLPLFHVHGLL-CGLLASLASGASVTLPAAGRFSASTFW---ADMRGAGATWytaVPTIHQIIIDRHTSK 273
Cdd:cd05906 204 GLTPQDVFLNWVPLDHVGGLVeLHLRAVYLGCQQVHVPTEEILADPLRWldlIDRYRVTITW---APNFAFALLNDLLEE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 274 PEA---EYPALRFIRS----CSASLAPAIMEKLEaAFGAP---VVEAYAMTEASHLMT-SNPLPEDGARKAG---SVGRA 339
Cdd:cd05906 281 IEDgtwDLSSLRYLVNageaVVAKTIRRLLRLLE-PYGLPpdaIRPAFGMTETCSGVIySRSFPTYDHSQALefvSLGRP 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 340 V-GQEMAILDEEGRRVEAGKSGEVCVRGANVTSGYKGNPEANEAAFR-FGWFHTGDIGVVDeEGYLRLVGRIKELINRGG 417
Cdd:cd05906 360 IpGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTeDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 418 EKISPIEVDSVL--LGHPAIAQAVAFGVPDAKYGEEINCAV-IPREGVSLGEEEVLAYCRRNLA-AFKVPKKVYI---AD 490
Cdd:cd05906 439 VNYYSHEIEAAVeeVPGVEPSFTAAFAVRDPGAETEELAIFfVPEYDLQDALSETLRAIRSVVSrEVGVSPAYLIplpKE 518
|
490
....*....|..
gi 1002261995 491 ELPKTATGKIQR 502
Cdd:cd05906 519 EIPKTSLGKIQR 530
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
168-511 |
5.33e-40 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 152.48 E-value: 5.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 168 HTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTLPaagRFSASTFWAD 247
Cdd:PLN03102 193 YTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMR---HVTAPEIYKN 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 248 MRGAGATWYTAVPTIHQIIIDRHTSKPEAEYPALRFIRSCSASlaPAIMEKLEAAFGAPVVEAYAMTEASHLMTS----- 322
Cdd:PLN03102 270 IEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPP--PAALVKKVQRLGFQVMHAYGLTEATGPVLFcewqd 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 323 --NPLPEDGARKAGSvgRAVGQEMAILDEEGRRVEAGKS--------GEVCVRGANVTSGYKGNPEANEAAFRFGWFHTG 392
Cdd:PLN03102 348 ewNRLPENQQMELKA--RQGVSILGLADVDVKNKETQESvprdgktmGEIVIKGSSIMKGYLKNPKATSEAFKHGWLNTG 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 393 DIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREG----------V 462
Cdd:PLN03102 426 DVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGettkedrvdkL 505
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1002261995 463 SLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQR---RIVAQHFVV 511
Cdd:PLN03102 506 VTRERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKpklRDIAKGLVV 557
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
52-503 |
5.81e-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: 150.21 E-value: 5.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNpegnvaaqaaasklglahtta 131
Cdd:cd17649 33 GVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLLLTH--------------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 slkdaagqvhlagfpasaaaaakdfanDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPl 211
Cdd:cd17649 92 ---------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFAS- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 FHVHGLLCGLLASLASGASVTLPAAGRFSASTFWADM-RGAGATwYTAVPT--IHQII--IDRHTSKPeaeYPALRFIRS 286
Cdd:cd17649 144 FNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMvRELGVT-VLDLPPayLQQLAeeADRTGDGR---PPSLRLYIF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 287 CSASLAPaimEKLEAAFGAPV--VEAYAMTEASHLMTSNPLPEDGARKAGSV--GRAVGQEMA-ILDEEGRRVEAGKSGE 361
Cdd:cd17649 220 GGEALSP---ELLRRWLKAPVrlFNAYGPTEATVTPLVWKCEAGAARAGASMpiGRPLGGRSAyILDADLNPVPVGVTGE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 362 VCVRGANVTSGYKGNPEANEAAF---RFG-----WFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHP 433
Cdd:cd17649 297 LYIGGEGLARGYLGRPELTAERFvpdPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHP 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002261995 434 AIAQAVAFGVPDAKYGEEINCaVIPREGVSLGE--EEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:cd17649 377 GVREAAVVALDGAGGKQLVAY-VVLRAAAAQPElrAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRK 447
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
52-503 |
8.14e-40 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 150.13 E-value: 8.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEGnvAAQAAASKLGLAHTTA 131
Cdd:cd12116 33 GVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTDDAL--PDRLPAGLPVLLLALA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 SLKDAAGQVHlagfpasaaaaakdFANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVL-P 210
Cdd:cd12116 111 AAAAAPAAPR--------------TPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTtY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 211 LFHVHGLlcGLLASLASGASVTL-PAAGRFSASTFWADMRGAGATWYTAVPTIHQIIIDrhtskpeAEYPALRFIRS-CS 288
Cdd:cd12116 177 AFDISLL--ELLLPLLAGARVVIaPRETQRDPEALARLIEAHSITVMQATPATWRMLLD-------AGWQGRAGLTAlCG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 289 A-SLAPAIMEKLeAAFGAPVVEAYAMTEASHLMTSNPL-PEDGARKAGsvGRAVGQEMAILDEEGRRVEAGKSGEVCVRG 366
Cdd:cd12116 248 GeALPPDLAARL-LSRVGSLWNLYGPTETTIWSTAARVtAAAGPIPIG--RPLANTQVYVLDAALRPVPPGVPGELYIGG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 367 ANVTSGYKGNPEANEAAFR---FG-----WFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQA 438
Cdd:cd12116 325 DGVAQGYLGRPALTAERFVpdpFAgpgsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQA 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002261995 439 VAFGVPDAKyGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:cd12116 405 AVVVREDGG-DRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRK 468
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
52-500 |
2.06e-39 |
|
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: 151.19 E-value: 2.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEG----------NVAAQAAA 121
Cdd:cd17634 105 GVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGvragrsvplkKNVDDALN 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 122 SKLGLAHTTASLK--------DAAGQVHLAGFPASAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLA-ASVQN 192
Cdd:cd17634 185 PNVTSVEHVIVLKrtgsdidwQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLvYAATT 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 193 IRAVYRL-------TEADATVIVLPLFHVHG-LLCGLLASLASGASVTlPAAGRFsastfWADMRGAGATWYTAVPTIHQ 264
Cdd:cd17634 265 MKYVFDYgpgdiywCTADVGWVTGHSYLLYGpLACGATTLLYEGVPNW-PTPARM-----WQVVDKHGVNILYTAPTAIR 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 265 IIIDRHTSKPEA-EYPALRFIRSCSASLAPAIME---KLEAAFGAPVVEAYAMTEASHLMTSnPLPEDGARKAGSVGRAV 340
Cdd:cd17634 339 ALMAAGDDAIEGtDRSSLRILGSVGEPINPEAYEwywKKIGKEKCPVVDTWWQTETGGFMIT-PLPGAIELKAGSATRPV 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 341 -GQEMAILDEEGRRVEAGKSGEVCVRGA--NVTSGYKGNPEANEAAF--RF-GWFHTGDIGVVDEEGYLRLVGRIKELIN 414
Cdd:cd17634 418 fGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHERFEQTYfsTFkGMYFSGDGARRDEDGYYWITGRSDDVIN 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 415 RGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEE---EVLAYCRRNLAAFKVPKKVYIADE 491
Cdd:cd17634 498 VAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPElyaELRNWVRKEIGPLATPDVVHWVDS 577
|
....*....
gi 1002261995 492 LPKTATGKI 500
Cdd:cd17634 578 LPKTRSGKI 586
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
158-477 |
4.90e-38 |
|
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: 145.19 E-value: 4.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 158 NDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLCGLLAsLASGASVTLPaag 237
Cdd:cd17640 85 NDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWHSYERSAEYFI-FACGCSQAYT--- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 238 rfSASTFWADMRGAGATWYTAVPTIHQII---IDRHTSKPEAEYPAL----------RFIRSCSASLAPAIMEKLEAAfG 304
Cdd:cd17640 161 --SIRTLKDDLKRVKPHYIVSVPRLWESLysgIQKQVSKSSPIKQFLflfflsggifKFGISGGGALPPHVDTFFEAI-G 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 305 APVVEAYAMTEASHLMTSNPLPEDgarKAGSVGRAV-GQEMAILDEEGRRV-EAGKSGEVCVRGANVTSGYKGNPEANEA 382
Cdd:cd17640 238 IEVLNGYGLTETSPVVSARRLKCN---VRGSVGRPLpGTEIKIVDPEGNVVlPPGEKGIVWVRGPQVMKGYYKNPEATSK 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 383 AFRF-GWFHTGDIGVVDEEGYLRLVGRIKELIN-RGGEKISPIEVDSVLLGHPAIAQAVAFG----------VPD----A 446
Cdd:cd17640 315 VLDSdGWFNTGDLGWLTCGGELVLTGRAKDTIVlSNGENVEPQPIEEALMRSPFIEQIMVVGqdqkrlgaliVPNfeelE 394
|
330 340 350
....*....|....*....|....*....|.
gi 1002261995 447 KYGEEINCAVIPREGVSLGEEEVLAYCRRNL 477
Cdd:cd17640 395 KWAKESGVKLANDRSQLLASKKVLKLYKNEI 425
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
159-500 |
5.18e-38 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 149.30 E-value: 5.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 159 DPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGASV---TLPA 235
Cdd:PRK08633 780 KPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVvyhPDPT 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 236 AGRFSASTfwadMRGAGATWYTAVPTIHQIIIDRHTSKPEaEYPALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTE 315
Cdd:PRK08633 860 DALGIAKL----VAKHRATILLGTPTFLRLYLRNKKLHPL-MFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATE 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 316 ASHLMTSNpLP---EDG-----ARKAGSVGRAV-GQEMAILD-EEGRRVEAGKSGEVCVRGANVTSGYKGNPEANEAAFR 385
Cdd:PRK08633 935 TSPVASVN-LPdvlAADfkrqtGSKEGSVGMPLpGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIK 1013
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 386 ----FGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVD---SVLLGHPAIAQAVAfGVPDAKYGEEIncAVIp 458
Cdd:PRK08633 1014 didgIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEeelAKALGGEEVVFAVT-AVPDEKKGEKL--VVL- 1089
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1002261995 459 regVSLGEEEVLAYCRR----NLAAFKVPKKVYIADELPKTATGKI 500
Cdd:PRK08633 1090 ---HTCGAEDVEELKRAikesGLPNLWKPSRYFKVEALPLLGSGKL 1132
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
158-502 |
7.21e-38 |
|
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: 146.07 E-value: 7.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 158 NDPSdvALFLhTSGTTSRPKGVPLTQRNLA-ASVQNIRAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTLPAA 236
Cdd:cd05928 174 QEPM--AIYF-TSGTTGSPKMAEHSHSSLGlGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGACVFVHHL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 237 GRFSASTFWADMRGAGATWYTAVPTIHQIIIDRHTSKpeAEYPALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEA 316
Cdd:cd05928 251 PRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSS--YKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTET 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 317 ShLMTSNPlpeDGAR-KAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVCVRGANVT-----SGYKGNPEANEAAFRFGWF 389
Cdd:cd05928 329 G-LICANF---KGMKiKPGSMGKASpPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRpfglfSGYVDNPEKTAATIRGDFY 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 390 HTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEEEV 469
Cdd:cd05928 405 LTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSHDPEQ 484
|
330 340 350
....*....|....*....|....*....|....*...
gi 1002261995 470 LA-----YCRRNLAAFKVPKKVYIADELPKTATGKIQR 502
Cdd:cd05928 485 LTkelqqHVKSVTAPYKYPRKVEFVQELPKTVTGKIQR 522
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
161-502 |
7.85e-38 |
|
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: 143.86 E-value: 7.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 161 SDVALFLHTSGTTSRPKGVPLTQRNLAasVQNIRAVYRLTEADATV---IVLPLFHVHGLLCgLLASLASGASVTLPAAG 237
Cdd:cd05974 85 DDPMLLYFTSGTTSKPKLVEHTHRSYP--VGHLSTMYWIGLKPGDVhwnISSPGWAKHAWSC-FFAPWNAGATVFLFNYA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 238 RFSASTFWADMRGAGATWYTAVPTIHQIIIDRHTSKPEAeypALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEAS 317
Cdd:cd05974 162 RFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDV---KLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETT 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 318 HLMTSNPlpeDGARKAGSVGRAV-GQEMAILDEEGRrveAGKSGEVCV-----RGANVTSGYKGNPEANEAAFRFGWFHT 391
Cdd:cd05974 239 ALVGNSP---GQPVKAGSMGRPLpGYRVALLDPDGA---PATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAMRGGYYRT 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 392 GDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEE---E 468
Cdd:cd05974 313 GDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPEtalE 392
|
330 340 350
....*....|....*....|....*....|....
gi 1002261995 469 VLAYCRRNLAAFKVPKKVYIAdELPKTATGKIQR 502
Cdd:cd05974 393 IFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRR 425
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
52-503 |
8.76e-38 |
|
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: 145.18 E-value: 8.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPE--GNVAAQAAASKLGLAHT 129
Cdd:cd17651 41 GVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLTHPAlaGELAVELVAVTLLDQPG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 130 TASLKDAAGQVHLagfpasaaaaakdfanDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVL 209
Cdd:cd17651 121 AAAGADAEPDPAL----------------DADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 210 PL---FHVHGLLcgllASLASGASVTL-PAAGRFSASTFWADMRGAGAT-WYTAVPTIHQIIidRHTSKPEAEYPALRFI 284
Cdd:cd17651 185 GLgfdVSVQEIF----STLCAGATLVLpPEEVRTDPPALAAWLDEQRISrVFLPTVALRALA--EHGRPLGVRLAALRYL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 285 RSC--SASLAPAIMEKLEAAFGAPVVEAYAMTEAsHLMTSNPLPEDGAR--KAGSVGRAV-GQEMAILDEEGRRVEAGKS 359
Cdd:cd17651 259 LTGgeQLVLTEDLREFCAGLPGLRLHNHYGPTET-HVVTALSLPGDPAAwpAPPPIGRPIdNTRVYVLDAALRPVPPGVP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 360 GEVCVRGANVTSGYKGNPEANEAAFRFGWF-------HTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGH 432
Cdd:cd17651 338 GELYIGGAGLARGYLNRPELTAERFVPDPFvpgarmyRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARH 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002261995 433 PAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:cd17651 418 PGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRR 488
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
162-499 |
5.74e-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: 341248 [Multi-domain] Cd Length: 364 Bit Score: 140.21 E-value: 5.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 162 DVALFLHTSGTTSRPKGVPLTQ----------RNLAASVQNIRAVYRLTEADATVIVL----PLFHVHGLLCGLlASLAS 227
Cdd:cd05924 4 DDLYILYTGGTTGMPKGVMWRQedifrmlmggADFGTGEFTPSEDAHKAAAAAAGTVMfpapPLMHGTGSWTAF-GGLLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 228 GASVTLPAAgRFSASTFWADMRGAGATWYTAV-PTIHQIIIDRHTSKPEAEYPALRFIRSCSASLAPAIMEKL-EAAFGA 305
Cdd:cd05924 83 GQTVVLPDD-RFDPEEVWRTIEKHKVTSMTIVgDAMARPLIDALRDAGPYDLSSLFAISSGGALLSPEVKQGLlELVPNI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 306 PVVEAYAMTEASHLMTSNPLPedGARKAGSVGRaVGQEMAILDEEGRRVEAGKSGE-VCVRGANVTSGYKGNPEANEAAF 384
Cdd:cd05924 162 TLVDAFGSSETGFTGSGHSAG--SGPETGPFTR-ANPDTVVLDDDGRVVPPGSGGVgWIARRGHIPLGYYGDEAKTAETF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 385 R----FGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPRE 460
Cdd:cd05924 239 PevdgVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLRE 318
|
330 340 350
....*....|....*....|....*....|....*....
gi 1002261995 461 GVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGK 499
Cdd:cd05924 319 GAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
52-503 |
1.07e-35 |
|
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: 138.87 E-value: 1.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITnpegnvaaqaaasklgLAHTTA 131
Cdd:cd12117 43 GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLT----------------DRSLAG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 SLKDAAGQVHLAGFPASAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVyRLTEADATVIVLPL 211
Cdd:cd12117 107 RAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNTNYV-TLGPDDRVLQTSPL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 ------FHVHG-LLCGllASLASGASVTLPAAGRFSAStfwADMRGAGATWYTAvPTIHQIIidrhtskpeAEYPA---- 280
Cdd:cd12117 186 afdastFEIWGaLLNG--ARLVLAPKGTLLDPDALGAL---IAEEGVTVLWLTA-ALFNQLA---------DEDPEcfag 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 281 LRFIRSCSASLAPAIMEK-LEAAFGAPVVEAYAMTEASHLMTSNPLPEdGARKAGSV--GRAVGQEMA-ILDEEGRRVEA 356
Cdd:cd12117 251 LRELLTGGEVVSPPHVRRvLAACPGLRLVNGYGPTENTTFTTSHVVTE-LDEVAGSIpiGRPIANTRVyVLDEDGRPVPP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 357 GKSGEVCVRGANVTSGYKGNPEANEAAF---RFG----WFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVL 429
Cdd:cd12117 330 GVPGELYVGGDGLALGYLNRPALTAERFvadPFGpgerLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAAL 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002261995 430 LGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSlgEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:cd12117 410 RAHPGVREAVVVVREDAGGDKRLVAYVVAEGALD--AAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRR 481
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
52-503 |
4.77e-35 |
|
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: 137.02 E-value: 4.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITnpegnvaaQAAASKLGLAHTTA 131
Cdd:cd12114 33 GVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT--------DGPDAQLDVAVFDV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 SLKDAAGQVhlagfpasAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPL 211
Cdd:cd12114 105 LILDLDALA--------APAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 ------FHVHGLLcgllaslASGASVTLPAAGRFSASTFWAD-MRGAGATWYTAVPTIHQIIIDrHTSKPEAEYPALRFI 284
Cdd:cd12114 177 sfdlsvYDIFGAL-------SAGATLVLPDEARRRDPAHWAElIERHGVTLWNSVPALLEMLLD-VLEAAQALLPSLRLV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 285 RSCSASLAPAIMEKLEAAF-GAPVVEAYAMTEAShlMTSNPLP---EDGARKAGSVGRAV-GQEMAILDEEGRRVEAGKS 359
Cdd:cd12114 249 LLSGDWIPLDLPARLRALApDARLISLGGATEAS--IWSIYHPideVPPDWRSIPYGRPLaNQRYRVLDPRGRDCPDWVP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 360 GEVCVRGANVTSGYKGNPEANEAAF-----RFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPA 434
Cdd:cd12114 327 GELWIGGRGVALGYLGDPELTAARFvthpdGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPG 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 435 IAQAVAFGVPDaKYGEEINCAVIPREGVS-LGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:cd12114 407 VARAVVVVLGD-PGGKRLAAFVVPDNDGTpIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRA 475
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
158-505 |
6.67e-35 |
|
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: 136.96 E-value: 6.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 158 NDPSDVALFLHTSGTTSRPKGVPLTQRNLAASV--QNIRAVYRLTEADATVIVLPLFHVHGLLCGLLaSLASGASV---- 231
Cdd:cd17639 85 GKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIagLGDRVPELLGPDDRYLAYLPLAHIFELAAENV-CLYRGGTIgygs 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 232 --TLpaagrFSASTF--WADMRGAGATWYTAVP----TIHQIIIDRHTSKPEAE-------YPA---------------- 280
Cdd:cd17639 164 prTL-----TDKSKRgcKGDLTEFKPTLMVGVPaiwdTIRKGVLAKLNPMGGLKrtlfwtaYQSklkalkegpgtpllde 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 281 -------------LRFIRSCSASLAPAIMEKLEAAFGaPVVEAYAMTEASHLMTSNpLPEDGArkAGSVGRAVG-QEMAI 346
Cdd:cd17639 239 lvfkkvraalggrLRYMLSGGAPLSADTQEFLNIVLC-PVIQGYGLTETCAGGTVQ-DPGDLE--TGRVGPPLPcCEIKL 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 347 LD-EEGRRVEAGKS--GEVCVRGANVTSGYKGNPEANEAAFRF-GWFHTGDIGVVDEEGYLRLVGRIKELI-NRGGEKIS 421
Cdd:cd17639 315 VDwEEGGYSTDKPPprGEILIRGPNVFKGYYKNPEKTKEAFDGdGWFHTGDIGEFHPDGTLKIIDRKKDLVkLQNGEYIA 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 422 PIEVDSVLLGHPAIAQAVAFGVPDAKYGEEIncaVIPREGV--------SLGEEEVLAYC------------------RR 475
Cdd:cd17639 395 LEKLESIYRSNPLVNNICVYADPDKSYPVAI---VVPNEKHltklaekhGVINSEWEELCedkklqkavlkslaetarAA 471
|
410 420 430
....*....|....*....|....*....|....*.
gi 1002261995 476 NLAAFKVPKKVYIADEL--PK----TATGKIQRRIV 505
Cdd:cd17639 472 GLEKFEIPQGVVLLDEEwtPEnglvTAAQKLKRKEI 507
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
161-509 |
2.06e-34 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 132.86 E-value: 2.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 161 SDVALFLHTSGTTSRPKGVPLTQRNLAASvqniravyrlteADAT----------VIVLPLFHVHGLLCGLLASLASGAS 230
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTAS------------ADAThdrlggpgqwLLALPAHHIAGLQVLVRSVIAGSEP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 231 VTLPAAGRFSASTFWADMRG-AGATWYTA-VPTihQIIidrhtsKPEAEYPALRFIRSCSASL-----APAIMEKLEAAF 303
Cdd:PRK07824 103 VELDVSAGFDPTALPRAVAElGGGRRYTSlVPM--QLA------KALDDPAATAALAELDAVLvgggpAPAPVLDAAAAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 304 GAPVVEAYAMTEASHLMTSNPLPEDGARkagsvgravgqemaiLDEEGRRVEAGksgevcvrGANVTSGYKgNPEANEAA 383
Cdd:PRK07824 175 GINVVRTYGMSETSGGCVYDGVPLDGVR---------------VRVEDGRIALG--------GPTLAKGYR-NPVDPDPF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 384 FRFGWFHTGDIGVVDEeGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVS 463
Cdd:PRK07824 231 AEPGWFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPA 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1002261995 464 LGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRRIVAQHF 509
Cdd:PRK07824 310 PTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRF 355
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
52-503 |
4.33e-34 |
|
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: 133.53 E-value: 4.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITnpegnvaaqaaasklglahtta 131
Cdd:cd17652 33 GVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLT---------------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 slkdaagqvhlagfpasaaaaakdfanDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTeADATVIVLPL 211
Cdd:cd17652 91 ---------------------------TPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVG-PGSRVLQFAS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 FHVHGLLCGLLASLASGASVTLPAAGRFSASTFWADM-RGAGATWYTAVPTIHQIIidrhtskPEAEYPALRFIRSCSAS 290
Cdd:cd17652 143 PSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLlREHRITHVTLPPAALAAL-------PPDDLPDLRTLVVAGEA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 291 LAPAIMEKLeaAFGAPVVEAYAMTEASHLMTSNPLPEDGARKAgsVGRAV-GQEMAILDEEGRRVEAGKSGEVCVRGANV 369
Cdd:cd17652 216 CPAELVDRW--APGRRMINAYGPTETTVCATMAGPLPGGGVPP--IGRPVpGTRVYVLDARLRPVPPGVPGELYIAGAGL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 370 TSGYKGNPEANEAAF---RFG-----WFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAf 441
Cdd:cd17652 292 ARGYLNRPGLTAERFvadPFGapgsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVV- 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002261995 442 GVPDAKYGEEINCA-VIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:cd17652 371 VVRDDRPGDKRLVAyVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRR 433
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
159-509 |
5.26e-34 |
|
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: 135.04 E-value: 5.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 159 DPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNI----RAVYRLTEADATVIVLPLFHVHGLLCgLLASLASGASVtlp 234
Cdd:cd05927 112 KPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVfkilEILNKINPTDVYISYLPLAHIFERVV-EALFLYHGAKI--- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 235 aaGRFSA--STFWADMRGAGATWYTAVP------------------TIHQIIIDRHTSKPEAEYPA-------------- 280
Cdd:cd05927 188 --GFYSGdiRLLLDDIKALKPTVFPGVPrvlnriydkifnkvqakgPLKRKLFNFALNYKLAELRSgvvraspfwdklvf 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 281 ----------LRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEASHLMTSNpLPEDgaRKAGSVGRAVG--------- 341
Cdd:cd05927 266 nkikqalggnVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLT-LPGD--TSVGHVGGPLPcaevklvdv 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 342 QEMAIL--DEEGRrveagksGEVCVRGANVTSGYKGNPEANEAAFRF-GWFHTGDIGVVDEEGYLRLVGRIKELINRG-G 417
Cdd:cd05927 343 PEMNYDakDPNPR-------GEVCIRGPNVFSGYYKDPEKTAEALDEdGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSqG 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 418 EKISPIEVDSVLLGHPAIAQAVAFG-----------VPDAKYGEEInCAVIPREGVSLGE--------EEVLA-----YC 473
Cdd:cd05927 416 EYVAPEKIENIYARSPFVAQIFVYGdslksflvaivVPDPDVLKEW-AASKGGGTGSFEElcknpevkKAILEdlvrlGK 494
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1002261995 474 RRNLAAFKVPKKVYIADELPK------TATGKIQRRIVAQHF 509
Cdd:cd05927 495 ENGLKGFEQVKAIHLEPEPFSvengllTPTFKLKRPQLKKYY 536
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
52-503 |
9.12e-34 |
|
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: 132.83 E-value: 9.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITnpegnvaaqaaasklglahtta 131
Cdd:cd12115 45 GVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT---------------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 slkdaagqvhlagfpasaaaaakdfanDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRlTEADATVIV--- 208
Cdd:cd12115 103 ---------------------------DPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFS-AEELAGVLAsts 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 209 ----LPLFHvhgllcgLLASLASGASVTLPAagrfSASTFWADMRGAGATWYTAVPTIHQIIIdRHTSKPeaeyPALRFI 284
Cdd:cd12115 155 icfdLSVFE-------LFGPLATGGKVVLAD----NVLALPDLPAAAEVTLINTVPSAAAELL-RHDALP----ASVRVV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 285 RSCSASLAPAIMEKLEAAF-GAPVVEAYAMTEASHLMTSNPLPEdGARKAGSVGRAVGQEMA-ILDEEGRRVEAGKSGEV 362
Cdd:cd12115 219 NLAGEPLPRDLVQRLYARLqVERVVNLYGPSEDTTYSTVAPVPP-GASGEVSIGRPLANTQAyVLDRALQPVPLGVPGEL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 363 CVRGANVTSGYKGNPEANEAAFRFGWFH-------TGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAI 435
Cdd:cd12115 298 YIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyrTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGV 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002261995 436 AQAVAFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:cd12115 378 REAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRS 445
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
306-505 |
2.06e-33 |
|
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: 133.84 E-value: 2.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 306 PVVEAYAMTE-ASHLMTsnPLPEDGARKAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVCVRGA--NVTSGYKGNPEANE 381
Cdd:cd05966 383 PIVDTWWQTEtGGIMIT--PLPGATPLKPGSATRPFfGIEPAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDHERYE 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 382 AAF--RF-GWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIP 458
Cdd:cd05966 461 DTYfsKFpGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTL 540
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1002261995 459 REGVSLGEE---EVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRRIV 505
Cdd:cd05966 541 KDGEEPSDElrkELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRIL 590
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
159-512 |
4.58e-33 |
|
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: 131.40 E-value: 4.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 159 DPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTLpaAGR 238
Cdd:cd05937 85 DPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLAL--SRK 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 239 FSASTFWADMRGAGATWYTAVPTIHQIIIDRHTSKPEAEYpalRFIRSCSASLAPAIMEKLEAAFGAPVV-EAYAMTEAS 317
Cdd:cd05937 163 FSASQFWKDVRDSGATIIQYVGELCRYLLSTPPSPYDRDH---KVRVAWGNGLRPDIWERFRERFNVPEIgEFYAATEGV 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 318 HLMTSNplpEDGARKAGSVGRA------------------VGQEMAILDEEG---RRVEAGKSGEVCVR--GANVTS--G 372
Cdd:cd05937 240 FALTNH---NVGDFGAGAIGHHglirrwkfenqvvlvkmdPETDDPIRDPKTgfcVRAPVGEPGEMLGRvpFKNREAfqG 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 373 YKGNPEANEA-----AFRFG--WFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPD 445
Cdd:cd05937 317 YLHNEDATESklvrdVFRKGdiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKV 396
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002261995 446 AKYGEEINCAVIPREGVSLGEEEVL-----AYCRRNLAAFKVPKKVYIADELPKTATGKIQRRIVAQHFVVP 512
Cdd:cd05937 397 PGHDGRAGCAAITLEESSAVPTEFTksllaSLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGVDP 468
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
52-503 |
7.92e-33 |
|
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: 130.28 E-value: 7.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEgnvaaqaaasklglahtta 131
Cdd:cd17650 33 GVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLTQPE------------------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 slkdaagqvhlagfpasaaaaakdfandpsDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPL 211
Cdd:cd17650 94 ------------------------------DLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQMAS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 FHVH---GLLCglLASLASGASVTLPAAGRFSASTFWADMRGAGATWYTAVPTIhqII-----IDRHTSKPeaeyPALRF 283
Cdd:cd17650 144 FSFDvfaGDFA--RSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPAL--IRpvmayVYRNGLDL----SAMRL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 284 IRSCSASLAPAIMEKLEAAFGAP--VVEAYAMTEASHLMTSNPLPEDGARKAGSV--GRAV-GQEMAILDEEGRRVEAGK 358
Cdd:cd17650 216 LIVGSDGCKAQDFKTLAARFGQGmrIINSYGVTEATIDSTYYEEGRDPLGDSANVpiGRPLpNTAMYVLDERLQPQPVGV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 359 SGEVCVRGANVTSGYKGNPEANEAAF---RFG----WFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLG 431
Cdd:cd17650 296 AGELYIGGAGVARGYLNRPELTAERFvenPFApgerMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLAR 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002261995 432 HPAIAQAVAFGVPDAKyGEEINCA-VIPREGVSLgeEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:cd17650 376 HPAIDEAVVAVREDKG-GEARLCAyVVAAATLNT--AELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRR 445
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
52-503 |
8.26e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 130.85 E-value: 8.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITnpEGNVAAQaaaskLGLAHTTA 131
Cdd:PRK12316 2049 GVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLT--QRHLLER-----LPLPAGVA 2121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 SLK-DAAGQVhlagfpASAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADaTVIVLP 210
Cdd:PRK12316 2122 RLPlDRDAEW------ADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPAD-CELQFM 2194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 211 LFHVHGLLCGLLASLASGASVTLPAAGRFSASTFWADMRGAGATWYTAVPTIHQIIID--RHTSKPeaeyPALRFIRSCS 288
Cdd:PRK12316 2195 SFSFDGAHEQWFHPLLNGARVLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEhaERDGRP----PAVRVYCFGG 2270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 289 ASLAPAIMEKLEAAFGAP-VVEAYAMTEAshlmTSNPL-----PEDGARKAGS-VGRAVGQEMA-ILDEEGRRVEAGKSG 360
Cdd:PRK12316 2271 EAVPAASLRLAWEALRPVyLFNGYGPTEA----VVTPLlwkcrPQDPCGAAYVpIGRALGNRRAyILDADLNLLAPGMAG 2346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 361 EVCVRGANVTSGYKGNPEANEAAF---RFG-----WFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGH 432
Cdd:PRK12316 2347 ELYLGGEGLARGYLNRPGLTAERFvpdPFSasgerLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAH 2426
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002261995 433 PAIAQAVAFGVpDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:PRK12316 2427 PAVREAVVVAQ-DGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRK 2496
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
52-503 |
1.17e-31 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 128.84 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEGNVAAQAAASKLGLAHTTA 131
Cdd:PRK08279 83 GVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLW 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 SLKDAAGQVHLAGFPASAAAAAKDFANDPS-------DVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADA 204
Cdd:PRK08279 163 VAGGDTLDDPEGYEDLAAAAAGAPTTNPASrsgvtakDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDV 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 205 TVIVLPLFHVHGLLCGLLASLASGASVTLpaAGRFSASTFWADMRGAGATWYTAVPTIHQIIIDRHTSKPEAEYPaLRFI 284
Cdd:PRK08279 243 LYCCLPLYHNTGGTVAWSSVLAAGATLAL--RRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPTDRDHR-LRLM 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 285 rsCSASLAPAIMEKLEAAFGAP-VVEAYAMTEAShLMTSNplpEDGarKAGSVGRA--------------VGQEMAILDE 349
Cdd:PRK08279 320 --IGNGLRPDIWDEFQQRFGIPrILEFYAASEGN-VGFIN---VFN--FDGTVGRVplwlahpyaivkydVDTGEPVRDA 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 350 EGR--RVEAGKSGEVC--VRGANVTSGYkGNPEANEA-----AFRFG--WFHTGDIGVVDEEGYLRLVGRIKELINRGGE 418
Cdd:PRK08279 392 DGRciKVKPGEVGLLIgrITDRGPFDGY-TDPEASEKkilrdVFKKGdaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGE 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 419 KISPIEVDSVLLGHPAIAQAVAFGVP----DAKYGEeinCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPK 494
Cdd:PRK08279 471 NVATTEVENALSGFPGVEEAVVYGVEvpgtDGRAGM---AAIVLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPELET 547
|
....*....
gi 1002261995 495 TATGKIQRR 503
Cdd:PRK08279 548 TGTFKYRKV 556
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
159-505 |
1.59e-31 |
|
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: 127.55 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 159 DPSDVALFLHTSGTTSRPKGVPLTQRN--LAASVQNIRAVYRLTEADATVIVLPLFHVHGLlCGLLASLASGASVTLPAA 236
Cdd:cd05915 151 PERAACGMAYTTGTTGLPKGVVYSHRAlvLHSLAASLVDGTALSEKDVVLPVVPMFHVNAW-CLPYAATLVGAKQVLPGP 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 237 GRFSASTFWADMRGAGATWYTAVPTIHQIIIDRHTSKpeAEYPALRFIRSCSASlAPAIMEKLEAAFGAPVVEAYAMTEA 316
Cdd:cd05915 230 RLDPASLVELFDGEGVTFTAGVPTVWLALADYLESTG--HRLKTLRRLVVGGSA-APRSLIARFERMGVEVRQGYGLTET 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 317 SHLMTS-------NPLPEDGAR--KAGSVGRAVGQEMAILDEEGRRV-EAGKSGEV-CVRGANVTSGYKGNPEANEA-AF 384
Cdd:cd05915 307 SPVVVQnfvkshlESLSEEEKLtlKAKTGLPIPLVRLRVADEEGRPVpKDGKALGEvQLKGPWITGGYYGNEEATRSaLT 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 385 RFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEInCAVIPREGVSL 464
Cdd:cd05915 387 PDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERP-LAVVVPRGEKP 465
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1002261995 465 GEEEVLAYCRRNLAAFK-VPKKVYIADELPKTATGKIQRRIV 505
Cdd:cd05915 466 TPEELNEHLLKAGFAKWqLPDAYVFAEEIPRTSAGKFLKRAL 507
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
52-442 |
2.04e-31 |
|
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: 127.20 E-value: 2.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEGNVAAQAAASKLGLAHTTA 131
Cdd:cd05932 27 GLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGKLDDWKAMAPGVPEGLISISL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 SLKDAA-GQVHLAGFPASAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLP 210
Cdd:cd05932 107 PPPSAAnCQYQWDDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 211 LFHVHGLLCGLLASLASGASVTLPAagrfSASTFWADMRGAGATWYTAVPTI----HQIIIDRhtsKPEAEYPAL----- 281
Cdd:cd05932 187 LAHVTERVFVEGGSLYGGVLVAFAE----SLDTFVEDVQRARPTLFFSVPRLwtkfQQGVQDK---IPQQKLNLLlkipv 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 282 ------------------RFIRSCSASLAPAIMEKLEAaFGAPVVEAYAMTEASHLMTSNplpEDGARKAGSVGRAV-GQ 342
Cdd:cd05932 260 vnslvkrkvlkglgldqcRLAGCGSAPVPPALLEWYRS-LGLNILEAYGMTENFAYSHLN---YPGRDKIGTVGNAGpGV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 343 EMAILDEegrrveagksGEVCVRGANVTSGYKGNPEANEAAFRF-GWFHTGDIGVVDEEGYLRLVGRIKELINRG-GEKI 420
Cdd:cd05932 336 EVRISED----------GEILVRSPALMMGYYKDPEATAEAFTAdGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYV 405
|
410 420
....*....|....*....|..
gi 1002261995 421 SPIEVDSVLLGHPAIAQAVAFG 442
Cdd:cd05932 406 APAPIENKLAEHDRVEMVCVIG 427
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
52-503 |
3.30e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 129.13 E-value: 3.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEgnvaaQAAASKLGLAHTTA 131
Cdd:PRK12467 558 GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSH-----LLAQLPVPAGLRSL 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 SLKDAAGQVhlagfpASAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTeADATVIVLPL 211
Cdd:PRK12467 633 CLDEPADLL------CGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLA-ADDSMLMVST 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 FHVHGLLCGLLASLASGASVTL-PAAGRFSASTFWADMRGAGATWYTAVPTIHQIIIDrhTSKPEAEYPALRFIRSCSAs 290
Cdd:PRK12467 706 FAFDLGVTELFGALASGATLHLlPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQ--ASRVALPRPQRALVCGGEA- 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 291 LAPAIMEKL-EAAFGAPVVEAYAMTEASHLMTSNPLPEDGARKAGS-VGRAV-GQEMAILDEEGRRVEAGKSGEVCVRGA 367
Cdd:PRK12467 783 LQVDLLARVrALGPGARLINHYGPTETTVGVSTYELSDEERDFGNVpIGQPLaNLGLYILDHYLNPVPVGVVGELYIGGA 862
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 368 NVTSGYKGNPEANEAAF---RFG-----WFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAV 439
Cdd:PRK12467 863 GLARGYHRRPALTAERFvpdPFGadggrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAV 942
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002261995 440 AFGVPDAKyGEEINCAVIPREGVSLGE-----EEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:PRK12467 943 VLAQPGDA-GLQLVAYLVPAAVADGAEhqatrDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRK 1010
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
165-506 |
6.79e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 125.88 E-value: 6.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 165 LFLHTSGTTSRPKGVPLTQR---NLAASVqNIRAVYRLTEADATVIVLPLFHvhGLLCGLLA-SLASGASVTlpAAGRFS 240
Cdd:PRK13383 178 IVLLTSGTTGKPKGVPRAPQlrsAVGVWV-TILDRTRLRTGSRISVAMPMFH--GLGLGMLMlTIALGGTVL--THRHFD 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 241 ASTFWADMRGAGATWYTAVPTIHQIIIDRHTS-KPEAEYPALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEAShl 319
Cdd:PRK13383 253 AEAALAQASLHRADAFTAVPVVLARILELPPRvRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVG-- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 320 MTSNPLPEDGARKAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVCVRGANVTSGYKGnpeANEAAFRFGWFHTGDIGVVD 398
Cdd:PRK13383 331 IGALATPADLRDAPETVGKPVaGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTD---GGGKAVVDGMTSTGDMGYLD 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 399 EEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLA 478
Cdd:PRK13383 408 NAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVS 487
|
330 340
....*....|....*....|....*...
gi 1002261995 479 AFKVPKKVYIADELPKTATGKIQRRIVA 506
Cdd:PRK13383 488 RFEQPRDINIVSSIPRNPTGKVLRKELP 515
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
162-502 |
8.30e-31 |
|
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: 124.39 E-value: 8.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 162 DVALFLHTSGTTSRPKgvpltqrnlAASVQNIRAVY---------RLTEADATVIVLPLFHVHGLLCGLLASLASGASVT 232
Cdd:cd05940 82 DAALYIYTSGTTGLPK---------AAIISHRRAWRggaffagsgGALPSDVLYTCLPLYHSTALIVGWSACLASGATLV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 233 LpaAGRFSASTFWADMRGAGATwytAVPTIHQIIIDRHTSKPEAEYPALRFIRSCSASLAPAIMEKLEAAFGAP-VVEAY 311
Cdd:cd05940 153 I--RKKFSASNFWDDIRKYQAT---IFQYIGELCRYLLNQPPKPTERKHKVRMIFGNGLRPDIWEEFKERFGVPrIAEFY 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 312 AMTEASHLMTSNPlpedgaRKAGSVGRA----------------VGQEMAILDEEGR--RVEAGKSGEVCVRGANVTS-- 371
Cdd:cd05940 228 AATEGNSGFINFF------GKPGAIGRNpsllrkvaplalvkydLESGEPIRDAEGRciKVPRGEPGLLISRINPLEPfd 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 372 GYKGNPEANEA----AFRFG--WFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPD 445
Cdd:cd05940 302 GYTDPAATEKKilrdVFKKGdaWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQV 381
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1002261995 446 AKYGEEINCAVIP-REGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQR 502
Cdd:cd05940 382 PGTDGRAGMAAIVlQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQK 439
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
52-503 |
8.38e-31 |
|
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: 127.67 E-value: 8.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIM----------FLaviraravaaPLNPAYTQEEFEFYLSDSGARLLITNpegnvaaqaaa 121
Cdd:COG1020 522 GVGPGDLVGVCLERSLEMVVAllavlkagaaYV----------PLDPAYPAERLAYMLEDAGARLVLTQ----------- 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 122 sklglAHTTASLKDAAGQVHL--AGFPASAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRL 199
Cdd:COG1020 581 -----SALAARLPELGVPVLAldALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGL 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 200 TEADatvIVLplfHVHGL-----LCGLLASLASGAS-VTLPAAGRFSASTFWADMRGAGATWYTAVPTIHQIIIDRHTSK 273
Cdd:COG1020 656 GPGD---RVL---QFASLsfdasVWEIFGALLSGATlVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEA 729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 274 PeaeyPALRFIRSCSASLAPAIMEKLEAAF-GAPVVEAYAMTEAS-----HLMTSNPLPEDGArkagSVGRAV-GQEMAI 346
Cdd:COG1020 730 L----PSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTvdstyYEVTPPDADGGSV----PIGRPIaNTRVYV 801
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 347 LDEEGRRVEAGKSGEVCVRGANVTSGYKGNPEANEAAF---RFG-----WFHTGDIGVVDEEGYLRLVGRI----KelIN 414
Cdd:COG1020 802 LDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFvadPFGfpgarLYRTGDLARWLPDGNLEFLGRAddqvK--IR 879
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 415 rgGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPK 494
Cdd:COG1020 880 --GFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPL 957
|
....*....
gi 1002261995 495 TATGKIQRR 503
Cdd:COG1020 958 TGNGKLDRL 966
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
52-503 |
2.33e-30 |
|
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: 123.59 E-value: 2.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITnpegnvaaqAAASKLGLAHTTA 131
Cdd:cd17655 43 GVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLT---------QSHLQPPIAFIGL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 SLKDAAGQVHlagfpaSAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADaTVIVLPL 211
Cdd:cd17655 114 IDLLDEDTIY------HEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHL-RVALFAS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 FHVHGLLCGLLASLASGASVTL-PAAGRFSASTFWADMRGAGATWYTAVPTIHQIIIDrhtSKPEAEYPALRFI---RSC 287
Cdd:cd17655 187 ISFDASVTEIFASLLSGNTLYIvRKETVLDGQALTQYIRQNRITIIDLTPAHLKLLDA---ADDSEGLSLKHLIvggEAL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 288 SASLAPAIMEKLEAAfgAPVVEAYAMTEASHLMTSNPLpEDGARKAGSV--GRAVGQ-EMAILDEEGRRVEAGKSGEVCV 364
Cdd:cd17655 264 STELAKKIIELFGTN--PTITNAYGPTETTVDASIYQY-EPETDQQVSVpiGKPLGNtRIYILDQYGRPQPVGVAGELYI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 365 RGANVTSGYKGNPEANEAAF---------RFgwFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAI 435
Cdd:cd17655 341 GGEGVARGYLNRPELTAEKFvddpfvpgeRM--YRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDI 418
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002261995 436 AQAVAFGVPDAKyGEEINCAVIPREGvSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:cd17655 419 KEAVVIARKDEQ-GQNYLCAYIVSEK-ELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRK 484
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
52-503 |
3.42e-30 |
|
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: 122.42 E-value: 3.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEGNvaaqaaasklglahtta 131
Cdd:cd17653 43 GVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLLTTDSPD----------------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 slkdaagqvhlagfpasaaaaakdfandpsDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADAtviVLPL 211
Cdd:cd17653 106 ------------------------------DLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSR---VAQV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 FHVhGLLCG---LLASLASGASVTLpaagRFSASTFWADMRGAGATwyTAVPTIHQIIidrhtskPEAEYPALRFI---- 284
Cdd:cd17653 153 LSI-AFDACigeIFSTLCNGGTLVL----ADPSDPFAHVARTVDAL--MSTPSILSTL-------SPQDFPNLKTIflgg 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 285 RSCSASLAPAimekleAAFGAPVVEAYAMTEASHLMTsnpLPEDGARKAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVC 363
Cdd:cd17653 219 EAVPPSLLDR------WSPGRRLYNAYGPTECTISST---MTELLPGQPVTIGKPIpNSTCYILDADLQPVPEGVVGEIC 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 364 VRGANVTSGYKGNPEANEAAFRFGWFH-------TGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDS-VLLGHPAI 435
Cdd:cd17653 290 ISGVQVARGYLGNPALTASKFVPDPFWpgsrmyrTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEvVLQSQPEV 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002261995 436 AQAVAFGVPDAKygeeinCAVIPREGVSlgEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:cd17653 370 TQAAAIVVNGRL------VAFVTPETVD--VDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRK 429
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
52-505 |
3.97e-30 |
|
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: 124.14 E-value: 3.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLIT-------------NPEGNVAAQ 118
Cdd:cd05968 112 GVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITadgftrrgrevnlKEEADKACA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 119 AAAS--------KLGLAHTTASLKDaagqvhLAGFPASAAAAAKDFANDPSDVALFLHTSGTTSRPKGV-------PLTQ 183
Cdd:cd05968 192 QCPTvekvvvvrHLGNDFTPAKGRD------LSYDEEKETAGDGAERTESEDPLMIIYTSGTTGKPKGTvhvhagfPLKA 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 184 RNLAASVQNIRAVYRLT-EADATVIVLPLFHVHGLLCGLLASLASGASvTLPAAGRFsastfWADMRGAGATWYTAVPTI 262
Cdd:cd05968 266 AQDMYFQFDLKPGDLLTwFTDLGWMMGPWLIFGGLILGATMVLYDGAP-DHPKADRL-----WRMVEDHEITHLGLSPTL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 263 HQIIIDRHTSKPEAE-YPALRFIRSCSASLAPAIMEKLEAAFGA---PVVEAYAMTEASHLMTSNPLPEDgaRKAGSVGR 338
Cdd:cd05968 340 IRALKPRGDAPVNAHdLSSLRVLGSTGEPWNPEPWNWLFETVGKgrnPIINYSGGTEISGGILGNVLIKP--IKPSSFNG 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 339 AV-GQEMAILDEEGRRVeAGKSGEVCVRGA--NVTSGYKGNPEANEAAF--RFG--WFHtGDIGVVDEEGYLRLVGRIKE 411
Cdd:cd05968 418 PVpGMKADVLDESGKPA-RPEVGELVLLAPwpGMTRGFWRDEDRYLETYwsRFDnvWVH-GDFAYYDEEGYFYILGRSDD 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 412 LINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGE---EEVLAYCRRNLAAFKVPKKVYI 488
Cdd:cd05968 496 TINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEalaEELMERVADELGKPLSPERILF 575
|
490
....*....|....*..
gi 1002261995 489 ADELPKTATGKIQRRIV 505
Cdd:cd05968 576 VKDLPKTRNAKVMRRVI 592
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
55-503 |
2.05e-29 |
|
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: 120.58 E-value: 2.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 55 PGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPegnvaaqaaasklglahttaslk 134
Cdd:cd17648 37 PDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDTGARVVITNS----------------------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 135 daagqvhlagfpasaaaaakdfandpSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRL-TEADATVIVLPLFH 213
Cdd:cd17648 94 --------------------------TDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGrDNGDEAVLFFSNYV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 214 VHGLLCGLLASLASGAS-VTLPAAGRFSASTFWADMRGAGATWYTAVPTIHQII-IDRHTSkpeaeypaLRFIRSCSASL 291
Cdd:cd17648 148 FDFFVEQMTLALLNGQKlVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQYdLARLPH--------LKRVDAAGEEF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 292 APAIMEKLEAAFGAPVVEAYAMTEASHLMTSNPLPEDgARKAGSVGRAVGQEMA-ILDEEGRRVEAGKSGEVCVRGANVT 370
Cdd:cd17648 220 TAPVFEKLRSRFAGLIINAYGPTETTVTNHKRFFPGD-QRFDKSLGRPVRNTKCyVLNDAMKRVPVGAVGELYLGGDGVA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 371 SGYKG-----------NPEANEAAFRFG----WFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAI 435
Cdd:cd17648 299 RGYLNrpeltaerflpNPFQTEQERARGrnarLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGV 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002261995 436 AQAVAFGVPDAKYGEE-----INCAVIPREGvSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:cd17648 379 RECAVVAKEDASQAQSriqkyLVGYYLPEPG-HVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVR 450
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
52-503 |
4.95e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 122.37 E-value: 4.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEGNVAAQAAASKLGLAHTTA 131
Cdd:PRK12316 3103 GVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDE 3182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 SLKDAAGQVHLagfpasaaaaakdfanDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTeADATVIVLPL 211
Cdd:PRK12316 3183 NYAEANPAIRT----------------MPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLG-VGDRVLQFTT 3245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 FHVHGLLCGLLASLASGASVTLPAAGRFSASTFWADM-RGAGATWYTAVPTIHQIIIDrhtSKPEAEYPALRFIRSCSAS 290
Cdd:PRK12316 3246 FSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELiNSEGVDVLHAYPSMLQAFLE---EEDAHRCTSLKRIVCGGEA 3322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 291 LAPAIMEKLEAafGAPVVEAYAMTEASHLMTSNPLPEDGARKAgSVGRAVGQEMA-ILDEEGRRVEAGKSGEVCVRGANV 369
Cdd:PRK12316 3323 LPADLQQQVFA--GLPLYNLYGPTEATITVTHWQCVEEGKDAV-PIGRPIANRACyILDGSLEPVPVGALGELYLGGEGL 3399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 370 TSGYKGNPEANEAAFRFGWF-------HTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFG 442
Cdd:PRK12316 3400 ARGYHNRPGLTAERFVPDPFvpgerlyRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLA 3479
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002261995 443 VPdakyGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:PRK12316 3480 VD----GRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRK 3536
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
343-508 |
7.23e-29 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 120.09 E-value: 7.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 343 EMAILDEEGRRVEAGKSGEVCVRGANVTSGYKGNPEANEAAF-RFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKIS 421
Cdd:PRK10946 364 EVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFdANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIA 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 422 PIEVDSVLLGHPAIAQAVAFGVPDAKYGEEiNCA-VIPREgvSLGEEEVLAYCR-RNLAAFKVPKKVYIADELPKTATGK 499
Cdd:PRK10946 444 AEEIENLLLRHPAVIHAALVSMEDELMGEK-SCAfLVVKE--PLKAVQLRRFLReQGIAEFKLPDRVECVDSLPLTAVGK 520
|
....*....
gi 1002261995 500 IQRRIVAQH 508
Cdd:PRK10946 521 VDKKQLRQW 529
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
159-464 |
2.57e-28 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 118.38 E-value: 2.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 159 DPSDVALFLHTSGTTSRPKGVPLTQRNLAAsvqNIRAVYRL---TEADATVIVLPLFHVHGLLCGLLASLASGASVTLpA 235
Cdd:PRK06334 181 DPEDVAVILFTSGTEKLPKGVPLTHANLLA---NQRACLKFfspKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVF-A 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 236 AGRFSASTFWADMRGAGATWYTAVPTIHQIIIdRHTSKPEAEYPALRFIRSCSASLAPAIMEKLEAAFgaPVV---EAYA 312
Cdd:PRK06334 257 YNPLYPKKIVEMIDEAKVTFLGSTPVFFDYIL-KTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTF--PHIqlrQGYG 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 313 MTEASHLMTSNplPEDGARKAGSVGRAV-GQEMAILDEEGR-RVEAGKSGEVCVRGANVTSGYKGNPEaNEAAFRFG--- 387
Cdd:PRK06334 334 TTECSPVITIN--TVNSPKHESCVGMPIrGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLGEDF-GQGFVELGget 410
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002261995 388 WFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHpaiaqavaFGVPDAKYGEEINCAVIPREGVSL 464
Cdd:PRK06334 411 WYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG--------FGQNAADHAGPLVVCGLPGEKVRL 479
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
52-505 |
3.08e-28 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 118.98 E-value: 3.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNpeGNVAAQAAASKLGLAhttA 131
Cdd:PRK06060 51 GLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTS--DALRDRFQPSRVAEA---A 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 SLKDAAGQVhlagfpasaaaaakdfanDPSD--------VALFLHTSGTTSRPKGVPLTQRNLAASVQNI-RAVYRLTEA 202
Cdd:PRK06060 126 ELMSEAARV------------------APGGyepmggdaLAYATYTSGTTGPPKAAIHRHADPLTFVDAMcRKALRLTPE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 203 DATVIVLPLFHVHGLLCGLLASLASGASV---TLPAAGRfSASTFWAdmRGAGATWYtAVPTIHQIIIDrhTSKPEAeYP 279
Cdd:PRK06060 188 DTGLCSARMYFAYGLGNSVWFPLATGGSAvinSAPVTPE-AAAILSA--RFGPSVLY-GVPNFFARVID--SCSPDS-FR 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 280 ALRFIRSCSASLAPAIMEKLEAAFGA-PVVEAYAMTEASHLMTSNPLPEdgaRKAGSVGRAVGQ-EMAILDEEGRRVEAG 357
Cdd:PRK06060 261 SLRCVVSAGEALELGLAERLMEFFGGiPILDGIGSTEVGQTFVSNRVDE---WRLGTLGRVLPPyEIRVVAPDGTTAGPG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 358 KSGEVCVRGANVTSGYKGNPEA---NEaafrfGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPA 434
Cdd:PRK06060 338 VEGDLWVRGPAIAKGYWNRPDSpvaNE-----GWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEA 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002261995 435 IAQAVAFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRR---NLAAFKVPKKVYIADELPKTATGKIQRRIV 505
Cdd:PRK06060 413 VAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGllnRLSAFKVPHRFAVVDRLPRTPNGKLVRGAL 486
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
52-513 |
3.16e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 120.06 E-value: 3.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITN----PEGNVAAQaaASKLGLA 127
Cdd:PRK12316 557 GVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQshlgRKLPLAAG--VQVLDLD 634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 128 HTTASLK---DAAGQVHLagfpasaaaaakdfanDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADA 204
Cdd:PRK12316 635 RPAAWLEgysEENPGTEL----------------NPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDT 698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 205 TVIVLPL-FHVHglLCGLLASLASGASVTLPAAG-RFSASTFWADMRGAGATWYTAVPTIHQIIIdrHTSKPEAEYPaLR 282
Cdd:PRK12316 699 VLQKTPFsFDVS--VWEFFWPLMSGARLVVAAPGdHRDPAKLVELINREGVDTLHFVPSMLQAFL--QDEDVASCTS-LR 773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 283 FIRSCSASLAPAIMEKLEA-AFGAPVVEAYAMTEASHLMTSNPLPEDGARKAgSVGRAVGQEMA-ILDEEGRRVEAGKSG 360
Cdd:PRK12316 774 RIVCSGEALPADAQEQVFAkLPQAGLYNLYGPTEAAIDVTHWTCVEEGGDSV-PIGRPIANLACyILDANLEPVPVGVLG 852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 361 EVCVRGANVTSGYKGNPEANEAAF---RFG----WFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHP 433
Cdd:PRK12316 853 ELYLAGRGLARGYHGRPGLTAERFvpsPFVagerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHP 932
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 434 AIAQAVAFgvpdAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR--------IV 505
Cdd:PRK12316 933 WVREAAVL----AVDGKQLVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKalpapeasVA 1008
|
....*...
gi 1002261995 506 AQHFVVPV 513
Cdd:PRK12316 1009 QQGYVAPR 1016
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
158-500 |
5.56e-28 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 118.91 E-value: 5.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 158 NDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTL---P 234
Cdd:PRK06814 790 RDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLypsP 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 235 AAGR--------------FSASTF---WADMrgagATWYtavptihqiiidrhtskpeaEYPALRFIRSCSASLAPAI-- 295
Cdd:PRK06814 870 LHYRiipeliydtnatilFGTDTFlngYARY----AHPY--------------------DFRSLRYVFAGAEKVKEETrq 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 296 --MEKleaaFGAPVVEAYAMTEASHLMTSN-PLpedgARKAGSVGRAV-GQEMAILDEEGrrVEAGksGEVCVRGANVTS 371
Cdd:PRK06814 926 twMEK----FGIRILEGYGVTETAPVIALNtPM----HNKAGTVGRLLpGIEYRLEPVPG--IDEG--GRLFVRGPNVML 993
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 372 GY--KGNPEANEAAfRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYG 449
Cdd:PRK06814 994 GYlrAENPGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKG 1072
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1002261995 450 EEIncaVIPREGVSLGEEEVLAYCRRNLAA-FKVPKKVYIADELPKTATGKI 500
Cdd:PRK06814 1073 ERI---ILLTTASDATRAAFLAHAKAAGASeLMVPAEIITIDEIPLLGTGKI 1121
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
306-504 |
2.38e-27 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 116.01 E-value: 2.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 306 PVVEAYAMTE-ASHLMTsnPLPedGAR--KAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVCV--------RGANvtsgy 373
Cdd:PRK00174 397 PIVDTWWQTEtGGIMIT--PLP--GATplKPGSATRPLpGIQPAVVDEEGNPLEGGEGGNLVIkdpwpgmmRTIY----- 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 374 kGNPEaneaafRF---------GWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVP 444
Cdd:PRK00174 468 -GDHE------RFvktyfstfkGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRP 540
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002261995 445 DAKYGEEINCAVIPREGVSLGEE---EVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRRI 504
Cdd:PRK00174 541 DDIKGQGIYAFVTLKGGEEPSDElrkELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRI 603
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
159-509 |
4.66e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 114.71 E-value: 4.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 159 DPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLT-EADATVIVLPLFHVHGLLCGLLASLASGASVTLPAAG 237
Cdd:PRK07768 150 GEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDvETDVMVSWLPLFHDMGMVGFLTVPMYFGAELVKVTPM 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 238 RFSASTF-WADMRGAGATWYTAVPTIHQIIIDRHTSK--PEAEY--PALRFIRSCSASLAPAIMEKLEAA---FGAP--- 306
Cdd:PRK07768 230 DFLRDPLlWAELISKYRGTMTAAPNFAYALLARRLRRqaKPGAFdlSSLRFALNGAEPIDPADVEDLLDAgarFGLRpea 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 307 VVEAYAMTEA-----------------------SHLMTSNPLPEDGARKAGSVGRAV-GQEMAILDEEGRRVEAGKSGEV 362
Cdd:PRK07768 310 ILPAYGMAEAtlavsfspcgaglvvdevdadllAALRRAVPATKGNTRRLATLGPPLpGLEVRVVDEDGQVLPPRGVGVI 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 363 CVRGANVTSGY---KGNPEANEAAfrfGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISP--IE-----VDSVLLGH 432
Cdd:PRK07768 390 ELRGESVTPGYltmDGFIPAQDAD---GWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPtdIEraaarVEGVRPGN 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 433 paiaqAVAFGVPDAKYGEEINCAViprEGVSLGEEEVLAYCRRNLAAFKV------PKKVYI--ADELPKTATGKIQRRI 504
Cdd:PRK07768 467 -----AVAVRLDAGHSREGFAVAV---ESNAFEDPAEVRRIRHQVAHEVVaevgvrPRNVVVlgPGSIPKTPSGKLRRAN 538
|
....*
gi 1002261995 505 VAQHF 509
Cdd:PRK07768 539 AAELV 543
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
169-505 |
5.40e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 112.82 E-value: 5.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 169 TSGTTSRPKGVPLT----QRNLAASVQNIRAvyrltEADATVIVL-PLFHVHGLLCGLLASLASGASVTLPAAG--RFSA 241
Cdd:PRK08308 109 SSGTTGEPKLIRRSwteiDREIEAYNEALNC-----EQDETPIVAcPVTHSYGLICGVLAALTRGSKPVIITNKnpKFAL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 242 stfwADMRGAGATWYTAVPTIHQIIidrhtskpeaeypalrfirscsASLAPaIMEKLEAAF--GAPVVEAYAMTEAShl 319
Cdd:PRK08308 184 ----NILRNTPQHILYAVPLMLHIL----------------------GRLLP-GTFQFHAVMtsGTPLPEAWFYKLRE-- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 320 MTSNPLPEDGARKAGSVgrAVGQEMAILDEEGrrveagksgeVCVRGANVTSGY-KGNPEanEAAFRFG--WFHTGDIGV 396
Cdd:PRK08308 235 RTTYMMQQYGCSEAGCV--SICPDMKSHLDLG----------NPLPHVSVSAGSdENAPE--EIVVKMGdkEIFTKDLGY 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 397 VDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLgeEEVLAYCRRN 476
Cdd:PRK08308 301 KSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDP--VQLREWCIQH 378
|
330 340
....*....|....*....|....*....
gi 1002261995 477 LAAFKVPKKVYIADELPKTATGKIQRRIV 505
Cdd:PRK08308 379 LAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
52-509 |
1.42e-26 |
|
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: 113.16 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPE--GNV-----AAQAAASKL 124
Cdd:cd05938 27 GLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVAPElqEAVeevlpALRADGVSV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 125 GLAHTTA------SLKDAAGQVhlAGFPASAAAAAKDFANDPsdvALFLHTSGTTSRPKGVPLTQRNLAASvQNIRAVYR 198
Cdd:cd05938 107 WYLSHTSntegviSLLDKVDAA--SDEPVPASLRAHVTIKSP---ALYIYTSGTTGLPKAARISHLRVLQC-SGFLSLCG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 199 LTEADATVIVLPLFHVHGLLCGLLASLASGASVTLpaAGRFSASTFWADMRGAGAtwytavpTIHQII--IDRH-TSKPE 275
Cdd:cd05938 181 VTADDVIYITLPLYHSSGFLLGIGGCIELGATCVL--KPKFSASQFWDDCRKHNV-------TVIQYIgeLLRYlCNQPQ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 276 AEYPALRFIRSCSAS-LAPAIMEKLEAAFG-APVVEAYAMTEAShLMTSNPlpedgARKAGSVGRA-------------- 339
Cdd:cd05938 252 SPNDRDHKVRLAIGNgLRADVWREFLRRFGpIRIREFYGSTEGN-IGFFNY-----TGKIGAVGRVsylykllfpfelik 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 340 --VGQEMAILDEEGRRVEAGKsGEVCVRGANVTS-----GYKGNPEANEA-----AFRFG--WFHTGDIGVVDEEGYLRL 405
Cdd:cd05938 326 fdVEKEEPVRDAQGFCIPVAK-GEPGLLVAKITQqspflGYAGDKEQTEKkllrdVFKKGdvYFNTGDLLVQDQQNFLYF 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 406 VGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEIN-CAVIPREGVSLGEEEVLAYCRRNLAAFKVPK 484
Cdd:cd05938 405 HDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHEGRIGmAAVKLKPGHEFDGKKLYQHVREYLPAYARPR 484
|
490 500
....*....|....*....|....*.
gi 1002261995 485 KVYIADELPKTATGKIQR-RIVAQHF 509
Cdd:cd05938 485 FLRIQDSLEITGTFKQQKvRLVEEGF 510
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
160-499 |
3.42e-26 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 112.88 E-value: 3.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 160 PSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTL-PAAgr 238
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLyPSP-- 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 239 fsastfwadmrgagaTWYTAVPtihQIIIDRH------TSKPEAEYPA---------LRFIRSCSASLAPAIMEKLEAAF 303
Cdd:PRK08043 442 ---------------LHYRIVP---ELVYDRNctvlfgTSTFLGNYARfanpydfarLRYVVAGAEKLQESTKQLWQDKF 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 304 GAPVVEAYAMTEASHLMTSN-PLpedgARKAGSVGRAV-GQEMAILDEEGrrVEAGksGEVCVRGANVTSGY-------- 373
Cdd:PRK08043 504 GLRILEGYGVTECAPVVSINvPM----AAKPGTVGRILpGMDARLLSVPG--IEQG--GRLQLKGPNIMNGYlrvekpgv 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 374 -----KGNPEANEAAfrfGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKY 448
Cdd:PRK08043 576 levptAENARGEMER---GWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASK 652
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1002261995 449 GEEIncaVIPREGVSLGEEEVLAYCRRN-LAAFKVPKKVYIADELPKTATGK 499
Cdd:PRK08043 653 GEAL---VLFTTDSELTREKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGK 701
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
52-513 |
9.09e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 112.36 E-value: 9.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITN----PEGNVAAQAAASKLGLA 127
Cdd:PRK12316 4597 GVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQshllQRLPIPDGLASLALDRD 4676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 128 HTTASLKDAAGQVHLagfpasaaaaakdfanDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADaTVI 207
Cdd:PRK12316 4677 EDWEGFPAHDPAVRL----------------HPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDD-RVL 4739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 208 VLPLFHVHGLLCGLLASLASGASVTLPAAGRFSASTFWADMRGAGATWYTAVPTIHQIIIDRhtSKPEAEYPALRFIRSC 287
Cdd:PRK12316 4740 QFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEH--AERDGEPPSLRVYCFG 4817
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 288 SASLAPAIMEK-LEAAFGAPVVEAYAMTEAShlMTSNPLPEDGARKAGSVGRAVGQEMA-----ILDEEGRRVEAGKSGE 361
Cdd:PRK12316 4818 GEAVAQASYDLaWRALKPVYLFNGYGPTETT--VTVLLWKARDGDACGAAYMPIGTPLGnrsgyVLDGQLNPLPVGVAGE 4895
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 362 VCVRGANVTSGYKGNPEANEAAF---RFG-----WFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHP 433
Cdd:PRK12316 4896 LYLGGEGVARGYLERPALTAERFvpdPFGapggrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHP 4975
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 434 AIAQAVAFGVPDAkYGEEINCAVIPREGVSLGEEEVLAYCR--------RNLAAFKVPKKVYIADELPKTATGKIQRR-- 503
Cdd:PRK12316 4976 AVREAVVIAQEGA-VGKQLVGYVVPQDPALADADEAQAELRdelkaalrERLPEYMVPAHLVFLARMPLTPNGKLDRKal 5054
|
490
....*....|....*.
gi 1002261995 504 ------IVAQHFVVPV 513
Cdd:PRK12316 5055 pqpdasLLQQAYVAPR 5070
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
182-511 |
1.02e-25 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 109.70 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 182 TQRNLAASVQNIRAVYRLTEADAtVIVLPLFHVHGLLcGLLASLASGasvtlpaaGRFSASTfWADMRGAGAT------- 254
Cdd:PRK07445 141 TWETLTASVQGFQRYFQLQQVNS-FCVLPLYHVSGLM-QFMRSFLTG--------GKLVILP-YKRLKSGQELppnpsdf 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 255 WYTAVPTIHQIIIDRHTskpeaeypalRFIRSCSASL---APAIMEKLEAA--FGAPVVEAYAMTE-ASHLMTSnpLPED 328
Cdd:PRK07445 210 FLSLVPTQLQRLLQLRP----------QWLAQFRTILlggAPAWPSLLEQArqLQLRLAPTYGMTEtASQIATL--KPDD 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 329 GARKAGSVGRavgqemaILDEEGRRVEAGKSGEVCVRGANVTSGYKgnPEANEAAfrfGWFHTGDIGVVDEEGYLRLVGR 408
Cdd:PRK07445 278 FLAGNNSSGQ-------VLPHAQITIPANQTGNITIQAQSLALGYY--PQILDSQ---GIFETDDLGYLDAQGYLHILGR 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 409 IKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGvSLGEEEVLAYCRRNLAAFKVPKKVYI 488
Cdd:PRK07445 346 NSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDP-SISLEELKTAIKDQLSPFKQPKHWIP 424
|
330 340
....*....|....*....|...
gi 1002261995 489 ADELPKTATGKIQRRIVAQHFVV 511
Cdd:PRK07445 425 VPQLPRNPQGKINRQQLQQIAVQ 447
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
159-509 |
1.23e-25 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 110.64 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 159 DPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAV--YRLTEADATVIVLPLFHVhgLLCGL-LASLASGASVTLPA 235
Cdd:PRK05620 179 DETTAAAICYSTGTTGAPKGVVYSHRSLYLQSLSLRTTdsLAVTHGESFLCCVPIYHV--LSWGVpLAAFMSGTPLVFPG 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 236 AGrFSASTFWADMRGAGATWYTAVPTIH-QIIIdrHTSKPEAEYPALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMT 314
Cdd:PRK05620 257 PD-LSAPTLAKIIATAMPRVAHGVPTLWiQLMV--HYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMT 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 315 EASHLMTSNPLPE--DGARKAG---SVGR-AVGQEMAILDEeGRRVEAG--KSGEVCVRGANVTSGYKGNP--------- 377
Cdd:PRK05620 334 ETSPVGTVARPPSgvSGEARWAyrvSQGRfPASLEYRIVND-GQVMESTdrNEGEIQVRGNWVTASYYHSPteegggaas 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 378 -----EANEAAFRF---GWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYG 449
Cdd:PRK05620 413 tfrgeDVEDANDRFtadGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWG 492
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002261995 450 EEINCAVIPREGVSLGEE---EVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRRIVAQHF 509
Cdd:PRK05620 493 ERPLAVTVLAPGIEPTREtaeRLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHL 555
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
160-475 |
2.41e-25 |
|
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: 109.75 E-value: 2.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 160 PSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEAD--ATVIV--LPLFHVHGLLCGLLASLASGASVTL-- 233
Cdd:cd05933 149 PNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATvgQESVVsyLPLSHIAAQILDIWLPIKVGGQVYFaq 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 234 PAAGRFS-ASTFwadmRGAGATWYTAVPTIHQIIIDR--------------------------HTSKPEAEYPALRFIR- 285
Cdd:cd05933 229 PDALKGTlVKTL----REVRPTAFMGVPRVWEKIQEKmkavgaksgtlkrkiaswakgvgletNLKLMGGESPSPLFYRl 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 286 -------------------SCSASLAPAIMEKLEAAFGA--PVVEAYAMTEASHLMT-SNPlpedGARKAGSVGRAV-GQ 342
Cdd:cd05933 305 akklvfkkvrkalgldrcqKFFTGAAPISRETLEFFLSLniPIMELYGMSETSGPHTiSNP----QAYRLLSCGKALpGC 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 343 EMAILDEEgrrveAGKSGEVCVRGANVTSGYKGNPEANEAAF-RFGWFHTGDIGVVDEEGYLRLVGRIKELI-NRGGEKI 420
Cdd:cd05933 381 KTKIHNPD-----ADGIGEICFWGRHVFMGYLNMEDKTEEAIdEDGWLHSGDLGKLDEDGFLYITGRIKELIiTAGGENV 455
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002261995 421 SPIEV-DSVLLGHPAIAQAVAFGvPDAKYGE---EINCAVIPREGVSLGE--EEVLAYCRR 475
Cdd:cd05933 456 PPVPIeDAVKKELPIISNAMLIG-DKRKFLSmllTLKCEVNPETGEPLDEltEEAIEFCRK 515
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
159-505 |
2.46e-25 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 109.99 E-value: 2.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 159 DPSDVALFLHTSGTTSRPKGVPLTQRNL---AASVQNIRAVYRLTE-----ADATVIVLPLFHVHG-LLCGLLASLASGA 229
Cdd:PLN02654 273 DAEDPLFLLYTSGSTGKPKGVLHTTGGYmvyTATTFKYAFDYKPTDvywctADCGWITGHSYVTYGpMLNGATVLVFEGA 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 230 SvTLPAAGRFsastfWADMRGAGATWYTAVPTIHQIIIdRHTSKPEAEYP--ALRFIRSCSASLAPAIMEKLEAAFG--- 304
Cdd:PLN02654 353 P-NYPDSGRC-----WDIVDKYKVTIFYTAPTLVRSLM-RDGDEYVTRHSrkSLRVLGSVGEPINPSAWRWFFNVVGdsr 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 305 APVVEAYAMTEASHLMTSnPLPEDGARKAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVCVRGA--NVTSGYKGNPEANE 381
Cdd:PLN02654 426 CPISDTWWQTETGGFMIT-PLPGAWPQKPGSATFPFfGVQPVIVDEKGKEIEGECSGYLCVKKSwpGAFRTLYGDHERYE 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 382 AAFrF----GWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVI 457
Cdd:PLN02654 505 TTY-FkpfaGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVT 583
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1002261995 458 PREGVSLGEE---EVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRRIV 505
Cdd:PLN02654 584 LVEGVPYSEElrkSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
160-470 |
7.55e-25 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 108.65 E-value: 7.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 160 PSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLcGLLASLASGAsvtlpAAGRF 239
Cdd:PLN02736 220 PEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYERV-NQIVMLHYGV-----AVGFY 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 240 SASTF--WADMRGAGATWYTAVPTIHQIIIDRHTSKP-----------EAEYPA-------------------------- 280
Cdd:PLN02736 294 QGDNLklMDDLAALRPTIFCSVPRLYNRIYDGITNAVkesgglkerlfNAAYNAkkqalengknpspmwdrlvfnkikak 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 281 ----LRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEASHLMTSNplpEDGARKAGSVGRAVGQ-EMAILD----EEG 351
Cdd:PLN02736 374 lggrVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGM---DEGDNLSGHVGSPNPAcEVKLVDvpemNYT 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 352 RRVEAGKSGEVCVRGANVTSGY-KGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRG-GEKISPIEVDSVL 429
Cdd:PLN02736 451 SEDQPYPRGEICVRGPIIFKGYyKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPEKIENVY 530
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1002261995 430 LGHPAIAQAVAfgvpdakYGEEINCAVIpreGVSLGEEEVL 470
Cdd:PLN02736 531 AKCKFVAQCFV-------YGDSLNSSLV---AVVVVDPEVL 561
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
52-507 |
1.17e-24 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 106.49 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLaviraravaaplnpAYTQeefefylsdSGARLLITNPEGNVAAQAA-ASKLGLAHTt 130
Cdd:PRK09029 49 GVVEGSGVALRGKNSPETLLAYL--------------ALLQ---------CGARVLPLNPQLPQPLLEElLPSLTLDFA- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 131 ASLKDAAGQVHLAGFPASAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLP 210
Cdd:PRK09029 105 LVLEGENTFSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQDSWLLSLP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 211 LFHVHGLlcGLLAS-LASGASVTLPAAGRFSASTfwadmrgAGATWYTAVPTIHQIIIDRHtskpeAEYPALRFIRSCSA 289
Cdd:PRK09029 185 LFHVSGQ--GIVWRwLYAGATLVVRDKQPLEQAL-------AGCTHASLVPTQLWRLLDNR-----SEPLSLKAVLLGGA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 290 SLAPAIMEKLEAaFGapvVEA---YAMTE-AShlmTSNPLPEDGARKAGSV--GRAVgqemaildeegRRVEagksGEVC 363
Cdd:PRK09029 251 AIPVELTEQAEQ-QG---IRCwcgYGLTEmAS---TVCAKRADGLAGVGSPlpGREV-----------KLVD----GEIW 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 364 VRGANVTSGY----KGNPEANEAafrfGWFHTGDIGVVDEeGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAV 439
Cdd:PRK09029 309 LRGASLALGYwrqgQLVPLVNDE----GWFATRDRGEWQN-GELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVF 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002261995 440 AFGVPDAKYGEEiNCAVIprEGVSLGEEEVLA-YCRRNLAAFKVPKKVYIADELPKTATGKIQRRIVAQ 507
Cdd:PRK09029 384 VVPVADAEFGQR-PVAVV--ESDSEAAVVNLAeWLQDKLARFQQPVAYYLLPPELKNGGIKISRQALKE 449
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
52-503 |
3.08e-24 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 107.56 E-value: 3.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPE--GNVAAQAAASKLGLAHT 129
Cdd:PRK05691 1177 GVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHllERLPQAEGVSAIALDSL 1256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 130 -TASLKDAAGQVHLagfpasaaaaakdfanDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIV 208
Cdd:PRK05691 1257 hLDSWPSQAPGLHL----------------HGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQK 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 209 LPL-FHVHGLLCglLASLASGASVTLPAAGRFSASTFWADM-RGAGATWYTAVPTIHQIIIDRHTSkpeAEYPALRFIRS 286
Cdd:PRK05691 1321 APIsFDVSVWEC--FWPLITGCRLVLAGPGEHRDPQRIAELvQQYGVTTLHFVPPLLQLFIDEPLA---AACTSLRRLFS 1395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 287 CSASLAPAIMEK-LEAAFGAPVVEAYAMTEASHLMTS-NPLPEDGARKagSVGRAVGQEMA-ILDEEGRRVEAGKSGEVC 363
Cdd:PRK05691 1396 GGEALPAELRNRvLQRLPQVQLHNRYGPTETAINVTHwQCQAEDGERS--PIGRPLGNVLCrVLDAELNLLPPGVAGELC 1473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 364 VRGANVTSGYKGNPeaNEAAFRF----------GWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHP 433
Cdd:PRK05691 1474 IGGAGLARGYLGRP--ALTAERFvpdplgedgaRLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQP 1551
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 434 AIAQAVAFgVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:PRK05691 1552 GVAQAAVL-VREGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRR 1620
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
52-503 |
3.84e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 107.17 E-value: 3.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNpegnvaaQAAASKLGLAHTTA 131
Cdd:PRK12467 1620 GVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQ-------SHLQARLPLPDGLR 1692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 SLKDAAGQVHLAGFPASAAAAAKdfanDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPl 211
Cdd:PRK12467 1693 SLVLDQEDDWLEGYSDSNPAVNL----APQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTS- 1767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 FHVHGLLCGLLASLASGASVTL--PAAGRfSASTFWADMRGAGATWYTAVPTIHQIIIdrHTSKPEAEYPALRFIRSCSA 289
Cdd:PRK12467 1768 FAFDVSVWELFWPLINGARLVIapPGAHR-DPEQLIQLIERQQVTTLHFVPSMLQQLL--QMDEQVEHPLSLRRVVCGGE 1844
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 290 SLAPAIMEKLEAAFGAP-VVEAYAMTEASHLMTSNPLpeDGARKAGSVGRAVGQEMA-----ILDEEGRRVEAGKSGEVC 363
Cdd:PRK12467 1845 ALEVEALRPWLERLPDTgLFNLYGPTETAVDVTHWTC--RRKDLEGRDSVPIGQPIAnlstyILDASLNPVPIGVAGELY 1922
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 364 VRGANVTSGYKGNPEANEAAF---RFG-----WFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAI 435
Cdd:PRK12467 1923 LGGVGLARGYLNRPALTAERFvadPFGtvgsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGV 2002
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002261995 436 AQAVAFGVpDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAA--------FKVPKKVYIADELPKTATGKIQRR 503
Cdd:PRK12467 2003 REAVVIAQ-DGANGKQLVAYVVPTDPGLVDDDEAQVALRAILKNhlkaslpeYMVPAHLVFLARMPLTPNGKLDRK 2077
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
52-512 |
5.66e-24 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 106.79 E-value: 5.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLItnpeGNVAAQAAASKLGLAHTTA 131
Cdd:PRK05691 2234 GVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLL----SDRALFEALGELPAGVARW 2309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 SLKDAAgqvhlaGFPASAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVivlpl 211
Cdd:PRK05691 2310 CLEDDA------AALAAYSDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCEL----- 2378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 fHVHGLLCG-----LLASLASGASVTLPAAGRFSASTFWADMRGAGATWYTAVPT----IHQIIIDRHTSKPeaeypaLR 282
Cdd:PRK05691 2379 -HFYSINFDaaserLLVPLLCGARVVLRAQGQWGAEEICQLIREQQVSILGFTPSygsqLAQWLAGQGEQLP------VR 2451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 283 FIRSCSASLAPAIMEKLEAAFgAPVV--EAYAMTEASHLMTSNPLPEDGARKAGSV--GRAVGQEMA-ILDEEGRRVEAG 357
Cdd:PRK05691 2452 MCITGGEALTGEHLQRIRQAF-APQLffNAYGPTETVVMPLACLAPEQLEEGAASVpiGRVVGARVAyILDADLALVPQG 2530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 358 KSGEVCVRGANVTSGYKGNPEAneAAFRF----------GWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDS 427
Cdd:PRK05691 2531 ATGELYVGGAGLAQGYHDRPGL--TAERFvadpfaadggRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIES 2608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 428 VLLGHPAIAQAVAFGVpDAKYGEE----INCAVIPREGVSLGE--EEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQ 501
Cdd:PRK05691 2609 RLLEHPAVREAVVLAL-DTPSGKQlagyLVSAVAGQDDEAQAAlrEALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLD 2687
|
490
....*....|....*....
gi 1002261995 502 RRIVA--------QHFVVP 512
Cdd:PRK05691 2688 RRALPapdpelnrQAYQAP 2706
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
99-502 |
8.51e-24 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 105.09 E-value: 8.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 99 LSDSGARLLITNPE----GNVAAQAAASKLGLAHTTASLKDAAGqvhlagfpasaaaaAKDFANDPSDVALFLHTSGTTS 174
Cdd:PRK09192 124 LASAQPAAIITPDEllpwVNEATHGNPLLHVLSHAWFKALPEAD--------------VALPRPTPDDIAYLQYSSGSTR 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 175 RPKGVPLTQRNLAAsvqNIRAVYR----LTEADATVIVLPLFHVHGLLCGLLASLASGASVTLPAAGRFSASTF-WADM- 248
Cdd:PRK09192 190 FPRGVIITHRALMA---NLRAISHdglkVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFARRPLqWLDLi 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 249 -RGAGATWYTavPTI-HQIIIDRHTSKPEAEYPALRF---------IRscsaslaPAIMEKLEAAFgAPV-------VEA 310
Cdd:PRK09192 267 sRNRGTISYS--PPFgYELCARRVNSKDLAELDLSCWrvagigadmIR-------PDVLHQFAEAF-APAgfddkafMPS 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 311 YAMTEASHLMTSNPL----------------------PEDGARKAGSV---GRAV-GQEMAILDEEGRRVEAGKSGEVCV 364
Cdd:PRK09192 337 YGLAEATLAVSFSPLgsgivveevdrdrleyqgkavaPGAETRRVRTFvncGKALpGHEIEIRNEAGMPLPERVVGHICV 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 365 RGANVTSGYKGNPEANEAAFRFGWFHTGDIGVVdEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQ--AVAFG 442
Cdd:PRK09192 417 RGPSLMSGYFRDEESQDVLAADGWLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRSgdAAAFS 495
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002261995 443 VPDAkyGEEINCAVIPREGVSLGEEEVLAYCRRNL--AAFKVPKKVYI--ADELPKTATGKIQR 502
Cdd:PRK09192 496 IAQE--NGEKIVLLVQCRISDEERRGQLIHALAALvrSEFGVEAAVELvpPHSLPRTSSGKLSR 557
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
169-506 |
1.24e-23 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 104.32 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 169 TSGTTSRPKGVPLTQRNLAASVQNIRAV----YRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTlpaAGRFSASTF 244
Cdd:PRK05857 177 TSGTTGEPKAVLLANRTFFAVPDILQKEglnwVTWVVGETTYSPLPATHIGGLWWILTCLMHGGLCVT---GGENTTSLL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 245 WADMRGAGATwYTAVPTIHQIIIDRHTSKpEAEYPALRFIRSCSASLAPAIMEKLEAAfGAPVVEAYAMTEAShlMTSNP 324
Cdd:PRK05857 254 EILTTNAVAT-TCLVPTLLSKLVSELKSA-NATVPSLRLVGYGGSRAIAADVRFIEAT-GVRTAQVYGLSETG--CTALC 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 325 LPEDGAR----KAGSVGRAV-GQEMAILDEEGRRVEAGKSGEVCVRG-------ANVTsGYKGNPEANEAAFRFGWFHTG 392
Cdd:PRK05857 329 LPTDDGSivkiEAGAVGRPYpGVDVYLAATDGIGPTAPGAGPSASFGtlwikspANML-GYWNNPERTAEVLIDGWVNTG 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 393 DIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLG-----EE 467
Cdd:PRK05857 408 DLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESaaralKH 487
|
330 340 350
....*....|....*....|....*....|....*....
gi 1002261995 468 EVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRRIVA 506
Cdd:PRK05857 488 TIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLA 526
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
159-442 |
1.37e-23 |
|
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: 104.43 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 159 DPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTLPAagr 238
Cdd:cd17641 156 KGEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIVNFPE--- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 239 fSASTFWADMRGAGATWYTAVPTIHQIII------------------------------DRHTSKPEAE----------- 277
Cdd:cd17641 233 -EPETMMEDLREIGPTFVLLPPRVWEGIAadvrarmmdatpfkrfmfelgmklglraldRGKRGRPVSLwlrlaswlada 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 278 --YPALR------FIRSCS---ASLAPAIMEKLEAaFGAPVVEAYAMTEASHLMTSNPlpeDGARKAGSVGravgqeMAI 346
Cdd:cd17641 312 llFRPLRdrlgfsRLRSAAtggAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHR---DGDVDPDTVG------VPF 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 347 LDEEGRRVEAGksgEVCVRGANVTSGYKGNPEANEAAF-RFGWFHTGDIGVVDEEGYLRLVGRIKELINRG-GEKISPIE 424
Cdd:cd17641 382 PGTEVRIDEVG---EILVRSPGVFVGYYKNPEATAEDFdEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSPQF 458
|
330
....*....|....*...
gi 1002261995 425 VDSVLLGHPAIAQAVAFG 442
Cdd:cd17641 459 IENKLKFSPYIAEAVVLG 476
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
424-499 |
2.83e-23 |
|
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: 93.38 E-value: 2.83e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002261995 424 EVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGK 499
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
160-509 |
3.56e-23 |
|
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: 102.57 E-value: 3.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 160 PSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTL-PAAGR 238
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLmPTRLF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 239 FSASTFWADMRGAGATWYTAVPTI-HQIIIDRHtsKPEAEY----PALRFIRSCSASLAPAIMEKLE---AAFG---APV 307
Cdd:cd05908 185 IRRPILWLKKASEHKATIVSSPNFgYKYFLKTL--KPEKANdwdlSSIRMILNGAEPIDYELCHEFLdhmSKYGlkrNAI 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 308 VEAYAMTEAS--------------------HLMTSNPLPE-DGARKAG----SVGRAVGQ-EMAILDEEGRRVEAGKSGE 361
Cdd:cd05908 263 LPVYGLAEASvgaslpkaqspfktitlgrrHVTHGEPEPEvDKKDSECltfvEVGKPIDEtDIRICDEDNKILPDGYIGH 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 362 VCVRGANVTSGYKGNPEANEAAFRF-GWFHTGDIGVVdEEGYLRLVGRIKELINRGGEKISP-------IEVDSVLLGhp 433
Cdd:cd05908 343 IQIRGKNVTPGYYNNPEATAKVFTDdGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPhdieriaEELEGVELG-- 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 434 aiaQAVAFGVPDAKY-GEEINCAVIPREgvslGEEEVLAYCRR---NLAAFK--VPKKVYIADELPKTATGKIQRRIVAQ 507
Cdd:cd05908 420 ---RVVACGVNNSNTrNEEIFCFIEHRK----SEDDFYPLGKKikkHLNKRGgwQINEVLPIRRIPKTTSGKVKRYELAQ 492
|
..
gi 1002261995 508 HF 509
Cdd:cd05908 493 RY 494
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
52-503 |
5.98e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 103.70 E-value: 5.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNpegnvaaQAAASKLGLAHTTA 131
Cdd:PRK12467 3141 GVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQ-------AHLLEQLPAPAGDT 3213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 SL----------KDAAGQVHLagfpasaaaaakdfanDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTe 201
Cdd:PRK12467 3214 ALtldrldlngySENNPSTRV----------------MGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELD- 3276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 202 ADATVIVLPLFHVHGLLCGLLASLASGASVTLPAAGRFSASTFWADMRGAGATWYTAVPTIHQIIIDRHTSkpeAEYPAL 281
Cdd:PRK12467 3277 ANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGG---ADCASL 3353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 282 RFIRSCSASLAPAIMEKLEAAFG-APVVEAYAMTEASHLMTSNPLPEDGARKAGSV--GRAVGQEMA-ILDEEGRRVEAG 357
Cdd:PRK12467 3354 DIYVFGGEAVPPAAFEQVKRKLKpRGLTNGYGPTEAVVTVTLWKCGGDAVCEAPYApiGRPVAGRSIyVLDGQLNPVPVG 3433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 358 KSGEVCVRGANVTSGYKGNPEAneAAFRF----------GWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDS 427
Cdd:PRK12467 3434 VAGELYIGGVGLARGYHQRPSL--TAERFvadpfsgsggRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEA 3511
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002261995 428 VLLGHPAIAQAVAFGVpDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:PRK12467 3512 RLLQHPSVREAVVLAR-DGAGGKQLVAYVVPADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRK 3586
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
52-503 |
6.41e-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: 101.36 E-value: 6.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEgnvaaqaaasklglahtta 131
Cdd:cd17644 46 GVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYILEDAQISVLLTQPE------------------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 slkdaagqvhlagfpasaaaaakdfandpsDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPL 211
Cdd:cd17644 107 ------------------------------NLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 -FHVHglLCGLLASLASGASVTL-PAAGRFSASTFWADMRGAGATWYTAVPTIHQIIIDRHTSKPEAEYPALRFIRSCSA 289
Cdd:cd17644 157 aFDVA--AEEIYVTLLSGATLVLrPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLPSSLRLVIVGGE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 290 SLAPAIMEKLEAAFGAPV--VEAYAMTEASHLMTSNPLPEDGARKAGSV--GRAVGQEMA-ILDEEGRRVEAGKSGEVCV 364
Cdd:cd17644 235 AVQPELVRQWQKNVGNFIqlINVYGPTEATIAATVCRLTQLTERNITSVpiGRPIANTQVyILDENLQPVPVGVPGELHI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 365 RGANVTSGYKGNPEANEAAFRFGWFH---------TGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAI 435
Cdd:cd17644 315 GGVGLARGYLNRPELTAEKFISHPFNsseserlykTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDV 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002261995 436 AQAVAFGVPDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:cd17644 395 KTAVVIVREDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRR 462
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
52-503 |
2.99e-22 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 101.27 E-value: 2.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITnpegnVAAQAA----ASKLGLA 127
Cdd:PRK10252 504 GVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLIT-----TADQLPrfadVPDLTSL 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 128 HTTASLKDAAGQVhlagfpasaaaaakDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVI 207
Cdd:PRK10252 579 CYNAPLAPQGAAP--------------LQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQ 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 208 VLPlfhvhgllCGllaslasgasvtlpaagrFSAST---FWADMrgAGATWYTAVPTIH------QIIIDRH-------- 270
Cdd:PRK10252 645 KTP--------CS------------------FDVSVwefFWPFI--AGAKLVMAEPEAHrdplamQQFFAEYgvttthfv 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 271 ---------TSKPEAEYPALRFIRS--CSASLAPA-IMEKLEAAFGAPVVEAYAMTEASHLMTSNPL-PEDGARKAGS-- 335
Cdd:PRK10252 697 psmlaafvaSLTPEGARQSCASLRQvfCSGEALPAdLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAfGEELAAVRGSsv 776
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 336 -VGRAV-GQEMAILDEEGRRVEAGKSGEVCVRGANVTSGYKGNPEANEAAFRFGWF-------HTGDIGVVDEEGYLRLV 406
Cdd:PRK10252 777 pIGYPVwNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermyRTGDVARWLDDGAVEYL 856
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 407 GRIKELINRGGEKISPIEVDSVLLGHPAIAQAVA----FGVPDAKYGEEINCA--VIPREGVSLGEEEVLAYCRRNLAAF 480
Cdd:PRK10252 857 GRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVThacvINQAAATGGDARQLVgyLVSQSGLPLDTSALQAQLRERLPPH 936
|
490 500
....*....|....*....|...
gi 1002261995 481 KVPKKVYIADELPKTATGKIQRR 503
Cdd:PRK10252 937 MVPVVLLQLDQLPLSANGKLDRK 959
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
159-411 |
1.07e-21 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 98.80 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 159 DPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIV--LPLFHVHGLLCGLLASLASGASVTL--- 233
Cdd:PRK08180 207 GPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEPPVLVdwLPWNHTFGGNHNLGIVLYNGGTLYIddg 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 234 -PAAGRFsASTFwADMRGAGATWYTAVPTIHQIIIDRHTSKPE-AE--YPALRFIRSCSASLAPAIMEKLEAAFGA---- 305
Cdd:PRK08180 287 kPTPGGF-DETL-RNLREISPTVYFNVPKGWEMLVPALERDAAlRRrfFSRLKLLFYAGAALSQDVWDRLDRVAEAtcge 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 306 --PVVEAYAMTEASHLMTSNPLPEDgarKAGSVGRAV-GQEMAILDEEGRRveagksgEVCVRGANVTSGYKGNPEANEA 382
Cdd:PRK08180 365 riRMMTGLGMTETAPSATFTTGPLS---RAGNIGLPApGCEVKLVPVGGKL-------EVRVKGPNVTPGYWRAPELTAE 434
|
250 260 270
....*....|....*....|....*....|....*
gi 1002261995 383 AF-RFGWFHTGDIG-VVDEE----GyLRLVGRIKE 411
Cdd:PRK08180 435 AFdEEGYYRSGDAVrFVDPAdperG-LMFDGRIAE 468
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
162-443 |
1.14e-21 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 97.53 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 162 DVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLCGlLASLASGASVTLPAagRFSA 241
Cdd:cd05910 86 EPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLFALFGPALG-LTSVIPDMDPTRPA--RADP 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 242 STFWADMRGAGATWYTAVPTIHQiIIDRHTSKPEAEYPALRFIRSCSASLAPAIMEKLEAAF--GAPVVEAYAMTEA--- 316
Cdd:cd05910 163 QKLVGAIRQYGVSIVFGSPALLE-RVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEAlpv 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 317 ----SH--LMTSNPLPEDGArkAGSVGRAV-GQEMAIL--DEEG-------RRVEAGKSGEVCVRGANVTSGYKGNPEAN 380
Cdd:cd05910 242 ssigSRelLATTTAATSGGA--GTCVGRPIpGVRVRIIeiDDEPiaewddtLELPRGEIGEITVTGPTVTPTYVNRPVAT 319
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002261995 381 EAA------FRFgWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGV 443
Cdd:cd05910 320 ALAkiddnsEGF-WHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV 387
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
159-503 |
1.42e-21 |
|
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: 97.61 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 159 DPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADAtviVL----PLFHVHglLCGLLASLASGASVTLP 234
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESR---VLqfasYTFDVS--ILEIFTTLAAGGCLCIP 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 235 A----AGRFSAStfwadMRGAGATWYTAVPTIHQIIidrhtsKPEaEYPALRFIrsCSA--SLAPAIMEKLeaAFGAPVV 308
Cdd:cd05918 179 SeedrLNDLAGF-----INRLRVTWAFLTPSVARLL------DPE-DVPSLRTL--VLGgeALTQSDVDTW--ADRVRLI 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 309 EAYAMTEASHLMTSNPLPEDGarKAGSVGRAVGQEMAILDEE--GRRVEAGKSGEVCVRGANVTSGYKGNPEANEAAF-- 384
Cdd:cd05918 243 NAYGPAECTIAATVSPVVPST--DPRNIGRPLGATCWVVDPDnhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFie 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 385 --------------RFgwFHTGDIGVVDEEGYLRLVGR----IK------EL------INRGGEKISPIEVDSVL-LGHP 433
Cdd:cd05918 321 dpawlkqegsgrgrRL--YRTGDLVRYNPDGSLEYVGRkdtqVKirgqrvELgeiehhLRQSLPGAKEVVVEVVKpKDGS 398
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002261995 434 AIAQAVAFGVPDakyGEEINCAVIPREGVSLGEE------EVLAYCRRNLAAFKVPKkVYIA-DELPKTATGKIQRR 503
Cdd:cd05918 399 SSPQLVAFVVLD---GSSSGSGDGDSLFLEPSDEfralvaELRSKLRQRLPSYMVPS-VFLPlSHLPLTASGKIDRR 471
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
52-503 |
4.78e-21 |
|
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: 96.00 E-value: 4.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNpegnvaaqaaasklglAHTTA 131
Cdd:cd17656 34 GVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLTQ----------------RHLKS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 SLKDAAGQVHLAG-FPASAAAAAKDFANDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRA-VYRLTEADATVIVL 209
Cdd:cd17656 98 KLSFNKSTILLEDpSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREkTNINFSDKVLQFAT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 210 PLFHVhgllC--GLLASLASGASVTL-PAAGR------------------FSASTFW---ADMRGAGATWYTAVPTI--- 262
Cdd:cd17656 178 CSFDV----CyqEIFSTLLSGGTLYIiREETKrdveqlfdlvkrhnievvFLPVAFLkfiFSEREFINRFPTCVKHIita 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 263 -HQIIIDRhtskpeaeyPALRFIRSCSASLApaimekleaafgapvvEAYAMTEAsHLMTSNPL-PEDGARKAGSVGRAV 340
Cdd:cd17656 254 gEQLVITN---------EFKEMLHEHNVHLH----------------NHYGPSET-HVVTTYTInPEAEIPELPPIGKPI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 341 GQ-EMAILDEEGRRVEAGKSGEVCVRGANVTSGYKGNPE------------ANEAAFRfgwfhTGDIGVVDEEGYLRLVG 407
Cdd:cd17656 308 SNtWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQEltaekffpdpfdPNERMYR-----TGDLARYLPDGNIEFLG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 408 RIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKyGEEINCAVIPREgVSLGEEEVLAYCRRNLAAFKVPKKVY 487
Cdd:cd17656 383 RADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDK-GEKYLCAYFVME-QELNISQLREYLAKQLPEYMIPSFFV 460
|
490
....*....|....*.
gi 1002261995 488 IADELPKTATGKIQRR 503
Cdd:cd17656 461 PLDQLPLTPNGKVDRK 476
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
159-446 |
5.15e-21 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 96.12 E-value: 5.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 159 DPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPLFHVHGLLCGLLASL-----ASGASVT- 232
Cdd:PRK09274 172 APDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLFALFGPALGMTSVIpdmdpTRPATVDp 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 233 ---LPAAGRFSASTfwadMRGAGATWYTavptihqiiIDRHTSKPEAEYPALRFIRSCSASLAPAIMEKLEAAF--GAPV 307
Cdd:PRK09274 252 aklFAAIERYGVTN----LFGSPALLER---------LGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAMLppDAEI 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 308 VEAYAMTEA---------SHLMTSNPLPEDGArkaGS-VGRAV-GQEMAILD---------EEGRRVEAGKSGEVCVRGA 367
Cdd:PRK09274 319 LTPYGATEAlpissiesrEILFATRAATDNGA---GIcVGRPVdGVEVRIIAisdapipewDDALRLATGEIGEIVVAGP 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 368 NVTSGYKGNPEANEAA-----FRFGWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQA--VA 440
Cdd:PRK09274 396 MVTRSYYNRPEATRLAkipdgQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSalVG 475
|
....*.
gi 1002261995 441 FGVPDA 446
Cdd:PRK09274 476 VGVPGA 481
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
52-503 |
9.56e-21 |
|
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: 94.54 E-value: 9.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 52 GVLPGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNPEgnvaaqaaasklglahtta 131
Cdd:cd17645 44 GVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILLTNPD------------------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 132 slkdaagqvhlagfpasaaaaakdfandpsDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIVLPl 211
Cdd:cd17645 105 ------------------------------DLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYAS- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 212 FHVHGLLCGLLASLASGASV-TLPAAGRFSASTFWADMRGAGATwYTAVPTihqiiidrhtskPEAEypalRFIRSCSAS 290
Cdd:cd17645 154 FSFDASAWEIFPHLTAGAALhVVPSERRLDLDALNDYFNQEGIT-ISFLPT------------GAAE----QFMQLDNQS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 291 LAPAIM--EKLEAAFGAP--VVEAYAMTEASHLMTSNPLpeDGARKAGSVGRAVGQ-EMAILDEEGRRVEAGKSGEVCVR 365
Cdd:cd17645 217 LRVLLTggDKLKKIERKGykLVNNYGPTENTVVATSFEI--DKPYANIPIGKPIDNtRVYILDEALQLQPIGVAGELCIA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 366 GANVTSGYKGNPEanEAAFRF---------GWFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIA 436
Cdd:cd17645 295 GEGLARGYLNRPE--LTAEKFivhpfvpgeRMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIE 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002261995 437 QAVAFGVPDAKYGEEINCAVIPREGVSLgeEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:cd17645 373 LAAVLAKEDADGRKYLVAYVTAPEEIPH--EELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRK 437
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
159-428 |
3.15e-20 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 93.68 E-value: 3.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 159 DPSDVALFLHTSGTTSRPKGVPLTQrnlAASVQNIRAVYRLTEADATVIV----LPLFHVHGLLCgLLASLASGASVTLP 234
Cdd:PRK05851 150 DSGGPAVLQGTAGSTGTPRTAILSP---GAVLSNLRGLNARVGLDAATDVgcswLPLYHDMGLAF-LLTAALAGAPLWLA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 235 AAGRFSASTF-WAD-MRGAGATwYTAVPTIHQIIIDRHTSK-PEAEYPALRFIRSCSASLAPAIMEKLEAA---FG---A 305
Cdd:PRK05851 226 PTTAFSASPFrWLSwLSDSRAT-LTAAPNFAYNLIGKYARRvSDVDLGALRVALNGGEPVDCDGFERFATAmapFGfdaG 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 306 PVVEAYAMTEASHLMTSnPLPEDG-------------ARKAGSVGRAV-GQEMAILDEEGRRVEAGKS-GEVCVRGANVT 370
Cdd:PRK05851 305 AAAPSYGLAESTCAVTV-PVPGIGlrvdevttddgsgARRHAVLGNPIpGMEVRISPGDGAAGVAGREiGEIEIRGASMM 383
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1002261995 371 SGYKGNPEANeaafRFGWFHTGDIGVVDEEGyLRLVGRIKELINRGGEKISPIEVDSV 428
Cdd:PRK05851 384 SGYLGQAPID----PDDWFPTGDLGYLVDGG-LVVCGRAKELITVAGRNIFPTEIERV 436
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
160-481 |
1.46e-18 |
|
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: 88.64 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 160 PSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIV--LPLFHVHGLLCGLLASLASGASVTL---- 233
Cdd:cd05921 164 PDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPPVLVdwLPWNHTFGGNHNFNLVLYNGGTLYIddgk 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 234 PAAGRFSASTfwADMRGAGATWYTAVPTIHQIII---DRHTSKPEAEYPALRFIRSCSASLAPAIMEKLEAAFGA----- 305
Cdd:cd05921 244 PMPGGFEETL--RNLREISPTVYFNVPAGWEMLVaalEKDEALRRRFFKRLKLMFYAGAGLSQDVWDRLQALAVAtvger 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 306 -PVVEAYAMTEASHLMTSNPLPEDgarKAGSVG-RAVGQEMaildeegRRVEAGKSGEVCVRGANVTSGYKGNPEANEAA 383
Cdd:cd05921 322 iPMMAGLGATETAPTATFTHWPTE---RSGLIGlPAPGTEL-------KLVPSGGKYEVRVKGPNVTPGYWRQPELTAQA 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 384 FrfgwfhtgdigvvDEEGYLRL------------------VGRIKE---LINRGGEKISPIEVDSVLLGHPAIAQAVAFG 442
Cdd:cd05921 392 F-------------DEEGFYCLgdaakladpddpakglvfDGRVAEdfkLASGTWVSVGPLRARAVAACAPLVHDAVVAG 458
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1002261995 443 ----------VPDAKYGEEINCAVIPREGVSLGEEEVLAYCRRNLAAFK 481
Cdd:cd05921 459 edraevgalvFPDLLACRRLVGLQEASDAEVLRHAKVRAAFRDRLAALN 507
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
169-507 |
1.65e-18 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 88.41 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 169 TSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEA-----------DATVIVL-PlfhvhgllcgllaSLASGAS-VTLPA 235
Cdd:PRK04813 151 TSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGpqflnqapysfDLSVMDLyP-------------TLASGGTlVALPK 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 236 agrfsastfwaDMrgagatwyTAVP-----TIHQIIIDRHTSKP-------------EAEYPALRFIRSCSASLAPAIME 297
Cdd:PRK04813 218 -----------DM--------TANFkqlfeTLPQLPINVWVSTPsfadmclldpsfnEEHLPNLTHFLFCGEELPHKTAK 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 298 KLEAAF-GAPVVEAYAMTEASHLMTS-----------NPLPedgarkagsVGRA-VGQEMAILDEEGRRVEAGKSGEVCV 364
Cdd:PRK04813 279 KLLERFpSATIYNTYGPTEATVAVTSieitdemldqyKRLP---------IGYAkPDSPLLIIDEEGTKLPDGEQGEIVI 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 365 RGANVTSGYKGNPEANEAAFRF----GWFHTGDIGVVDeEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAVA 440
Cdd:PRK04813 350 SGPSVSKGYLNNPEKTAEAFFTfdgqPAYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVV 428
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002261995 441 fgVPDAKYGEEIN--CAVIPREGVSLGEEEVLAYCRRNLA----AFKVPKK-VYIaDELPKTATGKIQRRIVAQ 507
Cdd:PRK04813 429 --VPYNKDHKVQYliAYVVPKEEDFEREFELTKAIKKELKerlmEYMIPRKfIYR-DSLPLTPNGKIDRKALIE 499
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
159-502 |
5.86e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 87.92 E-value: 5.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 159 DPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATVIV--LPLFHVHGLLCGLLASLASGASVTLPAA 236
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPDDVIVswLPLYHDMGLIGGLLQPIFSGVPCVLMSP 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 237 GRFSASTFwadmrgagaTWYTAVPTIHQIIidrhTSKPEAEYpalrfiRSCSASLAPAIMEKLE-----AAFGA--PVVE 309
Cdd:PRK05691 244 AYFLERPL---------RWLEAISEYGGTI----SGGPDFAY------RLCSERVSESALERLDlsrwrVAYSGsePIRQ 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 310 ----------------------AYAMTEASHLMTSNP-------LPEDGARKA--------GSVGRAVGQ---EMAILDE 349
Cdd:PRK05691 305 dslerfaekfaacgfdpdsffaSYGLAEATLFVSGGRrgqgipaLELDAEALArnraepgtGSVLMSCGRsqpGHAVLIV 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 350 EGRRVEA---GKSGEVCVRGANVTSGYKGNPEANEAAF--RFG--WFHTGDIGVVdEEGYLRLVGRIKE-LINRGG---- 417
Cdd:PRK05691 385 DPQSLEVlgdNRVGEIWASGPSIAHGYWRNPEASAKTFveHDGrtWLRTGDLGFL-RDGELFVTGRLKDmLIVRGHnlyp 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 418 ---EKISPIEVDSVLLGHPAiaqavAFGVPDAkyGEE-INCAVIPREGV--SLGEEEVLAYCRRNLA-AFK-VPKKVYIA 489
Cdd:PRK05691 464 qdiEKTVEREVEVVRKGRVA-----AFAVNHQ--GEEgIGIAAEISRSVqkILPPQALIKSIRQAVAeACQeAPSVVLLL 536
|
410
....*....|....*
gi 1002261995 490 D--ELPKTATGKIQR 502
Cdd:PRK05691 537 NpgALPKTSSGKLQR 551
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
160-413 |
9.75e-17 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 83.33 E-value: 9.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 160 PSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVY-----RLTEADATVIVLPLFHVhglLCGLLAS--LASGASVT 232
Cdd:PLN02430 219 PLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVDLFMeqfedKMTHDDVYLSFLPLAHI---LDRMIEEyfFRKGASVG 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 233 LpAAGRFSAstFWADMRGAGATWYTAVPTIHQIIID--------------------------------RH-TSKPEAEYP 279
Cdd:PLN02430 296 Y-YHGDLNA--LRDDLMELKPTLLAGVPRVFERIHEgiqkalqelnprrrlifnalykyklawmnrgySHkKASPMADFL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 280 A-----------LRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEASHLmTSNPLPEDGARkAGSVGR-AVGQEMAIl 347
Cdd:PLN02430 373 AfrkvkaklggrLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGP-TTLGFPDEMCM-LGTVGApAVYNELRL- 449
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002261995 348 dEEGRRVE-----AGKSGEVCVRGANVTSGYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELI 413
Cdd:PLN02430 450 -EEVPEMGydplgEPPRGEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLI 519
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
160-433 |
1.40e-16 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 82.86 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 160 PSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVY-RLTEADATVIVLPLFHVHGL-----LCGLLASLASGASVTL 233
Cdd:PLN02387 249 PNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVpKLGKNDVYLAYLPLAHILELaaesvMAAVGAAIGYGSPLTL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 234 P-AAGRFSASTFwADMRGAGATWYTAVPTIHQIIIDRHTSKPEAE---------------------------------YP 279
Cdd:PLN02387 329 TdTSNKIKKGTK-GDASALKPTLMTAVPAILDRVRDGVRKKVDAKgglakklfdiaykrrlaaiegswfgawglekllWD 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 280 AL-------------RFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEASHLMT-SNplPEDgarkaGSVGRaVGQEMA 345
Cdd:PLN02387 408 ALvfkkiravlggriRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATfSE--WDD-----TSVGR-VGPPLP 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 346 -----ILD-EEGRRVEAGK---SGEVCVRGANVTSGYKGNPEANEAAFRFG-----WFHTGDIGVVDEEGYLRLVGRIKE 411
Cdd:PLN02387 480 ccyvkLVSwEEGGYLISDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVYKVDergmrWFYTGDIGQFHPDGCLEIIDRKKD 559
|
330 340
....*....|....*....|...
gi 1002261995 412 LIN-RGGEKISPIEVDSVLLGHP 433
Cdd:PLN02387 560 IVKlQHGEYVSLGKVEAALSVSP 582
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
158-506 |
6.29e-16 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 80.76 E-value: 6.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 158 NDPSDValfLHTSGTTSRPKGVpltQRN-------LAASVQNI---RA--VYrLTEADATVIVLPLFHVHGLLCGLLASL 225
Cdd:PRK10524 233 NEPSYI---LYTSGTTGKPKGV---QRDtggyavaLATSMDTIfggKAgeTF-FCASDIGWVVGHSYIVYAPLLAGMATI 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 226 ASGASVTLPAAG-------------RFSASTFWADMRGAGATWytavptihqiiIDRH-TSKPEAEYPALRFIRSCSASL 291
Cdd:PRK10524 306 MYEGLPTRPDAGiwwrivekykvnrMFSAPTAIRVLKKQDPAL-----------LRKHdLSSLRALFLAGEPLDEPTASW 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 292 apaIMEKLeaafGAPVVEAYAMTEAS-HLMTSNPLPEDGARKAGSVGRAV-GQEMAILDEE-GRRVEAGKSGEVCVRGA- 367
Cdd:PRK10524 375 ---ISEAL----GVPVIDNYWQTETGwPILAIARGVEDRPTRLGSPGVPMyGYNVKLLNEVtGEPCGPNEKGVLVIEGPl 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 368 --NVTSGYKGNPEaneaafRF---GWFH-------TGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAI 435
Cdd:PRK10524 448 ppGCMQTVWGDDD------RFvktYWSLfgrqvysTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAV 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 436 AQAVAFGVPDAKYGEEINCAVIPREGVSLG--------EEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR-IVA 506
Cdd:PRK10524 522 AEVAVVGVKDALKGQVAVAFVVPKDSDSLAdrearlalEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRaIQA 601
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
159-413 |
4.18e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 78.23 E-value: 4.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 159 DPSDVALFLHTSGTTSRPKGVPLTQRNLAASV-QNIRAVyRLTEADATVIVLPLFHVHGLLCGLLASLAsGASVTL--PA 235
Cdd:PRK07769 178 NEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVlQVIDAL-EGQEGDRGVSWLPFFHDMGLITVLLPALL-GHYITFmsPA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 236 A-----GRfsastfW-----ADMRGAGATwYTAVPTI---HQIIidRHTSKpEAEYP----ALRFIRSCSASLAPAIMEK 298
Cdd:PRK07769 256 AfvrrpGR------WirelaRKPGGTGGT-FSAAPNFafeHAAA--RGLPK-DGEPPldlsNVKGLLNGSEPVSPASMRK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 299 LEAAFG------APVVEAYAMTEASHLMTSNPLPE---------------------DGARKA------GSVGRAvgQEMA 345
Cdd:PRK07769 326 FNEAFApyglppTAIKPSYGMAEATLFVSTTPMDEeptviyvdrdelnagrfvevpADAPNAvaqvsaGKVGVS--EWAV 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 346 ILD-EEGRRVEAGKSGEVCVRGANVTSGYKGNPEANEAAFR------------------FGWFHTGDIGVVdEEGYLRLV 406
Cdd:PRK07769 404 IVDpETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFQnilksrlseshaegapddALWVRTGDYGVY-FDGELYIT 482
|
....*..
gi 1002261995 407 GRIKELI 413
Cdd:PRK07769 483 GRVKDLV 489
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
162-503 |
6.56e-14 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 74.00 E-value: 6.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 162 DVALFLHTSGTTSRPKgvpltqrnlAASVQNIR----AV-----YRLTEADATVIVLPLFHVHGLLCGLLASLASGASVT 232
Cdd:cd05939 105 DKLFYIYTSGTTGLPK---------AAVIVHSRyyriAAgayyaFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 233 LPAagRFSASTFWADmrgagATWYTAvpTIHQII--IDRHT-SKPEAEYPALRFIR-SCSASLAPAIMEKLEAAFGAP-V 307
Cdd:cd05939 176 IRK--KFSASNFWDD-----CVKYNC--TIVQYIgeICRYLlAQPPSEEEQKHNVRlAVGNGLRPQIWEQFVRRFGIPqI 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 308 VEAYAMTEAshlmTSNPLPEDGARKA-GSVGRAVGQEMAI----LDEEGRRVEAGKSGeVCVR------GANVTSGYKGN 376
Cdd:cd05939 247 GEFYGATEG----NSSLVNIDNHVGAcGFNSRILPSVYPIrlikVDEDTGELIRDSDG-LCIPcqpgepGLLVGKIIQND 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 377 P------EANEAA---------FRFG--WFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAV 439
Cdd:cd05939 322 PlrrfdgYVNEGAtnkkiardvFKKGdsAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVV 401
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002261995 440 AFGV--PDAKYGEEINCAVIPREGVSLgeEEVLAYCRRNLAAFKVPKKVYIADELPKTATGKIQRR 503
Cdd:cd05939 402 VYGVevPGVEGRAGMAAIVDPERKVDL--DRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKT 465
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
158-420 |
1.17e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 73.47 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 158 NDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRavYRLT-------EADATVIVLPLFHVHGLLCgLLASLASGAS 230
Cdd:PTZ00216 261 ENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALE--DRLNdligppeEDETYCSYLPLAHIMEFGV-TNIFLARGAL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 231 V------TLpaagrfsASTF---WADMRGAGATWYTAVPTIHQII-------------IDR------HTS-----KPEAE 277
Cdd:PTZ00216 338 IgfgsprTL-------TDTFarpHGDLTEFRPVFLIGVPRIFDTIkkaveaklppvgsLKRrvfdhaYQSrlralKEGKD 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 278 YP----------------ALRFIRSCSASLAPAIMEKLEAAFGaPVVEAYAMTEAshlMTSNPLPEDGARKAGSVGRA-V 340
Cdd:PTZ00216 411 TPywnekvfsapravlggRVRAMLSGGGPLSAATQEFVNVVFG-MVIQGWGLTET---VCCGGIQRTGDLEPNAVGQLlK 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 341 GQEMAILDEEGRRV--EAGKSGEVCVRGANVTSGYKGNPEANEAAF-RFGWFHTGDIGVVDEEGYLRLVGRIKELI-NRG 416
Cdd:PTZ00216 487 GVEMKLLDTEEYKHtdTPEPRGEILLRGPFLFKGYYKQEELTREVLdEDGWFHTGDVGSIAANGTLRIIGRVKALAkNCL 566
|
....
gi 1002261995 417 GEKI 420
Cdd:PTZ00216 567 GEYI 570
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
160-503 |
5.08e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 72.12 E-value: 5.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 160 PSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATV--------IVLPLFhvhgllcgLLASLASGASV 231
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAqtasqsfdISVWQF--------LAAPLFGARVE 3939
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 232 TLPAAGRFSASTFWADMRGAGATWYTAVPTIhqiiIDRHTSKPEAEYPALRFIRSCSASLAPAIMEK-LEAAFGAPVVEA 310
Cdd:PRK05691 3940 IVPNAIAHDPQGLLAHVQAQGITVLESVPSL----IQGMLAEDRQALDGLRWMLPTGEAMPPELARQwLQRYPQIGLVNA 4015
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 311 YAMTEASHLMTSNPLpeDGARKAGS---VGRAV-GQEMAILDEEGRRVEAGKSGEVCVRGANVTSGYKGNPEANEAAF-- 384
Cdd:PRK05691 4016 YGPAECSDDVAFFRV--DLASTRGSylpIGSPTdNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFvp 4093
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 385 -RFG-----WFHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLLGHPAIAQAvAFGVPDAKYGEEINCAVIP 458
Cdd:PRK05691 4094 hPFGapgerLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREA-AVAVQEGVNGKHLVGYLVP 4172
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1002261995 459 REGVsLGEEEVLAYCRRNLAA----FKVPKKVYIADELPKTATGKIQRR 503
Cdd:PRK05691 4173 HQTV-LAQGALLERIKQRLRAelpdYMVPLHWLWLDRLPLNANGKLDRK 4220
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
161-451 |
1.53e-12 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 69.87 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 161 SDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLT-----EADATVIVLPLFHVH-------------------- 215
Cdd:PLN02861 220 TDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKVTdrvatEEDSYFSYLPLAHVYdqvietyciskgasigfwqg 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 216 --------------GLLCGL---LASLASGASVTLPAAGRFSASTF-------WADMRgAGATWYTAVPTIHQIIIDRht 271
Cdd:PLN02861 300 dirylmedvqalkpTIFCGVprvYDRIYTGIMQKISSGGMLRKKLFdfaynykLGNLR-KGLKQEEASPRLDRLVFDK-- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 272 sKPEAEYPALRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEA-SHLMTS--NPLPEDGArkagsvgraVGQEMAILD 348
Cdd:PLN02861 377 -IKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTEScGGCFTSiaNVFSMVGT---------VGVPMTTIE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 349 EEGRRV-EAG-------KSGEVCVRGANVTSGYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKELINRG-GEK 419
Cdd:PLN02861 447 ARLESVpEMGydalsdvPRGEICLRGNTLFSGYHKRQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSqGEY 526
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1002261995 420 ISPIEVDSVLLGHPAIAQAVAFG-----------VPDAKYGEE 451
Cdd:PLN02861 527 VAVENLENTYSRCPLIASIWVYGnsfesflvavvVPDRQALED 569
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
159-509 |
1.14e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 67.27 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 159 DPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVY-----RLTEADATVIV-LPLFHVHGLLCGLLASLASG--AS 230
Cdd:PRK05850 158 DLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDYfgdtgGVPPPDTTVVSwLPFYHDMGLVLGVCAPILGGcpAV 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 231 VTLPAAgrfsastF------WADMRGAGATWYTAVPTIHQIIIDRHTSkpEAEYPAL-----RFIRSCSASLAPAIMEKL 299
Cdd:PRK05850 238 LTSPVA-------FlqrparWMQLLASNPHAFSAAPNFAFELAVRKTS--DDDMAGLdlggvLGIISGSERVHPATLKRF 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 300 E---AAFGAP---VVEAYAMTEAS-HLMTSNP-LPEDGAR---KAGSVGRAVG-----------------QEMAILDEEG 351
Cdd:PRK05850 309 AdrfAPFNLRetaIRPSYGLAEATvYVATREPgQPPESVRfdyEKLSAGHAKRcetgggtplvsygsprsPTVRIVDPDT 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 352 RR-VEAGKSGEVCVRGANVTSGYKGNPEANEAAF------------RFGWFHTGDIGVVDeEGYLRLVGRIKELINRGGE 418
Cdd:PRK05850 389 CIeCPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgtpEGPWLRTGDLGFIS-EGELFIVGRIKDLLIVDGR 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 419 KISP--IE--VDSVLLGhpaiaQAVAFGVPDAkyGEEINCAVIP--REGVSLGEE-EVLAYCRRNL-AAFKVPKKVYIAD 490
Cdd:PRK05850 468 NHYPddIEatIQEITGG-----RVAAISVPDD--GTEKLVAIIElkKRGDSDEEAmDRLRTVKREVtSAISKSHGLSVAD 540
|
410 420
....*....|....*....|....*.
gi 1002261995 491 -------ELPKTATGKIQRRIVAQHF 509
Cdd:PRK05850 541 lvlvapgSIPITTSGKIRRAACVEQY 566
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
160-412 |
2.34e-11 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 66.20 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 160 PSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNI-----RAVYRLTEADATVIVLPLFHV-----------HG------- 216
Cdd:PLN02614 222 KSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVirllkSANAALTVKDVYLSYLPLAHIfdrvieecfiqHGaaigfwr 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 217 ----------------LLCGL---LASLASGASVTLPAAGRFSASTF-------WADMRgAGATWYTAVPTIHQIIIDRH 270
Cdd:PLN02614 302 gdvklliedlgelkptIFCAVprvLDRVYSGLQKKLSDGGFLKKFVFdsafsykFGNMK-KGQSHVEASPLCDKLVFNKV 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 271 TSKPEAEypaLRFIRSCSASLAPAIMEKLEAAFGAPVVEAYAMTEaSHLMTSNPLPeDGARKAGSVGRAVG----QEMAI 346
Cdd:PLN02614 381 KQGLGGN---VRIILSGAAPLASHVESFLRVVACCHVLQGYGLTE-SCAGTFVSLP-DELDMLGTVGPPVPnvdiRLESV 455
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002261995 347 LDEEGRRVEAGKSGEVCVRGANVTSGYKGNPEANEAAFRFGWFHTGDIGVVDEEGYLRLVGRIKEL 412
Cdd:PLN02614 456 PEMEYDALASTPRGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNI 521
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
160-411 |
2.46e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 66.22 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 160 PSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVyRLTEADATVIV----LPLFHVHGLLCGLLASLASGASVTL-- 233
Cdd:PRK12582 219 PDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQL-RPREPDPPPPVsldwMPWNHTMGGNANFNGLLWGGGTLYIdd 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 234 --PAAGRFSASTfwADMRGAGATWYTAVPTIHQIIIDRHTSKP---EAEYPALRFIRSCSASLAPAIMEKLEA----AFG 304
Cdd:PRK12582 298 gkPLPGMFEETI--RNLREISPTVYGNVPAGYAMLAEAMEKDDalrRSFFKNLRLMAYGGATLSDDLYERMQAlavrTTG 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 305 A--PVVEAYAMTEASHLMTSNPLPedgARKAGSVGRAV-GQEMAIldeegrrVEAGKSGEVCVRGANVTSGYKGNPEANE 381
Cdd:PRK12582 376 HriPFYTGYGATETAPTTTGTHWD---TERVGLIGLPLpGVELKL-------APVGDKYEVRVKGPNVTPGYHKDPELTA 445
|
250 260 270
....*....|....*....|....*....|....*.
gi 1002261995 382 AAF-RFGWFHTGDIGV-VD----EEGyLRLVGRIKE 411
Cdd:PRK12582 446 AAFdEEGFYRLGDAARfVDpddpEKG-LIFDGRVAE 480
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
337-506 |
1.62e-10 |
|
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: 63.44 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 337 GRAVGQEMAILDEEGRRVeAGKSGE-VCVRG-ANVTSGYKGNPEAN---EAAF-RFG--WFHtGDIGVVDEEGYLRLVGR 408
Cdd:cd05943 428 CRGLGMAVEAFDEEGKPV-WGEKGElVCTKPfPSMPVGFWNDPDGSryrAAYFaKYPgvWAH-GDWIEITPRGGVVILGR 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 409 IKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEE---EVLAYCRRNLAAFKVPKK 485
Cdd:cd05943 506 SDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDElrkRIRSTIRSALSPRHVPAK 585
|
170 180
....*....|....*....|....*
gi 1002261995 486 VYIADELPKTATGKIQ----RRIVA 506
Cdd:cd05943 586 IIAVPDIPRTLSGKKVevavKKIIA 610
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
159-510 |
3.11e-10 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 62.45 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 159 DPSDVALFLHTSGTTSRPKGVPLTQRNLAAS-VQNIRAVYRLTEADATVIVLPLFHVHGLLCGLLASLASGASVTLPAAG 237
Cdd:PRK12476 191 DTDDVSHLQYTSGSTRPPVGVEITHRAVGTNlVQMILSIDLLDRNTHGVSWLPLYHDMGLSMIGFPAVYGGHSTLMSPTA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 238 RFSASTFWADMRGAGATW---YTAVPTIHQIIIDRHTSKPEAEYPALRFIRSCSAS--LAPAIMEKLEAAF---GAP--- 306
Cdd:PRK12476 271 FVRRPQRWIKALSEGSRTgrvVTAAPNFAYEWAAQRGLPAEGDDIDLSNVVLIIGSepVSIDAVTTFNKAFapyGLPrta 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 307 VVEAYAMTEASHLM-TSNPLPEDGA----RKAGSVGRAV--------------------GQEMAILDEE-GRRVEAGKSG 360
Cdd:PRK12476 351 FKPSYGIAEATLFVaTIAPDAEPSVvyldREQLGAGRAVrvaadapnavahvscgqvarSQWAVIVDPDtGAELPDGEVG 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 361 EVCVRGANVTSGYKGNPEANEAAFRF-------------------GWFHTGDIGV-VDEEGYlrLVGRIKELINRGGEKI 420
Cdd:PRK12476 431 EIWLHGDNIGRGYWGRPEETERTFGAklqsrlaegshadgaaddgTWLRTGDLGVyLDGELY--ITGRIADLIVIDGRNH 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 421 SPIEVD-SVLLGHPAIAQ--AVAFGVPdakyGEEINCAVIPRE---GVSLGEE----EVL--AYCRRN-LAAFKVpkKVY 487
Cdd:PRK12476 509 YPQDIEaTVAEASPMVRRgyVTAFTVP----AEDNERLVIVAEraaGTSRADPapaiDAIraAVSRRHgLAVADV--RLV 582
|
410 420
....*....|....*....|...
gi 1002261995 488 IADELPKTATGKIQRRIVAQHFV 510
Cdd:PRK12476 583 PAGAIPRTTSGKLARRACRAQYL 605
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
346-507 |
4.10e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 62.45 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 346 ILDEEGRRVEAGKSGEVCVR----GANVTSGYKgNPEANEAAF-RF-GWFHTGDIGVVDEEGYLRLVGRIKELINRGGEK 419
Cdd:PTZ00237 446 ILSEDGKELNVNEIGEVAFKlpmpPSFATTFYK-NDEKFKQLFsKFpGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNK 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 420 ISPIEVDSVLLGHPAIAQAVAFGVPDAK-YGEEINCAVIPREG----VSLGE--EEVLAYCRRNLAAFKVPKKVYIADEL 492
Cdd:PTZ00237 525 VQLNTIETSILKHPLVLECCSIGIYDPDcYNVPIGLLVLKQDQsnqsIDLNKlkNEINNIITQDIESLAVLRKIIIVNQL 604
|
170
....*....|....*
gi 1002261995 493 PKTATGKIQRRIVAQ 507
Cdd:PTZ00237 605 PKTKTGKIPRQIISK 619
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
158-505 |
6.53e-09 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 58.29 E-value: 6.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 158 NDPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADATV-------IVLPLFHVHGLLCGLLASLASGAS 230
Cdd:PLN03051 116 APVESVTNILFSSGTTGEPKAIPWTHLSPLRCASDGWAHMDIQPGDVVCwptnlgwMMGPWLLYSAFLNGATLALYGGAP 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 231 VTlPAAGRFsastfwadMRGAGATWYTAVPTIhqIIIDRHTSKPEAEYPALRFIRS-CSASLAPAIMEKL----EAAFGA 305
Cdd:PLN03051 196 LG-RGFGKF--------VQDAGVTVLGLVPSI--VKAWRHTGAFAMEGLDWSKLRVfASTGEASAVDDVLwlssVRGYYK 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 306 PVVEAYAMTE-ASHLMTSNPLpEDGARKAGSVGrAVGQEMAILDEEGRR--VEAGKSGEVCVR------------GANVT 370
Cdd:PLN03051 265 PVIEYCGGTElASGYISSTLL-QPQAPGAFSTA-SLGTRFVLLNDNGVPypDDQPCVGEVALAppmlgasdrllnADHDK 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 371 SGYKGNP--EANEAAFRfgwfHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVLL-GHPAIAQAVAFGVPDAK 447
Cdd:PLN03051 343 VYYKGMPmyGSKGMPLR----RHGDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACDrAVAGIAETAAVGVAPPD 418
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002261995 448 YGEEINCAVIP----REGVSLGEEEVLAY-----CRRNL-AAFKVpKKVYIADELPKTATGKIQRRIV 505
Cdd:PLN03051 419 GGPELLVIFLVlgeeKKGFDQARPEALQKkfqeaIQTNLnPLFKV-SRVKIVPELPRNASNKLLRRVL 485
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
55-510 |
4.86e-07 |
|
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: 52.35 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 55 PGHVVALAFPNTVELVIMFLAVIRARAVAAPLNPAYTQEEFEFYLSDSGARLLITNpegnVAAQAAASKLGLAHTTASLK 134
Cdd:cd05905 39 PGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVALTV----EACLKGLPKKLLKSKTAAEI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 135 DA---------AGQVHLAGFPASAAAAAKDFANDPsDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADAT 205
Cdd:cd05905 115 AKkkgwpkildFVKIPKSKRSKLKKWGPHPPTRDG-DTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 206 VIVLPLFHVHGLLCGLLASLASGASVTLPAagrfsastfWADMRGAGATWYTAVP------------TIHQIIIDRHTSK 273
Cdd:cd05905 194 VTVLDFKSGLGLWHGCLLSVYSGHHTILIP---------PELMKTNPLLWLQTLSqykvrdayvklrTLHWCLKDLSSTL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 274 P--EAEYPALRFIRSC--------SASLAPAIMEKLEA----------AFGAPV-----VEAYAMTEASHLMTSN----- 323
Cdd:cd05905 265 AslKNRDVNLSSLRMCmvpcenrpRISSCDSFLKLFQTlglspravstEFGTRVnpficWQGTSGPEPSRVYLDMralrh 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 324 ---PLPEDGARKAGSV----GRAVGQEMAILDEEGRRV-EAGKSGEVCVRGANVTSGYKGNPEANEAAF------RFG-- 387
Cdd:cd05905 345 gvvRLDERDKPNSLPLqdsgKVLPGAQVAIVNPETKGLcKDGEIGEIWVNSPANASGYFLLDGETNDTFkvfpstRLStg 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 388 -----WFHTGDIGVV----------DEEGYLRLVGRIKELINRGGEKISPIE-VDSVLLGHPAIAQAVAFG-------VP 444
Cdd:cd05905 425 itnnsYARTGLLGFLrptkctdlnvEEHDLLFVVGSIDETLEVRGLRHHPSDiEATVMRVHPYRGRCAVFSitglvvvVA 504
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002261995 445 DAKYG-EEINCAVIPREGVSLGEE-EVLAYCrrnlAAFkVPKKVyiadeLPKTATGKIQRRIVAQHFV 510
Cdd:cd05905 505 EQPPGsEEEALDLVPLVLNAILEEhQVIVDC----VAL-VPPGS-----LPKNPLGEKQRMEIRQAFL 562
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
373-509 |
2.37e-06 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 50.46 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 373 YKGNPEANEAAFRfgwfHTGDIGVVDEEGYLRLVGRIKELINRGGEKISPIEVDSVL-LGHPAIAQAVAFGVPDAKYGEE 451
Cdd:PLN03052 579 FKGMPVFNGKILR----RHGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPPGGGPE 654
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002261995 452 INC--AVIPREGVSLGEEEVL-----AYCRRNL-AAFKVpKKVYIADELPKTATGKIQRRIVAQHF 509
Cdd:PLN03052 655 QLViaAVLKDPPGSNPDLNELkkifnSAIQKKLnPLFKV-SAVVIVPSFPRTASNKVMRRVLRQQL 719
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
198-497 |
4.12e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 46.25 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 198 RLTEADATVIVLPLFHVHGLLCGLLASLASGASVTLpaAGRFSASTFWADMRGAGATWYTAVPTIHQIIIDRHTSKPEAE 277
Cdd:PRK07868 642 ALDRRDTVYCLTPLHHESGLLVSLGGAVVGGSRIAL--SRGLDPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGN 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 278 YPALRFIRS-CSASLAPAIMEKLEAafgAPVVEAYAMTEASHLmtsnpLPEDGARKAGSVGRAVG-------------QE 343
Cdd:PRK07868 720 HPVRLFIGSgMPTGLWERVVEAFAP---AHVVEFFATTDGQAV-----LANVSGAKIGSKGRPLPgagrvelaaydpeHD 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 344 MAILDEEG--RRVEAGKSGEVCVR---GANVTSGYKgnpeanEAAFRFG--WFHTGDIGVVDEEGYLRLVGRIKELIN-- 414
Cdd:PRK07868 792 LILEDDRGfvRRAEVNEVGVLLARargPIDPTASVK------RGVFAPAdtWISTEYLFRRDDDGDYWLVDRRGSVIRta 865
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 415 RGGEKISPIEVDSVLLGhpAIAQAVAFGVPDAkyGEEIN-CAVIPREGVSLGEEEVLAYCRRnLAAFKVPKKVYIADELP 493
Cdd:PRK07868 866 RGPVYTEPVTDALGRIG--GVDLAVTYGVEVG--GRQLAvAAVTLRPGAAITAADLTEALAS-LPVGLGPDIVHVVPEIP 940
|
....
gi 1002261995 494 KTAT 497
Cdd:PRK07868 941 LSAT 944
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
159-491 |
1.09e-04 |
|
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: 44.75 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 159 DPSDVALFLHTSGTTSRPKGVPLTQRNLAASVQNIRAVYRLTEADA-TVIVLPLFHVHGLLCgLLASLASGAsvTLPAAG 237
Cdd:cd17632 221 DDDPLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASiTLNFMPMSHIAGRIS-LYGTLARGG--TAYFAA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 238 RFSASTFWADMRGAGATWYTAVPTIHQIIIDRHTSK----------PEAEYPALR-FIR------------SCSASLAPA 294
Cdd:cd17632 298 ASDMSTLFDDLALVRPTELFLVPRVCDMLFQRYQAEldrrsvagadAETLAERVKaELRervlggrllaavCGSAPLSAE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 295 IMEKLEAAFGAPVVEAYAMTEASHLMTSnplpedgarkaGSVGRAVGQEMAILD--EEG--RRVEAGKSGEVCVRGANVT 370
Cdd:cd17632 378 MKAFMESLLDLDLHDGYGSTEAGAVILD-----------GVIVRPPVLDYKLVDvpELGyfRTDRPHPRGELLVKTDTLF 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 371 SGYKGNPEANEAAF-RFGWFHTGDIgvVDEEGYLRLV---GRIKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDA 446
Cdd:cd17632 447 PGYYKRPEVTAEVFdEDGFYRTGDV--MAELGPDRLVyvdRRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNSER 524
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002261995 447 KYgeeINCAVIPREGVSLGEEEVLAYCR-----------RNLAAFKVPKKVYIADE 491
Cdd:cd17632 525 AY---LLAVVVPTQDALAGEDTARLRAAlaeslqriareAGLQSYEIPRDFLIETE 577
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
337-505 |
2.22e-04 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 44.02 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 337 GRAVGQEMAILDEEGRRVeAGKSGE-VCVRGA-NVTSGYKGNPEA---NEAAF-RFG--WFHtGDIGVVDEEGYLRLVGR 408
Cdd:PRK03584 442 CRGLGMAVEAWDEDGRPV-VGEVGElVCTKPFpSMPLGFWNDPDGsryRDAYFdTFPgvWRH-GDWIEITEHGGVVIYGR 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002261995 409 IKELINRGGEKISPIEVDSVLLGHPAIAQAVAFGVPDAKYGEEINCAVIPREGVSLGEE---EVLAYCRRNLAAFKVPKK 485
Cdd:PRK03584 520 SDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDDAlraRIRTTIRTNLSPRHVPDK 599
|
170 180
....*....|....*....|....
gi 1002261995 486 VYIADELPKTATGKIQ----RRIV 505
Cdd:PRK03584 600 IIAVPDIPRTLSGKKVelpvKKLL 623
|
|
| |
