|
Name |
Accession |
Description |
Interval |
E-value |
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
9-532 |
8.54e-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: 434.62 E-value: 8.54e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 9 LGELPTRAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFN 88
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 89 LRYRETDLADVVRRGGCKVLIFsgragpidfvalvqrslrsdlergslrtvlvgegvmpgaiswssledavyspaeqral 168
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT---------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 169 cerraackasdlALIVFTSGTTGRPKGVMHDH-SCVRSVRDRGRLWKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQ 247
Cdd:COG0318 103 ------------ALILYTSGTTGRPKGVMLTHrNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 248 VVMETFDANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRFGTlpSGletSAAIAVQVQRVF-----CPTVT 322
Cdd:COG0318 171 VLLPRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVV--SG---GAPLPPELLERFeerfgVRIVE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 323 GAGMSESwCWMCTCAIDEPEELRCHSSGRPLPGMEMRLIDPEtGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALdAD 402
Cdd:COG0318 246 GYGLTET-SPVVTVNPEDPGERRPGSVGRPLPGVEVRIVDED-GRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RD 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 403 GWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSElVPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAAT 482
Cdd:COG0318 323 GWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAA-HPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELD 401
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1828927390 483 EESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRKTALEAGLQ 532
Cdd:COG0318 402 AEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGALE 451
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
15-525 |
3.01e-132 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 394.27 E-value: 3.01e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 15 RAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRET 94
Cdd:PRK07656 13 RAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 95 DLADVVRRGGCKVLIFSGRAGPIDFVALVQRSlrsDLERGSLRTVLVGEGVMPGAISWSSledaVYSPAEQRalcERRAA 174
Cdd:PRK07656 93 EAAYILARGDAKALFVLGLFLGVDYSATTRLP---ALEHVVICETEEDDPHTEKMKTFTD----FLAAGDPA---ERAPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 175 CKASDLALIVFTSGTTGRPKGVMHDH-SCVRSVRDRGRLWKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQVVMETF 253
Cdd:PRK07656 163 VDPDDVADILFTSGTTGRPKGAMLTHrQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLPVF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 254 DANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRFGTlpSGletSAAIAVQVQRVF-----CPTV-TGAGMS 327
Cdd:PRK07656 243 DPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAV--TG---AASMPVALLERFeselgVDIVlTGYGLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 328 ESWCWMCTCAIDEPEELRCHSSGRPLPGMEMRLIDPEtGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDADGWLHS 407
Cdd:PRK07656 318 EASGVTTFNRLDDDRKTVAGTIGTAIAGVENKIVNEL-GEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 408 GDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEESII 487
Cdd:PRK07656 397 GDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEH-PAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEELI 475
|
490 500 510
....*....|....*....|....*....|....*...
gi 1828927390 488 AACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRKT 525
Cdd:PRK07656 476 AYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
1-523 |
4.69e-123 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 371.06 E-value: 4.69e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 1 MTDKDLpLLGELPTRAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRI 80
Cdd:PRK06187 1 MQDYPL-TIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 81 GAAAVPFNLRYRETDLADVVRRGGCKVLIFSGragpiDFVALVQRsLRSDLErgSLRTVLV-----GEGVMPGAISWSSL 155
Cdd:PRK06187 80 GAVLHPINIRLKPEEIAYILNDAEDRVVLVDS-----EFVPLLAA-ILPQLP--TVRTVIVegdgpAAPLAPEVGEYEEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 156 EDAVYSPAEQRALCERraackasDLALIVFTSGTTGRPKGVMHDH----SCVRSVRDRGRLwkvQPGETMLNYLPMFHLY 231
Cdd:PRK06187 152 LAAASDTFDFPDIDEN-------DAAAMLYTSGTTGHPKGVVLSHrnlfLHSLAVCAWLKL---SRDDVYLVIVPMFHVH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 232 SLSEAVLQcMYSGCRQVVMETFDANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRFGTlpSGletSAAIAV 311
Cdd:PRK06187 222 AWGLPYLA-LMAGAKQVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVI--YG---GAALPP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 312 QVQRVF-----CPTVTGAGMSEswcwMC---TCAIDEPE-----ELRChSSGRPLPGMEMRLIDPEtGKDVPP--GMPGE 376
Cdd:PRK06187 296 ALLREFkekfgIDLVQGYGMTE----TSpvvSVLPPEDQlpgqwTKRR-SAGRPLPGVEARIVDDD-GDELPPdgGEVGE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 377 MLFRCYSVMKGYFEDPEATAAALDaDGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVA 456
Cdd:PRK06187 370 IIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGH-PAVAEVA 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828927390 457 VIGIPEPRLVEVPVAYVVLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIR 523
Cdd:PRK06187 448 VIGVPDEKWGERPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
9-523 |
2.57e-120 |
|
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: 362.27 E-value: 2.57e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 9 LGELPTRAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFN 88
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 89 LRYRETDLADVVRRGGCKVLIfsgragpidfvalVQRSLRSDLERGslrtvlvgegvmpgaiswssledavyspaeqrAL 168
Cdd:cd05936 81 PLYTPRELEHILNDSGAKALI-------------VAVSFTDLLAAG--------------------------------AP 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 169 CERRAACKASDLALIVFTSGTTGRPKGVMHDH--------SCVRSVRDRGRlwkvqPGETMLNYLPMFHLYSLSEAVLQC 240
Cdd:cd05936 116 LGERVALTPEDVAVLQYTSGTTGVPKGAMLTHrnlvanalQIKAWLEDLLE-----GDDVVLAALPLFHVFGLTVALLLP 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 241 MYSGCRQVVMETFDANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRFGTlpSGletSAAIAVQVQRVF--- 317
Cdd:cd05936 191 LALGATIVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCI--SG---GAPLPVEVAERFeel 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 318 --CPTVTGAGMSESWCWMCTCAIDEPEELRchSSGRPLPGMEMRLIDPEtGKDVPPGMPGEMLFRCYSVMKGYFEDPEAT 395
Cdd:cd05936 266 tgVPIVEGYGLTETSPVVAVNPLDGPRKPG--SIGIPLPGTEVKIVDDD-GEELPPGEVGELWVRGPQVMKGYWNRPEET 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 396 AAALDaDGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVL 475
Cdd:cd05936 343 AEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEH-PAVAEAAVVGVPDPYSGEAVKAFVVL 420
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1828927390 476 RPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIR 523
Cdd:cd05936 421 KEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
5-538 |
2.31e-118 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 360.28 E-value: 2.31e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 5 DLPLL----GELPTRAAAKWPEQKAL-------EWatgamSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEA 73
Cdd:PRK08315 10 DVPLLeqtiGQLLDRTAARYPDREALvyrdqglRW-----TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 74 IFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLIFSGRAGPIDFVALVQrSLRSDL---ERGSL---------RTVLV 141
Cdd:PRK08315 85 QFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAADGFKDSDYVAMLY-ELAPELatcEPGQLqsarlpelrRVIFL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 142 GEGVMPGAISWSSL-EDAVYSPAEQraLCERRAACKASDLALIVFTSGTTGRPKGVMHDHscvRSVRDRGRLwkvqPGET 220
Cdd:PRK08315 164 GDEKHPGMLNFDELlALGRAVDDAE--LAARQATLDPDDPINIQYTSGTTGFPKGATLTH---RNILNNGYF----IGEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 221 MlNY---------LPMFHLYSLSEAVLQCMYSGCRQVVM-ETFDANTALDLIEQKSINILHGFETHY-ADLlrvqaERPR 289
Cdd:PRK08315 235 M-KLteedrlcipVPLYHCFGMVLGNLACVTHGATMVYPgEGFDPLATLAAVEEERCTALYGVPTMFiAEL-----DHPD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 290 ----NVGSLRFG-----TLPsgletsaaIAV--QVQ-RVFCPTVTGA-GMSESWCWMCTCAIDEPEELRCHSSGRPLPGM 356
Cdd:PRK08315 309 farfDLSSLRTGimagsPCP--------IEVmkRVIdKMHMSEVTIAyGMTETSPVSTQTRTDDPLEKRVTTVGRALPHL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 357 EMRLIDPETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENV 436
Cdd:PRK08315 381 EVKIVDPETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENI 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 437 SPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGK 516
Cdd:PRK08315 461 YPREIEEFLYTH-PKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGK 539
|
570 580
....*....|....*....|..
gi 1828927390 517 VQRAVIRKTALEaglQLKLVSQ 538
Cdd:PRK08315 540 IQKFKMREMMIE---ELGLQAA 558
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
13-519 |
7.42e-109 |
|
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: 331.50 E-value: 7.42e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 13 PTRAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYR 92
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 93 ETDLADVVRRGGCKVLIfsgragpidfvalvqrslrsdlergslrtvlvgegvmpgaiswssledavyspaeqralcerr 172
Cdd:cd17631 81 PPEVAYILADSGAKVLF--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 173 aackaSDLALIVFTSGTTGRPKGVMHDHscvrsvrdRGRLWKVQ---------PGETMLNYLPMFHLYSLSEAVLQCMYS 243
Cdd:cd17631 98 -----DDLALLMYTSGTTGRPKGAMLTH--------RNLLWNAVnalaaldlgPDDVLLVVAPLFHIGGLGVFTLPTLLR 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 244 GCRQVVMETFDANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRFGtLPSGLETSAAIAVQVQRVFCPTVTG 323
Cdd:cd17631 165 GGTVVILRKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAV-IYGGAPMPERLLRALQARGVKFVQG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 324 AGMSEswCWMCTCAIDePEELRCH--SSGRPLPGMEMRLIDPEtGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALdA 401
Cdd:cd17631 244 YGMTE--TSPGVTFLS-PEDHRRKlgSAGRPVFFVEVRIVDPD-GREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-R 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 402 DGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAA 481
Cdd:cd17631 319 DGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEH-PAVAEVAVIGVPDEKWGEAVVAVVVPRPGAEL 397
|
490 500 510
....*....|....*....|....*....|....*...
gi 1828927390 482 TEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQR 519
Cdd:cd17631 398 DEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
179-518 |
2.53e-106 |
|
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: 321.54 E-value: 2.53e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 179 DLALIVFTSGTTGRPKGVMHDH-SCVRSVRDRGRLWKVQPGETMLNYLPMFHLYSLSeAVLQCMYSGCRQVVMETFDANT 257
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHrNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 258 ALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRFGTLpSGLETSAAIAVQVQRVFCPTVTGA-GMSESWCWMCTC 336
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVS-GGAPLPPELLERFEEAPGIKLVNGyGLTETGGTVATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 337 AIDEPEElRCHSSGRPLPGMEMRLIDPETGkDVPPGMPGEMLFRCYSVMKGYFEDPEATAAAlDADGWLHSGDQGVVRPD 416
Cdd:cd04433 159 PPDDDAR-KPGSVGRPVPGVEVRIVDPDGG-ELPPGEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDED 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 417 GSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEESIIAACKGKIAS 496
Cdd:cd04433 236 GYLYIVGRLKDMIKSGGENVYPAEVEAVLLGH-PGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAP 314
|
330 340
....*....|....*....|..
gi 1828927390 497 FKVPKRVVVVAELPHTATGKVQ 518
Cdd:cd04433 315 YKVPRRVVFVDALPRTASGKID 336
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
15-432 |
3.81e-103 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 316.18 E-value: 3.81e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 15 RAAAKWPEQKALEWATGA-MSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRE 93
Cdd:pfam00501 3 RQAARTPDKTALEVGEGRrLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 94 TDLADVVRRGGCKVLIFSGragpiDFVALVQRSLRSDLERGSLRTVLVGEGVMPGaisWSSLEDAVYSPAEQRALcerrA 173
Cdd:pfam00501 83 EELAYILEDSGAKVLITDD-----ALKLEELLEALGKLEVVKLVLVLDRDPVLKE---EPLPEEAKPADVPPPPP----P 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 174 ACKASDLALIVFTSGTTGRPKGVMHDH-----SCVRSVRDRGRLWKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQV 248
Cdd:pfam00501 151 PPDPDDLAYIIYTSGTTGKPKGVMLTHrnlvaNVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 249 VME---TFDANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRFGTLpSGLETSAAIAVQVQRVFCPTVTGA- 324
Cdd:pfam00501 231 LPPgfpALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLS-GGAPLPPELARRFRELFGGALVNGy 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 325 GMSESWCWMCTCAIDEPEELRCHSSGRPLPGMEMRLIDPETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDADGW 404
Cdd:pfam00501 310 GLTETTGVVTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGW 389
|
410 420
....*....|....*....|....*...
gi 1828927390 405 LHSGDQGVVRPDGSIRFTGRYKEMLKVG 432
Cdd:pfam00501 390 YRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
3-528 |
2.31e-101 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 316.33 E-value: 2.31e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 3 DKDLPLL----GELPTRAAAKWPEQKALEWATGA--MSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFA 76
Cdd:PRK12583 10 GGDKPLLtqtiGDAFDATVARFPDREALVVRHQAlrYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 77 LWRIGAAAVPFNLRYRETDLADVVRRGGCKVLIFSGRAGPIDFVALVQRSLRS--DLERGSL---------RTVLVGEGV 145
Cdd:PRK12583 90 TARIGAILVNINPAYRASELEYALGQSGVRWVICADAFKTSDYHAMLQELLPGlaEGQPGALacerlpelrGVVSLAPAP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 146 MPGAISWSSLEDAVYSPAEQRaLCERRAACKASDLALIVFTSGTTGRPKGVMHDHScvrSVRDRGRLWKVQPGETMLNYL 225
Cdd:PRK12583 170 PPGFLAWHELQARGETVSREA-LAERQASLDRDDPINIQYTSGTTGFPKGATLSHH---NILNNGYFVAESLGLTEHDRL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 226 ----PMFHLYSLSEAVLQCMYSG-CRQVVMETFDANTALDLIEQKSINILHGFETHYAdllrVQAERPRNvGSLRFGTLP 300
Cdd:PRK12583 246 cvpvPLYHCFGMVLANLGCMTVGaCLVYPNEAFDPLATLQAVEEERCTALYGVPTMFI----AELDHPQR-GNFDLSSLR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 301 SGLETSAAIAVQVQR-----VFCPTVT-GAGMSESWCWMCTCAIDEPEELRCHSSGRPLPGMEMRLIDPEtGKDVPPGMP 374
Cdd:PRK12583 321 TGIMAGAPCPIEVMRrvmdeMHMAEVQiAYGMTETSPVSLQTTAADDLERRVETVGRTQPHLEVKVVDPD-GATVPRGEI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 375 GEMLFRCYSVMKGYFEDPEATAAALDADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILE 454
Cdd:PRK12583 400 GELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTH-PAVAD 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828927390 455 VAVIGIPEPRLVEVPVAYVVLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRKTALE 528
Cdd:PRK12583 479 VQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREISIE 552
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
33-518 |
1.77e-96 |
|
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: 301.44 E-value: 1.77e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 33 MSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLIFSG 112
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 113 ragpiDFVALVQRSLRsdlERGSLRTVLV----GEGVMPGAISWSSLEDAvysPAEQRALCERRAAckaSDLALIVFTSG 188
Cdd:cd05911 91 -----DGLEKVKEAAK---ELGPKDKIIVlddkPDGVLSIEDLLSPTLGE---EDEDLPPPLKDGK---DDTAAILYSSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 189 TTGRPKGVM--HDH--SCVRSVRDRGRLWkVQPGETMLNYLPMFHLYSLSeAVLQCMYSGCRQVVMETFDANTALDLIEQ 264
Cdd:cd05911 157 TTGLPKGVClsHRNliANLSQVQTFLYGN-DGSNDVILGFLPLYHIYGLF-TTLASLLNGATVIIMPKFDSELFLDLIEK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 265 KSINILHGFETHYADLLR---VQAERPRNVGSLRFGTLPSGLETSAAIAVQVQRVFCptVTGAGMSESWCwMCTCAIDEP 341
Cdd:cd05911 235 YKITFLYLVPPIAAALAKsplLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATI--KQGYGMTETGG-ILTVNPDGD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 342 EELrcHSSGRPLPGMEMRLIDPETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDADGWLHSGDQGVVRPDGSIRF 421
Cdd:cd05911 312 DKP--GSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 422 TGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEESIIAACKGKIASFK-VP 500
Cdd:cd05911 390 VDRKKELIKYKGFQVAPAELEAVLLEH-PGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYKqLR 468
|
490
....*....|....*...
gi 1828927390 501 KRVVVVAELPHTATGKVQ 518
Cdd:cd05911 469 GGVVFVDEIPKSASGKIL 486
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
9-528 |
1.09e-95 |
|
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: 300.91 E-value: 1.09e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 9 LGELPTRAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVpFN 88
Cdd:COG1021 27 LGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPV-FA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 89 L-RYRETDLADVVRRGGCKVLIFSGRAGPIDFVALVqRSLRSDLErgSLRTVLV-GEgvmpgAISWSSLEDAVYSPAEQR 166
Cdd:COG1021 106 LpAHRRAEISHFAEQSEAVAYIIPDRHRGFDYRALA-RELQAEVP--SLRHVLVvGD-----AGEFTSLDALLAAPADLS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 167 AlcerrAACKASDLALIVFTSGTTGRPKGV---MHDHSCvrSVRDRGRLWKVQPGETMLNYLPMFHLYSL-SEAVLQCMY 242
Cdd:COG1021 178 E-----PRPDPDDVAFFQLSGGTTGLPKLIprtHDDYLY--SVRASAEICGLDADTVYLAALPAAHNFPLsSPGVLGVLY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 243 SGCRQVVMETFDANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRFgtLPSG---LETSAAIAV------QV 313
Cdd:COG1021 251 AGGTVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRV--LQVGgakLSPELARRVrpalgcTL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 314 QRVFcptvtgaGMSESWCwmCTCAIDEPEELRCHSSGRPL-PGMEMRLIDPEtGKDVPPGMPGEMLFRCYSVMKGYFEDP 392
Cdd:COG1021 329 QQVF-------GMAEGLV--NYTRLDDPEEVILTTQGRPIsPDDEVRIVDED-GNPVPPGEVGELLTRGPYTIRGYYRAP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 393 EATAAALDADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAY 472
Cdd:COG1021 399 EHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAH-PAVHDAAVVAMPDEYLGERSCAF 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1828927390 473 VVLRpGAAATEESIIAACKGK-IASFKVPKRVVVVAELPHTATGKVQRAVIRKTALE 528
Cdd:COG1021 478 VVPR-GEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALAA 533
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
15-532 |
1.77e-92 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 293.56 E-value: 1.77e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 15 RAAAKWPEQKALEW-----ATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNL 89
Cdd:COG0365 17 RHAEGRGDKVALIWegedgEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 90 RYRETDLADVVRRGGCKVLI----FSGRAGPIDFVALVQRsLRSDLErgSLRTVLV-----GEGVMPGAISWsslEDAVy 160
Cdd:COG0365 97 GFGAEALADRIEDAEAKVLItadgGLRGGKVIDLKEKVDE-ALEELP--SLEHVIVvgrtgADVPMEGDLDW---DELL- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 161 spAEQRALCErRAACKASDLALIVFTSGTTGRPKGVMHDHSCVRSVRDR-GRLW-KVQPGETMLNYLPMFHLYSLSEAVL 238
Cdd:COG0365 170 --AAASAEFE-PEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATtAKYVlDLKPGDVFWCTADIGWATGHSYIVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 239 QCMYSGCRQVVME----TFDANTALDLIEQKSINILHGFETHYADLLRVQAERPR--NVGSLRfgTLPSGLET-SAAIAV 311
Cdd:COG0365 247 GPLLNGATVVLYEgrpdFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKkyDLSSLR--LLGSAGEPlNPEVWE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 312 QVQRVF-CPTVTGAGMSESWCWMCTCAIDEPeeLRCHSSGRPLPGMEMRLIDpETGKDVPPGMPGEMLFR--CYSVMKGY 388
Cdd:COG0365 325 WWYEAVgVPIVDGWGQTETGGIFISNLPGLP--VKPGSMGKPVPGYDVAVVD-EDGNPVPPGEEGELVIKgpWPGMFRGY 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 389 FEDPEATAAAL--DADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEP-RL 465
Cdd:COG0365 402 WNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSH-PAVAEAAVVGVPDEiRG 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 466 vEVPVAYVVLRPGAAATEE---SIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRKTALEAGLQ 532
Cdd:COG0365 481 -QVVKAFVVLKPGVEPSDElakELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGRPLG 549
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
9-524 |
3.45e-92 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 291.45 E-value: 3.45e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 9 LGELPTRAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFN 88
Cdd:PRK08316 13 IGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 89 LRYRETDLADVVRRGGCKVLIfsgrAGPiDFVALVQRSLRSDLERGSLRTVLVGEGVMPGaiSWSSLEDAvyspAEQRAL 168
Cdd:PRK08316 93 FMLTGEELAYILDHSGARAFL----VDP-ALAPTAEAALALLPVDTLILSLVLGGREAPG--GWLDFADW----AEAGSV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 169 CERRAACKASDLALIVFTSGTTGRPKGVMHDH--------SCVRSVrdrgrlwKVQPGETMLNYLPMFHLYSLSEAVLQC 240
Cdd:PRK08316 162 AEPDVELADDDLAQILYTSGTESLPKGAMLTHraliaeyvSCIVAG-------DMSADDIPLHALPLYHCAQLDVFLGPY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 241 MYSGCRQVVMETFDANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLR---FGtlpsgletsAAI-AVQVQRV 316
Cdd:PRK08316 235 LYVGATNVILDAPDPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRkgyYG---------ASImPVEVLKE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 317 FCPTVTGAGMseswcWMC--------TCAIDEPEE--LRCHSSGRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCYSVMK 386
Cdd:PRK08316 306 LRERLPGLRF-----YNCygqteiapLATVLGPEEhlRRPGSAGRPVLNVETRVVD-DDGNDVAPGEVGEIVHRSPQLML 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 387 GYFEDPEATAAALdADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLV 466
Cdd:PRK08316 380 GYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTH-PAVAEVAVIGLPDPKWI 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1828927390 467 EVPVAYVVLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRK 524
Cdd:PRK08316 458 EAVTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRE 515
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
9-530 |
1.31e-90 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 288.82 E-value: 1.31e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 9 LGELPTRAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFN 88
Cdd:PRK05605 34 LVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 89 LRYRETDLADVVRRGGCKVLIFSGRAGP-------------------IDFVALVQR-SLRSDLER-GSLRTVLVGEGvmP 147
Cdd:PRK05605 114 PLYTAHELEHPFEDHGARVAIVWDKVAPtverlrrttpletivsvnmIAAMPLLQRlALRLPIPAlRKARAALTGPA--P 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 148 GAISWSSLEDAVYSPAEQRALCERRAAckaSDLALIVFTSGTTGRPKGVMHDHSCVRSVRDRGRLWkvQPG-----ETML 222
Cdd:PRK05605 192 GTVPWETLVDAAIGGDGSDVSHPRPTP---DDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAW--VPGlgdgpERVL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 223 NYLPMFHLYSLSEAVLQCMYSGCRQVVMETFDANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRFG----- 297
Cdd:PRK05605 267 AALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAfsgam 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 298 TLPsgletsAAIAVQVQRVfcpT----VTGAGMSESwcwmCTCAIDEP--EELRCHSSGRPLPGMEMRLIDPET-GKDVP 370
Cdd:PRK05605 347 ALP------VSTVELWEKL---TggllVEGYGLTET----SPIIVGNPmsDDRRPGYVGVPFPDTEVRIVDPEDpDETMP 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 371 PGMPGEMLFRCYSVMKGYFEDPEATAAALdADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSElVP 450
Cdd:PRK05605 414 DGEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLRE-HP 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 451 DILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRKTALEAG 530
Cdd:PRK05605 492 GVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREELLEKL 571
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
21-524 |
1.57e-90 |
|
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: 286.13 E-value: 1.57e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 21 PEQKALEWATGAM--SYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLAD 98
Cdd:cd05926 1 PDAPALVVPGSTPalTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 99 VVRRGGCKVLIF-SGRAGPIDFVALVQRSLRSDLergslrTVLVGEGVMPGaiswsSLEDAVYSPAEQRALCERRAAcKA 177
Cdd:cd05926 81 YLADLGSKLVLTpKGELGPASRAASKLGLAILEL------ALDVGVLIRAP-----SAESLSNLLADKKNAKSEGVP-LP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 178 SDLALIVFTSGTTGRPKGVMHDH-SCVRSVRDRGRLWKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQVVMETFDAN 256
Cdd:cd05926 149 DDLALILHTSGTTGRPKGVPLTHrNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSAS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 257 TALDLIEQKSINILHGFETHYADLLRVQAERPRNV-GSLRFgtLPSGletSAAIAVQV----QRVF-CPTVTGAGMSESW 330
Cdd:cd05926 229 TFWPDVRDYNATWYTAVPTIHQILLNRPEPNPESPpPKLRF--IRSC---SASLPPAVlealEATFgAPVLEAYGMTEAA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 331 CWMCTCAIdEPEELRCHSSGRPLpGMEMRLIDpETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDADGWLHSGDQ 410
Cdd:cd05926 304 HQMTSNPL-PPGPRKPGSVGKPV-GVEVRILD-EDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 411 GVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEESIIAAC 490
Cdd:cd05926 381 GYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSH-PAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFC 459
|
490 500 510
....*....|....*....|....*....|....
gi 1828927390 491 KGKIASFKVPKRVVVVAELPHTATGKVQRAVIRK 524
Cdd:cd05926 460 RKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
183-523 |
1.32e-88 |
|
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: 276.47 E-value: 1.32e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 183 IVFTSGTTGRPKGVM--HdHSCVRSVRDRGRLWKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQV-VMETFDANTAL 259
Cdd:cd05917 7 IQFTSGTTGSPKGATltH-HNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVfPSPSFDPLAVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 260 DLIEQKSINILHGFETHYADLLrvqaERPR----NVGSLRFGTLPSGLETSAAIAVQVQRVFCPTVTGA-GMSESwCWMC 334
Cdd:cd05917 86 EAIEKEKCTALHGVPTMFIAEL----EHPDfdkfDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAyGMTET-SPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 335 TCA-IDEPEELRCHSSGRPLPGMEMRLIDPETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDADGWLHSGDQGVV 413
Cdd:cd05917 161 TQTrTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 414 RPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEESIIAACKGK 493
Cdd:cd05917 241 DEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTH-PKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKAYCKGK 319
|
330 340 350
....*....|....*....|....*....|
gi 1828927390 494 IASFKVPKRVVVVAELPHTATGKVQRAVIR 523
Cdd:cd05917 320 IAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
34-523 |
2.74e-88 |
|
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: 278.02 E-value: 2.74e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 34 SYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLIfsgr 113
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 114 agpidfvalvqrslrsdlergslrtvlvgegvmpgaiswssledavyspaeqralcerraackaSDLALIVFTSGTTGRP 193
Cdd:cd05934 81 ----------------------------------------------------------------VDPASILYTSGTTGPP 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 194 KGVMHDHSCV----RSVRDRGRLwkvQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQVVMETFDANTALDLIEQKSINI 269
Cdd:cd05934 97 KGVVITHANLtfagYYSARRFGL---GEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 270 lhgfeTHY----ADLLRVQAERPR-NVGSLRFGtlpSGLETSAAIAVQVQRVF-CPTVTGAGMSESwcwMCTCAIDEPEE 343
Cdd:cd05934 174 -----TNYlgamLSYLLAQPPSPDdRAHRLRAA---YGAPNPPELHEEFEERFgVRLLEGYGMTET---IVGVIGPRDEP 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 344 LRCHSSGRPLPGMEMRLIDPEtGKDVPPGMPGEMLFRC---YSVMKGYFEDPEATAAALdADGWLHSGDQGVVRPDGSIR 420
Cdd:cd05934 243 RRPGSIGRPAPGYEVRIVDDD-GQELPAGEPGELVIRGlrgWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFY 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 421 FTGRYKEMLKVGGENVSPQGVEQELSeLVPDILEVAVIGIPEP-RLVEVPvAYVVLRPGAAATEESIIAACKGKIASFKV 499
Cdd:cd05934 321 FVDRKKDMIRRRGENISSAEVERAIL-RHPAVREAAVVAVPDEvGEDEVK-AVVVLRPGETLDPEELFAFCEGQLAYFKV 398
|
490 500
....*....|....*....|....
gi 1828927390 500 PKRVVVVAELPHTATGKVQRAVIR 523
Cdd:cd05934 399 PRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
15-526 |
9.93e-88 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 280.79 E-value: 9.93e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 15 RAAAKWPEQKAL------EWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFN 88
Cdd:PRK13295 32 ACVASCPDKTAVtavrlgTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLM 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 89 LRYRETDLADVVRRGGCKVLIFSGRAGPIDFVALVQRsLRSDLErgSLRTVLVGEGvmPGAISWSSL------EDAvysP 162
Cdd:PRK13295 112 PIFRERELSFMLKHAESKVLVVPKTFRGFDHAAMARR-LRPELP--ALRHVVVVGG--DGADSFEALlitpawEQE---P 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 163 AEQRALCERRAAckASDLALIVFTSGTTGRPKGVMHDHSCVRS--VRDRGRLwKVQPGETMLNYLPMFHLYSLSEAVLQC 240
Cdd:PRK13295 184 DAPAILARLRPG--PDDVTQLIYTSGTTGEPKGVMHTANTLMAniVPYAERL-GLGADDVILMASPMAHQTGFMYGLMMP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 241 MYSGCRQVVMETFDANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLR-FgtLPSGLETSAAIAVQVQRVFCP 319
Cdd:PRK13295 261 VMLGATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRtF--LCAGAPIPGALVERARAALGA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 320 TVTGA-GMSESWCWMCTCaIDEPEELRCHSSGRPLPGMEMRLIDPEtGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAa 398
Cdd:PRK13295 339 KIVSAwGMTENGAVTLTK-LDDPDERASTTDGCPLPGVEVRVVDAD-GAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGT- 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 399 lDADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPG 478
Cdd:PRK13295 416 -DADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRH-PAIAQVAIVAYPDERLGERACAFVVPRPG 493
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1828927390 479 AAATEESIIAACKG-KIASFKVPKRVVVVAELPHTATGKVQRAVIRKTA 526
Cdd:PRK13295 494 QSLDFEEMVEFLKAqKVAKQYIPERLVVRDALPRTPSGKIQKFRLREML 542
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
7-519 |
1.30e-84 |
|
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: 271.42 E-value: 1.30e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 7 PLLGELPTRAAAKWPEQKAL-EWATG-AMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAA 84
Cdd:cd05904 5 LPLDSVSFLFASAHPSRPALiDAATGrALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 85 VPFNLRYRETDLADVVRRGGCKVlifsgragpidfvALVQRSLRSDLERGSLRTVLVGEGVMPGAISWSSLEDAvysPAE 164
Cdd:cd05904 85 TTANPLSTPAEIAKQVKDSGAKL-------------AFTTAELAEKLASLALPVVLLDSAEFDSLSFSDLLFEA---DEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 165 QRalceRRAACKASDLALIVFTSGTTGRPKGVMHDH-----SCVRSVRDRGRlwKVQPGETMLNYLPMFHLYSLSEAVLQ 239
Cdd:cd05904 149 EP----PVVVIKQDDVAALLYSSGTTGRSKGVMLTHrnliaMVAQFVAGEGS--NSDSEDVFLCVLPMFHIYGLSSFALG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 240 CMYSGCRQVVMETFDANTALDLIEQKSInilhgfeTHYA-------DLLRVQAERPRNVGSLRF---GTLPSGLETSAAI 309
Cdd:cd05904 223 LLRLGATVVVMPRFDLEELLAAIERYKV-------THLPvvppivlALVKSPIVDKYDLSSLRQimsGAAPLGKELIEAF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 310 AvqvqRVFcPTV---TGAGMSESWCwmCTCAIDEPEELRCH--SSGRPLPGMEMRLIDPETGKDVPPGMPGEMLFRCYSV 384
Cdd:cd05904 296 R----AKF-PNVdlgQGYGMTESTG--VVAMCFAPEKDRAKygSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 385 MKGYFEDPEATAAALDADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPqgveQELSELV---PDILEVAVIGIP 461
Cdd:cd05904 369 MKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAP----AELEALLlshPEILDAAVIPYP 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1828927390 462 EPRLVEVPVAYVVLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQR 519
Cdd:cd05904 445 DEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILR 502
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
32-524 |
2.28e-82 |
|
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: 263.47 E-value: 2.28e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 32 AMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLIFS 111
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 112 GRAGPIDFVAlvqrslrsdlergslrtvlvgegvMPGAIswssledavyspaeqralcerraackasdlALIVFTSGTTG 191
Cdd:cd05903 81 ERFRQFDPAA------------------------MPDAV------------------------------ALLLFTSGTTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 192 RPKGVMHDH-SCVRSVRDRGRLWKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQVVMETFDANTALDLIEQKSINIL 270
Cdd:cd05903 107 EPKGVMHSHnTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFM 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 271 HGFETHYADLLRVQAERPRNVGSLRFgTLPSGLETSAAIAVQVQRVFCPTVTGA-GMSESwCWMCTCAIDEPEELRCHSS 349
Cdd:cd05903 187 MGATPFLTDLLNAVEEAGEPLSRLRT-FVCGGATVPRSLARRAAELLGAKVCSAyGSTEC-PGAVTSITPAPEDRRLYTD 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 350 GRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDaDGWLHSGDQGVVRPDGSIRFTGRYKEML 429
Cdd:cd05903 265 GRPLPGVEIKVVD-DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 430 KVGGENVSPQGVEQELSElVPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEESIIAACKGK-IASFKVPKRVVVVAE 508
Cdd:cd05903 343 IRGGENIPVLEVEDLLLG-HPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQgVAKQYWPERLVHVDD 421
|
490
....*....|....*.
gi 1828927390 509 LPHTATGKVQRAVIRK 524
Cdd:cd05903 422 LPRTPSGKVQKFRLRE 437
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
179-519 |
3.68e-81 |
|
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: 256.66 E-value: 3.68e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 179 DLALIVFTSGTTGRPKGVMHDH-SCVRSVRDRGRLWKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQVVMETFDANT 257
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHrQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 258 ALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRFGTlpSGLETSAAIAVQVQRV---FCPTVTGAGMSESWCwMC 334
Cdd:cd17638 81 ILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAV--TGAATVPVELVRRMRSelgFETVLTAYGLTEAGV-AT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 335 TCAIDEPEELRCHSSGRPLPGMEMRLIDPetgkdvppgmpGEMLFRCYSVMKGYFEDPEATAAALDADGWLHSGDQGVVR 414
Cdd:cd17638 158 MCRPGDDAETVATTCGRACPGFEVRIADD-----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 415 PDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEESIIAACKGKI 494
Cdd:cd17638 227 ERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEH-PGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRERL 305
|
330 340
....*....|....*....|....*
gi 1828927390 495 ASFKVPKRVVVVAELPHTATGKVQR 519
Cdd:cd17638 306 ANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
9-533 |
5.59e-81 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 263.44 E-value: 5.59e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 9 LGELPT----RA-AAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAA 83
Cdd:PRK06178 30 HGERPLteylRAwARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 84 AVPFNLRYRETDLADVVRRGGCKVLIfsgragPIDFVALVQRSLRSDLergSLRTVLVGE--GVMPGAISW---SSLEDA 158
Cdd:PRK06178 110 HVPVSPLFREHELSYELNDAGAEVLL------ALDQLAPVVEQVRAET---SLRHVIVTSlaDVLPAEPTLplpDSLRAP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 159 VYSPAEQRALCERRAACKAS---------DLALIVFTSGTTGRPKGVMHDH---------SCVRSVRDRgrlwkvqPGET 220
Cdd:PRK06178 181 RLAAAGAIDLLPALRACTAPvplpppaldALAALNYTGGTTGMPKGCEHTQrdmvytaaaAYAVAVVGG-------EDSV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 221 MLNYLPMFHLYSLSEAVLQCMYSGCRQVVMETFDANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRfgtlp 300
Cdd:PRK06178 254 FLSFLPEFWIAGENFGLLFPLFSGATLVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLR----- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 301 sgletsAAIAVQVQRVFCPT-------VTGAGMSE-SW-------CWMCTCAI-DEPEELRCHSS--GRPLPGMEMRLID 362
Cdd:PRK06178 329 ------QVRVVSFVKKLNPDyrqrwraLTGSVLAEaAWgmtethtCDTFTAGFqDDDFDLLSQPVfvGLPVPGTEFKICD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 363 PETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALdADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVE 442
Cdd:PRK06178 403 FETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 443 QELSeLVPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEESIIAACKGKIASFKVPKrVVVVAELPHTATGKVqravi 522
Cdd:PRK06178 482 ALLG-QHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKV----- 554
|
570
....*....|.
gi 1828927390 523 RKTALEAGLQL 533
Cdd:PRK06178 555 RKQDLQALAEE 565
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
30-523 |
6.70e-80 |
|
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: 259.22 E-value: 6.70e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 30 TGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLI 109
Cdd:cd05959 27 AGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 110 FSGragpiDFVALVQRSLRSDLErgSLRTVLVGEGVMPGAISwSSLEDAVYSPAEQralcERRAACKASDLALIVFTSGT 189
Cdd:cd05959 107 VSG-----ELAPVLAAALTKSEH--TLVVLIVSGGAGPEAGA-LLLAELVAAEAEQ----LKPAATHADDPAFWLYSSGS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 190 TGRPKGVMHDHSCVRSVRDR--GRLWKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQVVM-ETFDANTALDLIEQKS 266
Cdd:cd05959 175 TGRPKGVVHLHADIYWTAELyaRNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMpERPTPAAVFKRIRRYR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 267 INILHGFETHYADLLRVQAERPRNVGSLRFGTlPSGLETSAAIAVQVQRVF-CPTVTGAGMSESWCWMCTcaiDEPEELR 345
Cdd:cd05959 255 PTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCV-SAGEALPAEVGERWKARFgLDILDGIGSTEMLHIFLS---NRPGRVR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 346 CHSSGRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDAdGWLHSGDQGVVRPDGSIRFTGRY 425
Cdd:cd05959 331 YGTTGKPVPGYEVELRD-EDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQG-EWTRTGDKYVRDDDGFYTYAGRA 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 426 KEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATE---ESIIAACKGKIASFKVPKR 502
Cdd:cd05959 409 DDMLKVSGIWVSPFEVESALVQH-PAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEaleEELKEFVKDRLAPYKYPRW 487
|
490 500
....*....|....*....|.
gi 1828927390 503 VVVVAELPHTATGKVQRAVIR 523
Cdd:cd05959 488 IVFVDELPKTATGKIQRFKLR 508
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
25-524 |
4.56e-79 |
|
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: 254.91 E-value: 4.56e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 25 ALEWATGAMSYAELDARIDRVACGLMRNG-VNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRG 103
Cdd:cd05941 4 AIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 104 GCKVLIfsgragpidfvalvqrslrsdlergslrtvlvgegvmpgaiswssledavyspaeqralcerraackasDLALI 183
Cdd:cd05941 84 EPSLVL---------------------------------------------------------------------DPALI 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 184 VFTSGTTGRPKGVMHDHSCVRS-VRDRGRLWKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQVVMETFDANTALDLI 262
Cdd:cd05941 95 LYTSGTTGRPKGVVLTHANLAAnVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISR 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 263 EQKSINILHGFETHYADLL--------RVQAERPRNVGSLRFgtLPSGletSAAIAVQVQRVFCpTVTGA------GMSE 328
Cdd:cd05941 175 LMPSITVFMGVPTIYTRLLqyyeahftDPQFARAAAAERLRL--MVSG---SAALPVPTLEEWE-AITGHtlleryGMTE 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 329 SwcwmcTCAIDEP--EELRCHSSGRPLPGMEMRLIDPETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDADGWLH 406
Cdd:cd05941 249 I-----GMALSNPldGERRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFK 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 407 SGDQGVVRPDGSIRFTGRYKEML-KVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAA-TEE 484
Cdd:cd05941 324 TGDLGVVDEDGYYWILGRSSVDIiKSGGYKVSALEIERVLLAH-PGVSECAVIGVPDPDWGERVVAVVVLRAGAAAlSLE 402
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1828927390 485 SIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRK 524
Cdd:cd05941 403 ELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
15-524 |
4.69e-77 |
|
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: 251.06 E-value: 4.69e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 15 RAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRET 94
Cdd:cd12118 12 RAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 95 DLADVVRRGGCKVLIFSGragPIDFVALVQRslrsdlergslrtvlvGEGvmpgaiswssledavySPAEQRALCERraa 174
Cdd:cd12118 92 EIAFILRHSEAKVLFVDR---EFEYEDLLAE----------------GDP----------------DFEWIPPADEW--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 175 ckasDLALIVFTSGTTGRPKGVMHDH-SCVRSVRDRGRLWKVQPGETMLNYLPMFHL----YSLSEAVLqcmysGCRQVV 249
Cdd:cd12118 134 ----DPIALNYTSGTTGRPKGVVYHHrGAYLNALANILEWEMKQHPVYLWTLPMFHCngwcFPWTVAAV-----GGTNVC 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 250 METFDANTALDLIEQKSINILHGFETHYADLL----RVQAERPRNVGSLRFGTLPSgletsAAIAVQVQRV-FCPTVTgA 324
Cdd:cd12118 205 LRKVDAKAIYDLIEKHKVTHFCGAPTVLNMLAnappSDARPLPHRVHVMTAGAPPP-----AAVLAKMEELgFDVTHV-Y 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 325 GMSESWCWMCTCAI-----DEPEELRCHSSGR---PLPGME-MRLIDPETGKDVP-PGMP-GEMLFRCYSVMKGYFEDPE 393
Cdd:cd12118 279 GLTETYGPATVCAWkpewdELPTEERARLKARqgvRYVGLEeVDVLDPETMKPVPrDGKTiGEIVFRGNIVMKGYLKNPE 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 394 ATAAALdADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSElVPDILEVAVIGIPEPRLVEVPVAYV 473
Cdd:cd12118 359 ATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYK-HPAVLEAAVVARPDEKWGEVPCAFV 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1828927390 474 VLRPGAAATEESIIAACKGKIASFKVPKRVVVVaELPHTATGKVQRAVIRK 524
Cdd:cd12118 437 ELKEGAKVTEEEIIAFCREHLAGFMVPKTVVFG-ELPKTSTGKIQKFVLRD 486
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
17-528 |
4.78e-77 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 252.36 E-value: 4.78e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 17 AAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDL 96
Cdd:PRK06164 20 ARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 97 ADVVRRGGCKVLIFSGRAGPIDFVAL---VQRSLRSDLERgsLRTVLVGEGVMPGAISWSSLED-AVYSPAEQRALCERr 172
Cdd:PRK06164 100 AHILGRGRARWLVVWPGFKGIDFAAIlaaVPPDALPPLRA--IAVVDDAADATPAPAPGARVQLfALPDPAPPAAAGER- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 173 aACKASDLALIVFTSGTTGRPKGVMHDHSC-VRSVRDRGRLWKVQPGETMLNYLPMFHLYSLSeAVLQCMYSGCRQVVME 251
Cdd:PRK06164 177 -AADPDAGALLFTTSGTTSGPKLVLHRQATlLRHARAIARAYGYDPGAVLLAALPFCGVFGFS-TLLGALAGGAPLVCEP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 252 TFDANTALDLIEQKSINILHGFETHYADLLRvQAERPRNVGSLRFGTLPSGLETSAAIAVQVQRVFCPTVTGAGMSESWC 331
Cdd:PRK06164 255 VFDAARTARALRRHRVTHTFGNDEMLRRILD-TAGERADFPSARLFGFASFAPALGELAALARARGVPLTGLYGSSEVQA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 332 WMCTCAIDEPEELRCHSSGRPL-PGMEMRLIDPETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDADGWLHSGDQ 410
Cdd:PRK06164 334 LVALQPATDPVSVRIEGGGRPAsPEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDL 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 411 GVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIpEPRLVEVPVAYVVLRPGAAATEESIIAAC 490
Cdd:PRK06164 414 GYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEAL-PGVAAAQVVGA-TRDGKTVPVAFVIPTDGASPDEAGLMAAC 491
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1828927390 491 KGKIASFKVPKRVVVVAELPHTATG---KVQRAVIRKTALE 528
Cdd:PRK06164 492 REALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMAQA 532
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
9-524 |
6.66e-77 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 253.87 E-value: 6.66e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 9 LGELPTRAAAKWPEQKAL-EWATGA---MSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAA 84
Cdd:COG1022 13 LPDLLRRRAARFPDRVALrEKEDGIwqsLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 85 VPfnlRYrETDLAD----VVRRGGCKVLIFSGRAgpidfvaLVQR--SLRSDLErgSLRTVLV----GEGVMPGAISWSS 154
Cdd:COG1022 93 VP---IY-PTSSAEevayILNDSGAKVLFVEDQE-------QLDKllEVRDELP--SLRHIVVldprGLRDDPRLLSLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 155 LEDAVYSPAEQRALCERRAACKASDLALIVFTSGTTGRPKGVMHDHSCVRS-VRDRGRLWKVQPGETMLNYLPMFHLYsl 233
Cdd:COG1022 160 LLALGREVADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSnARALLERLPLGPGDRTLSFLPLAHVF-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 234 sEAVLQ--CMYSGCRQV---------------------------------VMETFDA---------NTALDLIEQKSINI 269
Cdd:COG1022 238 -ERTVSyyALAAGATVAfaespdtlaedlrevkptfmlavprvwekvyagIQAKAEEagglkrklfRWALAVGRRYARAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 270 LHGFEthYADLLRVQ---AERP-----RNV--GSLRFgtLPSGletSAAIAVQVQRVFC----PTVTGAGMSESwcwMCT 335
Cdd:COG1022 317 LAGKS--PSLLLRLKhalADKLvfsklREAlgGRLRF--AVSG---GAALGPELARFFRalgiPVLEGYGLTET---SPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 336 CAIDEPEELRCHSSGRPLPGMEMRlIDPEtgkdvppgmpGEMLFRCYSVMKGYFEDPEATAAALDADGWLHSGDQGVVRP 415
Cdd:COG1022 387 ITVNRPGDNRIGTVGPPLPGVEVK-IAED----------GEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 416 DGSIRFTGRYKEMLKV-GGENVSPQGVEQELSELvPDILEVAVIGIPEPRLvevpVAYVVLRPGAA---ATEESI----- 486
Cdd:COG1022 456 DGFLRITGRKKDLIVTsGGKNVAPQPIENALKAS-PLIEQAVVVGDGRPFL----AALIVPDFEALgewAEENGLpytsy 530
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828927390 487 ----------------IAACKGKIASFKVPKRVVVVA--------ELphTATGKVQRAVIRK 524
Cdd:COG1022 531 aelaqdpevraliqeeVDRANAGLSRAEQIKRFRLLPkeftiengEL--TPTLKLKRKVILE 590
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
15-525 |
2.42e-75 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 247.10 E-value: 2.42e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 15 RAAAKWPEQKALEWATGA-MSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRE 93
Cdd:PRK07514 10 RAAFADRDAPFIETPDGLrYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 94 TDLAdvvrrggckvlIFSGRAGPIDFVAlvqrslrSDLERGSLRTVLVGEGV-----MPGAISWSSLEDAVYSPAEQRAl 168
Cdd:PRK07514 90 AELD-----------YFIGDAEPALVVC-------DPANFAWLSKIAAAAGAphvetLDADGTGSLLEAAAAAPDDFET- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 169 cerrAACKASDLALIVFTSGTTGRPKGVMHDH----SCVRSVRDrgrLWKVQPGETMLNYLPMFHLYSLSEAVLQCMYSG 244
Cdd:PRK07514 151 ----VPRGADDLAAILYTSGTTGRSKGAMLSHgnllSNALTLVD---YWRFTPDDVLIHALPIFHTHGLFVATNVALLAG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 245 CRQVVMETFDANTALDLIEQKSIniLHGFETHYADLLRVQAERPRNVGSLRF---GTLPSGLETSAAIAvqvQRvfcptv 321
Cdd:PRK07514 224 ASMIFLPKFDPDAVLALMPRATV--MMGVPTFYTRLLQEPRLTREAAAHMRLfisGSAPLLAETHREFQ---ER------ 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 322 TGA------GMSESWcwMCTcaiDEP--EELRCHSSGRPLPGMEMRLIDPETGKDVPPGMPGEMLFRCYSVMKGYFEDPE 393
Cdd:PRK07514 293 TGHaileryGMTETN--MNT---SNPydGERRAGTVGFPLPGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 394 ATAAALDADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYV 473
Cdd:PRK07514 368 KTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDEL-PGVVESAVIGVPHPDFGEGVTAVV 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1828927390 474 VLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRKT 525
Cdd:PRK07514 447 VPKPGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
33-522 |
2.69e-75 |
|
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: 244.70 E-value: 2.69e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 33 MSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLIFSg 112
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 113 ragpidfvalvqrslrsdlergslrtvlvgegvmpgaiswSSLEDavyspaeqralcerraackasdLALIVFTSGTTGR 192
Cdd:cd05935 81 ----------------------------------------SELDD----------------------LALIPYTSGTTGL 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 193 PKGVMHDHSCVRSVRDRGRLW-KVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQVVMETFDANTALDLIEQKSINILH 271
Cdd:cd05935 99 PKGCMHTHFSAAANALQSAVWtGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWT 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 272 GFETHYADLLRVQAERPRNVGSLR-FGTlpSGLETSAAIAVQVQRVF-CPTVTGAGMSESwcwMCTCAIDEPEELRCHSS 349
Cdd:cd05935 179 NIPTMLVDLLATPEFKTRDLSSLKvLTG--GGAPMPPAVAEKLLKLTgLRFVEGYGLTET---MSQTHTNPPLRPKLQCL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 350 GRPLPGMEMRLIDPETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDADG---WLHSGDQGVVRPDGSIRFTGRYK 426
Cdd:cd05935 254 GIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVK 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 427 EMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPG--AAATEESIIAACKGKIASFKVPKRVV 504
Cdd:cd05935 334 RMINVSGFKVWPAEVEAKLYKH-PAI*EVCVISVPDERVGEEVKAFIVLRPEyrGKVTEEDIIEWAREQMAAYKYPREVE 412
|
490
....*....|....*...
gi 1828927390 505 VVAELPHTATGKVQRAVI 522
Cdd:cd05935 413 FVDELPRSASGKILWRLL 430
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
14-529 |
7.88e-74 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 243.90 E-value: 7.88e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 14 TRAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRE 93
Cdd:PRK06155 28 ARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 94 TDLADVVRRGGCKVLIFSGragpiDFVALVQRSLRSDLERGslRTVLVGEgvmPGAISWSSLEDAV-YSPAEQRALCerr 172
Cdd:PRK06155 108 PQLEHILRNSGARLLVVEA-----ALLAALEAADPGDLPLP--AVWLLDA---PASVSVPAGWSTApLPPLDAPAPA--- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 173 AACKASDLALIVFTSGTTGRPKGVMHDHS-----CVRSVRDRGrlwkVQPGETMLNYLPMFHLYSLSeAVLQCMYSGCRQ 247
Cdd:PRK06155 175 AAVQPGDTAAILYTSGTTGPSKGVCCPHAqfywwGRNSAEDLE----IGADDVLYTTLPLFHTNALN-AFFQALLAGATY 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 248 VVMETFDANTALDLIEQksinilHGFETHY-----ADLLRVQAERPRNVGS-LRFGTLPSgleTSAAIAVQV-QRVFCPT 320
Cdd:PRK06155 250 VLEPRFSASGFWPAVRR------HGATVTYllgamVSILLSQPARESDRAHrVRVALGPG---VPAALHAAFrERFGVDL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 321 VTGAGMSESwcwMCTCAIDEPEElRCHSSGRPLPGMEMRLIDpETGKDVPPGMPGEMLFRC---YSVMKGYFEDPEATAA 397
Cdd:PRK06155 321 LDGYGSTET---NFVIAVTHGSQ-RPGSMGRLAPGFEARVVD-EHDQELPDGEPGELLLRAdepFAFATGYFGMPEKTVE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 398 ALDaDGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEpRLVEVPV-AYVVLR 476
Cdd:PRK06155 396 AWR-NLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSH-PAVAAAAVFPVPS-ELGEDEVmAAVVLR 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1828927390 477 PGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRKTALEA 529
Cdd:PRK06155 473 DGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVTA 525
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
21-519 |
3.42e-73 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 240.63 E-value: 3.42e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 21 PEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVV 100
Cdd:PRK03640 16 PDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 101 RRGGCKVLIFSGragpiDFVALVQRSLRSDlergslrtvlvgegvmpgaisWSSLEDAVYSPAEqraLCErraACKASDL 180
Cdd:PRK03640 96 DDAEVKCLITDD-----DFEAKLIPGISVK---------------------FAELMNGPKEEAE---IQE---EFDLDEV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 181 ALIVFTSGTTGRPKGVM-----HDHSCVRSVRDRGrlwkVQPGETMLNYLPMFHLYSLSEAVLQCMYsGCRQVVMETFDA 255
Cdd:PRK03640 144 ATIMYTSGTTGKPKGVIqtygnHWWSAVGSALNLG----LTEDDCWLAAVPIFHISGLSILMRSVIY-GMRVVLVEKFDA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 256 NTALDLIEQKSINILHGFETHYADLLRVQAERPRNvGSLRfGTLPSGLETSAAIAVQVQRVFCPTVTGAGMSESWCWMCT 335
Cdd:PRK03640 219 EKINKLLQTGGVTIISVVSTMLQRLLERLGEGTYP-SSFR-CMLLGGGPAPKPLLEQCKEKGIPVYQSYGMTETASQIVT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 336 CAIDEPEElRCHSSGRPLPGMEMRLIDpeTGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDaDGWLHSGDQGVVRP 415
Cdd:PRK03640 297 LSPEDALT-KLGSAGKPLFPCELKIEK--DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQ-DGWFKTGDIGYLDE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 416 DGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLrpGAAATEESIIAACKGKIA 495
Cdd:PRK03640 373 EGFLYVLDRRSDLIISGGENIYPAEIEEVLLSH-PGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVTEEELRHFCEEKLA 449
|
490 500
....*....|....*....|....
gi 1828927390 496 SFKVPKRVVVVAELPHTATGKVQR 519
Cdd:PRK03640 450 KYKVPKRFYFVEELPRNASGKLLR 473
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
23-523 |
8.27e-72 |
|
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: 235.82 E-value: 8.27e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 23 QKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRR 102
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 103 GGCKVLIFSgragpidfvalvqrslrsdlergslrtvlvgegvmpgaiswssledavyspaeqralcerraackASDLAL 182
Cdd:cd05919 81 CEARLVVTS-----------------------------------------------------------------ADDIAY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 183 IVFTSGTTGRPKGVMHDHSCVRSVRDR--GRLWKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQVVMETF-DANTAL 259
Cdd:cd05919 96 LLYSSGTTGPPKGVMHAHRDPLLFADAmaREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWpTAERVL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 260 DLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRFGTlPSGLETSAAIAVQVQRVF-CPTVTGAGMSES-WCWMCtca 337
Cdd:cd05919 176 ATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCV-SAGEALPRGLGERWMEHFgGPILDGIGATEVgHIFLS--- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 338 iDEPEELRCHSSGRPLPGMEMRLIDPEtGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALdADGWLHSGDQGVVRPDG 417
Cdd:cd05919 252 -NRPGAWRLGSTGRPVPGYEIRLVDEE-GHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 418 SIRFTGRYKEMLKVGGENVSPQGVEQELSElVPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATE---ESIIAACKGKI 494
Cdd:cd05919 329 WYTHAGRADDMLKVGGQWVSPVEVESLIIQ-HPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQEslaRDIHRHLLERL 407
|
490 500
....*....|....*....|....*....
gi 1828927390 495 ASFKVPKRVVVVAELPHTATGKVQRAVIR 523
Cdd:cd05919 408 SAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
21-520 |
1.24e-70 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 234.37 E-value: 1.24e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 21 PEQKALEWATGAMSYAELDARIDRVACGLM-RNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADV 99
Cdd:PRK06839 16 PDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 100 VRRGGCKVLI----FSGRAGPIDFVALVQRSLRSDlergslrtvlvgegvmpgaiSWSSLEDAVYSPAEQRAlcerraac 175
Cdd:PRK06839 96 LKDSGTTVLFvektFQNMALSMQKVSYVQRVISIT--------------------SLKEIEDRKIDNFVEKN-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 176 kASDLALIVFTSGTTGRPKG-VMHDHSCVRSVRDRGRLWKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQVVMETFD 254
Cdd:PRK06839 148 -ESASFIICYTSGTTGKPKGaVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 255 ANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRF---GTLPSGLETSAAIavqVQRVFcPTVTGAGMSESWC 331
Cdd:PRK06839 227 PTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWfynGGAPCPEELMREF---IDRGF-LFGQGFGMTETSP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 332 WMCTCAIDEPEElRCHSSGRPLPGMEMRLIDPETGkDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDaDGWLHSGDQG 411
Cdd:PRK06839 303 TVFMLSEEDARR-KVGSIGKPVLFCDYELIDENKN-KVEVGEVGELLIRGPNVMKEYWNRPDATEETIQ-DGWLCTGDLA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 412 VVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEESIIAACK 491
Cdd:PRK06839 380 RVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKL-SDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCR 458
|
490 500
....*....|....*....|....*....
gi 1828927390 492 GKIASFKVPKRVVVVAELPHTATGKVQRA 520
Cdd:PRK06839 459 LFLAKYKIPKEIVFLKELPKNATGKIQKA 487
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
16-518 |
1.93e-70 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 235.24 E-value: 1.93e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 16 AAAKWPEQKALEWATGAMSYAELDARIDRVACGLMR-NGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRET 94
Cdd:PRK08314 19 SARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 95 DLADVVRRGGCKVLIFSGRagpidfvaLVQRsLRSDLERGSLRTVLVG-------------------------EGVMPGA 149
Cdd:PRK08314 99 ELAHYVTDSGARVAIVGSE--------LAPK-VAPAVGNLRLRHVIVAqysdylpaepeiavpawlraepplqALAPGGV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 150 ISWSSLEDAVYSPAEQRAlcerraacKASDLALIVFTSGTTGRPKGVMHDHSCVRSVRDRGRLW-KVQPGETMLNYLPMF 228
Cdd:PRK08314 170 VAWKEALAAGLAPPPHTA--------GPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWsNSTPESVVLAVLPLF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 229 HLYSLSEAVLQCMYSGCRQVVMETFDANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRFGT-----LPsgl 303
Cdd:PRK08314 242 HVTGMVHSMNAPIYAGATVVLMPRWDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGgggaaMP--- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 304 etsAAIAVQVQRVF-CPTVTGAGMSESwcwMCTCAIDEPEELRCHSSGRPLPGMEMRLIDPETGKDVPPGMPGEMLFRCY 382
Cdd:PRK08314 319 ---EAVAERLKELTgLDYVEGYGLTET---MAQTHSNPPDRPKLQCLGIPTFGVDARVIDPETLEELPPGEVGEIVVHGP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 383 SVMKGYFEDPEATAAA---LDADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIG 459
Cdd:PRK08314 393 QVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKH-PAIQEACVIA 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828927390 460 IPEPRLVEVPVAYVVLRPGAAA--TEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQ 518
Cdd:PRK08314 472 TPDPRRGETVKAVVVLRPEARGktTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKIL 532
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
9-524 |
3.32e-70 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 234.64 E-value: 3.32e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 9 LGELPTRAAAKWPEQKALEWATGA-MSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPF 87
Cdd:PRK06087 25 LADYWQQTARAMPDKIAVVDNHGAsYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 88 NLRYRETDLADVVRRGGCKVLIFSGRAGPIDFVALVQrSLRSDLErgSLRTVLVGEGVMPG--AISWSS-LEDavYSPAE 164
Cdd:PRK06087 105 LPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVDLIL-PLQNQLP--QLQQIVGVDKLAPAtsSLSLSQiIAD--YEPLT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 165 QralcerrAACKASD-LALIVFTSGTTGRPKGVMHDHSCV----RSVRDR-GRLWKvqpgETMLNYLPMFHLYSLSEAVL 238
Cdd:PRK06087 180 T-------AITTHGDeLAAVLFTSGTEGLPKGVMLTHNNIlaseRAYCARlNLTWQ----DVFMMPAPLGHATGFLHGVT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 239 QCMYSGCRQVVMETFDANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRFgTLPSGLETSAAIAVQVQRVFC 318
Cdd:PRK06087 249 APFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRF-FLCGGTTIPKKVARECQQRGI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 319 PTVTGAGMSESwCWMCTCAIDEPEELRCHSSGRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAA 398
Cdd:PRK06087 328 KLLSVYGSTES-SPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVD-EARKTLPPGCEGEEASRGPNVFMGYLDEPELTARA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 399 LDADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPG 478
Cdd:PRK06087 406 LDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQH-PKIHDACVVAMPDERLGERSCAYVVLKAP 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1828927390 479 AA--ATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRK 524
Cdd:PRK06087 485 HHslTLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
34-524 |
5.20e-70 |
|
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: 233.29 E-value: 5.20e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 34 SYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLIFSgr 113
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVD-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 114 agpIDFVALVQRsLRSDLERgsLRTVLVG----EGVMPGAISWSSLEDAVyspAEQRALC------ERRAACkasdlalI 183
Cdd:cd12119 105 ---RDFLPLLEA-IAPRLPT--VEHVVVMtddaAMPEPAGVGVLAYEELL---AAESPEYdwpdfdENTAAA-------I 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 184 VFTSGTTGRPKGVMHDHscvRS-------VRDRGRLwKVQPGETMLNYLPMFHLYS--LSEAvlqCMYSGCRQVVMETF- 253
Cdd:cd12119 169 CYTSGTTGNPKGVVYSH---RSlvlhamaALLTDGL-GLSESDVVLPVVPMFHVNAwgLPYA---AAMVGAKLVLPGPYl 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 254 DANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRF-----GTLPSGL-ETSAAIAVQVqrvfcptVTGAGMS 327
Cdd:cd12119 242 DPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRvviggSAVPRSLiEAFEERGVRV-------IHAWGMT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 328 ESwCWMCTCAI----------DEPEELRChSSGRPLPGMEMRLIDPETGKdvppgMP------GEMLFRCYSVMKGYFED 391
Cdd:cd12119 315 ET-SPLGTVARppsehsnlseDEQLALRA-KQGRPVPGVELRIVDDDGRE-----LPwdgkavGELQVRGPWVTKSYYKN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 392 PEATAAaLDADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSElVPDILEVAVIGIPEPRLVEVPVA 471
Cdd:cd12119 388 DEESEA-LTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMA-HPAVAEAAVIGVPHPKWGERPLA 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1828927390 472 YVVLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRK 524
Cdd:cd12119 466 VVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
17-519 |
2.73e-69 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 231.50 E-value: 2.73e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 17 AAKWPEQKAL--EWATGAM---SYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRY 91
Cdd:PRK08008 17 ADVYGHKTALifESSGGVVrrySYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 92 RETDLADVVRRGGCKVLIFSGragpiDFVALVQRSLRSDleRGSLRTVLV---GEGVMPGAISWSSLEDAvySPAEqraL 168
Cdd:PRK08008 97 LREESAWILQNSQASLLVTSA-----QFYPMYRQIQQED--ATPLRHICLtrvALPADDGVSSFTQLKAQ--QPAT---L 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 169 CERRAaCKASDLALIVFTSGTTGRPKGVMHDHSCVR----------SVRDRGRLwkvqpgetmLNYLPMFHLYSLSEAVL 238
Cdd:PRK08008 165 CYAPP-LSTDDTAEILFTSGTTSRPKGVVITHYNLRfagyysawqcALRDDDVY---------LTVMPAFHIDCQCTAAM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 239 QCMYSGCRQVVMETFDANTALDLIEQKSINILHGFETHYADLLrVQAERP--RNvGSLR--FGTLPsgletsaaIAVQVQ 314
Cdd:PRK08008 235 AAFSAGATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLM-VQPPSAndRQ-HCLRevMFYLN--------LSDQEK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 315 RVFCPT-----VTGAGMSESWCWMCTcaiDEP-EELRCHSSGRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCY---SVM 385
Cdd:PRK08008 305 DAFEERfgvrlLTSYGMTETIVGIIG---DRPgDKRRWPSIGRPGFCYEAEIRD-DHNRPLPAGEIGEICIKGVpgkTIF 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 386 KGYFEDPEATAAALDADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRL 465
Cdd:PRK08008 381 KEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATH-PKIQDIVVVGIKDSIR 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1828927390 466 VEVPVAYVVLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQR 519
Cdd:PRK08008 460 DEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIK 513
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
14-524 |
5.50e-69 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 231.20 E-value: 5.50e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 14 TRAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRE 93
Cdd:PRK07786 24 ARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 94 TDLADVVRRGGCKVLIFSGRAGPidfVALVQRSLRSDLErgslrTVLVGEGvmpgaiswsSLEDAVYSPAEQraLCERRA 173
Cdd:PRK07786 104 PEIAFLVSDCGAHVVVTEAALAP---VATAVRDIVPLLS-----TVVVAGG---------SSDDSVLGYEDL--LAEAGP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 174 ACKASDL-----ALIVFTSGTTGRPKGVMHDHS--------CVRSVR-DRGRlwkvqpgETMLNYLPMFHLYSLSeAVLQ 239
Cdd:PRK07786 165 AHAPVDIpndspALIMYTSGTTGRPKGAVLTHAnltgqamtCLRTNGaDINS-------DVGFVGVPLFHIAGIG-SMLP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 240 CMYSGCRQVVMET--FDANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVgSLRF---GTLPSgletSAAIAVQVQ 314
Cdd:PRK07786 237 GLLLGAPTVIYPLgaFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDL-ALRVlswGAAPA----SDTLLRQMA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 315 RVFCPTVTGAGMSESWCWMCTCAIDEPEELR-CHSSGRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCYSVMKGYFEDPE 393
Cdd:PRK07786 312 ATFPEAQILAAFGQTEMSPVTCMLLGEDAIRkLGSVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 394 ATAAALDAdGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYV 473
Cdd:PRK07786 391 ATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASH-PDIVEVAVIGRADEKWGEVPVAVA 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1828927390 474 VLRPGAAATE-ESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRK 524
Cdd:PRK07786 469 AVRNDDAALTlEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRE 520
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
34-527 |
7.65e-68 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 227.00 E-value: 7.65e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 34 SYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLI---- 109
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLgdda 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 110 -FSGRAGPIDFVALVQrslrsdlergslrtvlvgegvmpgAISWSSLEDAVYSPAEQralcerraackasdLALIVFTSG 188
Cdd:PRK09088 104 vAAGRTDVEDLAAFIA------------------------SADALEPADTPSIPPER--------------VSLILFTSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 189 TTGRPKGVMHDHSCVRSVR-DRGRLWKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQVVMETFDANTALDLIEQKSI 267
Cdd:PRK09088 146 TSGQPKGVMLSERNLQQTAhNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLGDPAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 268 NILHGFET-HYADLLRVQ----AERPRNVGSLRFGTLPSGLETSAAIAVQvqrvFCPTVTGAGMSESWCWMCTCAIDEPE 342
Cdd:PRK09088 226 GITHYFCVpQMAQAFRAQpgfdAAALRHLTALFTGGAPHAAEDILGWLDD----GIPMVDGFGMSEAGTVFGMSVDCDVI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 343 ELRCHSSGRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDADGWLHSGDQGVVRPDGSIRFT 422
Cdd:PRK09088 302 RAKAGAAGIPTPTVQTRVVD-DQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 423 GRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEESIIAACKGKIASFKVPKR 502
Cdd:PRK09088 381 DRKKDMFISGGENVYPAEIEAVLADH-PGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKH 459
|
490 500
....*....|....*....|....*
gi 1828927390 503 VVVVAELPHTATGKVQRAVIRKTAL 527
Cdd:PRK09088 460 LRLVDALPRTASGKLQKARLRDALA 484
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
9-519 |
1.64e-67 |
|
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: 225.67 E-value: 1.64e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 9 LGELPTRAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFN 88
Cdd:cd05920 17 LGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 89 LRYRETDLADVVRRGGCKVLIFSGRAGPIDFVALVQRSLRSdlergslrtvlvgegvmpgaiswssledavyspaeqral 168
Cdd:cd05920 97 PSHRRSELSAFCAHAEAVAYIVPDRHAGFDHRALARELAES--------------------------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 169 cerraackASDLALIVFTSGTTGRPKGVMHDHS-CVRSVRDRGRLWKVQPGETMLNYLPMFHLYSLS-EAVLQCMYSGCR 246
Cdd:cd05920 138 --------IPEVALFLLSGGTTGTPKLIPRTHNdYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLAcPGVLGTLLAGGR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 247 QVVMETFDANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRF-----GTLPSGL--ETSAAIAVQVQRVFcp 319
Cdd:cd05920 210 VVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLlqvggARLSPALarRVPPVLGCTLQQVF-- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 320 tvtgaGMSESWcwMCTCAIDEPEELRCHSSGRPL-PGMEMRLIDPEtGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAA 398
Cdd:cd05920 288 -----GMAEGL--LNYTRLDDPDEVIIHTQGRPMsPDDEIRVVDEE-GNPVPPGEEGELLTRGPYTIRGYYRAPEHNARA 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 399 LDADGWLHSGDqgVVR--PDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLR 476
Cdd:cd05920 360 FTPDGFYRTGD--LVRrtPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRH-PAVHDAAVVAMPDELLGERSCAFVVLR 436
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1828927390 477 PGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQR 519
Cdd:cd05920 437 DPPPSAAQLRRFLRERGLAAYKLPDRIEFVDSLPLTAVGKIDK 479
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
17-523 |
8.55e-67 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 224.38 E-value: 8.55e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 17 AAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDL 96
Cdd:PRK06145 12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 97 ADVVRRGGCKVLI----FSGRAGPIDFVALVQRSLRSDLERgslrtvlVGEGVMPgaiswssledavyspaeqralCERR 172
Cdd:PRK06145 92 AYILGDAGAKLLLvdeeFDAIVALETPKIVIDAAAQADSRR-------LAQGGLE---------------------IPPQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 173 AACKASDLALIVFTSGTTGRPKGVMHDHSCVRsvrdrgrlWK---------VQPGETMLNYLPMFHLYSLSEAVLQCMYS 243
Cdd:PRK06145 144 AAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLH--------WKsidhvialgLTASERLLVVGPLYHVGAFDLPGIAVLWV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 244 GCRQVVMETFDANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRFgTLPSGLETSAAIAVQVQRVFCPT--V 321
Cdd:PRK06145 216 GGTLRIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAW-CIGGGEKTPESRIRDFTRVFTRAryI 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 322 TGAGMSEswcwmcTCAIDEPEEL-----RCHSSGRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATA 396
Cdd:PRK06145 295 DAYGLTE------TCSGDTLMEAgreieKIGSTGRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 397 AALdADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLR 476
Cdd:PRK06145 368 EAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYEL-PEVAEAAVIGVHDDRWGERITAVVVLN 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1828927390 477 PGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIR 523
Cdd:PRK06145 446 PGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
34-519 |
9.29e-67 |
|
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: 221.84 E-value: 9.29e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 34 SYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADvvrrggckvlifsgr 113
Cdd:cd05912 3 TFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAF--------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 114 agpidfvalvqrslrsdlergslrtvlvgegvmpgaiswsSLEDAvyspaeqralcerraACKASDLALIVFTSGTTGRP 193
Cdd:cd05912 68 ----------------------------------------QLKDS---------------DVKLDDIATIMYTSGTTGKP 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 194 KGV-----MHDHSCVRSVRDRGrlwkVQPGETMLNYLPMFHLYSLSeAVLQCMYSGCRQVVMETFDANTALDLIEQKSIN 268
Cdd:cd05912 93 KGVqqtfgNHWWSAIGSALNLG----LTEDDNWLCALPLFHISGLS-ILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVT 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 269 ILHGFETHYADLLRVQAERPRNvgSLRFGTLPSGLETSAAIAVQVQRVFcPTVTGAGMSESWCWMCTCAIDEPEElRCHS 348
Cdd:cd05912 168 IISVVPTMLQRLLEILGEGYPN--NLRCILLGGGPAPKPLLEQCKEKGI-PVYQSYGMTETCSQIVTLSPEDALN-KIGS 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 349 SGRPLPGMEMRLIDPetgkDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALdADGWLHSGDQGVVRPDGSIRFTGRYKEM 428
Cdd:cd05912 244 AGKPLFPVELKIEDD----GQPPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDL 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 429 LKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVL-RPgaaATEESIIAACKGKIASFKVPKRVVVVA 507
Cdd:cd05912 319 IISGGENIYPAEIEEVLLSH-PAIKEAGVVGIPDDKWGQVPVAFVVSeRP---ISEEELIAYCSEKLAKYKVPKKIYFVD 394
|
490
....*....|..
gi 1828927390 508 ELPHTATGKVQR 519
Cdd:cd05912 395 ELPRTASGKLLR 406
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
15-530 |
1.10e-66 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 225.21 E-value: 1.10e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 15 RAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRET 94
Cdd:PRK08162 26 RAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 95 DLADVVRRGGCKVLIfsgragpID--FVALVQRSLRsdlERGSLRTVLVGegvmpgaiswssLEDAVYSPAEQRALCERR 172
Cdd:PRK08162 106 SIAFMLRHGEAKVLI-------VDteFAEVAREALA---LLPGPKPLVID------------VDDPEYPGGRFIGALDYE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 173 AACKASD--------------LALiVFTSGTTGRPKGVMHDHscvrsvrdRGRL---------WKVQPGETMLNYLPMFH 229
Cdd:PRK08162 164 AFLASGDpdfawtlpadewdaIAL-NYTSGTTGNPKGVVYHH--------RGAYlnalsnilaWGMPKHPVYLWTLPMFH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 230 L----YSLSEAVlqcmySGCRQVVMETFDANTALDLIEQKSIN------ILHGFETHYADLLRVQAERPrnVGSLRFGTL 299
Cdd:PRK08162 235 CngwcFPWTVAA-----RAGTNVCLRKVDPKLIFDLIREHGVThycgapIVLSALINAPAEWRAGIDHP--VHAMVAGAA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 300 PSG--LETSAAIAVQVQRVFcptvtgaGMSESWCWMCTCAIDE-----PEELRCHSSGR---PLPGME-MRLIDPETGKD 368
Cdd:PRK08162 308 PPAavIAKMEEIGFDLTHVY-------GLTETYGPATVCAWQPewdalPLDERAQLKARqgvRYPLQEgVTVLDPDTMQP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 369 VP---PGMpGEMLFRCYSVMKGYFEDPEATAAALdADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQEL 445
Cdd:PRK08162 381 VPadgETI-GEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVL 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 446 SELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEESIIAACKGKIASFKVPKRvVVVAELPHTATGKVQRAVIRKT 525
Cdd:PRK08162 459 YRH-PAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKA-VVFGELPKTSTGKIQKFVLREQ 536
|
....*
gi 1828927390 526 ALEAG 530
Cdd:PRK08162 537 AKSLK 541
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
179-519 |
1.12e-65 |
|
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: 216.37 E-value: 1.12e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 179 DLALIVFTSGTTGRPKGVMHDHSCVRSVRDRGRL-WKVQPGETMLNYLPMFHLYSLSEAvLQCMYSGCRQVVMETFDANT 257
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHaMGLTEADVYLNMLPLFHIAGLNLA-LATFHAGGANVVMEKFDPAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 258 ALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRfgtLPSGLETSAAIavQVQRVFCPTV--TGAGMSESWCWMCT 335
Cdd:cd17637 80 ALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLR---HVLGLDAPETI--QRFEETTGATfwSLYGQTETSGLVTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 336 CAIDEpeelRCHSSGRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDaDGWLHSGDQGVVRP 415
Cdd:cd17637 155 SPYRE----RPGSAGRPGPLVRVRIVD-DNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFR-NGWHHTGDLGRFDE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 416 DGSIRFTGRY--KEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEESIIAACKGK 493
Cdd:cd17637 229 DGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEH-PAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFVGSR 307
|
330 340
....*....|....*....|....*.
gi 1828927390 494 IASFKVPKRVVVVAELPHTATGKVQR 519
Cdd:cd17637 308 IARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
10-523 |
6.55e-65 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 219.86 E-value: 6.55e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 10 GELPTRAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNL 89
Cdd:PRK06188 15 GHLLVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 90 RYRETDLADVVRRGGCKVLIfsgragpIDFVALVQRSLRSDLERGSLRTVLvGEGVMPGAISWSSLEDAvYSPAEQRAlc 169
Cdd:PRK06188 95 LGSLDDHAYVLEDAGISTLI-------VDPAPFVERALALLARVPSLKHVL-TLGPVPDGVDLLAAAAK-FGPAPLVA-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 170 errAACkASDLALIVFTSGTTGRPKGVMHDHscvRSVRDRGRL----WKVQPGETMLNYLPMFHLYSLSeaVLQCMYSGC 245
Cdd:PRK06188 164 ---AAL-PPDIAGLAYTGGTTGKPKGVMGTH---RSIATMAQIqlaeWEWPADPRFLMCTPLSHAGGAF--FLPTLLRGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 246 RQVVMETFDANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRfgTLPSGletSAAIA----VQVQRVFCPTV 321
Cdd:PRK06188 235 TVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLE--TVYYG---ASPMSpvrlAEAIERFGPIF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 322 TGA-GMSEswCWMCTCAI-------DEPEELRchSSGRPLPGMEMRLIDPEtGKDVPPGMPGEMLFRCYSVMKGYFEDPE 393
Cdd:PRK06188 310 AQYyGQTE--APMVITYLrkrdhdpDDPKRLT--SCGRPTPGLRVALLDED-GREVAQGEVGEICVRGPLVMDGYWNRPE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 394 ATAAALdADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYV 473
Cdd:PRK06188 385 ETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEH-PAVAQVAVIGVPDEKWGEAVTAVV 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1828927390 474 VLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIR 523
Cdd:PRK06188 463 VLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
17-522 |
1.04e-64 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 220.67 E-value: 1.04e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 17 AAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDL 96
Cdd:PRK06710 34 ASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTEREL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 97 ADVVRRGGCKVLIFSGRAGP-------------------IDFVALVQRSLRSDLERGSLRTVL-VGEGVMPGAisWSSLE 156
Cdd:PRK06710 114 EYQLHDSGAKVILCLDLVFPrvtnvqsatkiehvivtriADFLPFPKNLLYPFVQKKQSNLVVkVSESETIHL--WNSVE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 157 DAVYSPAEqrALCErraacKASDLALIVFTSGTTGRPKGVMHDHSCVRSVRDRGRLWK---VQPGETMLNYLPMFHLYSL 233
Cdd:PRK06710 192 KEVNTGVE--VPCD-----PENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLyncKEGEEVVLGVLPFFHVYGM 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 234 SEAVLQCMYSGCRQVVMETFDANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRfgtlpSGLETSAAIAVQV 313
Cdd:PRK06710 265 TAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIR-----ACISGSAPLPVEV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 314 QRVFcPTVTGAGMSESWCWMCTCAIDEPE---ELRCHSS-GRPLPGMEMRLIDPETGKDVPPGMPGEMLFRCYSVMKGYF 389
Cdd:PRK06710 340 QEKF-ETVTGGKLVEGYGLTESSPVTHSNflwEKRVPGSiGVPWPDTEAMIMSLETGEALPPGEIGEIVVKGPQIMKGYW 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 390 EDPEATAAALDaDGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVP 469
Cdd:PRK06710 419 NKPEETAAVLQ-DGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEH-EKVQEVVTIGVPDPYRGETV 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1828927390 470 VAYVVLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVI 522
Cdd:PRK06710 497 KAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
9-525 |
2.24e-64 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 219.03 E-value: 2.24e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 9 LGELPTRAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFN 88
Cdd:PRK07788 51 FAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 89 LRYRETDLADVVRRGGCKVLIFSGragpiDFVALVqRSLRSDLERgsLRTVLV-GEGVMPGAISWSSLEDAVYSPAEQRA 167
Cdd:PRK07788 131 TGFSGPQLAEVAAREGVKALVYDD-----EFTDLL-SALPPDLGR--LRAWGGnPDDDEPSGSTDETLDDLIAGSSTAPL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 168 LCERRAAckasdlALIVFTSGTTGRPKGVMHDH----SCVRSVRDRgRLWKVqpGETMLNYLPMFHLYSLSEAVLQCMYs 243
Cdd:PRK07788 203 PKPPKPG------GIVILTSGTTGTPKGAPRPEpsplAPLAGLLSR-VPFRA--GETTLLPAPMFHATGWAHLTLAMAL- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 244 GCRQVVMETFDANTALDLIEQKSINILHGFETHYADLLRVQAERP--RNVGSLRFgTLPSGLETSAAIAVQVQRVFCPTV 321
Cdd:PRK07788 273 GSTVVLRRRFDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLakYDTSSLKI-IFVSGSALSPELATRALEAFGPVL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 322 TGA-GMSE-SWcwmctCAIDEPEELRCHSS--GRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCYSVMKGYFE--DPEAt 395
Cdd:PRK07788 352 YNLyGSTEvAF-----ATIATPEDLAEAPGtvGRPPKGVTVKILD-ENGNEVPRGVVGRIFVGNGFPFEGYTDgrDKQI- 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 396 aaaldADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEP----RLvevpVA 471
Cdd:PRK07788 425 -----IDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGH-PDVVEAAVIGVDDEefgqRL----RA 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1828927390 472 YVVLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRKT 525
Cdd:PRK07788 495 FVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
17-530 |
1.32e-63 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 216.77 E-value: 1.32e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 17 AAKWPEQKAL-EWATGA-MSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRET 94
Cdd:PLN02246 33 LSEFSDRPCLiDGATGRvYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 95 DLADVVRRGGCKVLIFSGRAgpIDFVAlvqrslrsDLERGSLRTVLVGEGVMPGAISWSSLEDAVYSPAEQralcerrAA 174
Cdd:PLN02246 113 EIAKQAKASGAKLIITQSCY--VDKLK--------GLAEDDGVTVVTIDDPPEGCLHFSELTQADENELPE-------VE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 175 CKASDLALIVFTSGTTGRPKGVMHDH-SCVRSVR-----DRGRLWkVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQV 248
Cdd:PLN02246 176 ISPDDVVALPYSSGTTGLPKGVMLTHkGLVTSVAqqvdgENPNLY-FHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAIL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 249 VMETFDANTALDLIEQKSINIlhgfethyADL----LRVQAERPR----NVGSLRF---GTLPSGLETSAAI------AV 311
Cdd:PLN02246 255 IMPKFEIGALLELIQRHKVTI--------APFvppiVLAIAKSPVvekyDLSSIRMvlsGAAPLGKELEDAFraklpnAV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 312 QVQrvfcptvtGAGMSESW--CWMCTCAIDEPEELRCHSSGRPLPGMEMRLIDPETGKDVPPGMPGEMLFRCYSVMKGYF 389
Cdd:PLN02246 327 LGQ--------GYGMTEAGpvLAMCLAFAKEPFPVKSGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 390 EDPEATAAALDADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPqgveQELSELV---PDILEVAVIGIPEPRLV 466
Cdd:PLN02246 399 NDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAP----AELEALLishPSIADAAVVPMKDEVAG 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1828927390 467 EVPVAYVVLRPGAAATEESIiaacKGKIAS----FKVPKRVVVVAELPHTATGKVQRAVIRKtALEAG 530
Cdd:PLN02246 475 EVPVAFVVRSNGSEITEDEI----KQFVAKqvvfYKRIHKVFFVDSIPKAPSGKILRKDLRA-KLAAG 537
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
34-524 |
1.02e-60 |
|
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: 206.42 E-value: 1.02e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 34 SYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLIfsgr 113
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 114 agpidfvalvqrslrsdlergslrtvlvgegvmpgaiswssledavyspaeqralcerraaCKASDLALIVFTSGTTGRP 193
Cdd:cd05972 78 -------------------------------------------------------------TDAEDPALIYFTSGTTGLP 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 194 KGVMHDHSCVRSVRDRGRLW-KVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQVV--METFDANTALDLIEQKSINIL 270
Cdd:cd05972 97 KGVLHTHSYPLGHIPTAAYWlGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVyeGPRFDAERILELLERYGVTSF 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 271 HGFETHYADLLRVQAERpRNVGSLRfgTLPSGLE--TSAAIAVQVQRVFCPTVTGAGMSESwcwMCTCAIDEPEELRCHS 348
Cdd:cd05972 177 CGPPTAYRMLIKQDLSS-YKFSHLR--LVVSAGEplNPEVIEWWRAATGLPIRDGYGQTET---GLTVGNFPDMPVKPGS 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 349 SGRPLPGMEMRLIDPEtGKDVPPGMPGEMLFRC--YSVMKGYFEDPEATAAALdADGWLHSGDQGVVRPDGSIRFTGRYK 426
Cdd:cd05972 251 MGRPTPGYDVAIIDDD-GRELPPGEEGDIAIKLppPGLFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRAD 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 427 EMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEE---SIIAACKGKIASFKVPKRV 503
Cdd:cd05972 329 DIIKSSGYRIGPFEVESALLEH-PAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEElaeELQGHVKKVLAPYKYPREI 407
|
490 500
....*....|....*....|.
gi 1828927390 504 VVVAELPHTATGKVQRAVIRK 524
Cdd:cd05972 408 EFVEELPKTISGKIRRVELRD 428
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
28-516 |
2.31e-60 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 207.45 E-value: 2.31e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 28 WATGA-MSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCK 106
Cdd:PRK08276 6 APSGEvVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 107 VLIFSGRagpidfVALVQRSLRSDLERGsLRTVLVGEGVMPGAISWSSLEDAV--YSPAEQRALcerraackasdlALIV 184
Cdd:PRK08276 86 VLIVSAA------LADTAAELAAELPAG-VPLLLVVAGPVPGFRSYEEALAAQpdTPIADETAG------------ADML 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 185 FTSGTTGRPKGVMH-------DHSCVRSVRDRGRLWKVQPGETMLNYLPMFHlyslsEAVLQ-CMYS---GCRQVVMETF 253
Cdd:PRK08276 147 YSSGTTGRPKGIKRplpgldpDEAPGMMLALLGFGMYGGPDSVYLSPAPLYH-----TAPLRfGMSAlalGGTVVVMEKF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 254 DANTALDLIEQKSINILHGFETHYADLLRV-QAERPR-NVGSLRFGtlpsgLETSAAIAVQVQRV----FCPTV------ 321
Cdd:PRK08276 222 DAEEALALIERYRVTHSQLVPTMFVRMLKLpEEVRARyDVSSLRVA-----IHAAAPCPVEVKRAmidwWGPIIheyyas 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 322 TGAGMSeswcwmctCAIDePEELRCH--SSGRPLPGmEMRLIDpETGKDVPPGMPGEMLFRcysvMKGY-FE---DPEAT 395
Cdd:PRK08276 297 SEGGGV--------TVIT-SEDWLAHpgSVGKAVLG-EVRILD-EDGNELPPGEIGTVYFE----MDGYpFEyhnDPEKT 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 396 AAALDADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSeLVPDILEVAVIGIPEPRLVEVPVAYVVL 475
Cdd:PRK08276 362 AAARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLV-THPKVADVAVFGVPDEEMGERVKAVVQP 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1828927390 476 RPGAAATEE---SIIAACKGKIASFKVPKRVVVVAELPHTATGK 516
Cdd:PRK08276 441 ADGADAGDAlaaELIAWLRGRLAHYKCPRSIDFEDELPRTPTGK 484
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
16-516 |
2.82e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 207.82 E-value: 2.82e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 16 AAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETD 95
Cdd:PRK07798 12 VADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 96 LADVVRRGGCKVLIFSGRAGPIdfVAlvqrSLRSDLERgsLRTVLV-----GEGVMPGAISWsslEDAVYSPAEQRALCE 170
Cdd:PRK07798 92 LRYLLDDSDAVALVYEREFAPR--VA----EVLPRLPK--LRTLVVvedgsGNDLLPGAVDY---EDALAAGSPERDFGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 171 RraacKASDLaLIVFTSGTTGRPKGVMHDHSCVRSVRDRGRLW----------------KVQPGETMLNYLPMFHLYSLS 234
Cdd:PRK07798 161 R----SPDDL-YLLYTGGTTGMPKGVMWRQEDIFRVLLGGRDFatgepiedeeelakraAAGPGMRRFPAPPLMHGAGQW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 235 eAVLQCMYSGCRqVVMET---FDANTALDLIEQKSINIL----HGFETHYADLLRvqAERPRNVGSLrFGTLPSGLETSA 307
Cdd:PRK07798 236 -AAFAALFSGQT-VVLLPdvrFDADEVWRTIEREKVNVItivgDAMARPLLDALE--ARGPYDLSSL-FAIASGGALFSP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 308 AIAVQVQRVFcPTVT---GAGMSES-WCWMCTCAIDEPeelrchSSGRPL--PGMEMRLIDPEtGKDVPPGMPGE-MLFR 380
Cdd:PRK07798 311 SVKEALLELL-PNVVltdSIGSSETgFGGSGTVAKGAV------HTGGPRftIGPRTVVLDED-GNPVEPGSGEIgWIAR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 381 CYSVMKGYFEDPEATAAAL-DADG--WLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELsELVPDILEVAV 457
Cdd:PRK07798 383 RGHIPLGYYKDPEKTAETFpTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEAL-KAHPDVADALV 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1828927390 458 IGIPEPRLVEVPVAYVVLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGK 516
Cdd:PRK07798 462 VGVPDERWGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
9-531 |
3.27e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 207.59 E-value: 3.27e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 9 LGELPTRAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFN 88
Cdd:PRK07470 9 LAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 89 LRYRETDLADVVRRGGCKVLIFsgRAGPIDFVALVQRSlrsdleRGSLRTVLVGEGVMPGAiswsSLEDAVYSPAEQRAl 168
Cdd:PRK07470 89 FRQTPDEVAYLAEASGARAMIC--HADFPEHAAAVRAA------SPDLTHVVAIGGARAGL----DYEALVARHLGARV- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 169 ceRRAACKASDLALIVFTSGTTGRPKGVMHDHSCVRSVRDrGRLWKVQPGET----MLNYLPMFHLYSLsEAVLQcMYSG 244
Cdd:PRK07470 156 --ANAAVDHDDPCWFFFTSGTTGRPKAAVLTHGQMAFVIT-NHLADLMPGTTeqdaSLVVAPLSHGAGI-HQLCQ-VARG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 245 CRQVVM--ETFDANTALDLIEQKSINILHGFEThyadLLRVQAERP----RNVGSLRFgTLPSGLETSAAIAVQVQRVFC 318
Cdd:PRK07470 231 AATVLLpsERFDPAEVWALVERHRVTNLFTVPT----ILKMLVEHPavdrYDHSSLRY-VIYAGAPMYRADQKRALAKLG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 319 PT-VTGAGMSEswcwmCTCAI-----------DEPEeLRCHSSGRPLPGMEMRLIDPEtGKDVPPGMPGEMLFRCYSVMK 386
Cdd:PRK07470 306 KVlVQYFGLGE-----VTGNItvlppalhdaeDGPD-ARIGTCGFERTGMEVQIQDDE-GRELPPGETGEICVIGPAVFA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 387 GYFEDPEATAAALdADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLV 466
Cdd:PRK07470 379 GYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTH-PAVSEVAVLGVPDPVWG 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828927390 467 EVPVAYVVLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRKTALEAGL 531
Cdd:PRK07470 457 EVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREELEERGL 521
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
3-535 |
3.28e-60 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 209.81 E-value: 3.28e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 3 DKDLPL-LGELPTRAAAKWPEQKALEWATGA--------MSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEyveA 73
Cdd:PRK07529 20 ARDLPAsTYELLSRAAARHPDAPALSFLLDAdpldrpetWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPE---T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 74 IFALWRIGAA--AVPFNLRYRETDLADVVRRGGCKVLIfsgRAGP---IDFVALVQRSLRsdlERGSLRTVLV--GEGVM 146
Cdd:PRK07529 97 HFALWGGEAAgiANPINPLLEPEQIAELLRAAGAKVLV---TLGPfpgTDIWQKVAEVLA---ALPELRTVVEvdLARYL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 147 PGAISWSSLEDAVYSPA-------------EQRALCERRAacKASDLALIVFTSGTTGRPKGVMHDHSC-VRSVRDRGRL 212
Cdd:PRK07529 171 PGPKRLAVPLIRRKAHArildfdaelarqpGDRLFSGRPI--GPDDVAAYFHTGGTTGMPKLAQHTHGNeVANAWLGALL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 213 WKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGcRQVVMET---FDANTALD----LIEQKSINILHGFETHYADLLRVQA 285
Cdd:PRK07529 249 LGLGPGDTVFCGLPLFHVNALLVTGLAPLARG-AHVVLATpqgYRGPGVIAnfwkIVERYRINFLSGVPTVYAALLQVPV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 286 ERpRNVGSLRFGTlpSGletSAAIAVQVQRVF-----CPTVTGAGMSESwcwMCTCAIDEPE-ELRCHSSGRPLPGMEMR 359
Cdd:PRK07529 328 DG-HDISSLRYAL--CG---AAPLPVEVFRRFeaatgVRIVEGYGLTEA---TCVSSVNPPDgERRIGSVGLRLPYQRVR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 360 LI--DPETG--KDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDaDGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGEN 435
Cdd:PRK07529 399 VVilDDAGRylRDCAVDEVGVLCIAGPNVFSGYLEAAHNKGLWLE-DGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHN 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 436 VSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEESIIAACKGKIAS-FKVPKRVVVVAELPHTAT 514
Cdd:PRK07529 478 IDPAAIEEALLRH-PAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAELLAFARDHIAErAAVPKHVRILDALPKTAV 556
|
570 580
....*....|....*....|.
gi 1828927390 515 GKVQRAVIRKTALEAGLQLKL 535
Cdd:PRK07529 557 GKIFKPALRRDAIRRVLRAAL 577
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
31-524 |
1.59e-59 |
|
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: 205.07 E-value: 1.59e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 31 GAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLIF 110
Cdd:TIGR02262 29 SSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 111 SGRAGPIdFVALVQRSlrsdlerGSLRTVLVGEGVMPGAISWSSLedaVYSPAEQralcERRAACKASDLALIVFTSGTT 190
Cdd:TIGR02262 109 SGALLPV-IKAALGKS-------PHLEHRVVVGRPEAGEVQLAEL---LATESEQ----FKPAATQADDPAFWLYSSGST 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 191 GRPKGVMHDHSCVRSVRDR--GRLWKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQVVM-ETFDANTALDLIEQKSI 267
Cdd:TIGR02262 174 GMPKGVVHTHSNPYWTAELyaRNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMgERPTPDAVFDRLRRHQP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 268 NILHGFETHYADLLRVQAERPRNVGSLRFGTlPSGLETSAAIAVQVQRVF-CPTVTGAGMSESWCWMCTcaiDEPEELRC 346
Cdd:TIGR02262 254 TIFYGVPTLYAAMLADPNLPSEDQVRLRLCT-SAGEALPAEVGQRWQARFgVDIVDGIGSTEMLHIFLS---NLPGDVRY 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 347 HSSGRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDAdGWLHSGDQGVVRPDGSIRFTGRYK 426
Cdd:TIGR02262 330 GTSGKPVPGYRLRLVG-DGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTFQG-EWTRSGDKYVRNDDGSYTYAGRTD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 427 EMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEESIIAACKGKIASFKVPKRVVVV 506
Cdd:TIGR02262 408 DMLKVSGIYVSPFEIESALIQH-PAVLEAAVVGVADEDGLIKPKAFVVLRPGQTALETELKEHVKDRLAPYKYPRWIVFV 486
|
490
....*....|....*...
gi 1828927390 507 AELPHTATGKVQRAVIRK 524
Cdd:TIGR02262 487 DDLPKTATGKIQRFKLRE 504
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
16-523 |
2.33e-59 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 205.38 E-value: 2.33e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 16 AAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETD 95
Cdd:PRK13382 52 AAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 96 LADVVRRGGCKVLIFSGragpiDFVALVQRSLRSdlergslrtvlvgegvMPGA---ISWSSLEDAVYSPAEQRALCERR 172
Cdd:PRK13382 132 LAEVVTREGVDTVIYDE-----EFSATVDRALAD----------------CPQAtriVAWTDEDHDLTVEVLIAAHAGQR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 173 AACKASDLALIVFTSGTTGRPKGVMH----DHSCVRSVRDRGRlWKVQpgETMLNYLPMFHLYSLSEAVLQCMYSgCRQV 248
Cdd:PRK13382 191 PEPTGRKGRVILLTSGTTGTPKGARRsgpgGIGTLKAILDRTP-WRAE--EPTVIVAPMFHAWGFSQLVLAASLA-CTIV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 249 VMETFDANTALDLIEQKSINILHGFETHYADLLRVQAE--RPRNVGSLRFGTlPSGLETSAAIAVQVQRVFCPTV----- 321
Cdd:PRK13382 267 TRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEvrNRYSGRSLRFAA-ASGSRMRPDVVIAFMDQFGDVIynnyn 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 322 -TGAGMSeswcwmctcAIDEPEELRCH--SSGRPLPGMEMRLIDPEtGKDVPPGMPGEMLFRCYSVMKGYfedpeATAAA 398
Cdd:PRK13382 346 aTEAGMI---------ATATPADLRAApdTAGRPAEGTEIRILDQD-FREVPTGEVGTIFVRNDTQFDGY-----TSGST 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 399 LD-ADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRP 477
Cdd:PRK13382 411 KDfHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATH-PDVAEAAVIGVDDEQYGQRLAAFVVLKP 489
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1828927390 478 GAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIR 523
Cdd:PRK13382 490 GASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
21-520 |
4.87e-59 |
|
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: 202.37 E-value: 4.87e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 21 PEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVV 100
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 101 RRGGCKVLIfsgragpidfvalvqrslrsdlergslrtvlvgegvmpgaiswssledavyspaeqralcerraaCKASDL 180
Cdd:cd05930 81 EDSGAKLVL-----------------------------------------------------------------TDPDDL 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 181 ALIVFTSGTTGRPKGVMHDHSCVRS-VRDRGRLWKVQPGETMLnylpmfHLYSLS-----EAVLQCMYSGCRQVVM---E 251
Cdd:cd05930 96 AYVIYTSGSTGKPKGVMVEHRGLVNlLLWMQEAYPLTPGDRVL------QFTSFSfdvsvWEIFGALLAGATLVVLpeeV 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 252 TFDANTALDLIEQKSINILHGFETHYADLLrvQAERPRNVGSLRfgTLPSGLEtsaAIAVQVQRVFCPTVTGA------G 325
Cdd:cd05930 170 RKDPEALADLLAEEGITVLHLTPSLLRLLL--QELELAALPSLR--LVLVGGE---ALPPDLVRRWRELLPGArlvnlyG 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 326 MSESWCWMCTCAIDEPEELRCHSS-GRPLPGMEMRLIDPEtGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDADGW 404
Cdd:cd05930 243 PTEATVDATYYRVPPDDEEDGRVPiGRPIPNTRVYVLDEN-LRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPF 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 405 LH------SGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPG 478
Cdd:cd05930 322 GPgermyrTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAH-PGVREAAVVAREDGDGEKRLVAYVVPDEG 400
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1828927390 479 AAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRA 520
Cdd:cd05930 401 GELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRK 442
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
33-523 |
5.53e-59 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 201.94 E-value: 5.53e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 33 MSYAELDARIDRVACGLMRNGVNA-GDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGgckvlifs 111
Cdd:cd05958 11 WTYRDLLALANRIANVLVGELGIVpGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKA-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 112 gragpidfvalvqrslrsdlergslrtvlvgegvmpgaiswssledavyspAEQRALCERRAAcKASDLALIVFTSGTTG 191
Cdd:cd05958 83 ---------------------------------------------------RITVALCAHALT-ASDDICILAFTSGTTG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 192 RPKGVMHDHscvRSVRDRGRLWKVQ-----PGETMLNYLPMFHLYSLSEAVLQCMYSGCRQVVMETFDANTALDLIEQKS 266
Cdd:cd05958 111 APKATMHFH---RDPLASADRYAVNvlrlrEDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYK 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 267 INILHGFETHYADLLRVQAERPRNVGSLRFgTLPSGLETSAAIAVQVQRVF-CPTVTGAGMSESWCWMCTCAidePEELR 345
Cdd:cd05958 188 PTVLFTAPTAYRAMLAHPDAAGPDLSSLRK-CVSAGEALPAALHRAWKEATgIPIIDGIGSTEMFHIFISAR---PGDAR 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 346 CHSSGRPLPGMEMRLIDPEtGKDVPPGMPGEMLFRCYSvmkGYFEDPEATAAALDADGWLHSGDQGVVRPDGSIRFTGRY 425
Cdd:cd05958 264 PGATGKPVPGYEAKVVDDE-GNPVPDGTIGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRS 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 426 KEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATE---ESIIAACKGKIASFKVPKR 502
Cdd:cd05958 340 DDMIVSGGYNIAPPEVEDVLLQH-PAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPvlaRELQDHAKAHIAPYKYPRA 418
|
490 500
....*....|....*....|.
gi 1828927390 503 VVVVAELPHTATGKVQRAVIR 523
Cdd:cd05958 419 IEFVTELPRTATGKLQRFALR 439
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
7-519 |
3.99e-58 |
|
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: 201.20 E-value: 3.99e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 7 PLLGELPTRAAAKWPEQKALEWATGA--MSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAA 84
Cdd:cd05923 1 QTVFEMLRRAASRAPDACAIADPARGlrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 85 VPFNLRYRETDLADVVRRGGCKVLIFSGRAGPIDfvALVQRSLRsdlergslrtvLVGEGVMPGAISWSSLEDAVYSPAe 164
Cdd:cd05923 81 ALINPRLKAAELAELIERGEMTAAVIAVDAQVMD--AIFQSGVR-----------VLALSDLVGLGEPESAGPLIEDPP- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 165 qralcerraaCKASDLALIVFTSGTTGRPKGVMHDHscvRSVRDRGRLWKVQPG------ETMLNYLPMFHLYSLSEAVL 238
Cdd:cd05923 147 ----------REPEQPAFVFYTSGTTGLPKGAVIPQ---RAAESRVLFMSTQAGlrhgrhNVVLGLMPLYHVIGFFAVLV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 239 QCMYSGCRQVVMETFDANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRFGTLPSGLETSAAIAVQVQRVFC 318
Cdd:cd05923 214 AALALDGTYVVVEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 319 PTVTGAGMSESWcwmcTCAIDEpeELRCHSSGRPLPGMEMRLIDPETGKD--VPPGMPGEMLFRCYS--VMKGYFEDPEA 394
Cdd:cd05923 294 EKVNIYGTTEAM----NSLYMR--DARTGTEMRPGFFSEVRIVRIGGSPDeaLANGEEGELIVAAAAdaAFTGYLNQPEA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 395 TAAALdADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSeLVPDILEVAVIGIPEPRLVEVPVAYVV 474
Cdd:cd05923 368 TAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLS-RHPGVTEVVVIGVADERWGQSVTACVV 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1828927390 475 LRPGaAATEESIIAACK-GKIASFKVPKRVVVVAELPHTATGKVQR 519
Cdd:cd05923 446 PREG-TLSADELDQFCRaSELADFKRPRRYFFLDELPKNAMNKVLR 490
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
33-481 |
2.25e-57 |
|
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: 197.82 E-value: 2.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 33 MSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLIFSg 112
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 113 ragpidfvalvqrslrsdlergslrtvlvgegvmpgaiswssledavyspaeqralcerraacKASDLALIVFTSGTTGR 192
Cdd:cd05907 85 ---------------------------------------------------------------DPDDLATIIYTSGTTGR 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 193 PKGVMHDHSCVRS-VRDRGRLWKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQVVmeTFDANTALDLIEQKSINILH 271
Cdd:cd05907 102 PKGVMLSHRNILSnALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYF--ASSAETLLDDLSEVRPTVFL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 272 G----FETHYADLLRVQAERPRNV-------GSLRFgtLPSGletSAAIAVQVQRVF----CPTVTGAGMSEswcwmCT- 335
Cdd:cd05907 180 AvprvWEKVYAAIKVKAVPGLKRKlfdlavgGRLRF--AASG---GAPLPAELLHFFralgIPVYEGYGLTE-----TSa 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 336 -CAIDEPEELRCHSSGRPLPGMEMRlIDPEtgkdvppgmpGEMLFRCYSVMKGYFEDPEATAAALDADGWLHSGDQGVVR 414
Cdd:cd05907 250 vVTLNPPGDNRIGTVGKPLPGVEVR-IADD----------GEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEID 318
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1828927390 415 PDGSIRFTGRYKEMLKV-GGENVSPQGVEQELSElVPDILEVAVIGIPEPRLvevpVAYVVLRPGAAA 481
Cdd:cd05907 319 EDGFLHITGRKKDLIITsGGKNISPEPIENALKA-SPLISQAVVIGDGRPFL----VALIVPDPEALE 381
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
13-523 |
8.26e-57 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 197.99 E-value: 8.26e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 13 PTRAAAKWPEQKALEWA-TG-AMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLR 90
Cdd:PRK13391 3 PGIHAQTTPDKPAVIMAsTGeVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 91 YRETDLADVVRRGGCKVLIFSGRAgpidfvALVQRSLRSDLERGSLRTVLVGEGVMPGaisWSSLEDAVYSPAEQRALCE 170
Cdd:PRK13391 83 LTPAEAAYIVDDSGARALITSAAK------LDVARALLKQCPGVRHRLVLDGDGELEG---FVGYAEAVAGLPATPIADE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 171 RRAAckasdlaLIVFTSGTTGRPKGVMHDHSCVRSVRDRG------RLWKVQPGETMLNYLPMFHLYSLSeAVLQCMYSG 244
Cdd:PRK13391 154 SLGT-------DMLYSSGTTGRPKGIKRPLPEQPPDTPLPltaflqRLWGFRSDMVYLSPAPLYHSAPQR-AVMLVIRLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 245 CRQVVMETFDANTALDLIEQKSINILHGFETHYADLLRVQAE-RPR-NVGSLRfgtlpSGLETSAAIAVQVQRvfcptvt 322
Cdd:PRK13391 226 GTVIVMEHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEvRDKyDLSSLE-----VAIHAAAPCPPQVKE------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 323 gaGMSESW------CWMCT-----CAIDEPEEL-RCHSSGRPLPGmEMRLIDpETGKDVPPGMPGEMLFRCYSVMKgYFE 390
Cdd:PRK13391 294 --QMIDWWgpiiheYYAATeglgfTACDSEEWLaHPGTVGRAMFG-DLHILD-DDGAELPPGEPGTIWFEGGRPFE-YLN 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 391 DPEATAAALDADG-WLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSeLVPDILEVAVIGIPEPRLVEVP 469
Cdd:PRK13391 369 DPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLI-THPKVADAAVFGVPNEDLGEEV 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1828927390 470 VAYVVLRPGAAATE---ESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIR 523
Cdd:PRK13391 448 KAVVQPVDGVDPGPalaAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
15-524 |
1.54e-55 |
|
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: 195.54 E-value: 1.54e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 15 RAAAKwPEQKALEWATG------AMSYAELDARIDRVACGLMRNGvNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFN 88
Cdd:cd05931 2 RAAAR-PDRPAYTFLDDeggreeTLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 89 L--RYRETD-LADVVRRGGCKVLIFSGragpiDFVALVQRSLRSDLERGslrtvlvgegvMPGAISWSSLEDAVYSPAeq 165
Cdd:cd05931 80 PptPGRHAErLAAILADAGPRVVLTTA-----AALAAVRAFAASRPAAG-----------TPRLLVVDLLPDTSAADW-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 166 ralceRRAACKASDLALIVFTSGTTGRPKGVMHDHSCVRS-VRDRGRLWKVQPGETMLNYLPMFHLYSLSEAVLQCMYSG 244
Cdd:cd05931 142 -----PPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLAnVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 245 CRQVVMETFD----------------------ANTALDLI------EQKS-------INILHGFETHYADLLRVQAERpr 289
Cdd:cd05931 217 GPSVLMSPAAflrrplrwlrlisryratisaaPNFAYDLCvrrvrdEDLEgldlsswRVALNGAEPVRPATLRRFAEA-- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 290 nvgslrFGtlPSGLETSAaiavqvqrvFCPtvtGAGMSES-------WCWMCTCAI-DEPEELRCH-------------- 347
Cdd:cd05931 295 ------FA--PFGFRPEA---------FRP---SYGLAEAtlfvsggPPGTGPVVLrVDRDALAGRavavaaddpaarel 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 348 -SSGRPLPGMEMRLIDPETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATA------AALDADGWLHSGDQGVVRpDGSIR 420
Cdd:cd05931 355 vSCGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAetfgalAATDEGGWLRTGDLGFLH-DGELY 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 421 FTGRYKEMLKVGGENVSPQGVEQELSELVPDILE--VAVIGIPEPRLVEVPVAYVVLRPGAAATEESIIAACKGKIAS-F 497
Cdd:cd05931 434 ITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRPgcVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAReH 513
|
570 580 590
....*....|....*....|....*....|
gi 1828927390 498 KVPKRVVVVAE---LPHTATGKVQRAVIRK 524
Cdd:cd05931 514 GVAPADVVLVRpgsIPRTSSGKIQRRACRA 543
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
6-519 |
2.82e-55 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 194.33 E-value: 2.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 6 LPLLGELPTRAAAKWPEQKALEWATG--AMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAA 83
Cdd:PRK05852 15 GPRIADLVEVAATRLPEAPALVVTADriAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 84 AVPFNLRYRETDLADVVRRGGCKVLifsgragpidfvaLVQRSLRSDLERGSLR----TVLVGEGVMPGAISWSSLEDAV 159
Cdd:PRK05852 95 VVPLDPALPIAEQRVRSQAAGARVV-------------LIDADGPHDRAEPTTRwwplTVNVGGDSGPSGGTLSVHLDAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 160 YSPAEQRALCERRAAckasDLALIVFTSGTTGRPKGV-MHDHSCVRSVRDRGRLWKVQPGETMLNYLPMFHLYSLSEAVL 238
Cdd:PRK05852 162 TEPTPATSTPEGLRP----DDAMIMFTGGTTGLPKMVpWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 239 QCMYSGcRQVVMET---FDANTALDLIEQKSINILHGFET-HYADLLRVQAER-PRNVGSLRF-GTLPSGLETSAAIAVQ 312
Cdd:PRK05852 238 ATLASG-GAVLLPArgrFSAHTFWDDIKAVGATWYTAVPTiHQILLERAATEPsGRKPAALRFiRSCSAPLTAETAQALQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 313 vQRVFCPTVTGAGMSESWCWMCTCAID-----EPEELRCHSSGRPlPGMEMRLIDPEtGKDVPPGMPGEMLFRCYSVMKG 387
Cdd:PRK05852 317 -TEFAAPVVCAFGMTEATHQVTTTQIEgigqtENPVVSTGLVGRS-TGAQIRIVGSD-GLPLPAGAVGEVWLRGTTVVRG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 388 YFEDPEATAAALdADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVE 467
Cdd:PRK05852 394 YLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASH-PNVMEAAVFGVPDQLYGE 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1828927390 468 VPVAYVVLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQR 519
Cdd:PRK05852 472 AVAAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDR 523
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
34-520 |
1.26e-54 |
|
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: 190.35 E-value: 1.26e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 34 SYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLIFSGR 113
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 114 AGPIDFVAL-VQRSLRSDLERGSLRTVLVGEgvmpgaiswssledavyspaeqralcerraackasDLALIVFTSGTTGR 192
Cdd:TIGR01923 81 LEEKDFQADsLDRIEAAGRYETSLSASFNMD-----------------------------------QIATLMFTSGTTGK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 193 PKGV-----MHDHSCVRSVRDRGrlwkVQPGETMLNYLPMFHLYSLSeAVLQCMYSGCRQVVMETFdaNTALDLIEQKSI 267
Cdd:TIGR01923 126 PKAVphtfrNHYASAVGSKENLG----FTEDDNWLLSLPLYHISGLS-ILFRWLIEGATLRIVDKF--NQLLEMIANERV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 268 NILHGFETHYADLLRvQAERPRNVGSLRFGtlpsGLETSAAIAVQVQRVFCPTVTGAGMSESWCWMCTCAID-EPEELrc 346
Cdd:TIGR01923 199 THISLVPTQLNRLLD-EGGHNENLRKILLG----GSAIPAPLIEEAQQYGLPIYLSYGMTETCSQVTTATPEmLHARP-- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 347 hSSGRPLPGMEMRLIDPETGKdvppgmPGEMLFRCYSVMKGYFEDPEATAAaLDADGWLHSGDQGVVRPDGSIRFTGRYK 426
Cdd:TIGR01923 272 -DVGRPLAGREIKIKVDNKEG------HGEIMVKGANLMKGYLYQGELTPA-FEQQGWFNTGDIGELDGEGFLYVLGRRD 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 427 EMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEesIIAACKGKIASFKVPKRVVVV 506
Cdd:TIGR01923 344 DLIISGGENIYPEEIETVLYQH-PGIQEAVVVPKPDAEWGQVPVAYIVSESDISQAK--LIAYLTEKLAKYKVPIAFEKL 420
|
490
....*....|....
gi 1828927390 507 AELPHTATGKVQRA 520
Cdd:TIGR01923 421 DELPYNASGKILRN 434
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
34-524 |
7.53e-54 |
|
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: 190.43 E-value: 7.53e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 34 SYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVlIFSGR 113
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTI-VFCSK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 114 AGpIDFVALVQRSLRSdlergsLRTVLVGEGV--MPGAISWSSLEDAVYSPAEQRALCERRAACKASDLALIVFTSGTTG 191
Cdd:cd17642 125 KG-LQKVLNVQKKLKI------IKTIIILDSKedYKGYQCLYTFITQNLPPGFNEYDFKPPSFDRDEQVALIMNSSGSTG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 192 RPKGVM--HDHSCVR--SVRDRGRLWKVQPGETMLNYLPMFHLYSLSeAVLQCMYSGCRQVVMETFDANTALDLIEQKSI 267
Cdd:cd17642 198 LPKGVQltHKNIVARfsHARDPIFGNQIIPDTAILTVIPFHHGFGMF-TTLGYLICGFRVVLMYKFEEELFLRSLQDYKV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 268 NILHGFETHYADLLR---VQAERPRNVGSLRFGTLPSGLETSAAIAvqvQRVFCPTV-TGAGMSESwcwmcTCAI-DEPE 342
Cdd:cd17642 277 QSALLVPTLFAFFAKstlVDKYDLSNLHEIASGGAPLSKEVGEAVA---KRFKLPGIrQGYGLTET-----TSAIlITPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 343 E-LRCHSSGRPLPGMEMRLIDPETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDADGWLHSGDQGVVRPDGSIRF 421
Cdd:cd17642 349 GdDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFI 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 422 TGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEESIIAACKGKIASFK-VP 500
Cdd:cd17642 429 VDRLKSLIKYKGYQVPPAELESILLQH-PKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYVASQVSTAKrLR 507
|
490 500
....*....|....*....|....
gi 1828927390 501 KRVVVVAELPHTATGKVQRAVIRK 524
Cdd:cd17642 508 GGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
182-517 |
9.08e-54 |
|
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: 184.81 E-value: 9.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 182 LIVFTSGTTGRPKGVMHDHSCVRSVR-DRGRLWKVQPGETMLNYLPMFHLYSL--SEAVLQCmysGCRQVVMETFDANTA 258
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALLAQAlVLAVLQAIDEGTVFLNSGPLFHIGTLmfTLATFHA---GGTNVFVRRVDAEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 259 LDLIEQKSINilHGFETH--YADLLRVQAERPRNVGSLRFGtlPSGLETSAAIAVQVQRvFCPTVTGAGMSE-----SWC 331
Cdd:cd17636 81 LELIEAERCT--HAFLLPptIDQIVELNADGLYDLSSLRSS--PAAPEWNDMATVDTSP-WGRKPGGYGQTEvmglaTFA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 332 WMCTCAIDepeelrchSSGRPLPGMEMRLIDPEtGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALdADGWLHSGDQG 411
Cdd:cd17636 156 ALGGGAIG--------GAGRPSPLVQVRILDED-GREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT-RGGWHHTNDLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 412 VVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEESIIAACK 491
Cdd:cd17636 226 RREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQH-PAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCR 304
|
330 340
....*....|....*....|....*.
gi 1828927390 492 GKIASFKVPKRVVVVAELPHTATGKV 517
Cdd:cd17636 305 ARIASYKKPKSVEFADALPRTAGGAD 330
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
33-527 |
1.00e-52 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 188.05 E-value: 1.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 33 MSYAELDARIDRVACGLMRN-GVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLIFS 111
Cdd:PRK05677 50 LTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 112 GragpiDFVALVQRSL-RSDLER----------GSLRTVLVGEGV-----------MPGAISwssLEDAVYSPAEQRAlc 169
Cdd:PRK05677 130 A-----NMAHLAEKVLpKTGVKHvivtevadmlPPLKRLLINAVVkhvkkmvpayhLPQAVK---FNDALAKGAGQPV-- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 170 eRRAACKASDLALIVFTSGTTGRPKGVMHDH-SCVRSVRDRGRLWKVQPG---ETMLNYLPMFHLYSLSeavLQCMysgc 245
Cdd:PRK05677 200 -TEANPQADDVAVLQYTGGTTGVAKGAMLTHrNLVANMLQCRALMGSNLNegcEILIAPLPLYHIYAFT---FHCM---- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 246 rqVVMETFDANTAL-----------DLIEQKSINILhGFETHYADLLRVQAERPRNVGSLRFgTLPSGLETSAAIAVQVQ 314
Cdd:PRK05677 272 --AMMLIGNHNILIsnprdlpamvkELGKWKFSGFV-GLNTLFVALCNNEAFRKLDFSALKL-TLSGGMALQLATAERWK 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 315 RVF-CPTVTGAGMSESWCWMCtcaIDEPEELRCHSSGRPLPGMEMRLIDPEtGKDVPPGMPGEMLFRCYSVMKGYFEDPE 393
Cdd:PRK05677 348 EVTgCAICEGYGMTETSPVVS---VNPSQAIQVGTIGIPVPSTLCKVIDDD-GNELPLGEVGELCVKGPQVMKGYWQRPE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 394 ATAAALDADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYV 473
Cdd:PRK05677 424 ATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAAL-PGVLQCAAIGVPDEKSGEAIKVFV 502
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1828927390 474 VLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRKTAL 527
Cdd:PRK05677 503 VVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEEL 556
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
26-519 |
2.27e-51 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 184.27 E-value: 2.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 26 LEWATG-AMSYAELDARIDRVACGLMRN-GVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRrg 103
Cdd:PLN02574 59 IDSSTGfSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVV-- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 104 GCKVlifsgragpidfvALVQRSLRSDLERGSLR--TVLVGEGVM--PGAISWSSLEDAVYSPAEqralCERRAACKASD 179
Cdd:PLN02574 137 DCSV-------------GLAFTSPENVEKLSPLGvpVIGVPENYDfdSKRIEFPKFYELIKEDFD----FVPKPVIKQDD 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 180 LALIVFTSGTTGRPKGVMHDHSCVRS-----VRDRGRLWKVQPGETM-LNYLPMFHLYSLSEAVLQCMYSGCRQVVMETF 253
Cdd:PLN02574 200 VAAIMYSSGTTGASKGVVLTHRNLIAmvelfVRFEASQYEYPGSDNVyLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRF 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 254 DANTALDLIEQKSInilhgfeTHYA---DLLRVQAERPRNVGSLRFGTLPSGLETSAAIAVQVQRVFCPT------VTGA 324
Cdd:PLN02574 280 DASDMVKVIDRFKV-------THFPvvpPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTlphvdfIQGY 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 325 GMSESWCwMCTCAIDEPEELRCHSSGRPLPGMEMRLIDPETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDADGW 404
Cdd:PLN02574 353 GMTESTA-VGTRGFNTEKLSKYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 405 LHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEE 484
Cdd:PLN02574 432 LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISH-PEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQE 510
|
490 500 510
....*....|....*....|....*....|....*
gi 1828927390 485 SIIAACKGKIASFKVPKRVVVVAELPHTATGKVQR 519
Cdd:PLN02574 511 AVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILR 545
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
15-520 |
2.70e-51 |
|
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: 182.40 E-value: 2.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 15 RAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRET 94
Cdd:cd12117 5 EQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 95 DLADVVRRGGCKVLifsgragpidfvaLVQRSLrsdlergslrTVLVGEGVMPGAISWSSledavySPAEQRALcerRAA 174
Cdd:cd12117 85 RLAFMLADAGAKVL-------------LTDRSL----------AGRAGGLEVAVVIDEAL------DAGPAGNP---AVP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 175 CKASDLALIVFTSGTTGRPKGVMHDH-SCVRSVRDRGRLwKVQPGETMLNYLPmfhlYSLSEAVLQ---CMYSGCRQVVM 250
Cdd:cd12117 133 VSPDDLAYVMYTSGSTGRPKGVAVTHrGVVRLVKNTNYV-TLGPDDRVLQTSP----LAFDASTFEiwgALLNGARLVLA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 251 ET---FDANTALDLIEQKSINILH---GFETHYADllrvqaERPRNVGSLRfgTLPSGLEtsAAIAVQVQRVF--CPTVT 322
Cdd:cd12117 208 PKgtlLDPDALGALIAEEGVTVLWltaALFNQLAD------EDPECFAGLR--ELLTGGE--VVSPPHVRRVLaaCPGLR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 323 ---GAGMSESWCWMCTCAIDEPEELRCHSS-GRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAA 398
Cdd:cd12117 278 lvnGYGPTENTTFTTSHVVTELDEVAGSIPiGRPIANTRVYVLD-EDGRPVPPGVPGELYVGGDGLALGYLNRPALTAER 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 399 LDADGWL------HSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIP----EPRLvev 468
Cdd:cd12117 357 FVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAH-PGVREAVVVVREdaggDKRL--- 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1828927390 469 pVAYVVLRPGAAATEesIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRA 520
Cdd:cd12117 433 -VAYVVAEGALDAAE--LRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRR 481
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
14-520 |
3.85e-51 |
|
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: 182.16 E-value: 3.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 14 TRAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRE 93
Cdd:cd17651 2 ERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 94 TDLADVVRrggckvlifsgRAGPidFVALVQRSLRSDLergslrtvlvgegvmPGAISWSSLEDAVYSPAEQRAlcERRA 173
Cdd:cd17651 82 ERLAFMLA-----------DAGP--VLVLTHPALAGEL---------------AVELVAVTLLDQPGAAAGADA--EPDP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 174 ACKASDLALIVFTSGTTGRPKGVMHDHSCVRS-VRDRGRLWKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQVVMET 252
Cdd:cd17651 132 ALDADDLAYVIYTSGSTGRPKGVVMPHRSLANlVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 253 --FDANTALDLIEQKSINILHgFETHYADLLrVQAERPRNVGSLRFGTLPSGLEtsAAIAVQVQRVFCPTVTGA------ 324
Cdd:cd17651 212 vrTDPPALAAWLDEQRISRVF-LPTVALRAL-AEHGRPLGVRLAALRYLLTGGE--QLVLTEDLREFCAGLPGLrlhnhy 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 325 GMSESW---CWMCTCAIDEPEELRchSSGRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDA 401
Cdd:cd17651 288 GPTETHvvtALSLPGDPAAWPAPP--PIGRPIDNTRVYVLD-AALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVP 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 402 DGWL------HSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSElVPDILEVAVIGIPEPRLVEVPVAYVVL 475
Cdd:cd17651 365 DPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALAR-HPGVREAVVLAREDRPGEKRLVAYVVG 443
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1828927390 476 RPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRA 520
Cdd:cd17651 444 DPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRR 488
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
7-523 |
1.21e-50 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 182.14 E-value: 1.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 7 PLLGELPTRAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVP 86
Cdd:PRK07059 23 PSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 87 FNLRYRETDLADVVRRGGCKVLIFSGragpiDFVALVQRSLRsdleRGSLRTVLVG--------EGVM------------ 146
Cdd:PRK07059 103 VNPLYTPRELEHQLKDSGAEAIVVLE-----NFATTVQQVLA----KTAVKHVVVAsmgdllgfKGHIvnfvvrrvkkmv 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 147 -----PGAISWSsleDAVyspAEQRALCERRAACKASDLALIVFTSGTTGRPKGVMHDHSCVRSVRDRGRLW-----KVQ 216
Cdd:PRK07059 174 pawslPGHVRFN---DAL---AEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWlqpafEKK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 217 PGETMLNY---LPMFHLYSLSEAVLQCMYSGCRQVVMET-FDANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVG 292
Cdd:PRK07059 248 PRPDQLNFvcaLPLYHIFALTVCGLLGMRTGGRNILIPNpRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 293 SLRFgTLPSGLETSAAIAVQ-VQRVFCPTVTGAGMSESWCWMCTCAIDEPEelRCHSSGRPLPGMEMRLIDpETGKDVPP 371
Cdd:PRK07059 328 KLIV-ANGGGMAVQRPVAERwLEMTGCPITEGYGLSETSPVATCNPVDATE--FSGTIGLPLPSTEVSIRD-DDGNDLPL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 372 GMPGEMLFRCYSVMKGYFEDPEATAAALDADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEqELSELVPD 451
Cdd:PRK07059 404 GEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIE-EVVASHPG 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828927390 452 ILEVAVIGIPEPRLVEVPVAYVVlRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIR 523
Cdd:PRK07059 483 VLEVAAVGVPDEHSGEAVKLFVV-KKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
42-529 |
5.93e-50 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 180.38 E-value: 5.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 42 IDRV---ACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLIFSGRAgpid 118
Cdd:PLN02860 39 VDGVlslAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETC---- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 119 fvalvqRSLRSDLERGSLRT----VLVGEGVMPGAISWSSLEDAvySPAEQRALCERRA--ACKASDLALIVFTSGTTGR 192
Cdd:PLN02860 115 ------SSWYEELQNDRLPSlmwqVFLESPSSSVFIFLNSFLTT--EMLKQRALGTTELdyAWAPDDAVLICFTSGTTGR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 193 PKGVMHDHSCVrSVRDRGRLWKVQPGE--TMLNYLPMFHLYSLSEAVLQCMYSGCrQVVMETFDANTALDLIEQKSINIL 270
Cdd:PLN02860 187 PKGVTISHSAL-IVQSLAKIAIVGYGEddVYLHTAPLCHIGGLSSALAMLMVGAC-HVLLPKFDAKAALQAIKQHNVTSM 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 271 HGFETHYADLLRVQAERPRNVG--SLR-----FGTLPSGLETSAAIAVQVQRVFcptvTGAGMSESWCWMCTCAIDEP-- 341
Cdd:PLN02860 265 ITVPAMMADLISLTRKSMTWKVfpSVRkilngGGSLSSRLLPDAKKLFPNAKLF----SAYGMTEACSSLTFMTLHDPtl 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 342 --------EELRCHSS----------GRPLPGMEMRLIDPETGKDvppgmpGEMLFRCYSVMKGYFEDPEATAAALDADG 403
Cdd:PLN02860 341 espkqtlqTVNQTKSSsvhqpqgvcvGKPAPHVELKIGLDESSRV------GRILTRGPHVMLGYWGQNSETASVLSNDG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 404 WLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATE 483
Cdd:PLN02860 415 WLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQH-PGVASVVVVGVPDSRLTEMVVACVRLRDGWIWSD 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828927390 484 ESIIAACKGKIAS---------------FKVPKRVVVVAE-LPHTATGKVQRAVIRKTALEA 529
Cdd:PLN02860 494 NEKENAKKNLTLSsetlrhhcreknlsrFKIPKLFVQWRKpFPLTTTGKIRRDEVRREVLSH 555
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
32-523 |
2.16e-49 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 177.97 E-value: 2.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 32 AMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLIfs 111
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLI-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 112 graGPIDFVALVQRSLRSDLERGSLRT---VLVGEGVMP-------GAISWSS-LEDavYSPAEQRALCERRAackasdl 180
Cdd:PRK12406 89 ---AHADLLHGLASALPAGVTVLSVPTppeIAAAYRISPalltppaGAIDWEGwLAQ--QEPYDGPPVPQPQS------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 181 alIVFTSGTTGRPKGVMHD----HSCVRSVRDRGRLWKVQPGETMLNYLPMFH----LYSLSEAVLqcmysGCRQVVMET 252
Cdd:PRK12406 157 --MIYTSGTTGHPKGVRRAaptpEQAAAAEQMRALIYGLKPGIRALLTGPLYHsapnAYGLRAGRL-----GGVLVLQPR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 253 FDANTALDLIEQKSINILHGFETHYADLLRVQAERPR--NVGSLRFGTlpsglETSAAIAVQVQR--------VFCP--- 319
Cdd:PRK12406 230 FDPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAkyDVSSLRHVI-----HAAAPCPADVKRamiewwgpVIYEyyg 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 320 -----TVTGAGmSESWcwmctcaIDEPeelrcHSSGRPLPGMEMRLIDpETGKDVPPGMPGEMlfrcYSVMKG-----YF 389
Cdd:PRK12406 305 stesgAVTFAT-SEDA-------LSHP-----GTVGKAAPGAELRFVD-EDGRPLPQGEIGEI----YSRIAGnpdftYH 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 390 EDPEATAAaLDADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSElVPDILEVAVIGIPEPRLVEVP 469
Cdd:PRK12406 367 NKPEKRAE-IDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHA-VPGVHDCAVFGIPDAEFGEAL 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1828927390 470 VAYVVLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIR 523
Cdd:PRK12406 445 MAVVEPQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
34-530 |
4.78e-49 |
|
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: 177.47 E-value: 4.78e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 34 SYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPF-------NLRYRETDLADVVRR-GGC 105
Cdd:cd05906 41 SYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLtvpptydEPNARLRKLRHIWQLlGSP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 106 KVLIFSGRAGPIDFVALVQRSLRSDLergslrtvlvgegvmpgaISWSSLEDAvYSPAEQRAlcerraaCKASDLALIVF 185
Cdd:cd05906 121 VVLTDAELVAEFAGLETLSGLPGIRV------------------LSIEELLDT-AADHDLPQ-------SRPDDLALLML 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 186 TSGTTGRPKGVMHDH-----SCVRSVRDRGRlwkvQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQV--VMETFDANTA 258
Cdd:cd05906 175 TSGSTGFPKAVPLTHrnilaRSAGKIQHNGL----TPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVhvPTEEILADPL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 259 --LDLIEQKSINILHG---FETHYADLLRVQAERPRNVGSLRFgtLPSGLE-TSAAIAVQVQR----------VFCPtvt 322
Cdd:cd05906 251 rwLDLIDRYRVTITWApnfAFALLNDLLEEIEDGTWDLSSLRY--LVNAGEaVVAKTIRRLLRllepyglppdAIRP--- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 323 GAGMSESwCWMCTCAI-----DEPEELRCHSSGRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAA 397
Cdd:cd05906 326 AFGMTET-CSGVIYSRsfptyDHSQALEFVSLGRPIPGVSMRIVD-DEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 398 ALDADGWLHSGDQGVVRpDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvpDILEV---AVIGIPEPRLV--EVPVAY 472
Cdd:cd05906 404 AFTEDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEV--PGVEPsftAAFAVRDPGAEteELAIFF 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828927390 473 V---VLRPGAAATEESIiaackGKIASFKV---PKRVVVVA--ELPHTATGKVQRAVIRKtALEAG 530
Cdd:cd05906 481 VpeyDLQDALSETLRAI-----RSVVSREVgvsPAYLIPLPkeEIPKTSLGKIQRSKLKA-AFEAG 540
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
15-523 |
8.11e-49 |
|
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: 176.92 E-value: 8.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 15 RAAAKWPEQKALEWATGA-----MSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNL 89
Cdd:cd05970 25 AMAKEYPDKLALVWCDDAgeeriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 90 RYRETDLADVVRRGGCKVLIFSGRAGPIDFVALVQRSLRSDLERgslrtVLVGEGVMPGaisWSSLEDAVyspAEQRALC 169
Cdd:cd05970 105 QLTAKDIVYRIESADIKMIVAIAEDNIPEEIEKAAPECPSKPKL-----VWVGDPVPEG---WIDFRKLI---KNASPDF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 170 ERRAAC---KASDLALIVFTSGTTGRPKGVMHDHSCVRSVRDRGRLWK-VQPGEtmlnylpmFHLYSLSEAVLQCMY--- 242
Cdd:cd05970 174 ERPTANsypCGEDILLVYFSSGTTGMPKMVEHDFTYPLGHIVTAKYWQnVREGG--------LHLTVADTGWGKAVWgki 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 243 -----SGCRQVV--METFDANTALDLIEQKSINILHGFETHYADLLRVQAERpRNVGSLRFGTL------PSGLET-SAA 308
Cdd:cd05970 246 ygqwiAGAAVFVydYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSR-YDLSSLRYCTTagealnPEVFNTfKEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 309 IAVQVQRVFCPT---VTGAGMSeswcWMctcaidepeELRCHSSGRPLPGMEMRLIDPEtGKDVPPGMPGEMLFRC---- 381
Cdd:cd05970 325 TGIKLMEGFGQTettLTIATFP----WM---------EPKPGSMGKPAPGYEIDLIDRE-GRSCEAGEEGEIVIRTskgk 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 382 -YSVMKGYFEDPEATAAALDaDGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEqelSELV--PDILEVAVI 458
Cdd:cd05970 391 pVGLFGGYYKDAEKTAEVWH-DGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVE---SALIqhPAVLECAVT 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1828927390 459 GIPEPRLVEVPVAYVVLRPGAAATEE---SIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIR 523
Cdd:cd05970 467 GVPDPIRGQVVKATIVLAKGYEPSEElkkELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
34-465 |
3.10e-48 |
|
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: 173.70 E-value: 3.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 34 SYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLIfsgr 113
Cdd:cd17640 7 TYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 114 agpidfvalvqrslrsdLERGSlrtvlvgegvmpgaiswssledavyspaeqralcerraackaSDLALIVFTSGTTGRP 193
Cdd:cd17640 83 -----------------VENDS------------------------------------------DDLATIIYTSGTTGNP 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 194 KGVMHDH-SCVRSVRdrgRLWKV---QPGETMLNYLPMFHLY--SLSEAVLQCmysGCRQVVmetfdantaldlieqKSI 267
Cdd:cd17640 104 KGVMLTHaNLLHQIR---SLSDIvppQPGDRFLSILPIWHSYerSAEYFIFAC---GCSQAY---------------TSI 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 268 NILHgfethyADLLRVQ----AERPRNVGSLR-----------------FGTLPSGLETSAAI------AVQVQRVF--- 317
Cdd:cd17640 163 RTLK------DDLKRVKphyiVSVPRLWESLYsgiqkqvsksspikqflFLFFLSGGIFKFGIsgggalPPHVDTFFeai 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 318 -CPTVTGAGMSEswcwmcTCAIDEPEELRCH---SSGRPLPGMEMRLIDPETGKDVPPGMPGEMLFRCYSVMKGYFEDPE 393
Cdd:cd17640 237 gIEVLNGYGLTE------TSPVVSARRLKCNvrgSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPE 310
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828927390 394 ATAAALDADGWLHSGDQGVVRPDGSIRFTGRYKEMLKV-GGENVSPQGVEQELSElVPDILEVAVIGIPEPRL 465
Cdd:cd17640 311 ATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLsNGENVEPQPIEEALMR-SPFIEQIMVVGQDQKRL 382
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
26-528 |
4.58e-48 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 175.17 E-value: 4.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 26 LEWATG-AMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYveAIFALWRIGAAAV--PFNLRYRETDLADVVRR 102
Cdd:PLN02330 48 VEAVTGkAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEY--GIVALGIMAAGGVfsGANPTALESEIKKQAEA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 103 GGCKVLIfsgragpidfvalvqrslRSDLERGSLR-----TVLVGEGVMPGAISWSSLEDAVYSPAEQRALCErraaCKA 177
Cdd:PLN02330 126 AGAKLIV------------------TNDTNYGKVKglglpVIVLGEEKIEGAVNWKELLEAADRAGDTSDNEE----ILQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 178 SDLALIVFTSGTTGRPKGVMHDHscvRSVRDR--GRLWKVQP---GE-TMLNYLPMFHLYSLSEAVLQCMYSGCRQVVME 251
Cdd:PLN02330 184 TDLCALPFSSGTTGISKGVMLTH---RNLVANlcSSLFSVGPemiGQvVTLGLIPFFHIYGITGICCATLRNKGKVVVMS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 252 TFDANTALD-LIEQKS----------INILHGFETHYADLLRVQAERPRNVGSLRFGTLPSGLETSAAiAVQVQRVFcpt 320
Cdd:PLN02330 261 RFELRTFLNaLITQEVsfapivppiiLNLVKNPIVEEFDLSKLKLQAIMTAAAPLAPELLTAFEAKFP-GVQVQEAY--- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 321 vtgaGMSESWCwmCTCAIDEPEE----LRCHSSGRPLPGMEMRLIDPETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATA 396
Cdd:PLN02330 337 ----GLTEHSC--ITLTHGDPEKghgiAKKNSVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETD 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 397 AALDADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLR 476
Cdd:PLN02330 411 RTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTH-PSVEDAAVVPLPDEEAGEIPAACVVIN 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1828927390 477 PGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRKTALE 528
Cdd:PLN02330 490 PKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLS 541
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
34-457 |
7.00e-48 |
|
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: 171.29 E-value: 7.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 34 SYAELDARIDRVACGL-MRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLifsg 112
Cdd:TIGR01733 1 TYRELDERANRLARHLrAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 113 ragpidfvaLVQRSLRSDLERgslrtvLVGEGVMPGAISWSSLEDAVYSPAeqralceRRAACKASDLALIVFTSGTTGR 192
Cdd:TIGR01733 77 ---------LTDSALASRLAG------LVLPVILLDPLELAALDDAPAPPP-------PDAPSGPDDLAYVIYTSGSTGR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 193 PKGVMHDHSC-VRSVRDRGRLWKVQPGETMLNYLPMFHLYSLSEaVLQCMYSGCRQVV----METFDANTALDLIEQKSI 267
Cdd:TIGR01733 135 PKGVVVTHRSlVNLLAWLARRYGLDPDDRVLQFASLSFDASVEE-IFGALLAGATLVVppedEERDDAALLAALIAEHPV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 268 NILHGFETHYADLLRVQAERPRNVGSLRFGtlpsGLETSAAIAVQVQRVFCPT--VTGAGMSESWCWmCTCAIDEPEELR 345
Cdd:TIGR01733 214 TVLNLTPSLLALLAAALPPALASLRLVILG----GEALTPALVDRWRARGPGArlINLYGPTETTVW-STATLVDPDDAP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 346 CHSS---GRPLPGMEMRLIDPEtGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDADG--------WLHSGDQGVVR 414
Cdd:TIGR01733 289 RESPvpiGRPLANTRLYVLDDD-LRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPfaggdgarLYRTGDLVRYL 367
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1828927390 415 PDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAV 457
Cdd:TIGR01733 368 PDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRH-PGVREAVV 409
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
34-527 |
9.79e-48 |
|
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: 171.92 E-value: 9.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 34 SYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPfnlryretdladvvrrggckvlIFSgr 113
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICP----------------------LFS-- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 114 agpidfvALVQRSLRSDLERGSLRTVLVGEgvmpgaiswssledavyspaeqrALCERRaacKASDLALIVFTSGTTGRP 193
Cdd:cd05969 58 -------AFGPEAIRDRLENSEAKVLITTE-----------------------ELYERT---DPEDPTLLHYTSGTTGTP 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 194 KGVMHDHSCVRS----------VRDRGRLW-KVQPGetmlnylpmfHLYSLSEAVLQCMYSGCRQVVME-TFDANTALDL 261
Cdd:cd05969 105 KGVLHVHDAMIFyyftgkyvldLHPDDIYWcTADPG----------WVTGTVYGIWAPWLNGVTNVVYEgRFDAESWYGI 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 262 IEQKSINILHGFETHYADLLRVQAE--RPRNVGSLRFgtLPSGLE--TSAAIAVQVQRVFCPTVTGAGMSESWCWM---C 334
Cdd:cd05969 175 IERVKVTVWYTAPTAIRMLMKEGDElaRKYDLSSLRF--IHSVGEplNPEAIRWGMEVFGVPIHDTWWQTETGSIMianY 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 335 TCaidepEELRCHSSGRPLPGMEMRLIDpETGKDVPPGMPGEMLFR--CYSVMKGYFEDPEATAAALdADGWLHSGDQGV 412
Cdd:cd05969 253 PC-----MPIKPGSMGKPLPGVKAAVVD-ENGNELPPGTKGILALKpgWPSMFRGIWNDEERYKNSF-IDGWYLTGDLAY 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 413 VRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEE---SIIAA 489
Cdd:cd05969 326 RDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEH-PAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDElkeEIINF 404
|
490 500 510
....*....|....*....|....*....|....*...
gi 1828927390 490 CKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRKTAL 527
Cdd:cd05969 405 VRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKEL 442
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
15-526 |
3.34e-47 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 173.08 E-value: 3.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 15 RAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRN-GVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRE 93
Cdd:PRK12492 32 RSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 94 TDLADVVRRGGCKVLIFSGRAGpidfvALVQRSLrSDLERGSLRTVLVGEgVMPGAISW--SSLEDAVYS--PA------ 163
Cdd:PRK12492 112 REMRHQFKDSGARALVYLNMFG-----KLVQEVL-PDTGIEYLIEAKMGD-LLPAAKGWlvNTVVDKVKKmvPAyhlpqa 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 164 --------EQRALCERRAACKASDLALIVFTSGTTGRPKGVMHDH-----------SCVRSVRDRGR-LWKvQPGETMLN 223
Cdd:PRK12492 185 vpfkqalrQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHgnlvanmlqvrACLSQLGPDGQpLMK-EGQEVMIA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 224 YLPMFHLYSLSEAVLQCMYSGCRQVVMET-FDANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRfGTLPSG 302
Cdd:PRK12492 264 PLPLYHIYAFTANCMCMMVSGNHNVLITNpRDIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKDLDFSALK-LTNSGG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 303 LETSAAIAVQVQRVF-CPTVTGAGMSESWCWMCTcaidEP--EELRCHSSGRPLPGMEMRLIDPEtGKDVPPGMPGEMLF 379
Cdd:PRK12492 343 TALVKATAERWEQLTgCTIVEGYGLTETSPVAST----NPygELARLGTVGIPVPGTALKVIDDD-GNELPLGERGELCI 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 380 RCYSVMKGYFEDPEATAAALDADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPqgveQELSELV---PDILEVA 456
Cdd:PRK12492 418 KGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYP----NEIEDVVmahPKVANCA 493
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 457 VIGIPEPRLVEVPVAYVVLRPGAAATEEsIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRKTA 526
Cdd:PRK12492 494 AIGVPDERSGEAVKLFVVARDPGLSVEE-LKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDIA 562
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
53-523 |
4.15e-47 |
|
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: 171.02 E-value: 4.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 53 GVNAGDKVGLLVSNGPEYVEAIFALWRIGA--AAVPFNLRYRETDLADVVRRGGCKVLIFSG---RAGPIDFVAlvqrsl 127
Cdd:cd05929 38 GVWIADGVYIYLINSILTVFAAAAAWKCGAcpAYKSSRAPRAEACAIIEIKAAALVCGLFTGggaLDGLEDYEA------ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 128 rsdlERGSLRTVLVGEGVMPGAISWSSledavyspaeqralcerraackasdlalivftsGTTGRPKGVMHDHSCVRSVR 207
Cdd:cd05929 112 ----AEGGSPETPIEDEAAGWKMLYSG---------------------------------GTTGRPKGIKRGLPGGPPDN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 208 DRGRLWKV----QPGETMLNYLPMFHLYSLSeAVLQCMYSGCRQVVMETFDANTALDLIEQKSINILHGFETHYADLLRV 283
Cdd:cd05929 155 DTLMAAALgfgpGADSVYLSPAPLYHAAPFR-WSMTALFMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 284 qaerPRNV-GSLRFGTLPSGLETSAAIAVQVQRVFC----PTV-------TGAGMseswcwmctCAIDEPEELRcH--SS 349
Cdd:cd05929 234 ----PEAVrNAYDLSSLKRVIHAAAPCPPWVKEQWIdwggPIIweyyggtEGQGL---------TIINGEEWLT-HpgSV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 350 GRPLPGmEMRLIDpETGKDVPPGMPGEMLFRCySVMKGYFEDPEATAAALDADGWLHSGDQGVVRPDGSIRFTGRYKEML 429
Cdd:cd05929 300 GRAVLG-KVHILD-EDGNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 430 KVGGENVSPQGVEQELSeLVPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATE---ESIIAACKGKIASFKVPKRVVVV 506
Cdd:cd05929 377 ISGGVNIYPQEIENALI-AHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTalaEELIAFLRDRLSRYKCPRSIEFV 455
|
490
....*....|....*..
gi 1828927390 507 AELPHTATGKVQRAVIR 523
Cdd:cd05929 456 AELPRDDTGKLYRRLLR 472
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
34-523 |
6.29e-46 |
|
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: 166.84 E-value: 6.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 34 SYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFnlryretdladvvrrggckvlifsgr 113
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPL-------------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 114 agpidFVALVQRSLRSDLERGSLRTVLVGEgvmpgaiswssledavyspaeqralcerraackASDLALIVFTSGTTGRP 193
Cdd:cd05971 62 -----FALFGPEALEYRLSNSGASALVTDG---------------------------------SDDPALIIYTSGTTGPP 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 194 KGVMHDHSCVRsvrdrGRLwkvqPGETM-LNYLPMF-HLY----------SLSEAVLQCMYSG-----CRqvvMETFDAN 256
Cdd:cd05971 104 KGALHAHRVLL-----GHL----PGVQFpFNLFPRDgDLYwtpadwawigGLLDVLLPSLYFGvpvlaHR---MTKFDPK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 257 TALDLIEQKSINilHGFETHYADLLRVQAERPRNVGSLRFGTLPSGLETSAAIAVQ-VQRVFCPTVTGA-GMSESWCWMC 334
Cdd:cd05971 172 AALDLMSRYGVT--TAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGwAREQFGVEVNEFyGQTECNLVIG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 335 TCAIDEPeeLRCHSSGRPLPGMEMRLIDPEtGKDVPPGMPGEMLFR--CYSVMKGYFEDPEATAAALdADGWLHSGDQGV 412
Cdd:cd05971 250 NCSALFP--IKPGSMGKPIPGHRVAIVDDN-GTPLPPGEVGEIAVElpDPVAFLGYWNNPSATEKKM-AGDWLLTGDLGR 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 413 VRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEE---SIIAA 489
Cdd:cd05971 326 KDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKH-PAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDAlarEIQEL 404
|
490 500 510
....*....|....*....|....*....|....
gi 1828927390 490 CKGKIASFKVPKRVVVVAELPHTATGKVQRAVIR 523
Cdd:cd05971 405 VKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
15-530 |
1.20e-44 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 165.79 E-value: 1.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 15 RAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRET 94
Cdd:PLN02479 28 RAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 95 DLADVVRRGGCKVLIFSGragpiDFVALVQRSLR--SDLERGSLR----TVLVGEGVMPGaiswsSLEDAVyspaeQRAL 168
Cdd:PLN02479 108 TIAFLLEHSKSEVVMVDQ-----EFFTLAEEALKilAEKKKSSFKppllIVIGDPTCDPK-----SLQYAL-----GKGA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 169 CERRAACKASD--------------LALiVFTSGTTGRPKGVMHDHscvrsvrdRGR---------LWKVQPGETMLNYL 225
Cdd:PLN02479 173 IEYEKFLETGDpefawkppadewqsIAL-GYTSGTTASPKGVVLHH--------RGAylmalsnalIWGMNEGAVYLWTL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 226 PMFHL----YSLSEAVLqCMYSGC-RQVvmetfDANTALDLIEQKSINILHGFETHYADLLRVQAER-----PRNVGSLR 295
Cdd:PLN02479 244 PMFHCngwcFTWTLAAL-CGTNIClRQV-----TAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSEtilplPRVVHVMT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 296 FGTLPsgleTSAAIAVQVQRVFCPTVTgAGMSESWCWMCTCA---------IDEPEELRCHSSGRPLpGME-MRLIDPET 365
Cdd:PLN02479 318 AGAAP----PPSVLFAMSEKGFRVTHT-YGLSETYGPSTVCAwkpewdslpPEEQARLNARQGVRYI-GLEgLDVVDTKT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 366 GKDVPP--GMPGEMLFRCYSVMKGYFEDPEATAAALdADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQ 443
Cdd:PLN02479 392 MKPVPAdgKTMGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVEN 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 444 ELSeLVPDILEVAVIGIPEPRLVEVPVAYVVLRPGA-----AATEESIIAACKGKIASFKVPKRvVVVAELPHTATGKVQ 518
Cdd:PLN02479 471 VVY-THPAVLEASVVARPDERWGESPCAFVTLKPGVdksdeAALAEDIMKFCRERLPAYWVPKS-VVFGPLPKTATGKIQ 548
|
570
....*....|..
gi 1828927390 519 RAVIRKTALEAG 530
Cdd:PLN02479 549 KHVLRAKAKEMG 560
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
33-526 |
2.24e-44 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 165.05 E-value: 2.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 33 MSYAELDARIDRVACGLMRN-GVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLIFS 111
Cdd:PRK08751 51 ITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 112 GRAG----------PIDFVALVQRSLRSDLERGSLRTV-------LVGEGVMPGAISWSsledavyspaEQRALCERRAA 174
Cdd:PRK08751 131 DNFGttvqqviadtPVKQVITTGLGDMLGFPKAALVNFvvkyvkkLVPEYRINGAIRFR----------EALALGRKHSM 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 175 CK----ASDLALIVFTSGTTGRPKGVMHDHSCVRSVRDRGRLW-----KVQPG-ETMLNYLPMFHLYSLSEAVLQCM-YS 243
Cdd:PRK08751 201 PTlqiePDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWlagtgKLEEGcEVVITALPLYHIFALTANGLVFMkIG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 244 GCRQVVMETFDANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRFgTLPSGLETSAAIAVQVQRVF-CPTVT 322
Cdd:PRK08751 281 GCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKM-TLGGGMAVQRSVAERWKQVTgLTLVE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 323 GAGMSESWCWMCTCAIDEPEelRCHSSGRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDAD 402
Cdd:PRK08751 360 AYGLTETSPAACINPLTLKE--YNGSIGLPIPSTDACIKD-DAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDAD 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 403 GWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEqELSELVPDILEVAVIGIPEPRLVEVpVAYVVLRPGAAAT 482
Cdd:PRK08751 437 GWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIE-DVIAMMPGVLEVAAVGVPDEKSGEI-VKVVIVKKDPALT 514
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1828927390 483 EESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRKTA 526
Cdd:PRK08751 515 AEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAA 558
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
34-525 |
4.02e-44 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 164.15 E-value: 4.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 34 SYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLIFSgr 113
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITD-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 114 agpIDFVALVQRsLRSDLERGSLRTVLVGEGVMP-----GAISWSSLEDAVYSPAEQRALCERRAACkasdlalIVFTSG 188
Cdd:PRK06018 119 ---LTFVPILEK-IADKLPSVERYVVLTDAAHMPqttlkNAVAYEEWIAEADGDFAWKTFDENTAAG-------MCYTSG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 189 TTGRPKGVMHDHscvRS------VRDRGRLWKVQPGETMLNYLPMFHLYSLSEAvLQCMYSGCRqVVM--ETFDANTALD 260
Cdd:PRK06018 188 TTGDPKGVLYSH---RSnvlhalMANNGDALGTSAADTMLPVVPLFHANSWGIA-FSAPSMGTK-LVMpgAKLDGASVYE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 261 LIEQKSINILHGFETHYADLLR-VQAERprnvgsLRFGTLPSGLETSAAIAVQVQRVF----CPTVTGAGMSESWCWMCT 335
Cdd:PRK06018 263 LLDTEKVTFTAGVPTVWLMLLQyMEKEG------LKLPHLKMVVCGGSAMPRSMIKAFedmgVEVRHAWGMTEMSPLGTL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 336 CAI-----DEPEELRCH---SSGRPLPGMEMRLIDPEtGKDVP--PGMPGEMLFRCYSVMKGYFEdpeATAAALDADGWL 405
Cdd:PRK06018 337 AALkppfsKLPGDARLDvlqKQGYPPFGVEMKITDDA-GKELPwdGKTFGRLKVRGPAVAAAYYR---VDGEILDDDGFF 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 406 HSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQeLSELVPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEES 485
Cdd:PRK06018 413 DTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLEN-LAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREE 491
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1828927390 486 IIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRKT 525
Cdd:PRK06018 492 ILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQ 531
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
21-520 |
7.53e-44 |
|
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: 161.69 E-value: 7.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 21 PEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVV 100
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 101 RRGGCKVLifsgragpidfvaLVQRSLRSDLERGSLRTVLVGegvmpgaiswsslEDAVYSPAeqralcERRAACKASDL 180
Cdd:cd12116 81 EDAEPALV-------------LTDDALPDRLPAGLPVLLLAL-------------AAAAAAPA------APRTPVSPDDL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 181 ALIVFTSGTTGRPKGVMHDHSCV----RSVRDRGRLwkvQPGETMLNYLPMFHLYSLSEAVLQCMYSGcrQVVM----ET 252
Cdd:cd12116 129 AYVIYTSGSTGRPKGVVVSHRNLvnflHSMRERLGL---GPGDRLLAVTTYAFDISLLELLLPLLAGA--RVVIapreTQ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 253 FDANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRFG-TLPSGL-ETSAAIAVQVQRVFCPTvtgagmsESW 330
Cdd:cd12116 204 RDPEALARLIEAHSITVMQATPATWRMLLDAGWQGRAGLTALCGGeALPPDLaARLLSRVGSLWNLYGPT-------ETT 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 331 CWMCTCAIDepEELRCHSSGRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDADGWLHS--- 407
Cdd:cd12116 277 IWSTAARVT--AAAGPIPIGRPLANTQVYVLD-AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPgsr 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 408 ----GDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVpVAYVVLRPGAAATE 483
Cdd:cd12116 354 lyrtGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAH-PGVAQAAVVVREDGGDRRL-VAYVVLKAGAAPDA 431
|
490 500 510
....*....|....*....|....*....|....*..
gi 1828927390 484 ESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRA 520
Cdd:cd12116 432 AALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRK 468
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
2-520 |
1.06e-43 |
|
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: 166.57 E-value: 1.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 2 TDKDLP---LLGELPTRAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALW 78
Cdd:COG1020 468 TAAPYPadaTLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 79 RIGAAAVPFNLRYRETDLADVVRRGGCKVLifsgragpidfvaLVQRSLRSDLERGSLRTVLVGEGVMPGAiswssleda 158
Cdd:COG1020 548 KAGAAYVPLDPAYPAERLAYMLEDAGARLV-------------LTQSALAARLPELGVPVLALDALALAAE--------- 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 159 vysPAEqralcERRAACKASDLALIVFTSGTTGRPKGVMHDH-SCVRSVRDRGRLWKVQPGETMLnylpMFHLYSLSEAV 237
Cdd:COG1020 606 ---PAT-----NPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHrALVNLLAWMQRRYGLGPGDRVL----QFASLSFDASV 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 238 LQ---CMYSGCRQVVM---ETFDANTALDLIEQKSINILHGFETHYADLLRVQAERPRnvgSLRFgTLPSGLETSAAIAV 311
Cdd:COG1020 674 WEifgALLSGATLVLAppeARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEALP---SLRL-VLVGGEALPPELVR 749
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 312 QVQRVF--CPTVTGAGMSESWCWMCTCAIDEPEELRCHSS-GRPLPGMEMRLIDpETGKDVPPGMPGEMlfrcY----SV 384
Cdd:COG1020 750 RWRARLpgARLVNLYGPTETTVDSTYYEVTPPDADGGSVPiGRPIANTRVYVLD-AHLQPVPVGVPGEL----YiggaGL 824
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 385 MKGYFEDPEATAAA-----LDADG--WLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAV 457
Cdd:COG1020 825 ARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQH-PGVREAVV 903
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828927390 458 IGIPEPRLVEVPVAYVVLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRA 520
Cdd:COG1020 904 VAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRL 966
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
32-519 |
1.52e-43 |
|
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: 160.69 E-value: 1.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 32 AMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLifs 111
Cdd:cd05914 7 PLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 112 gragpidFValvqrslrSDLErgslrtvlvgegvmpgaiswssledavyspaeqralcerraackasDLALIVFTSGTTG 191
Cdd:cd05914 84 -------FV--------SDED----------------------------------------------DVALINYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 192 RPKGVMHDH----SCVRSVRdrgRLWKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQVVMEtfDANTALDLIEQKS- 266
Cdd:cd05914 103 NSKGVMLTYrnivSNVDGVK---EVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLD--KIPSAKIIALAFAq 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 267 INILHGFETHYADL-LRVQAERPRNVGSL----------------------------RFGTLPSGletSAAIAVQVQRVF 317
Cdd:cd05914 178 VTPTLGVPVPLVIEkIFKMDIIPKLTLKKfkfklakkinnrkirklafkkvheafggNIKEFVIG---GAKINPDVEEFL 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 318 ----CPTVTGAGMSESWCWMCTcaiDEPEELRCHSSGRPLPGMEMRLIDPEtgkdvPPGMPGEMLFRCYSVMKGYFEDPE 393
Cdd:cd05914 255 rtigFPYTIGYGMTETAPIISY---SPPNRIRLGSAGKVIDGVEVRIDSPD-----PATGEGEIIVRGPNVMKGYYKNPE 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 394 ATAAALDADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVG-GENVSPQGVEQELSELvPDILEvAVIGIPEPRLVEVPVAY 472
Cdd:cd05914 327 ATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNM-PFVLE-SLVVVQEKKLVALAYID 404
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1828927390 473 VVLRPGAAATEESIIAACK--------GKIASF-KVPKRVVVVAELPHTATGKVQR 519
Cdd:cd05914 405 PDFLDVKALKQRNIIDAIKwevrdkvnQKVPNYkKISKVKIVKEEFEKTPKGKIKR 460
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
40-523 |
1.80e-43 |
|
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: 160.68 E-value: 1.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 40 ARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAA----AVPFNLRYRETDLADVVRRGGCKVlifsgrag 115
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRI-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 116 pidfvALVQRSLRSdlergSLRTVLVgegVMPGAISWSSLEDAVyspaEQRALCERRAACKaSDLALIVFTSGTTGRPKG 195
Cdd:cd05922 73 -----VLADAGAAD-----RLRDALP---ASPDPGTVLDADGIR----AARASAPAHEVSH-EDLALLLYTSGSTGSPKL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 196 VMHDH----SCVRSVRDRgrlWKVQPGETMLNYLPMFHLYSLSEaVLQCMYSGCRQVVMETFDANTAL-DLIEQKSINIL 270
Cdd:cd05922 135 VRLSHqnllANARSIAEY---LGITADDRALTVLPLSYDYGLSV-LNTHLLRGATLVLTNDGVLDDAFwEDLREHGATGL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 271 HGFETHYADLLRVqAERPRNVGSLRFGTlpsglETSAAIAVQVQRVFCPTVTGA------GMSESWCWMctcAIDEPEEL 344
Cdd:cd05922 211 AGVPSTYAMLTRL-GFDPAKLPSLRYLT-----QAGGRLPQETIARLRELLPGAqvyvmyGQTEATRRM---TYLPPERI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 345 --RCHSSGRPLPGMEMrLIDPETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDADGWLHSGDQGVVRPDGSIRFT 422
Cdd:cd05922 282 leKPGSIGLAIPGGEF-EILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIV 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 423 GRYKEMLKVGGENVSPQGVEQELSElVPDILEVAVIGIPEPrLVEVPVAYVVLRPGAAATEesIIAACKGKIASFKVPKR 502
Cdd:cd05922 361 GRRDRMIKLFGNRISPTEIEAAARS-IGLIIEAAAVGLPDP-LGEKLALFVTAPDKIDPKD--VLRSLAERLPPYKVPAT 436
|
490 500
....*....|....*....|.
gi 1828927390 503 VVVVAELPHTATGKVQRAVIR 523
Cdd:cd05922 437 VRVVDELPLTASGKVDYAALR 457
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
15-526 |
5.21e-43 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 161.73 E-value: 5.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 15 RAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRET 94
Cdd:PLN03102 22 RASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 95 DLADVVRRGGCKVLiFSGRagpiDFVALVQRSLR---SDLERGSLRTVLVGEGVMPGAISWSSLE-DAVYSPAEQRALCE 170
Cdd:PLN03102 102 SIAAILRHAKPKIL-FVDR----SFEPLAREVLHllsSEDSNLNLPVIFIHEIDFPKRPSSEELDyECLIQRGEPTPSLV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 171 RRAAC--KASDLALIVFTSGTTGRPKGVMHDH-----SCVRSVRDrgrlWKVQPGETMLNYLPMFHL--YSLSEAVLQcm 241
Cdd:PLN03102 177 ARMFRiqDEHDPISLNYTSGTTADPKGVVISHrgaylSTLSAIIG----WEMGTCPVYLWTLPMFHCngWTFTWGTAA-- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 242 ySGCRQVVMETFDANTALDLIEQKSINILHGFETHYADLLR----VQAERPRNVGSLRFGTLPsgletSAAIAVQVQRVF 317
Cdd:PLN03102 251 -RGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKgnslDLSPRSGPVHVLTGGSPP-----PAALVKKVQRLG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 318 CPTVTGAGMSESWCWMCTCAI-DE----PE----ELRCHSSGRPLPGMEMRLIDPETGKDVPPG--MPGEMLFRCYSVMK 386
Cdd:PLN03102 325 FQVMHAYGLTEATGPVLFCEWqDEwnrlPEnqqmELKARQGVSILGLADVDVKNKETQESVPRDgkTMGEIVIKGSSIMK 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 387 GYFEDPEATAAALDaDGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSeLVPDILEVAVIGIPEPRLV 466
Cdd:PLN03102 405 GYLKNPKATSEAFK-HGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLY-KYPKVLETAVVAMPHPTWG 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 467 EVPVAYVVLRPGAAATEE----------SIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRKTA 526
Cdd:PLN03102 483 ETPCAFVVLEKGETTKEDrvdklvtrerDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIA 552
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
34-523 |
1.38e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 159.49 E-value: 1.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 34 SYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLIFSgr 113
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFD-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 114 agpIDFVALVQrslrsdlergslrtVLVGEgvMPGAISWSSLEDAVYSPAEQRALCERRAACKASDLAL----------- 182
Cdd:PRK07008 119 ---LTFLPLVD--------------ALAPQ--CPNVKGWVAMTDAAHLPAGSTPLLCYETLVGAQDGDYdwprfdenqas 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 183 -IVFTSGTTGRPKGVMHDH-SCVR-------------SVRDrgrlwkvqpgeTMLNYLPMFHL------YSlseavlqCM 241
Cdd:PRK07008 180 sLCYTSGTTGNPKGALYSHrSTVLhaygaalpdamglSARD-----------AVLPVVPMFHVnawglpYS-------AP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 242 YSGCRQVVM-ETFDANTALDLIEQKSINILHGFETHYADLLR-VQAerprnvGSLRFGTL-----------PSGLET-SA 307
Cdd:PRK07008 242 LTGAKLVLPgPDLDGKSLYELIEAERVTFSAGVPTVWLGLLNhMRE------AGLRFSTLrrtviggsacpPAMIRTfED 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 308 AIAVQVqrvfcptVTGAGMSE-----SWCWMCTCAIDEPEELRCH---SSGRPLPGMEMRLIDPEtGKDVP-PGMP-GEM 377
Cdd:PRK07008 316 EYGVEV-------IHAWGMTEmsplgTLCKLKWKHSQLPLDEQRKlleKQGRVIYGVDMKIVGDD-GRELPwDGKAfGDL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 378 LFRCYSVMKGYFEdpeATAAALDaDGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQeLSELVPDILEVAV 457
Cdd:PRK07008 388 QVRGPWVIDRYFR---GDASPLV-DGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIEN-VAVAHPAVAEAAC 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828927390 458 IGIPEPRLVEVPVAYVVLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIR 523
Cdd:PRK07008 463 IACAHPKWDERPLLVVVKRPGAEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
33-524 |
1.62e-42 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 157.29 E-value: 1.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 33 MSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLIfsg 112
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 113 ragpidfvalvqrslrsdlergslrtvlvgegvmpgaiswssledavySPAEQRALCerraackASDLALIVFTSGTTGR 192
Cdd:cd05973 78 ------------------------------------------------TDAANRHKL-------DSDPFVMMFTSGTTGL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 193 PKGVMHDHSCVRS----------VRDRGRLWKV-QPGETmlnylpmfhlYSLSEAVLQCMYSGCRQVVMET-FDANTALD 260
Cdd:cd05973 103 PKGVPVPLRALAAfgaylrdavdLRPEDSFWNAaDPGWA----------YGLYYAITGPLALGHPTILLEGgFSVESTWR 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 261 LIEQKSINILHGFETHYADLLRVQAERPRNVGsLRFGTLPSGLE---------TSAAIAVQVQRVFCPTVTGAGMSESWc 331
Cdd:cd05973 173 VIERLGVTNLAGSPTAYRLLMAAGAEVPARPK-GRLRRVSSAGEpltpevirwFDAALGVPIHDHYGQTELGMVLANHH- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 332 wmctcAIDEPeeLRCHSSGRPLPGMEMRLIDpETGKDVPPGMPGE----------MLFRcysvmkGYFEDPEATAAAlda 401
Cdd:cd05973 251 -----ALEHP--VHAGSAGRAMPGWRVAVLD-DDGDELGPGEPGRlaidiansplMWFR------GYQLPDTPAIDG--- 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 402 dGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAA 481
Cdd:cd05973 314 -GYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEH-PAVAEAAVIGVPDPERTEVVKAFVVLRGGHEG 391
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1828927390 482 TEE---SIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRK 524
Cdd:cd05973 392 TPAladELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
178-528 |
2.24e-42 |
|
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: 155.33 E-value: 2.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 178 SDLALIVFTSGTTGRPKGVMHDHS-CVRSVRDRGRLWKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGcRQVVMET---F 253
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSnEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASG-AHVVLAGpagY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 254 DANTALD----LIEQKSINILHGFETHYADLLRVQAERprNVGSLRFGtlpsgLETSAAIAVQVQRVF-----CPTVTGA 324
Cdd:cd05944 81 RNPGLFDnfwkLVERYRITSLSTVPTVYAALLQVPVNA--DISSLRFA-----MSGAAPLPVELRARFedatgLPVVEGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 325 GMSEswcwmCTC--AIDEPE-ELRCHSSGRPLP--GMEMRLIDPETG--KDVPPGMPGEMLFRCYSVMKGYFEDpEATAA 397
Cdd:cd05944 154 GLTE-----ATClvAVNPPDgPKRPGSVGLRLPyaRVRIKVLDGVGRllRDCAPDEVGEICVAGPGVFGGYLYT-EGNKN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 398 ALDADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRP 477
Cdd:cd05944 228 AFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRH-PAVAFAGAVGQPDAHAGELPVAYVQLKP 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1828927390 478 GAAATEESIIAACKGKIAS-FKVPKRVVVVAELPHTATGKVQRAVIRKTALE 528
Cdd:cd05944 307 GAVVEEEELLAWARDHVPErAAVPKHIEVLEELPVTAVGKVFKPALRADAIH 358
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
21-520 |
3.68e-42 |
|
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: 157.43 E-value: 3.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 21 PEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVV 100
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 101 RRGGCKVLIfsgragpIDFVALVQRSLRSDLergslrTVLVGEGVMPGAISWSSLEDAvyspaeqralcerraackaSDL 180
Cdd:cd12114 81 ADAGARLVL-------TDGPDAQLDVAVFDV------LILDLDALAAPAPPPPVDVAP-------------------DDL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 181 ALIVFTSGTTGRPKGVMHDH-SCVRSVRDRGRLWKVQPGETMLnylpmfhlySLSE-----------AVLqcmySGCRQV 248
Cdd:cd12114 129 AYVIFTSGSTGTPKGVMISHrAALNTILDINRRFAVGPDDRVL---------ALSSlsfdlsvydifGAL----SAGATL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 249 VM----ETFDANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRfGTLPSG----LETSAAIAVQvqRVFCPT 320
Cdd:cd12114 196 VLpdeaRRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLR-LVLLSGdwipLDLPARLRAL--APDARL 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 321 VTGAGMSESWCWMCTCAIDE-PEELRCHSSGRPLPGMEMRLIDPEtGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAAL 399
Cdd:cd12114 273 ISLGGATEASIWSIYHPIDEvPPDWRSIPYGRPLANQRYRVLDPR-GRDCPDWVPGELWIGGRGVALGYLGDPELTAARF 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 400 --DADG--WLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEP---RLvevpVAY 472
Cdd:cd12114 352 vtHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAH-PGVARAVVVVLGDPggkRL----AAF 426
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1828927390 473 VVLRP-GAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRA 520
Cdd:cd12114 427 VVPDNdGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRA 475
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
21-520 |
7.98e-42 |
|
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: 155.93 E-value: 7.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 21 PEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYretdladvv 100
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAY--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 101 rrggckvlifsgragPIDFVALVqrslrsdLERGSLRTVLVgegvmpgaiswssledavyspaeqralcerraacKASDL 180
Cdd:cd17643 72 ---------------PVERIAFI-------LADSGPSLLLT----------------------------------DPDDL 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 181 ALIVFTSGTTGRPKGVMHDHSCVRSV-RDRGRLWKVQPGETMLnylpMFHLYSLSEAVLQ---CMYSGCRQVVMETFDAN 256
Cdd:cd17643 96 AYVIYTSGSTGRPKGVVVSHANVLALfAATQRWFGFNEDDVWT----LFHSYAFDFSVWEiwgALLHGGRLVVVPYEVAR 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 257 TA---LDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRFGTLpsGLE--TSAAIAVQVQRVFCPT---VTGAGMSE 328
Cdd:cd17643 172 SPedfARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIF--GGEalEAAMLRPWAGRFGLDRpqlVNMYGITE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 329 SwCWMCTCAIDEPEELRCHSS---GRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATA-------AA 398
Cdd:cd17643 250 T-TVHVTFRPLDAADLPAAAAspiGRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAerfvanpFG 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 399 LDADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVI----GIPEPRLVevpvAYVV 474
Cdd:cd17643 328 GPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATH-PSVRDAAVIvredEPGDTRLV----AYVV 402
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1828927390 475 LRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRA 520
Cdd:cd17643 403 ADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRA 448
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
16-519 |
8.20e-42 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 157.08 E-value: 8.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 16 AAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETD 95
Cdd:PRK13383 44 TAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 96 LADVVRRGGCKVLIFSGragpiDFVAlvqrslrsdlergslRTVLVGEGVmpgaiswssledAVYSPAEQRAL-CERRAA 174
Cdd:PRK13383 124 LAAALRAHHISTVVADN-----EFAE---------------RIAGADDAV------------AVIDPATAGAEeSGGRPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 175 CKASDlALIVFTSGTTGRPKGVMHDHScVRS-------VRDRGRLwkvQPGETMLNYLPMFHLYSLSEAVLQCMYSGCrQ 247
Cdd:PRK13383 172 VAAPG-RIVLLTSGTTGKPKGVPRAPQ-LRSavgvwvtILDRTRL---RTGSRISVAMPMFHGLGLGMLMLTIALGGT-V 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 248 VVMETFDANTALdliEQKSINILHGFETHYADLLRV----QAERPRN-VGSLRFgTLPSGLETSAAIAVQVQRVFCPTV- 321
Cdd:PRK13383 246 LTHRHFDAEAAL---AQASLHRADAFTAVPVVLARIlelpPRVRARNpLPQLRV-VMSSGDRLDPTLGQRFMDTYGDILy 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 322 TGAGMSEswcwMCTCAIDEPEELR--CHSSGRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCYSVMKGYfEDPEATAAAl 399
Cdd:PRK13383 322 NGYGSTE----VGIGALATPADLRdaPETVGKPVAGCPVRILD-RNNRPVGPRVTGRIFVGGELAGTRY-TDGGGKAVV- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 400 daDGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGA 479
Cdd:PRK13383 395 --DGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAH-PAVADNAVIGVPDERFGHRLAAFVVLHPGS 471
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1828927390 480 AATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQR 519
Cdd:PRK13383 472 GVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLR 511
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
5-526 |
1.08e-41 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 157.07 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 5 DLPLlGELPTRAAAkwPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAA 84
Cdd:PRK10946 24 DLPL-TDILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVAP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 85 VPFNLRYRETDLADVVRRGGCKVLIFSgRAGPI----DFValvqRSLRSdlERGSLRTVLVGegvmpGAISWSSLEDAVY 160
Cdd:PRK10946 101 VNALFSHQRSELNAYASQIEPALLIAD-RQHALfsddDFL----NTLVA--EHSSLRVVLLL-----NDDGEHSLDDAIN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 161 SPAEQRALcerrAACKASDLALIVFTSGTTGRPKGVMHDHS-CVRSVRDRGRLWKVQPGETMLNYLPMFHLYSLSE-AVL 238
Cdd:PRK10946 169 HPAEDFTA----TPSPADEVAFFQLSGGSTGTPKLIPRTHNdYYYSVRRSVEICGFTPQTRYLCALPAAHNYPMSSpGAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 239 QCMYSGCRQVVMETFDANTALDLIEQKSINI----------------LHGFETHYADLLRVQaerprnVGSLRFGtlpsg 302
Cdd:PRK10946 245 GVFLAGGTVVLAPDPSATLCFPLIEKHQVNVtalvppavslwlqaiaEGGSRAQLASLKLLQ------VGGARLS----- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 303 lETSAA-----IAVQVQRVFcptvtgaGMSESWcwMCTCAIDEPEELRCHSSGRPL-PGMEMRLIDpETGKDVPPGMPGE 376
Cdd:PRK10946 314 -ETLARripaeLGCQLQQVF-------GMAEGL--VNYTRLDDSDERIFTTQGRPMsPDDEVWVAD-ADGNPLPQGEVGR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 377 MLFRCYSVMKGYFEDPEATAAALDADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSeLVPDILEVA 456
Cdd:PRK10946 383 LMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLL-RHPAVIHAA 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 457 VIGIPEPRLVEVPVAYVVLRPGAAATEESIIAACKGkIASFKVPKRVVVVAELPHTATGKVQRAVIRKTA 526
Cdd:PRK10946 462 LVSMEDELMGEKSCAFLVVKEPLKAVQLRRFLREQG-IAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWL 530
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
9-523 |
2.50e-41 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 156.37 E-value: 2.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 9 LGELPTRAAAKWPEQKALEWATGAMSYAELDARiDRVACGLMRN--GVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVP 86
Cdd:PRK08974 25 LVDMFEQAVARYADQPAFINMGEVMTFRKLEER-SRAFAAYLQNglGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 87 FNLRYRETDLADVVRRGGCK-VLIFSGRAG---------PIDFVALVqrSLRSDLERGSlRTV----------LVGEGVM 146
Cdd:PRK08974 104 VNPLYTPRELEHQLNDSGAKaIVIVSNFAHtlekvvfktPVKHVILT--RMGDQLSTAK-GTLvnfvvkyikrLVPKYHL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 147 PGAISWSSledaVYSPAEQRALCerRAACKASDLALIVFTSGTTGRPKGVMHDHSCVRS-----------VRDRGRLWKV 215
Cdd:PRK08974 181 PDAISFRS----ALHKGRRMQYV--KPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLAnleqakaaygpLLHPGKELVV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 216 QPgetmlnyLPMFHLYSLSEAVLQCMYSGCRQVVMET-FDANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSL 294
Cdd:PRK08974 255 TA-------LPLYHIFALTVNCLLFIELGGQNLLITNpRDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 295 RFgTLPSGLETSAAIAVQVQRVF-CPTVTGAGMSESWCWMCTCaidePEELRCH--SSGRPLPGMEMRLIDPEtGKDVPP 371
Cdd:PRK08974 328 KL-SVGGGMAVQQAVAERWVKLTgQYLLEGYGLTECSPLVSVN----PYDLDYYsgSIGLPVPSTEIKLVDDD-GNEVPP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 372 GMPGEMLFRCYSVMKGYFEDPEATAAALDaDGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEqELSELVPD 451
Cdd:PRK08974 402 GEPGELWVKGPQVMLGYWQRPEATDEVIK-DGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIE-DVVMLHPK 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828927390 452 ILEVAVIGIPEPRLVEVPVAYVVLRpGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIR 523
Cdd:PRK08974 480 VLEVAAVGVPSEVSGEAVKIFVVKK-DPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
172-526 |
3.66e-41 |
|
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: 154.80 E-value: 3.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 172 RAACKASDLALIVFTSGTTGRPKGVMHDH----SCVRSVRDRGRLwkvQPGETMLNYLPMFHLYSLSEAVLQCMYSGcrq 247
Cdd:cd05909 141 VAPVQPDDPAVILFTSGSEGLPKGVVLSHknllANVEQITAIFDP---NPEDVVFGALPFFHSFGLTGCLWLPLLSG--- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 248 vvMETFDANTALD------LIEQKSINILHGFETHYADLLRvqAERPRNVGSLRFgtLPSGLET-SAAIAVQVQRVF-CP 319
Cdd:cd05909 215 --IKVVFHPNPLDykkipeLIYDKKATILLGTPTFLRGYAR--AAHPEDFSSLRL--VVAGAEKlKDTLRQEFQEKFgIR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 320 TVTGAGMSEswcwMCTC-AIDEPEELRCHSS-GRPLPGMEMRLIDPETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAA 397
Cdd:cd05909 289 ILEGYGTTE----CSPViSVNTPQSPNKEGTvGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSF 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 398 ALdADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELVPDILEVAVIGIPEPRLVEvpvAYVVLRP 477
Cdd:cd05909 365 AF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAVVSVPDGRKGE---KIVLLTT 440
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1828927390 478 GAAATEESIIAACK-GKIASFKVPKRVVVVAELPHTATGKVQRAVIRKTA 526
Cdd:cd05909 441 TTDTDPSSLNDILKnAGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
17-519 |
4.77e-41 |
|
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: 153.56 E-value: 4.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 17 AAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYretdl 96
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASS----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 97 advvrrggckvlifsgragPIDFVALVQRSLRSdlergslrTVLVGEGvmpgaiswssledavyspaeqralcerraack 176
Cdd:cd05945 76 -------------------PAERIREILDAAKP--------ALLIADG-------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 177 aSDLALIVFTSGTTGRPKGVMHDHSCVRSVRDrgrlW-----KVQPGETMLNYLP------MFHLY-SL-SEAVLQC--- 240
Cdd:cd05945 97 -DDNAYIIFTSGSTGRPKGVQISHDNLVSFTN----WmlsdfPLGPGDVFLNQAPfsfdlsVMDLYpALaSGATLVPvpr 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 241 -MYSGCRQVVMEtfdantaldlIEQKSINILHGFETHYADLLRVQAERPRNVGSLRfGTLPSGLETSAAIAVQVQRVF-- 317
Cdd:cd05945 172 dATADPKQLFRF----------LAEHGITVWVSTPSFAAMCLLSPTFTPESLPSLR-HFLFCGEVLPHKTARALQQRFpd 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 318 CPTVTGAGMSESwcwMCTCAIDE--PEELRCHSS---GRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCYSVMKGYFEDP 392
Cdd:cd05945 241 ARIYNTYGPTEA---TVAVTYIEvtPEVLDGYDRlpiGYAKPGAKLVILD-EDGRPVPPGEKGELVISGPSVSKGYLNNP 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 393 EATAAALDAD---GWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSElVPDILEVAVIGIPEPRLVEVP 469
Cdd:cd05945 317 EKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQ-VPGVKEAVVVPKYKGEKVTEL 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1828927390 470 VAYVVLRPGAAATEESIIAA-CKGKIASFKVPKRVVVVAELPHTATGKVQR 519
Cdd:cd05945 396 IAFVVPKPGAEAGLTKAIKAeLAERLPPYMIPRRFVYLDELPLNANGKIDR 446
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
9-520 |
8.75e-41 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 152.86 E-value: 8.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 9 LGELPTRAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFN 88
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 89 LRYRETDLADVVRRGGCKVLIfsgragpidfvalvqrslrsdlergslrtvlvgegvmpgaiswssledavyspaeqral 168
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVL----------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 169 cerraaCKASDLALIVFTSGTTGRPKGVMHDHscvRSVRDRGRlWKVQ--PGETMLNYLPM----FHLySLSEAVLQCMY 242
Cdd:cd12115 102 ------TDPDDLAYVIYTSGSTGRPKGVAIEH---RNAAAFLQ-WAAAafSAEELAGVLAStsicFDL-SVFELFGPLAT 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 243 SGCrqVVMetfdANTALDLIE---QKSINILHGFETHYADLLRVQAeRPRNVGSLRFG--TLPSGLETSAAIAVQVQRVF 317
Cdd:cd12115 171 GGK--VVL----ADNVLALPDlpaAAEVTLINTVPSAAAELLRHDA-LPASVRVVNLAgePLPRDLVQRLYARLQVERVV 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 318 cptvTGAGMSESWCWMCTCAIdEPEELRCHSSGRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAA 397
Cdd:cd12115 244 ----NLYGPSEDTTYSTVAPV-PPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 398 ALDADGWL------HSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGI----PEPRLVe 467
Cdd:cd12115 318 RFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSI-PGVREAVVVAIgdaaGERRLV- 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1828927390 468 vpvAYVVLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRA 520
Cdd:cd12115 396 ---AYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRS 445
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
146-522 |
8.82e-41 |
|
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: 153.91 E-value: 8.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 146 MPGAISWSSL-EDAVyspaeQRALCERRAAC-----KASDLALIVFTSGTTGRPKGVMHDHSCVRS----VRDRGRLWkV 215
Cdd:cd17639 55 IPIVTVYATLgEDAL-----IHSLNETECSAiftdgKPDDLACIMYTSGSTGNPKGVMLTHGNLVAgiagLGDRVPEL-L 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 216 QPGETMLNYLPMFHLYSLSeAVLQCMYSGCR------QVVMETFDANTALDLIE-------------------------- 263
Cdd:cd17639 129 GPDDRYLAYLPLAHIFELA-AENVCLYRGGTigygspRTLTDKSKRGCKGDLTEfkptlmvgvpaiwdtirkgvlaklnp 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 264 ----QKSI----------NILHGFETHYADllRVQAERPRNV--GSLRFgtLPSGletSAAIAVQVQR----VFCPTVTG 323
Cdd:cd17639 208 mgglKRTLfwtayqsklkALKEGPGTPLLD--ELVFKKVRAAlgGRLRY--MLSG---GAPLSADTQEflniVLCPVIQG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 324 AGMSESWCWMCtcaIDEPEELRCHSSGRPLPGMEMRLIDPETGK---DVPPgmP-GEMLFRCYSVMKGYFEDPEATAAAL 399
Cdd:cd17639 281 YGLTETCAGGT---VQDPGDLETGRVGPPLPCCEIKLVDWEEGGystDKPP--PrGEILIRGPNVFKGYYKNPEKTKEAF 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 400 DADGWLHSGDQGVVRPDGSIRFTGRYKEMLKV-GGENVSPQGVEQELSElVPDILEVAVIGIP-EPRlvevPVAYVV--- 474
Cdd:cd17639 356 DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLqNGEYIALEKLESIYRS-NPLVNNICVYADPdKSY----PVAIVVpne 430
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828927390 475 --LRPGA---------------------AATEESIIAACKGKIASFKVPKRVVVVAEL--PH----TATGKVQRAVI 522
Cdd:cd17639 431 khLTKLAekhgvinseweelcedkklqkAVLKSLAETARAAGLEKFEIPQGVVLLDEEwtPEnglvTAAQKLKRKEI 507
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
10-520 |
1.90e-40 |
|
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: 152.81 E-value: 1.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 10 GELPTRAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNL 89
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 90 RYRETDLADVVRRGGCKVLifsgragpidfvaLVQRSLRSDLERGSLRTVLVGEGvmpgaisWSSLEDAVYSPAEQRAlc 169
Cdd:cd17646 81 GYPADRLAYMLADAGPAVV-------------LTTADLAARLPAGGDVALLGDEA-------LAAPPATPPLVPPRPD-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 170 erraackasDLALIVFTSGTTGRPKGVMHDHscvRSVRDRGRLWK----VQPGETMLNYLPMFHLYSLSEaVLQCMYSGC 245
Cdd:cd17646 139 ---------NLAYVIYTSGSTGRPKGVMVTH---AGIVNRLLWMQdeypLGPGDRVLQKTPLSFDVSVWE-LFWPLVAGA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 246 RQVVMET---FDANTALDLIEQKSINILHGFEThyadLLRV--QAERPRNVGSLRFgTLPSGLETSAAIAVQVQRVF-CP 319
Cdd:cd17646 206 RLVVARPgghRDPAYLAALIREHGVTTCHFVPS----MLRVflAEPAAGSCASLRR-VFCSGEALPPELAARFLALPgAE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 320 TVTGAGMSESWCWMCTCAIDEPEELRCHSSGRPLPGMEMRLIDPEtGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAAL 399
Cdd:cd17646 281 LHNLYGPTEAAIDVTHWPVRGPAETPSVPIGRPVPNTRLYVLDDA-LRPVPVGVPGELYLGGVQLARGYLGRPALTAERF 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 400 DADGWLH------SGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYV 473
Cdd:cd17646 360 VPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAH-PAVTHAVVVARAAPAGAARLVGYV 438
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1828927390 474 VLRPGAAA-TEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRA 520
Cdd:cd17646 439 VPAAGAAGpDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRA 486
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
15-524 |
1.77e-39 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 149.00 E-value: 1.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 15 RAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRET 94
Cdd:cd17653 5 RIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 95 DLADVVRRGGCKVLIFsgragpidfvalvqrslrsdlergslrtvlvgegvmpgaiswssledavyspaeqralcerraA 174
Cdd:cd17653 85 RIQAILRTSGATLLLT---------------------------------------------------------------T 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 175 CKASDLALIVFTSGTTGRPKGVMHDHSCVRSVRD--RGRLwKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGcrQVVMET 252
Cdd:cd17653 102 DSPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSqpPARL-DVGPGSRVAQVLSIAFDACIGEIFSTLCNGG--TLVLAD 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 253 fDANTALDLIeqKSINILHGFETHYADLlrvqaeRPR---NVGSLRFG--TLPSGLETSAAIAVQVQRVFCPTVTgagms 327
Cdd:cd17653 179 -PSDPFAHVA--RTVDALMSTPSILSTL------SPQdfpNLKTIFLGgeAVPPSLLDRWSPGRRLYNAYGPTEC----- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 328 eswcwMCTCAIDEPEELRCHSSGRPLPGMEMRLIDPETgKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDADGWLH- 406
Cdd:cd17653 245 -----TISSTMTELLPGQPVTIGKPIPNSTCYILDADL-QPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPg 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 407 -----SGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELVPDILEVAVIgIPEPRLVevpvAYVVlrPgAAA 481
Cdd:cd17653 319 srmyrTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAI-VVNGRLV----AFVT--P-ETV 390
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1828927390 482 TEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRK 524
Cdd:cd17653 391 DVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
9-527 |
1.91e-39 |
|
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: 151.87 E-value: 1.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 9 LGELPTRAAAKWPEQKAlewATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFN 88
Cdd:cd05968 71 LADTRTRPALRWEGEDG---TSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 89 LRYRETDLADVVRRGGCKVLI----FSGRAGPIDFVALVQRSLRSDLergSLRTVLVGEGVmpGAISWSSLEDAVYSPAE 164
Cdd:cd05968 148 SGFGKEAAATRLQDAEAKALItadgFTRRGREVNLKEEADKACAQCP---TVEKVVVVRHL--GNDFTPAKGRDLSYDEE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 165 QRALCERRAACKASDLALIVFTSGTTGRPKGVMHDHSC--VRSVRDRGRLWKVQPGETMLNYLPM------FHLY-SLSE 235
Cdd:cd05968 223 KETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGfpLKAAQDMYFQFDLKPGDLLTWFTDLgwmmgpWLIFgGLIL 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 236 AVLQCMYSGcrqvvMETFDANTAL-DLIEQKSINILhGFETHYADLLRVQAERPRN---VGSLR-FGTL--PSGLETSAA 308
Cdd:cd05968 303 GATMVLYDG-----APDHPKADRLwRMVEDHEITHL-GLSPTLIRALKPRGDAPVNahdLSSLRvLGSTgePWNPEPWNW 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 309 IAVQVQRVFCPTVTGAGMSE-SWCWMCTCAIdepEELRCHSSGRPLPGMEMRLIDpETGKDVPPGMpGEMLFRC--YSVM 385
Cdd:cd05968 377 LFETVGKGRNPIINYSGGTEiSGGILGNVLI---KPIKPSSFNGPVPGMKADVLD-ESGKPARPEV-GELVLLApwPGMT 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 386 KGYFEDP----EATAAALDaDGWLHsGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEqelSELV--PDILEVAVIG 459
Cdd:cd05968 452 RGFWRDEdrylETYWSRFD-NVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIE---SVLNahPAVLESAAIG 526
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828927390 460 IPEPRLVEVPVAYVVLRPGAAATE---ESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRKTAL 527
Cdd:cd05968 527 VPHPVKGEAIVCFVVLKPGVTPTEalaEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYL 597
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
179-524 |
2.20e-39 |
|
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: 145.94 E-value: 2.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 179 DLALIVFTSGTTGRPKGVMHDHSC-VRSVRDRGRLWKVQPGETMLNYLPMFHLYSLSeAVLQCMYSGCRQVVMETFDANt 257
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANlLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLA-ILVRSLLAGAELVLLERNQAL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 258 aldlieqkSINILHGFETHYA----DLLRV-----QAERPRNVGSLRFGTLPsgleTSAAIAVQVQRVFCPTVTGAGMSE 328
Cdd:cd17630 79 --------AEDLAPPGVTHVSlvptQLQRLldsgqGPAALKSLRAVLLGGAP----IPPELLERAADRGIPLYTTYGMTE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 329 SWCWMCTCAIDEPEElrcHSSGRPLPGMEMRLIDPetgkdvppgmpGEMLFRCYSVMKGYFEDPEATAaaLDADGWLHSG 408
Cdd:cd17630 147 TASQVATKRPDGFGR---GGVGVLLPGRELRIVED-----------GEIWVGGASLAMGYLRGQLVPE--FNEDGWFTTK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 409 DQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELsELVPDILEVAVIGIPEPRLVEVPVAYVVLRPGaaATEESIIA 488
Cdd:cd17630 211 DLGELHADGRLTVLGRADNMIISGGENIQPEEIEAAL-AAHPAVRDAFVVGVPDEELGQRPVAVIVGRGP--ADPAELRA 287
|
330 340 350
....*....|....*....|....*....|....*.
gi 1828927390 489 ACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRK 524
Cdd:cd17630 288 WLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
27-524 |
3.00e-39 |
|
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: 150.44 E-value: 3.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 27 EWatgaMSYAELDARIDRVACGLMRNGVN--AGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFnlrYrETdladvvrrgg 104
Cdd:cd05927 4 EW----ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPL---Y-DT---------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 105 ckvlifsgrAGP--IDFValvqrslrsdLERGSLRTVLVGEGVMpgAISWSSLED---AVYSPAEQRalcerraacKASD 179
Cdd:cd05927 66 ---------LGPeaIEYI----------LNHAEISIVFCDAGVK--VYSLEEFEKlgkKNKVPPPPP---------KPED 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 180 LALIVFTSGTTGRPKGVMHDH-----SCVRSVRDRGRLWKVQPGETMLNYLPMFHLYslsEAVLQCM----------YSG 244
Cdd:cd05927 116 LATICYTSGTTGNPKGVMLTHgnivsNVAGVFKILEILNKINPTDVYISYLPLAHIF---ERVVEALflyhgakigfYSG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 245 CRQVVME-------------------TFDA----------------NTALDLiEQKSINILHGFETHYADLL---RVQAe 286
Cdd:cd05927 193 DIRLLLDdikalkptvfpgvprvlnrIYDKifnkvqakgplkrklfNFALNY-KLAELRSGVVRASPFWDKLvfnKIKQ- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 287 rpRNVGSLRFgtLPSGletSAAIAVQVQRVF-----CPTVTGAGMSESwcwMCTCAIDEPEELRCHSSGRPLPGMEMRLI 361
Cdd:cd05927 271 --ALGGNVRL--MLTG---SAPLSPEVLEFLrvalgCPVLEGYGQTEC---TAGATLTLPGDTSVGHVGGPLPCAEVKLV 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 362 D-PETG---KDVPPGmpGEMLFRCYSVMKGYFEDPEATAAALDADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVG-GENV 436
Cdd:cd05927 341 DvPEMNydaKDPNPR--GEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSqGEYV 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 437 SPQGVEQ--ELSELVPDI------LEVAVIGI--PEPrlvEVPVAYVVLRPGAAAT---------------EESIIAACK 491
Cdd:cd05927 419 APEKIENiyARSPFVAQIfvygdsLKSFLVAIvvPDP---DVLKEWAASKGGGTGSfeelcknpevkkailEDLVRLGKE 495
|
570 580 590
....*....|....*....|....*....|....*....
gi 1828927390 492 GKIASFKVPKRVVVVAELPH------TATGKVQRAVIRK 524
Cdd:cd05927 496 NGLKGFEQVKAIHLEPEPFSvengllTPTFKLKRPQLKK 534
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
15-524 |
1.27e-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: 148.38 E-value: 1.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 15 RAAAKWPEQKALEWATGA-----MSYAELD------ARIDRVACGLMRngvnaGDKVGLLVSNGPEYVEAIFALWRIGAA 83
Cdd:cd05928 19 EKAGKRPPNPALWWVNGKgdevkWSFRELGslsrkaANVLSGACGLQR-----GDRVAVILPRVPEWWLVNVACIRTGLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 84 AVPFNLRYRETDLADVVRRGGCKVLIFSGRAGP-IDFVALVQRSLRSDLergslrtvLVGEGVMPGaisWSSLEDAVYSP 162
Cdd:cd05928 94 FIPGTIQLTAKDILYRLQASKAKCIVTSDELAPeVDSVASECPSLKTKL--------LVSEKSRDG---WLNFKELLNEA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 163 AEQRALCErraaCKASDLALIVFTSGTTGRPKGVMHDHSCV-RSVRDRGRLW-KVQPGETMLNYLPMFHLYSLSEAVLQC 240
Cdd:cd05928 163 STEHHCVE----TGSQEPMAIYFTSGTTGSPKMAEHSHSSLgLGLKVNGRYWlDLTASDIMWNTSDTGWIKSAWSSLFEP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 241 MYSGCRQVV--METFDANTALDLIEQKSINILHGFETHYADLLRvqaerpRNVGSLRFGTLPSGLETSAAIAVQVQ---- 314
Cdd:cd05928 239 WIQGACVFVhhLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQ------QDLSSYKFPSLQHCVTGGEPLNPEVLekwk 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 315 -RVFCPTVTGAGMSESwcwMCTCAIDEPEELRCHSSGRPLPGMEMRLIDpETGKDVPPGMPGEMLFRC-----YSVMKGY 388
Cdd:cd05928 313 aQTGLDIYEGYGQTET---GLICANFKGMKIKPGSMGKASPPYDVQIID-DNGNVLPPGTEGDIGIRVkpirpFGLFSGY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 389 FEDPEATAAALDADGWLhSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEV 468
Cdd:cd05928 389 VDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEH-PAVVESAVVSSPDPIRGEV 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828927390 469 PVAYVVLRPG-AAATEESIIAA----CKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRK 524
Cdd:cd05928 467 VKAFVVLAPQfLSHDPEQLTKElqqhVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
183-519 |
2.72e-38 |
|
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: 142.93 E-value: 2.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 183 IVFTSGTTGRPKGVMHDH-SCVRSVRDRGRLWKVQPGETMLNYLPMFHLYSLSeAVLQCMYSGCRQVVMETFDANTALDL 261
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSErSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLY-GAISALYLGGTFIGQRKFNPKSWIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 262 IEQKSINILHGFETHYADLLRVQaerpRNVGSLRfGTLPSGLETSAAIAVQVQRVF--CPTVTGAGMSE-SW-CWMCtca 337
Cdd:cd17633 84 INQYNATVIYLVPTMLQALARTL----EPESKIK-SIFSSGQKLFESTKKKLKNIFpkANLIEFYGTSElSFiTYNF--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 338 idePEELR-CHSSGRPLPGMEMRLIDPETGKDVPPGMPGEMLFRCYSVMKGYfedpeataaalDADGWLHSGDQGVVRPD 416
Cdd:cd17633 156 ---NQESRpPNSVGRPFPNVEIEIRNADGGEIGKIFVKSEMVFSGYVRGGFS-----------NPDGWMSVGDIGYVDEE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 417 GSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVlrpGAAATEESIIAACKGKIAS 496
Cdd:cd17633 222 GYLYLVGRESDMIIIGGINIFPTEIESVLKAI-PGIEEAIVVGIPDARFGEIAVALYS---GDKLTYKQLKRFLKQKLSR 297
|
330 340
....*....|....*....|...
gi 1828927390 497 FKVPKRVVVVAELPHTATGKVQR 519
Cdd:cd17633 298 YEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
9-517 |
4.64e-38 |
|
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: 147.72 E-value: 4.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 9 LGELPTRAAAKWPEQKALEWATgaMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFN 88
Cdd:cd17634 63 LRENGDRTAIIYEGDDTSQSRT--ISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 89 LRYRETDLADVVRRGGCKVLIFSG---RAG-PIDFVALVQRSLrsDLERGSLRTVLV--GEGV----MPGAISWSSLEDA 158
Cdd:cd17634 141 GGFAPEAVAGRIIDSSSRLLITADggvRAGrSVPLKKNVDDAL--NPNVTSVEHVIVlkRTGSdidwQEGRDLWWRDLIA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 159 VYSPAEQRAlcerraACKASDLALIVFTSGTTGRPKGVMHDHS--CVRSVRDRGRLWKVQPGE-----TMLNYLpMFHLY 231
Cdd:cd17634 219 KASPEHQPE------AMNAEDPLFILYTSGTTGKPKGVLHTTGgyLVYAATTMKYVFDYGPGDiywctADVGWV-TGHSY 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 232 ----SLSEAVLQCMYSGcrqvVMETFDANTALDLIEQKSINILHGFETHYADLLRV--QAERPRNVGSLR--FGT-LPSG 302
Cdd:cd17634 292 llygPLACGATTLLYEG----VPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAgdDAIEGTDRSSLRilGSVgEPIN 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 303 LETSAAIAVQVQRVFCPTVTGAGMSESwCWMCTCAIDEPEELRCHSSGRPLPGMEMRLIDPEtGKDVPPGMPGEMLFRCY 382
Cdd:cd17634 368 PEAYEWYWKKIGKEKCPVVDTWWQTET-GGFMITPLPGAIELKAGSATRPVFGVQPAVVDNE-GHPQPGGTEGNLVITDP 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 383 --SVMKGYFEDPEATAAALDA--DGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEqelSELV--PDILEVA 456
Cdd:cd17634 446 wpGQTRTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIE---SVLVahPKVAEAA 522
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828927390 457 VIGIPEPRLVEVPVAYVVLRPGAAATEE---SIIAACKGKIASFKVPKRVVVVAELPHTATGKV 517
Cdd:cd17634 523 VVGIPHAIKGQAPYAYVVLNHGVEPSPElyaELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
178-519 |
1.52e-37 |
|
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: 141.24 E-value: 1.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 178 SDLALIVFTSGTTGRPKGVMHDHSCVRSVRD----RGRLWKVqpGETMLNYLPMFHLYSLSEAVLQCMYSGCRQVVMETF 253
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDilqkEGLNWVV--GDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 254 DANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRFGTLPSGLETSAAIAVQVQRVFCPTVTGAGMSESWCWM 333
Cdd:cd17635 79 TYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 334 CTCAIDEPEELrcHSSGRPLPGMEMRLIDPEtGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALdADGWLHSGDQGVV 413
Cdd:cd17635 159 CLPTDDDSIEI--NAVGRPYPGVDVYLAATD-GIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGER 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 414 RPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSElVPDILEVAVIGIPEPRLVEVPVAYVVLrpgAAATEESIIAACKGK 493
Cdd:cd17635 235 REDGFLFITGRSSESINCGGVKIAPDEVERIAEG-VSGVQECACYEISDEEFGELVGLAVVA---SAELDENAIRALKHT 310
|
330 340 350
....*....|....*....|....*....|
gi 1828927390 494 IAS----FKVPKRVVVVAELPHTATGKVQR 519
Cdd:cd17635 311 IRRelepYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
185-528 |
2.10e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 144.15 E-value: 2.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 185 FTSGTTGRPKGVMHDH-SCVRSVRDRGRLWKVQPGETMLNYLPMFHLYSLSEAVlQCMYSGCRQVVMETFDANTALDLIE 263
Cdd:PRK07638 150 FTSGSTGKPKAFLRAQqSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAI-STLYVGQTVHLMRKFIPNQVLDKLE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 264 QKSINILHGFETHYADLLRVQA--ERPRNVGSlrfgtlpSGLETSAAIAVQVQRVFcPTVTG---AGMSE-SWCwmcTCA 337
Cdd:PRK07638 229 TENISVMYTVPTMLESLYKENRviENKMKIIS-------SGAKWEAEAKEKIKNIF-PYAKLyefYGASElSFV---TAL 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 338 IDEPEELRCHSSGRPLPGMEMRlIDPETGKDVPPGMPGEMLFRCYSVMKGYFEDpEATAAALDADGWLHSGDQGVVRPDG 417
Cdd:PRK07638 298 VDEESERRPNSVGRPFHNVQVR-ICNEAGEEVQKGEIGTVYVKSPQFFMGYIIG-GVLARELNADGWMTVRDVGYEDEEG 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 418 SIRFTGRYKEMLKVGGENVSPQGVEQELSElVPDILEVAVIGIPEPRLVEVPVAYVvlrpGAAATEESIIAACKGKIASF 497
Cdd:PRK07638 376 FIYIVGREKNMILFGGINIFPEEIESVLHE-HPAVDEIVVIGVPDSYWGEKPVAII----KGSATKQQLKSFCLQRLSSF 450
|
330 340 350
....*....|....*....|....*....|.
gi 1828927390 498 KVPKRVVVVAELPHTATGKVQRAVIRKTALE 528
Cdd:PRK07638 451 KIPKEWHFVDEIPYTNSGKIARMEAKSWIEN 481
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
34-524 |
2.65e-37 |
|
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: 144.15 E-value: 2.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 34 SYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLIfsgr 113
Cdd:cd05932 8 TWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALF---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 114 AGPIDFVAlvqrSLRSDLERGSLRTVLVGEGVMPGAISWSSLEdAVYSPAEQRALCErraackASDLALIVFTSGTTGRP 193
Cdd:cd05932 84 VGKLDDWK----AMAPGVPEGLISISLPPPSAANCQYQWDDLI-AQHPPLEERPTRF------PEQLATLIYTSGTTGQP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 194 KGVMHDHSCVRSVRDRG-RLWKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQVVMETFDANTA-------------- 258
Cdd:cd05932 153 KGVMLTFGSFAWAAQAGiEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTFVEdvqrarptlffsvp 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 259 ----------LDLIEQKSINILhgfethyadlLRVQAerprnVGSLRFGTLPSGL-------------ETSAAIAVQVQR 315
Cdd:cd05932 233 rlwtkfqqgvQDKIPQQKLNLL----------LKIPV-----VNSLVKRKVLKGLgldqcrlagcgsaPVPPALLEWYRS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 316 VFCPTVTGAGMSESWCWmctCAIDEPEELRCHSSGRPLPGMEMRlIDPEtgkdvppgmpGEMLFRCYSVMKGYFEDPEAT 395
Cdd:cd05932 298 LGLNILEAYGMTENFAY---SHLNYPGRDKIGTVGNAGPGVEVR-ISED----------GEILVRSPALMMGYYKDPEAT 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 396 AAALDADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVG-GENVSPQGVEQELSELvPDILEVAVIG--IPEPRLVEVPVAY 472
Cdd:cd05932 364 AEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEH-DRVEMVCVIGsgLPAPLALVVLSEE 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828927390 473 VVLRPGAAATEE------SIIAACKGKIASFKVPKRVVVVAELPH------TATGKVQRAVIRK 524
Cdd:cd05932 443 ARLRADAFARAEleaslrAHLARVNSTLDSHEQLAGIVVVKDPWSidngilTPTLKIKRNVLEK 506
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
176-529 |
4.68e-37 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 146.61 E-value: 4.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 176 KASDLALIVFTSGTTGRPKGVMHDH----SCVRSVRDrgrLWKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQV-VM 250
Cdd:PRK08633 780 KPDDTATIIFSSGSEGEPKGVMLSHhnilSNIEQISD---VFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVyHP 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 251 ETFDANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLR--------------------FGTLPS----GLETS 306
Cdd:PRK08633 857 DPTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRlvvagaeklkpevadafeekFGIRILegygATETS 936
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 307 AAIAVQVQRVFCPtvtgagmsESWcwmctcaidepeELRCH---SSGRPLPGMEMRLIDPETGKDVPPGMPGEMLFRCYS 383
Cdd:PRK08633 937 PVASVNLPDVLAA--------DFK------------RQTGSkegSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQ 996
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 384 VMKGYFEDPEATAAAL---DADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELVPD-ILEVAVIG 459
Cdd:PRK08633 997 VMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGeEVVFAVTA 1076
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828927390 460 IPEPRLVEVPVayVVLRPGAAATEE--SIIAACkgKIASFKVPKRVVVVAELPHTATGKVQRAVIRKTALEA 529
Cdd:PRK08633 1077 VPDEKKGEKLV--VLHTCGAEDVEElkRAIKES--GLPNLWKPSRYFKVEALPLLGSGKLDLKGLKELALAL 1144
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
12-519 |
8.03e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 142.44 E-value: 8.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 12 LPTRAAAKWPEQKALEWATGAMSYAELDARIDRVAcglmrNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRY 91
Cdd:PRK07787 5 NPAAVAAAADIADAVRIGGRVLSRSDLAGAATAVA-----ERVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 92 RETDLADVVRRGGCKVLIfsGRAGPidfvalvqrslrsdlERGSLRTVlvgeGVMPGAISWSSLEDavysPAEQRAlcer 171
Cdd:PRK07787 80 GVAERRHILADSGAQAWL--GPAPD---------------DPAGLPHV----PVRLHARSWHRYPE----PDPDAP---- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 172 raackasdlALIVFTSGTTGRPKGVMHDHSCVRSVRDR-GRLWKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQVVM 250
Cdd:PRK07787 131 ---------ALIVYTSGTTGPPKGVVLSRRAIAADLDAlAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 251 ETFD-ANTALDLIEQKSIniLHGFETHYADLLRVQAErPRNVGSLRFgtLPSGletSAAIAVQV---------QRVfcpt 320
Cdd:PRK07787 202 GRPTpEAYAQALSEGGTL--YFGVPTVWSRIAADPEA-ARALRGARL--LVSG---SAALPVPVfdrlaaltgHRP---- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 321 VTGAGMSESwcwMCTCAIDEPEELRCHSSGRPLPGMEMRLIDpETGKDVP--PGMPGEMLFRCYSVMKGYFEDPEATAAA 398
Cdd:PRK07787 270 VERYGMTET---LITLSTRADGERRPGWVGLPLAGVETRLVD-EDGGPVPhdGETVGELQVRGPTLFDGYLNRPDATAAA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 399 LDADGWLHSGDQGVVRPDGSIRFTGRYK-EMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVlrP 477
Cdd:PRK07787 346 FTADGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGH-PGVREAAVVGVPDDDLGQRIVAYVV--G 422
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1828927390 478 GAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQR 519
Cdd:PRK07787 423 ADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLK 464
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-538 |
4.41e-36 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 144.33 E-value: 4.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 7 PLLGELPTRAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVP 86
Cdd:PRK12316 2003 PGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVP 2082
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 87 FNLRYRETDLADVVRRGGCKVLifsgragpidfvaLVQRSLRSDLErgslrtvlvgegvMPGAISWSSLEDAVYSPAEQR 166
Cdd:PRK12316 2083 LDPNYPAERLAYMLEDSGAALL-------------LTQRHLLERLP-------------LPAGVARLPLDRDAEWADYPD 2136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 167 ALCERRAAckASDLALIVFTSGTTGRPKGVMHDHS-CVRSVRDRGRLWKVQPGETMLNYLPmfhlYSLSEAVLQCMYS-- 243
Cdd:PRK12316 2137 TAPAVQLA--GENLAYVIYTSGSTGLPKGVAVSHGaLVAHCQAAGERYELSPADCELQFMS----FSFDGAHEQWFHPll 2210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 244 -GCRQVVM--ETFDANTALDLIEQKSINILHgFETHYADLLRVQAERPRNVGSLR---FG--TLPSGLETSAAIAVQVQR 315
Cdd:PRK12316 2211 nGARVLIRddELWDPEQLYDEMERHGVTILD-FPPVYLQQLAEHAERDGRPPAVRvycFGgeAVPAASLRLAWEALRPVY 2289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 316 VFcptvTGAGMSES------WcwmcTCAIDEPEELRCHSSGRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCYSVMKGYF 389
Cdd:PRK12316 2290 LF----NGYGPTEAvvtpllW----KCRPQDPCGAAYVPIGRALGNRRAYILD-ADLNLLAPGMAGELYLGGEGLARGYL 2360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 390 EDPEATAAALDADGWLH-------SGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVI---G 459
Cdd:PRK12316 2361 NRPGLTAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAH-PAVREAVVVaqdG 2439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1828927390 460 IPEPRLvevpVAYVVLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRKTALEAGLQLKLVSQ 538
Cdd:PRK12316 2440 ASGKQL----VAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVAPQ 2514
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
13-523 |
1.35e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 139.37 E-value: 1.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 13 PTRAAAKWPEQKALEWA-TG-AMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLR 90
Cdd:PRK13390 3 PGTHAQIAPDRPAVIVAeTGeQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 91 YRETDLADVVRRGGCKVLIFSGragPIDFVAlvqRSLRSDLErgsLRTVLVGEgvMPGAISWSSLEDAVYSP-AEQralc 169
Cdd:PRK13390 83 LTAPEADYIVGDSGARVLVASA---ALDGLA---AKVGADLP---LRLSFGGE--IDGFGSFEAALAGAGPRlTEQ---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 170 erraACKAsdlaLIVFTSGTTGRPKGVMHDHScVRSVRDRGR--------LWKVQPGETMLNYLPMFHLYSLSEAVLQCM 241
Cdd:PRK13390 148 ----PCGA----VMLYSSGTTGFPKGIQPDLP-GRDVDAPGDpivaiaraFYDISESDIYYSSAPIYHAAPLRWCSMVHA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 242 YSGCrQVVMETFDANTALDLIEQKSINILHGFETHYADLLRVQAE-RPR-NVGSLRfgtlpSGLETSAAIAVQVQRV--- 316
Cdd:PRK13390 219 LGGT-VVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLLKLDADvRTRyDVSSLR-----AVIHAAAPCPVDVKHAmid 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 317 --------FCPTVTGAGMSeswcwmctcAIDEPEELRCHSS-GRPLPGmEMRLIDpETGKDVPPGMPGEMLFRCYSVMKG 387
Cdd:PRK13390 293 wlgpivyeYYSSTEAHGMT---------FIDSPDWLAHPGSvGRSVLG-DLHICD-DDGNELPAGRIGTVYFERDRLPFR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 388 YFEDPEATAAALDADG--WLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSeLVPDILEVAVIGIPEPRL 465
Cdd:PRK13390 362 YLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALT-MHPAVHDVAVIGVPDPEM 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828927390 466 VEVPVAYVVLRPGAAATEE---SIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIR 523
Cdd:PRK13390 441 GEQVKAVIQLVEGIRGSDElarELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
33-434 |
3.20e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 140.11 E-value: 3.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 33 MSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALW--RIGAAAVPFNLRyrETDLADVVRRGGCKVLIF 110
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWsqSMVAATVYANLG--EDALAYALRETECKAIVC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 111 SGRAGPiDFVALVQrslrsdlERGSLRTVLVGEGVMPGA--------ISWSSLEDAVYSPAEQRALcerRAACKASDLAL 182
Cdd:PTZ00216 200 NGKNVP-NLLRLMK-------SGGMPNTTIIYLDSLPASvdtegcrlVAWTDVVAKGHSAGSHHPL---NIPENNDDLAL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 183 IVFTSGTTGRPKGVMHDH----SCVRSVRDRGR--LWKVQPGETMLNYLPMFHLYSLseAVLQCMYS-------GCRQVV 249
Cdd:PTZ00216 269 IMYTSGTTGDPKGVMHTHgsltAGILALEDRLNdlIGPPEEDETYCSYLPLAHIMEF--GVTNIFLArgaligfGSPRTL 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 250 METFdANTALDLIEQKSInILHG----FEThyadlLR--VQAERPRnVGSL-----------RFGTLPSGLET------- 305
Cdd:PTZ00216 347 TDTF-ARPHGDLTEFRPV-FLIGvpriFDT-----IKkaVEAKLPP-VGSLkrrvfdhayqsRLRALKEGKDTpywnekv 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 306 ----------------------SAAIAVQVQRVFCPTVTGAGMSESwcwMCTCAIDEPEELRCHSSGRPLPGMEMRLIDP 363
Cdd:PTZ00216 419 fsapravlggrvramlsgggplSAATQEFVNVVFGMVIQGWGLTET---VCCGGIQRTGDLEPNAVGQLLKGVEMKLLDT 495
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828927390 364 ETGK--DVPPgmP-GEMLFRCYSVMKGYFEDPEATAAALDADGWLHSGDQGVVRPDGSIRFTGRYKEMLK-VGGE 434
Cdd:PTZ00216 496 EEYKhtDTPE--PrGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKnCLGE 568
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
1-533 |
4.87e-35 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 138.22 E-value: 4.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 1 MTDKDLPLLGELPT-------RAAAKWPEQKALEWATG--AMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYV 71
Cdd:PRK05857 1 MGGKKFQAMPQLPStvldrvfEQARQQPEAIALRRCDGtsALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 72 EAIFALWRIGAAAVPF--NL------RYRE-TDLADVVRRGGCKVlifsgragpidfvalVQRSLRSDLERGSLRTVLVG 142
Cdd:PRK05857 81 LSVLACAKLGAIAVMAdgNLpiaaieRFCQiTDPAAALVAPGSKM---------------ASSAVPEALHSIPVIAVDIA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 143 EGVMPGAISwsslEDAVYsPAEQRALcerraacKASDLALIVFTSGTTGRPKGVMHDHSCVRSV----RDRGRLW-KVQP 217
Cdd:PRK05857 146 AVTRESEHS----LDAAS-LAGNADQ-------GSEDPLAMIFTSGTTGEPKAVLLANRTFFAVpdilQKEGLNWvTWVV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 218 GETMLNYLPMFHLYSLSeAVLQCMYSGCRQVvmeTFDANTAlDLIEqksinILHGFETHYADLlrVQAERPRNVGSLRFG 297
Cdd:PRK05857 214 GETTYSPLPATHIGGLW-WILTCLMHGGLCV---TGGENTT-SLLE-----ILTTNAVATTCL--VPTLLSKLVSELKSA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 298 --TLPS----GLETSAAIAVQVQRVFCPTVTGA---GMSESWCW-MCTCAIDEP-EELRCHSSGRPLPGMEMRLIDPE-T 365
Cdd:PRK05857 282 naTVPSlrlvGYGGSRAIAADVRFIEATGVRTAqvyGLSETGCTaLCLPTDDGSiVKIEAGAVGRPYPGVDVYLAATDgI 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 366 GKDVPPGMP----GEMLFRCYSVMKGYFEDPEATAAALdADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGV 441
Cdd:PRK05857 362 GPTAPGAGPsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 442 EQeLSELVPDILEVAVIGIPEPR---LVEVPV--AYVVLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGK 516
Cdd:PRK05857 441 DR-IAEGVSGVREAACYEIPDEEfgaLVGLAVvaSAELDESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGK 519
|
570
....*....|....*..
gi 1828927390 517 VQRAVIRKTALEAGLQL 533
Cdd:PRK05857 520 VMRASLAAAATADKARV 536
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
21-520 |
5.19e-35 |
|
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: 136.73 E-value: 5.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 21 PEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYretdladvv 100
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEY--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 101 rrggckvlifsgragPidfvalVQRsLRSDLERGSLRTVLVGEGvmpgaiswssledavyspaeqralcerraackaSDL 180
Cdd:cd17649 72 ---------------P------AER-LRYMLEDSGAGLLLTHHP---------------------------------RQL 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 181 ALIVFTSGTTGRPKGVMHDH-SCVRSVRDRGRLWKVQPGETMLNYLPmFHLYSLSEAVLQCMYSGCRQVVMET---FDAN 256
Cdd:cd17649 97 AYVIYTSGSTGTPKGVAVSHgPLAAHCQATAERYGLTPGDRELQFAS-FNFDGAHEQLLPPLICGACVVLRPDelwASAD 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 257 TALDLIEQKSINILHgFETHYADLLRVQAER--PRNVGSLRFgtLPSGLEtsaAIAVQVQRVFCPT----VTGAGMSE-- 328
Cdd:cd17649 176 ELAEMVRELGVTVLD-LPPAYLQQLAEEADRtgDGRPPSLRL--YIFGGE---ALSPELLRRWLKApvrlFNAYGPTEat 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 329 --SWCWMCtcaidEPEELRCHSS---GRPLPGMEMRLIDPETGKdVPPGMPGEMLFRCYSVMKGYFEDPEATAAAL--DA 401
Cdd:cd17649 250 vtPLVWKC-----EAGAARAGASmpiGRPLGGRSAYILDADLNP-VPVGVTGELYIGGEGLARGYLGRPELTAERFvpDP 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 402 DG-----WLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIP---EPRLvevpVAYV 473
Cdd:cd17649 324 FGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEH-PGVREAAVVALDgagGKQL----VAYV 398
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1828927390 474 VLRPGAAATE--ESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRA 520
Cdd:cd17649 399 VLRAAAAQPElrAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRK 447
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
34-531 |
6.07e-35 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 138.49 E-value: 6.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 34 SYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLIFSGr 113
Cdd:PRK04319 75 TYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTP- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 114 agpidfvALVQRSLRSDLErgSLRTV-LVGEGV--MPGAISWSSLEDAvyspAEQRALCErraACKASDLALIVFTSGTT 190
Cdd:PRK04319 154 -------ALLERKPADDLP--SLKHVlLVGEDVeeGPGTLDFNALMEQ----ASDEFDIE---WTDREDGAILHYTSGST 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 191 GRPKGVMHDHSCV-------RSV---RDRGRLW-KVQPG-ETMLNY---LPMFHlyslseavlqcmysGCRQVVMET-FD 254
Cdd:PRK04319 218 GKPKGVLHVHNAMlqhyqtgKYVldlHEDDVYWcTADPGwVTGTSYgifAPWLN--------------GATNVIDGGrFS 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 255 ANTALDLIEQKSINILHGFETHYADLLRVQAERPR--NVGSLRFgTLPSGLETSAAIAVQVQRVFcptvtGAGMSESWcW 332
Cdd:PRK04319 284 PERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKkyDLSSLRH-ILSVGEPLNPEVVRWGMKVF-----GLPIHDNW-W 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 333 MC-TCAI---DEP-EELRCHSSGRPLPGMEMRLIDPEtGKDVPPGMPGEMLFR--CYSVMKGYFEDPEATAAALdADGWL 405
Cdd:PRK04319 357 MTeTGGImiaNYPaMDIKPGSMGKPLPGIEAAIVDDQ-GNELPPNRMGNLAIKkgWPSMMRGIWNNPEKYESYF-AGDWY 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 406 HSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEE- 484
Cdd:PRK04319 435 VSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEH-PAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEEl 513
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1828927390 485 --SIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRktALEAGL 531
Cdd:PRK04319 514 keEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK--AWELGL 560
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
33-526 |
1.53e-34 |
|
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: 135.00 E-value: 1.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 33 MSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGckvlifsg 112
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 113 ragpidfvalvqrslrsdlergslrtvlvgegvmpgaiswssledAVYSPAEQralcerraACKASDLALIVFTSGTTGR 192
Cdd:cd05974 73 ---------------------------------------------AVYAAVDE--------NTHADDPMLLYFTSGTTSK 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 193 PKGVMHDHSCVRSVRDRGRLW-KVQPGETMLNY-LPMFHLYSLSEAVLQCMYSGCRQVVMET-FDANTALDLIEQKSINI 269
Cdd:cd05974 100 PKLVEHTHRSYPVGHLSTMYWiGLKPGDVHWNIsSPGWAKHAWSCFFAPWNAGATVFLFNYArFDAKRVLAALVRYGVTT 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 270 LHGFETHYADLlrVQAERPRNVGSLRfGTLPSGLETSAAIAVQVQRVFCPTV-TGAGMSESwcwmcTCAI-DEP-EELRC 346
Cdd:cd05974 180 LCAPPTVWRML--IQQDLASFDVKLR-EVVGAGEPLNPEVIEQVRRAWGLTIrDGYGQTET-----TALVgNSPgQPVKA 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 347 HSSGRPLPGMEMRLIDPETGkdvpPGMPGEMLF-----RCYSVMKGYFEDPEATAAALdADGWLHSGDQGVVRPDGSIRF 421
Cdd:cd05974 252 GSMGRPLPGYRVALLDPDGA----PATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTY 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 422 TGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEE---SIIAACKGKIASFK 498
Cdd:cd05974 327 VGRADDVFKSSDYRISPFELESVLIEH-PAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPEtalEIFRFSRERLAPYK 405
|
490 500
....*....|....*....|....*...
gi 1828927390 499 VPKRvVVVAELPHTATGKVQRAVIRKTA 526
Cdd:cd05974 406 RIRR-LEFAELPKTISGKIRRVELRRRE 432
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
8-519 |
2.36e-34 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 139.15 E-value: 2.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 8 LLGELPTRAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPF 87
Cdd:PRK05691 1132 WLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPL 1211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 88 NLRYRETDLADVVRRGGCKVLifsgragpidfvaLVQRSLRSDLERgslrtvlvGEGVMpgAISWSSLEDAVYsPAEQRA 167
Cdd:PRK05691 1212 DPDYPAERLAYMLADSGVELL-------------LTQSHLLERLPQ--------AEGVS--AIALDSLHLDSW-PSQAPG 1267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 168 LcerraACKASDLALIVFTSGTTGRPKGVMHDHSCVRSvrdrgRL------WKVQPGETMLNYLPMfhlySLSEAVLQCM 241
Cdd:PRK05691 1268 L-----HLHGDNLAYVIYTSGSTGQPKGVGNTHAALAE-----RLqwmqatYALDDSDVLMQKAPI----SFDVSVWECF 1333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 242 Y---SGCRQVVM---ETFDANTALDLIEQKSINILHgfetHYADLLRVQAERPR--NVGSLRfgTLPSGLET-SAAI--- 309
Cdd:PRK05691 1334 WpliTGCRLVLAgpgEHRDPQRIAELVQQYGVTTLH----FVPPLLQLFIDEPLaaACTSLR--RLFSGGEAlPAELrnr 1407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 310 ------AVQVQRVFCPTVTGAGMSEswcWMCTCAIDEPEELrchssGRPLPGMEMRLIDPETGKdVPPGMPGEMLFRCYS 383
Cdd:PRK05691 1408 vlqrlpQVQLHNRYGPTETAINVTH---WQCQAEDGERSPI-----GRPLGNVLCRVLDAELNL-LPPGVAGELCIGGAG 1478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 384 VMKGYFEDPEATAAAL--DADG-----WLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVA 456
Cdd:PRK05691 1479 LARGYLGRPALTAERFvpDPLGedgarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQ-PGVAQAA 1557
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828927390 457 VI---GIPEPRLvevpVAYVVLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQR 519
Cdd:PRK05691 1558 VLvreGAAGAQL----VGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDR 1619
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
17-519 |
4.26e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 138.17 E-value: 4.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 17 AAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDL 96
Cdd:PRK12316 521 VERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERL 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 97 ADVVRRGGCKVLIFSGRAGP-IDFVALVQRSlrsDLERGSLrtvlvgegvmpgaisWSsleDAVYSPAEQRALCerraac 175
Cdd:PRK12316 601 AYMLEDSGVQLLLSQSHLGRkLPLAAGVQVL---DLDRPAA---------------WL---EGYSEENPGTELN------ 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 176 kASDLALIVFTSGTTGRPKGVMHDHSC----VRSVRDRgrlWKVQPGETMLNYLPMFHLYSLSEAVLQCMySGCRQVVM- 250
Cdd:PRK12316 654 -PENLAYVIYTSGSTGKPKGAGNRHRAlsnrLCWMQQA---YGLGVGDTVLQKTPFSFDVSVWEFFWPLM-SGARLVVAa 728
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 251 --ETFDANTALDLIEQKSINILHGFETHYADLLrvQAERPRNVGSLRFGTLpSGLETSAAIAVQVQR---------VFCP 319
Cdd:PRK12316 729 pgDHRDPAKLVELINREGVDTLHFVPSMLQAFL--QDEDVASCTSLRRIVC-SGEALPADAQEQVFAklpqaglynLYGP 805
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 320 TVTGAGMSeswCWMCTcaidePEELRCHSSGRPLPGMEMRLIDPEtGKDVPPGMPGEMLFRCYSVMKGYFEDPEATA--- 396
Cdd:PRK12316 806 TEAAIDVT---HWTCV-----EEGGDSVPIGRPIANLACYILDAN-LEPVPVGVLGELYLAGRGLARGYHGRPGLTAerf 876
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 397 -AALDADG--WLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVevpvAYV 473
Cdd:PRK12316 877 vPSPFVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEH-PWVREAAVLAVDGKQLV----GYV 951
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1828927390 474 VLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQR 519
Cdd:PRK12316 952 VLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDR 997
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
32-524 |
4.63e-33 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 132.82 E-value: 4.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 32 AMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRyretdladvvrrggckvLIFS 111
Cdd:PRK09192 49 ALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLP-----------------MGFG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 112 GRAGPIDfvalvqrSLRSDLERGSLRTVLVGEGVMP--GAISWSSLEDAVYSPAEQRALCERRAAC---KASDLALIVFT 186
Cdd:PRK09192 112 GRESYIA-------QLRGMLASAQPAAIITPDELLPwvNEATHGNPLLHVLSHAWFKALPEADVALprpTPDDIAYLQYS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 187 SGTTGRPKGVMHDHSCVRS-----VRDRgrlWKVQPGETMLNYLPMFHLYSLSEAVLQCM-------------------- 241
Cdd:PRK09192 185 SGSTRFPRGVIITHRALMAnlraiSHDG---LKVRPGDRCVSWLPFYHDMGLVGFLLTPVatqlsvdylptrdfarrplq 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 242 -------------------YSGC-RQVVMETFdanTALDLIEQKSINIlhGFETHYADLLRVQAERPRNVGSLRFGTLPS 301
Cdd:PRK09192 262 wldlisrnrgtisysppfgYELCaRRVNSKDL---AELDLSCWRVAGI--GADMIRPDVLHQFAEAFAPAGFDDKAFMPS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 302 -GL-ETSAAIA-------VQVQRVFCPTVTGAGMSESwcwmctcAIDEPEELR----ChssGRPLPGMEMRLIDpETGKD 368
Cdd:PRK09192 337 yGLaEATLAVSfsplgsgIVVEEVDRDRLEYQGKAVA-------PGAETRRVRtfvnC---GKALPGHEIEIRN-EAGMP 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 369 VPPGMPGEMLFRCYSVMKGYFEDPEaTAAALDADGWLHSGDQGVVRpDGSIRFTGRYKEMLKVGGENVSPQGVEqELSEL 448
Cdd:PRK09192 406 LPERVVGHICVRGPSLMSGYFRDEE-SQDVLAADGWLDTGDLGYLL-DGYLYITGRAKDLIIINGRNIWPQDIE-WIAEQ 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 449 VPDIL--EVAVIGIPEPRlVEVPVAYVVLRPGAAATEESIIAACKGKI-ASFKVPKRVVVVA--ELPHTATGKVQRAVIR 523
Cdd:PRK09192 483 EPELRsgDAAAFSIAQEN-GEKIVLLVQCRISDEERRGQLIHALAALVrSEFGVEAAVELVPphSLPRTSSGKLSRAKAK 561
|
.
gi 1828927390 524 K 524
Cdd:PRK09192 562 K 562
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
21-526 |
9.53e-33 |
|
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: 130.74 E-value: 9.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 21 PEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVV 100
Cdd:cd05918 13 PDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHPLQRLQEIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 101 RRGGCKVLIfsgragpidfvalvqrslrsdlergslrtvlvgegvmpgaiswssledavyspaeqralcerraACKASDL 180
Cdd:cd05918 93 QDTGAKVVL----------------------------------------------------------------TSSPSDA 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 181 ALIVFTSGTTGRPKGVMHDH-SCVRSVRDRGRLWKVQPGETMLNylpmFHLY----SLSEAVLQCMYSGC--------R- 246
Cdd:cd05918 109 AYVIFTSGSTGKPKGVVIEHrALSTSALAHGRALGLTSESRVLQ----FASYtfdvSILEIFTTLAAGGClcipseedRl 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 247 ---QVVMETFDANTAldlieqksinilhGFETHYADLLRvqaerPRNVGSLRfgTLPSGLEtsaAIAVQVQRVFCPTVT- 322
Cdd:cd05918 185 ndlAGFINRLRVTWA-------------FLTPSVARLLD-----PEDVPSLR--TLVLGGE---ALTQSDVDTWADRVRl 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 323 --GAGMSEswCWMCTCAIDEPEELRCHSSGRPLPGMeMRLIDPET-GKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAA- 398
Cdd:cd05918 242 inAYGPAE--CTIAATVSPVVPSTDPRNIGRPLGAT-CWVVDPDNhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAf 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 399 LDADGWLH------------SGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELVPDILEVAVI------GI 460
Cdd:cd05918 319 IEDPAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEvvkpkdGS 398
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1828927390 461 PEPRLV-------------EVPVAYVVLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRKTA 526
Cdd:cd05918 399 SSPQLVafvvldgsssgsgDGDSLFLEPSDEFRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELA 477
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
8-523 |
5.35e-32 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 130.54 E-value: 5.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 8 LLGELPTRAA-AKWPEQKALeWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVP 86
Cdd:PRK06060 6 LAGLLAEQASeAGWYDRPAF-YAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 87 FNLRYRETDLADVVRRGGCKVLIFSGragpidfvalvqrSLRsdlERGSLRTVLVGEGVMPGAiswSSLEDAVYSPAEQR 166
Cdd:PRK06060 85 ANPELHRDDHALAARNTEPALVVTSD-------------ALR---DRFQPSRVAEAAELMSEA---ARVAPGGYEPMGGD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 167 ALcerraackasdlALIVFTSGTTGRPKGVMHDHSCVRSVRD---RGRLwKVQPGETMLNYLPMFHLYSLSEAVLQCMYS 243
Cdd:PRK06060 146 AL------------AYATYTSGTTGPPKAAIHRHADPLTFVDamcRKAL-RLTPEDTGLCSARMYFAYGLGNSVWFPLAT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 244 GCRQVVMET-FDANTALDLIEQKSINILHGFETHYADLlrVQAERPRNVGSLRFgTLPSGLETSAAIAVQVQRVF--CPT 320
Cdd:PRK06060 213 GGSAVINSApVTPEAAAILSARFGPSVLYGVPNFFARV--IDSCSPDSFRSLRC-VVSAGEALELGLAERLMEFFggIPI 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 321 VTGAGMSESWCWMCTCAIDEpeeLRCHSSGRPLPGMEMRLIDPEtGKDVPPGMPGEMLFRCYSVMKGYFEDPEATaaaLD 400
Cdd:PRK06060 290 LDGIGSTEVGQTFVSNRVDE---WRLGTLGRVLPPYEIRVVAPD-GTTAGPGVEGDLWVRGPAIAKGYWNRPDSP---VA 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 401 ADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSElVPDILEVAVIGIPEPRLVEVPVAYVVlrPGAA 480
Cdd:PRK06060 363 NEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIE-DEAVAEAAVVAVRESTGASTLQAFLV--ATSG 439
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1828927390 481 A-TEESIIAACK----GKIASFKVPKRVVVVAELPHTATGKVQRAVIR 523
Cdd:PRK06060 440 AtIDGSVMRDLHrgllNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
177-516 |
6.09e-32 |
|
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: 126.34 E-value: 6.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 177 ASDLaLIVFTSGTTGRPKGVMHDHSCVRSVRDRGRL----------WKVQ-----PGETMLNYLPMFHLYSLSEAVLQCM 241
Cdd:cd05924 3 ADDL-YILYTGGTTGMPKGVMWRQEDIFRMLMGGADfgtgeftpseDAHKaaaaaAGTVMFPAPPLMHGTGSWTAFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 242 YSGCRQVVMETFDANTALDLIEQKSINILHGFETHYA----DLLRvqAERPRNVGSLRfgTLPSGletSAAIAVQVQRVF 317
Cdd:cd05924 82 GGQTVVLPDDRFDPEEVWRTIEKHKVTSMTIVGDAMArpliDALR--DAGPYDLSSLF--AISSG---GALLSPEVKQGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 318 C---PTVT---GAGMSESWCWMCTCAIDEPeelrcHSSG-RPLPGMEMRLIDPEtGKDVPPGMPGE-MLFRCYSVMKGYF 389
Cdd:cd05924 155 LelvPNITlvdAFGSSETGFTGSGHSAGSG-----PETGpFTRANPDTVVLDDD-GRVVPPGSGGVgWIARRGHIPLGYY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 390 EDPEATAAAL-DADG--WLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELsELVPDILEVAVIGIPEPRLV 466
Cdd:cd05924 229 GDEAKTAETFpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEAL-KSHPAVYDVLVVGRPDERWG 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1828927390 467 EVPVAYVVLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGK 516
Cdd:cd05924 308 QEVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
17-519 |
2.37e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 130.08 E-value: 2.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 17 AAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDL 96
Cdd:PRK12316 3067 VERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERL 3146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 97 ADVVRRGGCKVLifsgragpidfvaLVQRSLRSDLERGSLRTVlvgegVMPGAISWSSLEDAVYSPAEqralcerraack 176
Cdd:PRK12316 3147 AYMLEDSGAQLL-------------LSQSHLRLPLAQGVQVLD-----LDRGDENYAEANPAIRTMPE------------ 3196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 177 asDLALIVFTSGTTGRPKGVMHDHSCVRS-VRDRGRLWKVQPGETMLNYLPmFHLYSLSEAVLQCMYSGCRQVVMETFDA 255
Cdd:PRK12316 3197 --NLAYVIYTSGSTGKPKGVGIRHSALSNhLCWMQQAYGLGVGDRVLQFTT-FSFDVFVEELFWPLMSGARVVLAGPEDW 3273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 256 NT---ALDLIEQKSINILHGFETHYADLLrvQAERPRNVGSLRFG-----TLPSGLETSAAIAVQVQRVFCPTVTGAgms 327
Cdd:PRK12316 3274 RDpalLVELINSEGVDVLHAYPSMLQAFL--EEEDAHRCTSLKRIvcggeALPADLQQQVFAGLPLYNLYGPTEATI--- 3348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 328 esWCWMCTCAIDEPEELrchSSGRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDADGW--- 404
Cdd:PRK12316 3349 --TVTHWQCVEEGKDAV---PIGRPIANRACYILD-GSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpg 3422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 405 ---LHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSElVPDILEVAVIGIPEPRLvevpVAYVVLRPGAAA 481
Cdd:PRK12316 3423 erlYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLE-HPWVREAVVLAVDGRQL----VAYVVPEDEAGD 3497
|
490 500 510
....*....|....*....|....*....|....*...
gi 1828927390 482 TEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQR 519
Cdd:PRK12316 3498 LREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDR 3535
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
15-519 |
5.21e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 128.74 E-value: 5.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 15 RAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRET 94
Cdd:PRK12467 520 AQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQD 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 95 DLADVVRRGGCKVLifsgragpidfvaLVQRSLRSDLER-GSLRTVLVgegvmpgaiswssleDAVYSPAEQRALCERRA 173
Cdd:PRK12467 600 RLAYMLDDSGVRLL-------------LTQSHLLAQLPVpAGLRSLCL---------------DEPADLLCGYSGHNPEV 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 174 ACKASDLALIVFTSGTTGRPKGVMHDH-SCVRSVRDRGRLWKVQPGETMLnylpMFHLYSLSEAVLQ---CMYSGCRQVV 249
Cdd:PRK12467 652 ALDPDNLAYVIYTSGSTGQPKGVAISHgALANYVCVIAERLQLAADDSML----MVSTFAFDLGVTElfgALASGATLHL 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 250 M---ETFDANTALDLIEQKSINILHGFETHYADLLRV-QAERPRNVGSLRFGTlpSGLETSAAIAVQVQRVFCPTVTGAG 325
Cdd:PRK12467 728 LppdCARDAEAFAALMADQGVTVLKIVPSHLQALLQAsRVALPRPQRALVCGG--EALQVDLLARVRALGPGARLINHYG 805
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 326 MSESWCWMCTCAI-DEPEELRCHSSGRPLPGMEMRLIDPETgKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDAD-- 402
Cdd:PRK12467 806 PTETTVGVSTYELsDEERDFGNVPIGQPLANLGLYILDHYL-NPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDpf 884
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 403 ----GWLH-SGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVpVAYVVLRP 477
Cdd:PRK12467 885 gadgGRLYrTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQ-PGVREAVVLAQPGDAGLQL-VAYLVPAA 962
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1828927390 478 GA-----AATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQR 519
Cdd:PRK12467 963 VAdgaehQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDR 1009
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
60-530 |
8.31e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 125.95 E-value: 8.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 60 VGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLIfsgragpidfvalvqrslrsdLERGSLRTV 139
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVL---------------------TESAHAELL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 140 lvgEGVMPG--AISWSSLEDAVYSPAEQRALCERRAAcKASDLALIVFTSGTTGRPKGVMHDHSCV----RSVRDRgrlW 213
Cdd:PRK07867 116 ---DGLDPGvrVINVDSPAWADELAAHRDAEPPFRVA-DPDDLFMLIFTSGTSGDPKAVRCTHRKVasagVMLAQR---F 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 214 KVQPGETMLNYLPMFHlyslSEAVLQC----MYSGCRQVVMETFDANTALDLIeqksinilHGFETHYAD-----LLRVQ 284
Cdd:PRK07867 189 GLGPDDVCYVSMPLFH----SNAVMAGwavaLAAGASIALRRKFSASGFLPDV--------RRYGATYANyvgkpLSYVL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 285 A--ERPRNV-GSLR--FGTlpsglETSA-AIAVQVQRVFCPTVTGAGMSESwcwmcTCAIDEPEELRCHSSGRPLPGMEm 358
Cdd:PRK07867 257 AtpERPDDAdNPLRivYGN-----EGAPgDIARFARRFGCVVVDGFGSTEG-----GVAITRTPDTPPGALGPLPPGVA- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 359 rLIDPETGKDVPPGMP------------GEM-------LFRcysvmkGYFEDPEATAAALdADGWLHSGDQGVVRPDGSI 419
Cdd:PRK07867 326 -IVDPDTGTECPPAEDadgrllnadeaiGELvntagpgGFE------GYYNDPEADAERM-RGGVYWSGDLAYRDADGYA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 420 RFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEESIIA--ACKGKIASF 497
Cdd:PRK07867 398 YFAGRLGDWMRVDGENLGTAPIERILLRY-PDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEflAAQPDLGPK 476
|
490 500 510
....*....|....*....|....*....|...
gi 1828927390 498 KVPKRVVVVAELPHTATGKVQRAVIRKTALEAG 530
Cdd:PRK07867 477 QWPSYVRVCAELPRTATFKVLKRQLSAEGVDCA 509
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
8-519 |
1.02e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 127.97 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 8 LLGELPTRAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPF 87
Cdd:PRK12467 3096 LVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPL 3175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 88 NLRYRETDLADVVRRGGCKVLifsgragpidfvaLVQRSLRSDLERGSLRTVLVGEGVMPGAISWSSLEDAVyspaeqra 167
Cdd:PRK12467 3176 DPEYPRERLAYMIEDSGVKLL-------------LTQAHLLEQLPAPAGDTALTLDRLDLNGYSENNPSTRV-------- 3234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 168 lcerraacKASDLALIVFTSGTTGRPKGVMHDHSC-VRSVRDRGRLWKVQPGETMLNYLPmFHLYSLSEAVLQCMYSGCR 246
Cdd:PRK12467 3235 --------MGENLAYVIYTSGSTGKPKGVGVRHGAlANHLCWIAEAYELDANDRVLLFMS-FSFDGAQERFLWTLICGGC 3305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 247 QVVM--ETFDANTALDLIEQKSINILHgFETHYADLLrVQAERPRNVGSLRFGTLpSGLETSAAIAVQVQRVFCPT--VT 322
Cdd:PRK12467 3306 LVVRdnDLWDPEELWQAIHAHRISIAC-FPPAYLQQF-AEDAGGADCASLDIYVF-GGEAVPPAAFEQVKRKLKPRglTN 3382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 323 GAGMSES------WcwmcTCAIDEPEELRCHSSGRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATA 396
Cdd:PRK12467 3383 GYGPTEAvvtvtlW----KCGGDAVCEAPYAPIGRPVAGRSIYVLD-GQLNPVPVGVAGELYIGGVGLARGYHQRPSLTA 3457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 397 AALDAD------GWLH-SGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVp 469
Cdd:PRK12467 3458 ERFVADpfsgsgGRLYrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQH-PSVREAVVLARDGAGGKQL- 3535
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1828927390 470 VAYVVLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQR 519
Cdd:PRK12467 3536 VAYVVPADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDR 3585
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
21-520 |
1.88e-30 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 123.52 E-value: 1.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 21 PEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYretdladvv 100
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAY--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 101 rrggckvlifsgragPIDFVALVqrslrsdlergslrtvlvgegvmpgaiswssLEDAvyspaeqralcerRAAC---KA 177
Cdd:cd17652 72 ---------------PAERIAYM-------------------------------LADA-------------RPALlltTP 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 178 SDLALIVFTSGTTGRPKGVMHDHSCVRS-VRDRGRLWKVQPGETMLNylpmFHLYSLSEAVLQ-CM--YSGCRQVVMETF 253
Cdd:cd17652 93 DNLAYVIYTSGSTGRPKGVVVTHRGLANlAAAQIAAFDVGPGSRVLQ----FASPSFDASVWElLMalLAGATLVLAPAE 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 254 DANTALDLieqksinilhgfethyADLLRvqAER-------PRNVGSLRFGTLPSGL-------ETSAAIAVQ--VQRVF 317
Cdd:cd17652 169 ELLPGEPL----------------ADLLR--EHRithvtlpPAALAALPPDDLPDLRtlvvageACPAELVDRwaPGRRM 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 318 C----PTVT--GAGMSEswcwmCTCAIDEPeelrchSSGRPLPGMEMRLIDPETgKDVPPGMPGEMLFRCYSVMKGYFED 391
Cdd:cd17652 231 InaygPTETtvCATMAG-----PLPGGGVP------PIGRPVPGTRVYVLDARL-RPVPPGVPGELYIAGAGLARGYLNR 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 392 PEATAAALDAD------GWLH-SGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVI----GI 460
Cdd:cd17652 299 PGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEH-PGVAEAVVVvrddRP 377
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 461 PEPRLVevpvAYVVLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRA 520
Cdd:cd17652 378 GDKRLV----AYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRR 433
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
21-526 |
3.28e-30 |
|
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: 124.74 E-value: 3.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 21 PEQKALEW---ATGA---MSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAA-AVPFNlRYRE 93
Cdd:cd05967 65 GDQIALIYdspVTGTertYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIhSVVFG-GFAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 94 TDLAdvVRRGGCK-VLIFSGRAG-----PIDFVALVQRSLRSD---------LERGSLRTVLVGEGvmpGAISWSSLeda 158
Cdd:cd05967 144 KELA--SRIDDAKpKLIVTASCGiepgkVVPYKPLLDKALELSghkphhvlvLNRPQVPADLTKPG---RDLDWSEL--- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 159 vyspaeqRALCERR--AACKASDLALIVFTSGTTGRPKGVMHDHS--CVRSVRDRGRLWKVQPGET-------------- 220
Cdd:cd05967 216 -------LAKAEPVdcVPVAATDPLYILYTSGTTGKPKGVVRDNGghAVALNWSMRNIYGIKPGDVwwaasdvgwvvghs 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 221 MLNYLPMFHlyslseavlqcmysGCRQVVME-----TFDANTALDLIEQ----------KSINILHGFETHyADLLRvqa 285
Cdd:cd05967 289 YIVYGPLLH--------------GATTVLYEgkpvgTPDPGAFWRVIEKyqvnalftapTAIRAIRKEDPD-GKYIK--- 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 286 erPRNVGSLRfgTL--------PSGLE-TSAAIAVQVQRVFCPTVTGagmsesWCWMCTCAIDEPEELRCHSSGRPLPGM 356
Cdd:cd05967 351 --KYDLSSLR--TLflagerldPPTLEwAENTLGVPVIDHWWQTETG------WPITANPVGLEPLPIKAGSPGKPVPGY 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 357 EMRLIDpETGKDVPPGMPGEMLFRCY---SVMKGYFEDPEATAAAL--DADGWLHSGDQGVVRPDGSIRFTGRYKEMLKV 431
Cdd:cd05967 421 QVQVLD-EDGEPVGPNELGNIVIKLPlppGCLLTLWKNDERFKKLYlsKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINV 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 432 GGENVSPQGVEQELSeLVPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEES----IIAACKGKIASFKVPKRVVVVA 507
Cdd:cd05967 500 AGHRLSTGEMEESVL-SHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEElekeLVALVREQIGPVAAFRLVIFVK 578
|
570
....*....|....*....
gi 1828927390 508 ELPHTATGKVQRAVIRKTA 526
Cdd:cd05967 579 RLPKTRSGKILRRTLRKIA 597
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
11-519 |
5.66e-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: 122.82 E-value: 5.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 11 ELPTRAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLR 90
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 91 YRETDLADVVRRGGCKVLIFSGR-AGPIDFVALVQRSLRSDLERGSLrtvlvgegvmpgaiswSSLEdavyspaeqralc 169
Cdd:cd17655 81 YPEERIQYILEDSGADILLTQSHlQPPIAFIGLIDLLDEDTIYHEES----------------ENLE------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 170 errAACKASDLALIVFTSGTTGRPKGVMHDH-SCVRSVRDRGRLWKVQPGETMLNYLPmFHLYSLSEAVLQCMYSGCRQV 248
Cdd:cd17655 132 ---PVSKSDDLAYVIYTSGSTGKPKGVMIEHrGVVNLVEWANKVIYQGEHLRVALFAS-ISFDASVTEIFASLLSGNTLY 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 249 VM---ETFDANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRFGtlpsGLETSAAIAVQVQRVFC--PTVTG 323
Cdd:cd17655 208 IVrkeTVLDGQALTQYIRQNRITIIDLTPAHLKLLDAADDSEGLSLKHLIVG----GEALSTELAKKIIELFGtnPTITN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 324 A-GMSESwCWMCTCAIDEPEELRCHSS--GRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALD 400
Cdd:cd17655 284 AyGPTET-TVDASIYQYEPETDQQVSVpiGKPLGNTRIYILD-QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 401 ADGWL------HSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSeLVPDILEVAVIGIPEPRLVEVPVAYVV 474
Cdd:cd17655 362 DDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLL-QHPDIKEAVVIARKDEQGQNYLCAYIV 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1828927390 475 LRPGAAATEESIIAAckGKIASFKVPKRVVVVAELPHTATGKVQR 519
Cdd:cd17655 441 SEKELPVAQLREFLA--RELPDYMIPSYFIKLDEIPLTPNGKVDR 483
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-532 |
8.22e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 125.07 E-value: 8.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 7 PLLGELPTRAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVP 86
Cdd:PRK12316 4551 RCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVP 4630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 87 FNLRYRETDLADVVRRGGCKVLifsgragpidfvaLVQRSLRSDLErgslrtvlVGEGVMPGAISWSSLEDAVYSPAEQR 166
Cdd:PRK12316 4631 LDPEYPRERLAYMMEDSGAALL-------------LTQSHLLQRLP--------IPDGLASLALDRDEDWEGFPAHDPAV 4689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 167 ALcerraacKASDLALIVFTSGTTGRPKGVMHDH-SCVRSVRDRGRLWKVQPGETMLNYLPmfhlYSLSEAVLQCMYSGC 245
Cdd:PRK12316 4690 RL-------HPDNLAYVIYTSGSTGRPKGVAVSHgSLVNHLHATGERYELTPDDRVLQFMS----FSFDGSHEGLYHPLI 4758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 246 R--QVVM---ETFDANTALDLIEQKSINILHgFETHYADLLRVQAERPRNVGSLR---FG--TLPSGLETSAAIAVQVQR 315
Cdd:PRK12316 4759 NgaSVVIrddSLWDPERLYAEIHEHRVTVLV-FPPVYLQQLAEHAERDGEPPSLRvycFGgeAVAQASYDLAWRALKPVY 4837
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 316 VFcptvTGAGMSESWCWMC--TCAIDEPEELRCHSSGRPLPGMEMRLIDPETGKdVPPGMPGEMLFRCYSVMKGYFEDPE 393
Cdd:PRK12316 4838 LF----NGYGPTETTVTVLlwKARDGDACGAAYMPIGTPLGNRSGYVLDGQLNP-LPVGVAGELYLGGEGVARGYLERPA 4912
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 394 ATAA-----ALDADG--WLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLV 466
Cdd:PRK12316 4913 LTAErfvpdPFGAPGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREH-PAVREAVVIAQEGAVGK 4991
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828927390 467 EVpVAYVVLRPGAAATEESIIAAC--------KGKIASFKVPKRVVVVAELPHTATGKVQRAVIRKtaLEAGLQ 532
Cdd:PRK12316 4992 QL-VGYVVPQDPALADADEAQAELrdelkaalRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQ--PDASLL 5062
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
15-524 |
3.45e-29 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 121.52 E-value: 3.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 15 RAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRET 94
Cdd:PRK08279 45 EAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 95 DLADVVRRGGCKVLIfsgrAGPiDFVALVQrSLRSDLERGSLRTVLVG-EGVMPGAisWSSLEDAVY-SPAEQRALcerR 172
Cdd:PRK08279 125 VLAHSLNLVDAKHLI----VGE-ELVEAFE-EARADLARPPRLWVAGGdTLDDPEG--YEDLAAAAAgAPTTNPAS---R 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 173 AACKASDLALIVFTSGTTGRPK-GVMHDHSCVRSVRDRGRLWKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQVVME 251
Cdd:PRK08279 194 SGVTAKDTAFYIYTSGTTGLPKaAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRR 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 252 TFDANTALDLIEQKSInilhgfeTHY---ADLLRV---QAERPRNVG-SLRfgtlpsgletsaaiavqvqrvfcpTVTGA 324
Cdd:PRK08279 274 KFSASRFWDDVRRYRA-------TAFqyiGELCRYllnQPPKPTDRDhRLR------------------------LMIGN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 325 GMS-ESW-CWMCTCAIDEPEEL---------------RCHSSGR-PLPGME-MRLI--DPETG----------KDVPPGM 373
Cdd:PRK08279 323 GLRpDIWdEFQQRFGIPRILEFyaasegnvgfinvfnFDGTVGRvPLWLAHpYAIVkyDVDTGepvrdadgrcIKVKPGE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 374 PGEMLFRCYSvmKGYFE---DPEATAAAL------DADGWLHSGDqgVVRPD--GSIRF------TGRYKemlkvgGENV 436
Cdd:PRK08279 403 VGLLIGRITD--RGPFDgytDPEASEKKIlrdvfkKGDAWFNTGD--LMRDDgfGHAQFvdrlgdTFRWK------GENV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 437 SPQGVEQELSElVPDILEVAVIGipeprlVEVP-------VAYVVLRPGAAATEESIIAACKGKIASFKVPKRVVVVAEL 509
Cdd:PRK08279 473 ATTEVENALSG-FPGVEEAVVYG------VEVPgtdgragMAAIVLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPEL 545
|
570
....*....|....*
gi 1828927390 510 PHTATGKVQRAVIRK 524
Cdd:PRK08279 546 ETTGTFKYRKVDLRK 560
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
15-526 |
7.06e-29 |
|
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: 120.74 E-value: 7.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 15 RAAAKWPEQKALEW------ATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAA-AVPF 87
Cdd:cd05966 61 RHLKERGDKVAIIWegdepdQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVhSVVF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 88 ------NLRYRETDladvvrrGGCKVLI----FSGRAGPIDFVALVQRSLRsdlERGSLRTVLV----GEGV--MPGAIS 151
Cdd:cd05966 141 agfsaeSLADRIND-------AQCKLVItadgGYRGGKVIPLKEIVDEALE---KCPSVEKVLVvkrtGGEVpmTEGRDL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 152 WssLEDAVyspAEQRALCERrAACKASDLALIVFTSGTTGRPKGVMHD-----------HSCVRSVRDRGRLWKVQ---- 216
Cdd:cd05966 211 W--WHDLM---AKQSPECEP-EWMDSEDPLFILYTSGSTGKPKGVVHTtggyllyaattFKYVFDYHPDDIYWCTAdigw 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 217 -PGETMLNYLPmfhlysLSEAVLQCMYSGcrqvVMETFDANTALDLIEQKSINILHGFETHYADLLRVQAERPR--NVGS 293
Cdd:cd05966 285 iTGHSYIVYGP------LANGATTVMFEG----TPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKkhDLSS 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 294 LR-FGTL--PsgletsaaIAVQVQRVF--------CPTVTGAGMSESWCWMCTC---AIDepeeLRCHSSGRPLPGMEMR 359
Cdd:cd05966 355 LRvLGSVgeP--------INPEAWMWYyevigkerCPIVDTWWQTETGGIMITPlpgATP----LKPGSATRPFFGIEPA 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 360 LIDPETGKdVPPGMPGEMLFR--CYSVMKGYFEDPEATaaaLDA-----DGWLHSGDqGVVR-PDGSIRFTGRYKEMLKV 431
Cdd:cd05966 423 ILDEEGNE-VEGEVEGYLVIKrpWPGMARTIYGDHERY---EDTyfskfPGYYFTGD-GARRdEDGYYWITGRVDDVINV 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 432 GGENVSPQGVEQELSElVPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEE---SIIAACKGKIASFKVPKRVVVVAE 508
Cdd:cd05966 498 SGHRLGTAEVESALVA-HPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDElrkELRKHVRKEIGPIATPDKIQFVPG 576
|
570
....*....|....*...
gi 1828927390 509 LPHTATGKVQRAVIRKTA 526
Cdd:cd05966 577 LPKTRSGKIMRRILRKIA 594
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
33-442 |
2.51e-28 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 119.43 E-value: 2.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 33 MSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFnlrYrETDLADVVrrggcKVLIFSG 112
Cdd:PLN02736 79 MTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPL---Y-DTLGPDAV-----KFIVNHA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 113 RAGPIDFVALVQRSLRSDL-ERGSLRTVLV---GEGVMPGAISWSSLEDAVYSPAEQRALCERRAAC--KASDLALIVFT 186
Cdd:PLN02736 150 EVAAIFCVPQTLNTLLSCLsEIPSVRLIVVvggADEPLPSLPSGTGVEIVTYSKLLAQGRSSPQPFRppKPEDVATICYT 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 187 SGTTGRPKGVMHDH-SCVRSVRDRGRLWKVQPGETMLNYLPMFHLYSLSEAVLqCMYSGC-----RQVVMETFDANTAL- 259
Cdd:PLN02736 230 SGTTGTPKGVVLTHgNLIANVAGSSLSTKFYPSDVHISYLPLAHIYERVNQIV-MLHYGVavgfyQGDNLKLMDDLAALr 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 260 -----------DLIEQKSINILHG--------FETHYA----------------DLLRVQAERPRNVGSLRFgtLPSGle 304
Cdd:PLN02736 309 ptifcsvprlyNRIYDGITNAVKEsgglkerlFNAAYNakkqalengknpspmwDRLVFNKIKAKLGGRVRF--MSSG-- 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 305 tSAAIAVQVQ---RV-FCPTVT-GAGMSESWCWMCTCaiDEPEELRCHSsGRPLPGMEMRLID-PE---TGKDVPpgMP- 374
Cdd:PLN02736 385 -ASPLSPDVMeflRIcFGGRVLeGYGMTETSCVISGM--DEGDNLSGHV-GSPNPACEVKLVDvPEmnyTSEDQP--YPr 458
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1828927390 375 GEMLFRCYSVMKGYFEDPEATAAALDADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVG-GENVSPQGVE 442
Cdd:PLN02736 459 GEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPEKIE 527
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
152-524 |
3.05e-27 |
|
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: 114.89 E-value: 3.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 152 WSSLEDAvYSPAEQRALCERraackASDLALIVFTSGTTGRPKGVMH-DHSCVRSVRDRGRLWKVQPGETMLNYLPMFHL 230
Cdd:cd05908 86 WNTLKNP-YLITEEEVLCEL-----ADELAFIQFSSGSTGDPKGVMLtHENLVHNMFAILNSTEWKTKDRILSWMPLTHD 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 231 YSLSEAVLQCMYSGCRQVVMET--------------------------FDANTALDLIEQKSIN---------ILHGFET 275
Cdd:cd05908 160 MGLIAFHLAPLIAGMNQYLMPTrlfirrpilwlkkasehkativsspnFGYKYFLKTLKPEKANdwdlssirmILNGAEP 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 276 HYADLLRVQAERPRNVGSLRFGTLPS-GLeTSAAIAVQVQRVFCPTVT----------GAGMSEswcwmctcaID--EPE 342
Cdd:cd05908 240 IDYELCHEFLDHMSKYGLKRNAILPVyGL-AEASVGASLPKAQSPFKTitlgrrhvthGEPEPE---------VDkkDSE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 343 ELRCHSSGRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDADGWLHSGDQGVVRpDGSIRFT 422
Cdd:cd05908 310 CLTFVEVGKPIDETDIRICD-EDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFIR-NGRLVIT 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 423 GRYKEMLKVGGENVSPQGVEQELSELVPDIL-EVAVIGI--PEPRLVEVpVAYVVLRpgaaATEESIIAACKgKIASFkV 499
Cdd:cd05908 388 GREKDIIFVNGQNVYPHDIERIAEELEGVELgRVVACGVnnSNTRNEEI-FCFIEHR----KSEDDFYPLGK-KIKKH-L 460
|
410 420 430
....*....|....*....|....*....|..
gi 1828927390 500 PKR-------VVVVAELPHTATGKVQRAVIRK 524
Cdd:cd05908 461 NKRggwqineVLPIRRIPKTTSGKVKRYELAQ 492
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1-530 |
5.05e-27 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 116.42 E-value: 5.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 1 MTDK-DLPL-LGELPTRAAAKWPEQKALEWATGA------MSYAELDARIDRVACGLMRNGVnAGDKVGLLVSNGPEYVE 72
Cdd:PRK05691 1 MMDAfELPLtLVQALQRRAAQTPDRLALRFLADDpgegvvLSYRDLDLRARTIAAALQARAS-FGDRAVLLFPSGPDYVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 73 AIFALWRIGAAAVPF-----NLRYRETDLADVVRRGGCKVLIFsgragpidfVALVQRSLRSdlergslrtvlVGEGVMP 147
Cdd:PRK05691 80 AFFGCLYAGVIAVPAyppesARRHHQERLLSIIADAEPRLLLT---------VADLRDSLLQ-----------MEELAAA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 148 GAISWSSLEDAVYSPAEQRalceRRAACKASDLALIVFTSGTTGRPKGVMHDHSCVRS----VRdRGRLWKVQPGETMLN 223
Cdd:PRK05691 140 NAPELLCVDTLDPALAEAW----QEPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVAneqlIR-HGFGIDLNPDDVIVS 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 224 YLPMFHLYSLSEAVLQCMYSGCRQVVMET--FDANTA--LDLIEQKSINILHGFETHY---------ADLLRVQAERPRN 290
Cdd:PRK05691 215 WLPLYHDMGLIGGLLQPIFSGVPCVLMSPayFLERPLrwLEAISEYGGTISGGPDFAYrlcservseSALERLDLSRWRV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 291 VGSlrfGTLPSGLETSAAIAVQVQRV-FCPTVTGA--GMSESWCWMC---------TCAIDEPEELRCH----------S 348
Cdd:PRK05691 295 AYS---GSEPIRQDSLERFAEKFAACgFDPDSFFAsyGLAEATLFVSggrrgqgipALELDAEALARNRaepgtgsvlmS 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 349 SGRPLPGMEMRLIDPETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAA---LDADGWLHSGDQGVVRpDGSIRFTGRY 425
Cdd:PRK05691 372 CGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfveHDGRTWLRTGDLGFLR-DGELFVTGRL 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 426 KEMLKVGGENVSPQGVEQELSELVPDILE--VAVIGIPEPRLVEVPVAYVVLRPGA-AATEESIIAACKGKIASF--KVP 500
Cdd:PRK05691 451 KDMLIVRGHNLYPQDIEKTVEREVEVVRKgrVAAFAVNHQGEEGIGIAAEISRSVQkILPPQALIKSIRQAVAEAcqEAP 530
|
570 580 590
....*....|....*....|....*....|..
gi 1828927390 501 KRVVVV--AELPHTATGKVQRAVIRkTALEAG 530
Cdd:PRK05691 531 SVVLLLnpGALPKTSSGKLQRSACR-LRLADG 561
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
14-488 |
5.36e-27 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 114.61 E-value: 5.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 14 TRAAAKWPEQKALEWATGA----------MSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAA 83
Cdd:PRK09274 13 PRAAQERPDQLAVAVPGGRgadgklaydeLSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 84 AVpfnlryretdladVVRRG-GCKVL--IFSgRAGPIDFV----ALVQRSLRSDLERGSLRTVLVGEGVMPGAISWSSLE 156
Cdd:PRK09274 93 PV-------------LVDPGmGIKNLkqCLA-EAQPDAFIgipkAHLARRLFGWGKPSVRRLVTVGGRLLWGGTTLATLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 157 DAvySPAEQRALcerrAACKASDLALIVFTSGTTGRPKGVM--HDHSC--VRSVRDrgrLWKVQPGETMlnyLPMFHLYS 232
Cdd:PRK09274 159 RD--GAAAPFPM----ADLAPDDMAAILFTSGSTGTPKGVVytHGMFEaqIEALRE---DYGIEPGEID---LPTFPLFA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 233 LSEAVLqcmysGCRQVVMEtFD------ANTA--LDLIEQKSINILHGFEThyadLLRVQAERPRNVGSlrfgTLPS--- 301
Cdd:PRK09274 227 LFGPAL-----GMTSVIPD-MDptrpatVDPAklFAAIERYGVTNLFGSPA----LLERLGRYGEANGI----KLPSlrr 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 302 ----GLETSAAIAVQVQRVFCPTV---TGAGMSESwcwMCTCAIDEPEELRCHSS----------GRPLPGMEMRLIDPE 364
Cdd:PRK09274 293 visaGAPVPIAVIERFRAMLPPDAeilTPYGATEA---LPISSIESREILFATRAatdngagicvGRPVDGVEVRIIAIS 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 365 TG--------KDVPPGMPGEMLFRCYSVMKGYFEDPEATAAA--LDADG--WLHSGDQGVVRPDGSIRFTGRYKEMLKVG 432
Cdd:PRK09274 370 DApipewddaLRLATGEIGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLGYLDAQGRLWFCGRKAHRVETA 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1828927390 433 GENVSPQGVEQELSELvPDILEVAVIGIPEPRLVeVPVAYVVLRPGAAATEESIIA 488
Cdd:PRK09274 450 GGTLYTIPCERIFNTH-PGVKRSALVGVGVPGAQ-RPVLCVELEPGVACSKSALYQ 503
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
2-519 |
6.23e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 116.41 E-value: 6.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 2 TDKDLP---LLGELPTRAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALW 78
Cdd:PRK12467 1566 THTGYPlarLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAIL 1645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 79 RIGAAAVPFNLRYRETDLADVVRRGGCKVLifsgragpidfvaLVQRSLRSDLErgslrtvlVGEGVmpgaiswSSLE-D 157
Cdd:PRK12467 1646 KAGGAYVPLDPEYPRERLAYMIEDSGIELL-------------LTQSHLQARLP--------LPDGL-------RSLVlD 1697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 158 AVYSPAEQRALCERRAACKASDLALIVFTSGTTGRPKGVMHDHS-CVRSVRDRGRLWKVQPGETMLnylpMFHLYSLSEA 236
Cdd:PRK12467 1698 QEDDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGaLVNRLCATQEAYQLSAADVVL----QFTSFAFDVS 1773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 237 VLQCMY---SGCRQVVM---ETFDANTALDLIEQKSINILHGFETHYADLLRV--QAERPRNVGSLRFGtlpsGLETSAA 308
Cdd:PRK12467 1774 VWELFWpliNGARLVIAppgAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMdeQVEHPLSLRRVVCG----GEALEVE 1849
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 309 IAVQVQRVFCPT--VTGAGMSES------WcwmcTCAIDEPEELRCHSSGRPLPGMEMRLIDpETGKDVPPGMPGEMLFR 380
Cdd:PRK12467 1850 ALRPWLERLPDTglFNLYGPTETavdvthW----TCRRKDLEGRDSVPIGQPIANLSTYILD-ASLNPVPIGVAGELYLG 1924
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 381 CYSVMKGYFEDPEATAAALDAD------GWLH-SGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDIL 453
Cdd:PRK12467 1925 GVGLARGYLNRPALTAERFVADpfgtvgSRLYrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQ-GGVR 2003
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828927390 454 EVAVIGIpEPRLVEVPVAYVVLRPGAAATEESIIAACKGKIAS--------FKVPKRVVVVAELPHTATGKVQR 519
Cdd:PRK12467 2004 EAVVIAQ-DGANGKQLVAYVVPTDPGLVDDDEAQVALRAILKNhlkaslpeYMVPAHLVFLARMPLTPNGKLDR 2076
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
28-459 |
6.45e-27 |
|
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: 114.76 E-value: 6.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 28 WATgaMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEY----VEAIFAlwriGAAAV-------PFNLRY-RETD 95
Cdd:cd05933 6 WHT--LTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWfiaaVGAIFA----GGIAVgiyttnsPEACQYvAETS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 96 LADVV----RRGGCKVLIFSGRAGPIDfvALVQrsLRSDLERGslrtvlvgegvMPGAISWSSLED-AVYSPAEQraLCE 170
Cdd:cd05933 80 EANILvvenQKQLQKILQIQDKLPHLK--AIIQ--YKEPLKEK-----------EPNLYSWDEFMElGRSIPDEQ--LDA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 171 RRAACKASDLALIVFTSGTTGRPKGVM--HD------HSCVRSVRDRGrlwKVQPGETMLNYLPMFH------------- 229
Cdd:cd05933 143 IISSQKPNQCCTLIYTSGTTGMPKGVMlsHDnitwtaKAASQHMDLRP---ATVGQESVVSYLPLSHiaaqildiwlpik 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 230 ---------------------------------------LYSLSEAVLQCMY------SGCRQVVMETfdaNTALDLIEQ 264
Cdd:cd05933 220 vggqvyfaqpdalkgtlvktlrevrptafmgvprvwekiQEKMKAVGAKSGTlkrkiaSWAKGVGLET---NLKLMGGES 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 265 KSInilhgFETHYADLLRVQAERpRNVGSLRFGTLPSGletSAAIAVQVQRVF----CPTVTGAGMSEswcwmCTCA--I 338
Cdd:cd05933 297 PSP-----LFYRLAKKLVFKKVR-KALGLDRCQKFFTG---AAPISRETLEFFlslnIPIMELYGMSE-----TSGPhtI 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 339 DEPEELRCHSSGRPLPGMEMRLIDPETGKDvppgmpGEMLFRCYSVMKGYFEDPEATAAALDADGWLHSGDQGVVRPDGS 418
Cdd:cd05933 363 SNPQAYRLLSCGKALPGCKTKIHNPDADGI------GEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGF 436
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1828927390 419 IRFTGRYKEMLKV-GGENVSPQGVEQELSELVPDILEVAVIG 459
Cdd:cd05933 437 LYITGRIKELIITaGGENVPPVPIEDAVKKELPIISNAMLIG 478
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
34-481 |
3.57e-26 |
|
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: 112.52 E-value: 3.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 34 SYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFnlrYRET---DLADVVRRGGCKVlIF 110
Cdd:cd17641 13 TWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGI---YQDSmaeEVAYLLNYTGARV-VI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 111 SGRAGPIDFVALVQRSLRSdlergsLRTVLVGE--GVMPGAISW-SSLEDAV-----YSPAEQRALCERRAACKASDLAL 182
Cdd:cd17641 89 AEDEEQVDKLLEIADRIPS------VRYVIYCDprGMRKYDDPRlISFEDVValgraLDRRDPGLYEREVAAGKGEDVAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 183 IVFTSGTTGRPKGVMHDH-----SCVRSVRDRGRLwkvqPGETMLNYLP----MFHLYSLSEAVLqcmysgCRQVVMETF 253
Cdd:cd17641 163 LCTTSGTTGKPKLAMLSHgnflgHCAAYLAADPLG----PGDEYVSVLPlpwiGEQMYSVGQALV------CGFIVNFPE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 254 DANTAL-DLIE------------------QKSINIL-----------HGFETHYADLLRVQAERPRNVGS---------- 293
Cdd:cd17641 233 EPETMMeDLREigptfvllpprvwegiaaDVRARMMdatpfkrfmfeLGMKLGLRALDRGKRGRPVSLWLrlaswladal 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 294 --------LRFGTLPSGLETSAAIAVQVQRVF----CPTVTGAGMSEswcwMCTCAIDEPE-ELRCHSSGRPLPGMEMRL 360
Cdd:cd17641 313 lfrplrdrLGFSRLRSAATGGAALGPDTFRFFhaigVPLKQLYGQTE----LAGAYTVHRDgDVDPDTVGVPFPGTEVRI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 361 IDPetgkdvppgmpGEMLFRCYSVMKGYFEDPEATAAALDADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVG-GENVSPQ 439
Cdd:cd17641 389 DEV-----------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSPQ 457
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1828927390 440 GVEQELsELVPDILEVAVIGIPEPRLvevpVAYVVLRPGAAA 481
Cdd:cd17641 458 FIENKL-KFSPYIAEAVVLGAGRPYL----TAFICIDYAIVG 494
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
60-530 |
4.72e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 111.66 E-value: 4.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 60 VGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLIfsgragpidfVALVQRSLRSDLERGSLRTV 139
Cdd:PRK13388 55 VGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLLV----------TDAEHRPLLDGLDLPGVRVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 140 LVGEGVMPGAISwsslEDAVYSPAeqralcerrAACKASDLALIVFTSGTTGRPKGVMHDHSCV-RSVRDRGRLWKVQPG 218
Cdd:PRK13388 125 DVDTPAYAELVA----AAGALTPH---------REVDAMDPFMLIFTSGTTGAPKAVRCSHGRLaFAGRALTERFGLTRD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 219 ETMLNYLPMFHlyslSEAVLQ----CMYSGCRQVVMETFDANTALDLIEQKSINILHGFETHYADLLrVQAERPRNVGSl 294
Cdd:PRK13388 192 DVCYVSMPLFH----SNAVMAgwapAVASGAAVALPAKFSASGFLDDVRRYGATYFNYVGKPLAYIL-ATPERPDDADN- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 295 rfgTLPSGLETSAA---IAVQVQRVFCPTVTGAGMSESWCwMCTCAIDEPEElrchSSGRPLPGMEmrLIDPETGKDVPP 371
Cdd:PRK13388 266 ---PLRVAFGNEASprdIAEFSRRFGCQVEDGYGSSEGAV-IVVREPGTPPG----SIGRGAPGVA--IYNPETLTECAV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 372 GM-------------PGEMLFRCYSVM-KGYFEDPEATAAALdADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVS 437
Cdd:PRK13388 336 ARfdahgallnadeaIGELVNTAGAGFfEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLS 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 438 PQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEESIIA--ACKGKIASFKVPKRVVVVAELPHTATG 515
Cdd:PRK13388 415 AAPIERILLRH-PAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAflAAQPDLGTKAWPRYVRIAADLPSTATN 493
|
490
....*....|....*
gi 1828927390 516 KVQRAVIRKTALEAG 530
Cdd:PRK13388 494 KVLKRELIAQGWATG 508
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
21-517 |
3.77e-25 |
|
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: 108.26 E-value: 3.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 21 PEQKALEWATGAMSYAELDARIDRVACGLMRNG-VNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYretdladv 99
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSY-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 100 vrrggckvlifsgragPIDFVALVqrslrsdLERGSLRTVLVGegvmpgaiswssledavyspaeqralcerraackASD 179
Cdd:cd17648 73 ----------------PDERIQFI-------LEDTGARVVITN----------------------------------STD 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 180 LALIVFTSGTTGRPKGVMHDHSCVRSVRD--RGRLWKVQPG-ETML---NYLPMFHLYSLSEAVLqcmySGCRQVVME-- 251
Cdd:cd17648 96 LAYAIYTSGTTGKPKGVLVEHGSVVNLRTslSERYFGRDNGdEAVLffsNYVFDFFVEQMTLALL----NGQKLVVPPde 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 252 -TFDANTALDLIEQKSINILHGfethyadllrvqaeRPRNVGSLRFGTLPS-------GLETSAAIAVQVQRVFC-PTVT 322
Cdd:cd17648 172 mRFDPDRFYAYINREKVTYLSG--------------TPSVLQQYDLARLPHlkrvdaaGEEFTAPVFEKLRSRFAgLIIN 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 323 GAGMSESWcwMCTCAIDEPEELRCHSS-GRPLPGMEMRLIDPETgKDVPPGMPGEMLFRCYSVMKGYFEDPEATA----- 396
Cdd:cd17648 238 AYGPTETT--VTNHKRFFPGDQRFDKSlGRPVRNTKCYVLNDAM-KRVPVGAVGELYLGGDGVARGYLNRPELTAerflp 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 397 --------AALDADGWLH-SGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSElVPDILEVAVI-----GIPE 462
Cdd:cd17648 315 npfqteqeRARGRNARLYkTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALAS-YPGVRECAVVakedaSQAQ 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1828927390 463 PRLVEVPVAYVVLRPGAAaTEESIIAACKGKIASFKVPKRVVVVAELPHTATGKV 517
Cdd:cd17648 394 SRIQKYLVGYYLPEPGHV-PESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
41-524 |
6.68e-25 |
|
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: 108.29 E-value: 6.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 41 RIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLIFSGragpiDFV 120
Cdd:cd05915 33 RARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDP-----NLL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 121 ALVQRSLrsdlergslrTVLVGEGVMPGAIS-WSSLEDAVYSPAEQRALCERRAACkasDLALIVFTSGTTGRPKGVMHD 199
Cdd:cd05915 108 PLVEAIR----------GELKTVQHFVVMDEkAPEGYLAYEEALGEEADPVRVPER---AACGMAYTTGTTGLPKGVVYS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 200 H-SCVRSVRDRGRL--WKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQVVMETFDANTALD-LIEQKSINIlhGFET 275
Cdd:cd05915 175 HrALVLHSLAASLVdgTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPASLVElFDGEGVTFT--AGVP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 276 HYADLL-----RVQAERPRNVGSLRFGTLPSG--LETSAAIAVQVQRVF-CPTVTGAGMSESWC--WMctcAIDEPEELR 345
Cdd:cd05915 253 TVWLALadyleSTGHRLKTLRRLVVGGSAAPRslIARFERMGVEVRQGYgLTETSPVVVQNFVKshLE---SLSEEEKLT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 346 CHS-SGRPLPGMEMRLIDPETGKDVPPGMPGEML-FRCYSVMKGYFEDPEATAAALDADGWLHSGDQGVVRPDGSIRFTG 423
Cdd:cd05915 330 LKAkTGLPIPLVRLRVADEEGRPVPKDGKALGEVqLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKD 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 424 RYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPgAAATEESIIAACKGKIASFK-VPKR 502
Cdd:cd05915 410 RLKDLIKSGGEWISSVDLENALMGH-PKVKEAAVVAIPHPKWQERPLAVVVPRG-EKPTPEELNEHLLKAGFAKWqLPDA 487
|
490 500
....*....|....*....|..
gi 1828927390 503 VVVVAELPHTATGKVQRAVIRK 524
Cdd:cd05915 488 YVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
165-530 |
1.07e-24 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 108.90 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 165 QRALCERraacKASDLALIVFTSGTTGRPKGVMHDHSC-------VRSVRDRGrlwkvqPGETMLNYLPMFHLYSLSEAV 237
Cdd:PRK06814 784 LVYFCNR----DPDDPAVILFTSGSEGTPKGVVLSHRNllanraqVAARIDFS------PEDKVFNALPVFHSFGLTGGL 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 238 LQCMYSGCRqvvmeTFDANTALD------LIEQKSINILHG---FETHYA---------DLLRVQA------ERPRNVGS 293
Cdd:PRK06814 854 VLPLLSGVK-----VFLYPSPLHyriipeLIYDTNATILFGtdtFLNGYAryahpydfrSLRYVFAgaekvkEETRQTWM 928
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 294 LRFGTlpsgletsaaiavqvqRVFcptvTGAGMSESwcwMCTCAIDEPEELRCHSSGRPLPGMEMRLiDPETGKDvppgM 373
Cdd:PRK06814 929 EKFGI----------------RIL----EGYGVTET---APVIALNTPMHNKAGTVGRLLPGIEYRL-EPVPGID----E 980
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 374 PGEMLFRCYSVMKGYF--EDPEATAAAldADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELVPD 451
Cdd:PRK06814 981 GGRLFVRGPNVMLGYLraENPGVLEPP--ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPD 1058
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 452 ILEvAVIGIPEPRLVEvpvAYVVLRPGAAATEESIIAACKGKIAS-FKVPKRVVVVAELPHTATGKVQRAVIRKTALEAG 530
Cdd:PRK06814 1059 ALH-AAVSIPDARKGE---RIILLTTASDATRAAFLAHAKAAGASeLMVPAEIITIDEIPLLGTGKIDYVAVTKLAEEAA 1134
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
32-524 |
1.26e-24 |
|
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: 106.67 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 32 AMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLIFs 111
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 112 gragpidfvalvqrslrsdlergslrtvlvgegvmpgaiswssledavyspaeqralcerraackasDLALIVFTSGTTG 191
Cdd:cd05940 82 -------------------------------------------------------------------DAALYIYTSGTTG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 192 RPK-GVMHDHSCVRSVRDRGRLWKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQVVMETFDANTALDLIEQKSINIL 270
Cdd:cd05940 95 LPKaAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATIF 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 271 hgfeTHYADLLR-------VQAERPRNV---------GSL------RFGtLPSGLETSAAIAVQVQRVFCPTVTGA-GMS 327
Cdd:cd05940 175 ----QYIGELCRyllnqppKPTERKHKVrmifgnglrPDIweefkeRFG-VPRIAEFYAATEGNSGFINFFGKPGAiGRN 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 328 ESWcwmctCAIDEPEEL-RC-HSSGRPLPGMEMRLIdpetgkDVPPGMPGEMLFRCYSV--MKGYFeDPEATAAAL---- 399
Cdd:cd05940 250 PSL-----LRKVAPLALvKYdLESGEPIRDAEGRCI------KVPRGEPGLLISRINPLepFDGYT-DPAATEKKIlrdv 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 400 --DADGWLHSGDqgVVRPD--GSIRFTGRYKEMLKVGGENVSPQGVEQELSeLVPDILEVAVIGIPEPRLV-EVPVAYVV 474
Cdd:cd05940 318 fkKGDAWFNTGD--LMRLDgeGFWYFVDRLGDTFRWKGENVSTTEVAAVLG-AFPGVEEANVYGVQVPGTDgRAGMAAIV 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1828927390 475 LRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRK 524
Cdd:cd05940 395 LQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
17-519 |
3.62e-24 |
|
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: 105.59 E-value: 3.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 17 AAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDL 96
Cdd:cd17644 10 VERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 97 ADVVRRGGCKVLIFSGragpidfvalvqrslrsdlergslrtvlvgegvmpgaiswssledavyspaeqralcerraack 176
Cdd:cd17644 90 TYILEDAQISVLLTQP---------------------------------------------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 177 aSDLALIVFTSGTTGRPKGVMHDHscvRSVRDRGRLWKVQPGETMLNYLPMFHLYSL---SEAVLQCMYSGCrQVVMET- 252
Cdd:cd17644 106 -ENLAYVIYTSGSTGKPKGVMIEH---QSLVNLSHGLIKEYGITSSDRVLQFASIAFdvaAEEIYVTLLSGA-TLVLRPe 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 253 ---FDANTALDLIEQKSINILHgFETHYADLLRvqaerprNVGSLRFGTLPSGL-----------ETSAAIAVQVQRVFC 318
Cdd:cd17644 181 emrSSLEDFVQYIQQWQLTVLS-LPPAYWHLLV-------LELLLSTIDLPSSLrlvivggeavqPELVRQWQKNVGNFI 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 319 PTVTGAGMSESWCWMCTCAIDEPEELRCHSS--GRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATA 396
Cdd:cd17644 253 QLINVYGPTEATIAATVCRLTQLTERNITSVpiGRPIANTQVYILD-ENLQPVPVGVPGELHIGGVGLARGYLNRPELTA 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 397 AALDADGWLHS--------GDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEV 468
Cdd:cd17644 332 EKFISHPFNSSeserlyktGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQH-NDVKTAVVIVREDQPGNKR 410
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1828927390 469 PVAYVVLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQR 519
Cdd:cd17644 411 LVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDR 461
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
178-525 |
7.34e-24 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 102.82 E-value: 7.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 178 SDLALIVFTSGTTGRPKGVMHDHSCVRSVRDRGRLWKVQPGETMLNyLPMFHLYSLsEAVLQCMYSGCRQVVMetfDANT 257
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLGGPGQWLLA-LPAHHIAGL-QVLVRSVIAGSEPVEL---DVSA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 258 ALDLIEQKSINILHGFETHYADLLRVQAER----PRNVGSLRF--GTLPSGLETSAAIAVQVQRVFCPTVTGAGMSEswc 331
Cdd:PRK07824 110 GFDPTALPRAVAELGGGRRYTSLVPMQLAKalddPAATAALAEldAVLVGGGPAPAPVLDAAAAAGINVVRTYGMSE--- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 332 wmcTCAidepeelRCHSSGRPLPGMEMRLIDpetgkdvppgmpGEMLFRCYSVMKGYFEDPEATAAAldADGWLHSGDQG 411
Cdd:PRK07824 187 ---TSG-------GCVYDGVPLDGVRVRVED------------GRIALGGPTLAKGYRNPVDPDPFA--EPGWFRTDDLG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 412 VVRpDGSIRFTGRYKEMLKVGGENVSPQGVEQELSElVPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEESIIAACK 491
Cdd:PRK07824 243 ALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALAT-HPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLEALRAHVA 320
|
330 340 350
....*....|....*....|....*....|....
gi 1828927390 492 GKIASFKVPKRVVVVAELPHTATGKVQRAVIRKT 525
Cdd:PRK07824 321 RTLDRTAAPRELHVVDELPRRGIGKVDRRALVRR 354
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
2-524 |
3.26e-22 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 100.24 E-value: 3.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 2 TDKDLPL-LGELPTRAAAKWPEQKALEWATGAM---SYAELDARIDRVACGLMRN-GVNAGDKVGLLVSNGPEYVEAIFA 76
Cdd:PRK05620 4 TMQDVPLsLTRILEYGSTVHGDTTVTTWGGAEQeqtTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 77 LWRIGAAAVPFNLRYRETDLADVVRRGGCKVLIFSGRagpidfvaLVQRSLRSDLERGSLRTVLV--------GEGVMPG 148
Cdd:PRK05620 84 VACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPR--------LAEQLGEILKECPCVRAVVFigpsdadsAAAHMPE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 149 AISWSSLE------DAVYSPAEQralcERRAAckasdlALIVFTSGTTGRPKGVMHDHSCV----RSVRDRGRLwKVQPG 218
Cdd:PRK05620 156 GIKVYSYEalldgrSTVYDWPEL----DETTA------AAICYSTGTTGAPKGVVYSHRSLylqsLSLRTTDSL-AVTHG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 219 ETMLNYLPMFHLYSLSEAVLQCMySGCRQVVM-ETFDANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRfg 297
Cdd:PRK05620 225 ESFLCCVPIYHVLSWGVPLAAFM-SGTPLVFPgPDLSAPTLAKIIATAMPRVAHGVPTLWIQLMVHYLKNPPERMSLQ-- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 298 TLPSGLETSAAIAVQV--QRVFCPTVTGAGMSEswcwmcTCAID-----------EPEELRCHSSGRPLPGMEMRLIDPE 364
Cdd:PRK05620 302 EIYVGGSAVPPILIKAweERYGVDVVHVWGMTE------TSPVGtvarppsgvsgEARWAYRVSQGRFPASLEYRIVNDG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 365 TGKDVPPGMPGEMLFRCYSVMKGYFEDP----------------EATAAALDADGWLHSGDQGVVRPDGSIRFTGRYKEM 428
Cdd:PRK05620 376 QVMESTDRNEGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDV 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 429 LKVGGENVSPQGVEQELSElVPDILEVAVIGIPEPRLVEVPVAYVVLRPG---AAATEESIIAACKGKIASFKVPKRVVV 505
Cdd:PRK05620 456 IRSGGEWIYSAQLENYIMA-APEVVECAVIGYPDDKWGERPLAVTVLAPGiepTRETAERLRDQLRDRLPNWMLPEYWTF 534
|
570
....*....|....*....
gi 1828927390 506 VAELPHTATGKVQRAVIRK 524
Cdd:PRK05620 535 VDEIDKTSVGKFDKKDLRQ 553
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
21-520 |
4.06e-22 |
|
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: 99.08 E-value: 4.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 21 PEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVV 100
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 101 RRGGCKVLIfsgragpidfvalvqrslrsdlergslrtvlvgegVMPGaiswssledavyspaeqralcerraackasDL 180
Cdd:cd17650 81 EDSGAKLLL-----------------------------------TQPE------------------------------DL 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 181 ALIVFTSGTTGRPKGVMHDHSCVRSV----RDRGRLWKVQPgetmlNYLPM----FHLYS--LSEAVLQ--CMYSGCRQV 248
Cdd:cd17650 96 AYVIYTSGTTGKPKGVMVEHRNVAHAahawRREYELDSFPV-----RLLQMasfsFDVFAgdFARSLLNggTLVICPDEV 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 249 VMETfdaNTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRFGTLPSGLETSAAIAVQVQRVFCPTVT--GAGM 326
Cdd:cd17650 171 KLDP---AALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGMRIinSYGV 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 327 SEswcwmcTC--------AIDEPEELRCHSSGRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAA- 397
Cdd:cd17650 248 TE------ATidstyyeeGRDPLGDSANVPIGRPLPNTAMYVLD-ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAEr 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 398 ----ALDADGWLH-SGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAY 472
Cdd:cd17650 321 fvenPFAPGERMYrTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARH-PAIDEAVVAVREDKGGEARLCAY 399
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1828927390 473 VVlrPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRA 520
Cdd:cd17650 400 VV--AAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRR 445
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
2-520 |
6.75e-22 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 100.12 E-value: 6.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 2 TDKDLPL--LGELPTRAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWR 79
Cdd:PRK10252 451 TAVEIPEttLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVE 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 80 IGAAAVPFNLRYRETDLADVVRRGGCKVLIFSGRagpidfvalvQRSLRSDLERGSLRTVlvgegvmpgaiswssleDAV 159
Cdd:PRK10252 531 AGAAWLPLDTGYPDDRLKMMLEDARPSLLITTAD----------QLPRFADVPDLTSLCY-----------------NAP 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 160 YSPAEQRALceRRAACkaSDLALIVFTSGTTGRPKGVMHDHscvRSVRDRgRLWkvqpgetmlnylpMFHLYSLSEA--V 237
Cdd:PRK10252 584 LAPQGAAPL--QLSQP--HHTAYIIFTSGSTGRPKGVMVGQ---TAIVNR-LLW-------------MQNHYPLTADdvV 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 238 LQ---C------------MYSGCRqVVMETFDAN---TAL-DLIEQKSINILHGFETHYADLLRVQAER--PRNVGSLR- 295
Cdd:PRK10252 643 LQktpCsfdvsvweffwpFIAGAK-LVMAEPEAHrdpLAMqQFFAEYGVTTTHFVPSMLAAFVASLTPEgaRQSCASLRq 721
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 296 -FGT---LPSGL--ETSAAIAVQVQRVFCPTvtGAGMSESWcWMCtcaidEPEELRCHSS-----GRPLPGMEMRLIDpE 364
Cdd:PRK10252 722 vFCSgeaLPADLcrEWQQLTGAPLHNLYGPT--EAAVDVSW-YPA-----FGEELAAVRGssvpiGYPVWNTGLRILD-A 792
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 365 TGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDADGWL------HSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSP 438
Cdd:PRK10252 793 RMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIEL 872
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 439 QGVEQELSELvPDILEVAVI----------GIPEPRLVevpvAYVVLRPGAAATEESIIAACKGKIASFKVPKRVVVVAE 508
Cdd:PRK10252 873 GEIDRAMQAL-PDVEQAVTHacvinqaaatGGDARQLV----GYLVSQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQ 947
|
570
....*....|..
gi 1828927390 509 LPHTATGKVQRA 520
Cdd:PRK10252 948 LPLSANGKLDRK 959
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
15-526 |
9.48e-22 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 98.87 E-value: 9.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 15 RAAAKWPEQKALEWA---TG---AMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAA-AVPF 87
Cdd:PRK10524 61 RHLAKRPEQLALIAVsteTDeerTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIhSVVF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 88 ------NLRYRETDLAdvvrrggcKVLIFSGRAG-----PIDFVALVQRSLRSdLERGSLRTVLVGEGVMPGAisWSSLE 156
Cdd:PRK10524 141 ggfashSLAARIDDAK--------PVLIVSADAGsrggkVVPYKPLLDEAIAL-AQHKPRHVLLVDRGLAPMA--RVAGR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 157 DAVYSPaEQRALCERRAAC---KASDLALIVFTSGTTGRPKGVMhdhscvrsvRDRG-----------RLWKVQPGETml 222
Cdd:PRK10524 210 DVDYAT-LRAQHLGARVPVewlESNEPSYILYTSGTTGKPKGVQ---------RDTGgyavalatsmdTIFGGKAGET-- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 223 nylpMF----------HLYSLSEAVLqcmySGCRQVVMETF----DANTALDLIEQKSINILHGFETHyADLLRVQAE-- 286
Cdd:PRK10524 278 ----FFcasdigwvvgHSYIVYAPLL----AGMATIMYEGLptrpDAGIWWRIVEKYKVNRMFSAPTA-IRVLKKQDPal 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 287 -RPRNVGSLRFGTL-------PSGLETSAAIAVQVQRVFCPTVTGagmsesWCWMCTCAIDEPEELRCHSSGRPLPGMEM 358
Cdd:PRK10524 349 lRKHDLSSLRALFLagepldePTASWISEALGVPVIDNYWQTETG------WPILAIARGVEDRPTRLGSPGVPMYGYNV 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 359 RLIDPETGKDVPPGMPGEMLFR------CYSVMKG--------YFEdpeataaalDADGWLHSG-DQGVVRPDGSIRFTG 423
Cdd:PRK10524 423 KLLNEVTGEPCGPNEKGVLVIEgplppgCMQTVWGdddrfvktYWS---------LFGRQVYSTfDWGIRDADGYYFILG 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 424 RYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGA--------AATEESIIAACKGKIA 495
Cdd:PRK10524 494 RTDDVINVAGHRLGTREIEESISSH-PAVAEVAVVGVKDALKGQVAVAFVVPKDSDsladrearLALEKEIMALVDSQLG 572
|
570 580 590
....*....|....*....|....*....|.
gi 1828927390 496 SFKVPKRVVVVAELPHTATGKVQRAVIRKTA 526
Cdd:PRK10524 573 AVARPARVWFVSALPKTRSGKLLRRAIQAIA 603
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
17-519 |
1.63e-21 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 99.47 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 17 AAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDL 96
Cdd:PRK05691 2198 AARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERL 2277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 97 ADVVRRGGCKVLIfsgragpidfvalvqrslrsdlergSLRTVLVGEGVMPGAISWSSLED-----AVYSPAEQRALCER 171
Cdd:PRK05691 2278 HYMIEDSGIGLLL-------------------------SDRALFEALGELPAGVARWCLEDdaaalAAYSDAPLPFLSLP 2332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 172 RaackasDLALIVFTSGTTGRPKGVMHDHSCV----RSVRDRgrlWKVQPGETMLnylpmfHLYSL-----SEAVLQCMY 242
Cdd:PRK05691 2333 Q------HQAYLIYTSGSTGKPKGVVVSHGEIamhcQAVIER---FGMRADDCEL------HFYSInfdaaSERLLVPLL 2397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 243 SGCRQVVME--TFDANTALDLIEQKSINILhGFETHY----ADLLRVQAErprnvgslrfgTLPSGLETSAAIAV----- 311
Cdd:PRK05691 2398 CGARVVLRAqgQWGAEEICQLIREQQVSIL-GFTPSYgsqlAQWLAGQGE-----------QLPVRMCITGGEALtgehl 2465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 312 -QVQRVFCPTV--TGAGMSESWCWMCTCAIdePEELRCHSSGRPLP---GMEMRLIDPETGKDVPPGMPGEMLFRCYSVM 385
Cdd:PRK05691 2466 qRIRQAFAPQLffNAYGPTETVVMPLACLA--PEQLEEGAASVPIGrvvGARVAYILDADLALVPQGATGELYVGGAGLA 2543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 386 KGYFEDPEATAAALDADGWLH-------SGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSElVPDILEVAVI 458
Cdd:PRK05691 2544 QGYHDRPGLTAERFVADPFAAdggrlyrTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLE-HPAVREAVVL 2622
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828927390 459 GIPEPRLVEVpVAYVVLRPGA------AATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQR 519
Cdd:PRK05691 2623 ALDTPSGKQL-AGYLVSAVAGqddeaqAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDR 2688
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
441-516 |
1.97e-21 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 87.99 E-value: 1.97e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828927390 441 VEQELSElVPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGK 516
Cdd:pfam13193 2 VESALVS-HPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
21-520 |
2.55e-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: 96.77 E-value: 2.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 21 PEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVV 100
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 101 RRGGCKVLifsgragpidfvaLVQRSLRSDLERGSLRTVLVGEGVMPGAISWSSLEDAvyspaeqralcerraackASDL 180
Cdd:cd17656 82 LDSGVRVV-------------LTQRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINN------------------SDDL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 181 ALIVFTSGTTGRPKGVMHDHscvrsvrdrgrlwkvqpgETMLNYLPMFHLYSL---SEAVLQ---CMYSGCRQVVMETFD 254
Cdd:cd17656 131 LYIIYTSGTTGKPKGVQLEH------------------KNMVNLLHFEREKTNinfSDKVLQfatCSFDVCYQEIFSTLL 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 255 ANTALDLIE---QKSINILHGF-ETHYADLLRVQAERPRNVGSLR--FGTLPSGLETSAAIAVQV------QRVF----C 318
Cdd:cd17656 193 SGGTLYIIReetKRDVEQLFDLvKRHNIEVVFLPVAFLKFIFSERefINRFPTCVKHIITAGEQLvitnefKEMLhehnV 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 319 PTVTGAGMSESWCwMCTCAID-EPEELRCHSSGRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAA 397
Cdd:cd17656 273 HLHNHYGPSETHV-VTTYTINpEAEIPELPPIGKPISNTWIYILD-QEQQLQPQGIVGELYISGASVARGYLNRQELTAE 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 398 ALDADGW------LHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSElVPDILEVAVIGIPEPRLVEVPVA 471
Cdd:cd17656 351 KFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLN-HPGVSEAVVLDKADDKGEKYLCA 429
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1828927390 472 YVVlrPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRA 520
Cdd:cd17656 430 YFV--MEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRK 476
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
34-520 |
4.02e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 96.60 E-value: 4.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 34 SYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLA-------DVVRRGGCK 106
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAvwaedtlRVIGMIGAK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 107 VLIFSGragPIDFVALVqrslrsdLERGSLRTVLVGEGVMPGaiswssledavysPAEQRALCErraackaSDLALIVFT 186
Cdd:PRK07768 111 AVVVGE---PFLAAAPV-------LEEKGIRVLTVADLLAAD-------------PIDPVETGE-------DDLALMQLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 187 SGTTGRPKGVMHDH----SCVRSVRDRGRLWKVQpgETMLNYLPMFHLYSLSEAVLQCMYSGCRQVVMETFD--ANTAL- 259
Cdd:PRK07768 161 SGSTGSPKAVQITHgnlyANAEAMFVAAEFDVET--DVMVSWLPLFHDMGMVGFLTVPMYFGAELVKVTPMDflRDPLLw 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 260 -DLIEQKSINILHGFETHY---ADLLRVQAERPR-NVGSLRF---GTLPSGLETSAAIAVQVQRV-FCPTVTGA--GMSE 328
Cdd:PRK07768 239 aELISKYRGTMTAAPNFAYallARRLRRQAKPGAfDLSSLRFalnGAEPIDPADVEDLLDAGARFgLRPEAILPayGMAE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 329 S---------WCWMCTCAID--------------EPEELRCHSSGRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCYSVM 385
Cdd:PRK07768 319 AtlavsfspcGAGLVVDEVDadllaalrravpatKGNTRRLATLGPPLPGLEVRVVD-EDGQVLPPRGVGVIELRGESVT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 386 KGYFeDPEATAAALDADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSElVPDILE--VAVIGIPEP 463
Cdd:PRK07768 398 PGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAAR-VEGVRPgnAVAVRLDAG 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828927390 464 RLVEvpvAYVVLRPGAAATEESIIAACKGKIASFKV------PKRVVVVA--ELPHTATGKVQRA 520
Cdd:PRK07768 476 HSRE---GFAVAVESNAFEDPAEVRRIRHQVAHEVVaevgvrPRNVVVLGpgSIPKTPSGKLRRA 537
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
34-525 |
7.03e-21 |
|
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: 96.19 E-value: 7.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 34 SYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGA---AAVPfnlryrETDLADVVRRGG---CKV 107
Cdd:cd05943 100 TWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAiwsSCSP------DFGVPGVLDRFGqiePKV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 108 LI------FSGRAGPI-DFVALVQRSLRSDLErgslrTVLVGEGVMPGAI------SWSSLEDAVYSPAEQRALCERraa 174
Cdd:cd05943 174 LFavdaytYNGKRHDVrEKVAELVKGLPSLLA-----VVVVPYTVAAGQPdlskiaKALTLEDFLATGAAGELEFEP--- 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 175 CKASDLALIVFTSGTTGRPKGVMHDH--SCVRSVRDRGRLWKVQPGETMLNYLP----MFH-----LYSLSEAVLqcmYS 243
Cdd:cd05943 246 LPFDHPLYILYSSGTTGLPKCIVHGAggTLLQHLKEHILHCDLRPGDRLFYYTTcgwmMWNwlvsgLAVGATIVL---YD 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 244 GCRQVVmetfDANTALDLIEQKSINILhGFETHYADLLRVQAERPRNVGSLRfgTLPSGLETSAAIAVQVQ--------- 314
Cdd:cd05943 323 GSPFYP----DTNALWDLADEEGITVF-GTSAKYLDALEKAGLKPAETHDLS--SLRTILSTGSPLKPESFdyvydhikp 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 315 RVFCPTVTGaGMSESWCWMCTCAIDE--PEELRChssgrPLPGMEMRLIDPEtGKDVpPGMPGEML----FRCYSVmkGY 388
Cdd:cd05943 396 DVLLASISG-GTDIISCFVGGNPLLPvyRGEIQC-----RGLGMAVEAFDEE-GKPV-WGEKGELVctkpFPSMPV--GF 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 389 FEDPEAT---AAALDADG--WLHsGDQGVVRPDGSIRFTGRYKEMLKvggenvsPQGVEQELSEL------VPDILEVAV 457
Cdd:cd05943 466 WNDPDGSryrAAYFAKYPgvWAH-GDWIEITPRGGVVILGRSDGTLN-------PGGVRIGTAEIyrvvekIPEVEDSLV 537
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828927390 458 IGIPEPRLVEVPVAYVVLRPGAAATEE---SIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRKT 525
Cdd:cd05943 538 VGQEWKDGDERVILFVKLREGVELDDElrkRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKI 608
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
179-461 |
7.78e-21 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 96.04 E-value: 7.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 179 DLALIVFTSGTTGRPKGVMHDHSCVRSvRDRGRLWKVQPGET--MLNYLPMFHLYSLSEAVLQCMYSGCRQV-VMETFDA 255
Cdd:PRK06334 184 DVAVILFTSGTEKLPKGVPLTHANLLA-NQRACLKFFSPKEDdvMMSFLPPFHAYGFNSCTLFPLLSGVPVVfAYNPLYP 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 256 NTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLRFGTLpSGLETSAAIAVQVQRVFcPTVT---GAGMSESWCW 332
Cdd:PRK06334 263 KKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVI-GGDAFKDSLYQEALKTF-PHIQlrqGYGTTECSPV 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 333 MCTCAIDEPEELRChsSGRPLPGMEMRLIDPETGKDVPPGMPGEMLFRCYSVMKGYF-EDPEATAAALDADGWLHSGDQG 411
Cdd:PRK06334 341 ITINTVNSPKHESC--VGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLG 418
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1828927390 412 VVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSE-----LVPDILEVAVIGIP 461
Cdd:PRK06334 419 YVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEgfgqnAADHAGPLVVCGLP 473
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
168-529 |
1.56e-20 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 95.55 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 168 LCERRAACK--ASDLALIVFTSGTTGRPKGVMHDHSC-------VRSVRDrgrlwkVQPGETMLNYLPMFHLYSLSEAVL 238
Cdd:PRK08043 353 LMPRLAQVKqqPEDAALILFTSGSEGHPKGVVHSHKSllanveqIKTIAD------FTPNDRFMSALPLFHSFGLTVGLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 239 QCMYSGCR----------QVVMEtfdantaldLIEQKSINILHGFET---HYADLlrvqaERPRNVGSLRFgtLPSGLET 305
Cdd:PRK08043 427 TPLLTGAEvflypsplhyRIVPE---------LVYDRNCTVLFGTSTflgNYARF-----ANPYDFARLRY--VVAGAEK 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 306 SAAIAVQV-QRVF-CPTVTGAGMSEswcwmctCA----IDEPEELRCHSSGRPLPGMEMRLIDpetgkdvPPGMP--GEM 377
Cdd:PRK08043 491 LQESTKQLwQDKFgLRILEGYGVTE-------CApvvsINVPMAAKPGTVGRILPGMDARLLS-------VPGIEqgGRL 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 378 LFRCYSVMKGYF--EDP---EATAAA-----LDAdGWLHSGDqgVVRPD--GSIRFTGRYKEMLKVGGENVSPQGVEQEL 445
Cdd:PRK08043 557 QLKGPNIMNGYLrvEKPgvlEVPTAEnargeMER-GWYDTGD--IVRFDeqGFVQIQGRAKRFAKIAGEMVSLEMVEQLA 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 446 SELVPDILEVAVIgIPEPRLVEvpvAYVVLRPGAAATEESIIAACKGK-IASFKVPKRVVVVAELPHTATGKVQRAVIRK 524
Cdd:PRK08043 634 LGVSPDKQHATAI-KSDASKGE---ALVLFTTDSELTREKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGKPDFVTLKS 709
|
....*
gi 1828927390 525 TALEA 529
Cdd:PRK08043 710 MVDEP 714
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
15-526 |
2.76e-20 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 94.44 E-value: 2.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 15 RAAAKWPEQKALEW------ATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAA-AVPF 87
Cdd:PRK00174 75 RHLKTRGDKVAIIWegddpgDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVhSVVF 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 88 N------LRYRETDladvvrrGGCKVLIFSG---RAG-PIDFVALVQRSLRSDlerGSLRTVLV----GEGV--MPGA-I 150
Cdd:PRK00174 155 GgfsaeaLADRIID-------AGAKLVITADegvRGGkPIPLKANVDEALANC---PSVEKVIVvrrtGGDVdwVEGRdL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 151 SWSSLEDAV--YSPAEqralcerraACKASDLALIVFTSGTTGRPKGVMHD--------HSCVRSVRDrgrlwkVQPGE- 219
Cdd:PRK00174 225 WWHELVAGAsdECEPE---------PMDAEDPLFILYTSGSTGKPKGVLHTtggylvyaAMTMKYVFD------YKDGDv 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 220 -------------TMLNYLPmfhlysLSEAVLQCMYSGcrqvVMETFDANTALDLIEQKSINILHGFETHYADLLRVQAE 286
Cdd:PRK00174 290 ywctadvgwvtghSYIVYGP------LANGATTLMFEG----VPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 287 RPR--NVGSLR-FGTlpsgletsaaiavqV------------QRVF----CPTVTGAGMSESWCWMCT---CAIDepeeL 344
Cdd:PRK00174 360 HPKkyDLSSLRlLGS--------------VgepinpeawewyYKVVggerCPIVDTWWQTETGGIMITplpGATP----L 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 345 RCHSSGRPLPGMEMRLIDpETGKDVPPGM----------PGEML--------FRcysvmKGYFEDpeataaaldADGWLH 406
Cdd:PRK00174 422 KPGSATRPLPGIQPAVVD-EEGNPLEGGEggnlvikdpwPGMMRtiygdherFV-----KTYFST---------FKGMYF 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 407 SGDqGVVR-PDGSIRFTGRYKEMLKVGGENVSPQGVEqelSELV--PDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATE 483
Cdd:PRK00174 487 TGD-GARRdEDGYYWITGRVDDVLNVSGHRLGTAEIE---SALVahPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSD 562
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1828927390 484 E------SIIAACKGKIASfkvPKRVVVVAELPHTATGKVQRAVIRKTA 526
Cdd:PRK00174 563 ElrkelrNWVRKEIGPIAK---PDVIQFAPGLPKTRSGKIMRRILRKIA 608
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
17-529 |
9.21e-20 |
|
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: 92.49 E-value: 9.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 17 AAKWPEQKAL-------EWATgaMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNL 89
Cdd:cd05921 5 ARQAPDRTWLaeregngGWRR--VTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 90 RY--RETDLA------DVVRRGgckvLIFSGRAGPIdfvalvQRSLRSDLERGSLRTVLVGEGVMPGAISWSSLedAVYS 161
Cdd:cd05921 83 AYslMSQDLAklkhlfELLKPG----LVFAQDAAPF------ARALAAIFPLGTPLVVSRNAVAGRGAISFAEL--AATP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 162 PAEqrALCERRAACKASDLALIVFTSGTTGRPKGVMHDHSCVRSVRDRGR-LWKVQPGE--TMLNYLPMFHLYSLSEAVL 238
Cdd:cd05921 151 PTA--AVDAAFAAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEqTYPFFGEEppVLVDWLPWNHTFGGNHNFN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 239 QCMYSGCRQVV-----METFDANTALDLIEQKSI---NILHGFETHYADLLRVQAERPR---NVGSLRFG--TLPSGL-E 304
Cdd:cd05921 229 LVLYNGGTLYIddgkpMPGGFEETLRNLREISPTvyfNVPAGWEMLVAALEKDEALRRRffkRLKLMFYAgaGLSQDVwD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 305 TSAAIAVQVQRVFCPTVTGAGMSES--WCWMCTcaidEPEElRCHSSGRPLPGMEMRLidpetgkdVPPGMPGEMLFRCY 382
Cdd:cd05921 309 RLQALAVATVGERIPMMAGLGATETapTATFTH----WPTE-RSGLIGLPAPGTELKL--------VPSGGKYEVRVKGP 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 383 SVMKGYFEDPEATAAALDADGWLHSGDQGVV----RPDGSIRFTGRYKEMLKV-GGENVS-----PQGVeQELSELVPDI 452
Cdd:cd05921 376 NVTPGYWRQPELTAQAFDEEGFYCLGDAAKLadpdDPAKGLVFDGRVAEDFKLaSGTWVSvgplrARAV-AACAPLVHDA 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 453 LeVAVIGIPEPRLVEVPVAYVVLR--------PGAAATEESIIAACKGKIASFKVP--------KRVVVVAELPHTATGK 516
Cdd:cd05921 455 V-VAGEDRAEVGALVFPDLLACRRlvglqeasDAEVLRHAKVRAAFRDRLAALNGEatgsssriARALLLDEPPSIDKGE 533
|
570 580
....*....|....*....|..
gi 1828927390 517 V-------QRAVI--RKTALEA 529
Cdd:cd05921 534 ItdkgyinQRAVLerRAALVER 555
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
34-524 |
6.02e-19 |
|
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: 89.41 E-value: 6.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 34 SYAELDARIDRVACGLMRN-GVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLIfsg 112
Cdd:cd05937 7 TYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVI--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 113 ragpidfvalvqrslrsdlergslrtvlvgegvmpgaiswssledavYSPAeqralcerraackasDLALIVFTSGTTGR 192
Cdd:cd05937 84 -----------------------------------------------VDPD---------------DPAILIYTSGTTGL 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 193 PKGV-MHDHSCVRSVRDRGRLWKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQVVMETFDANTAL-DLIEQKSINI- 269
Cdd:cd05937 102 PKAAaISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWkDVRDSGATIIq 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 270 ---------LHGFETHYADLLRVQAE-----RPRNVGSL--RFGtLPSGLETSAA---IAVQVQRVFCPTVTGAGMSESW 330
Cdd:cd05937 182 yvgelcrylLSTPPSPYDRDHKVRVAwgnglRPDIWERFreRFN-VPEIGEFYAAtegVFALTNHNVGDFGAGAIGHHGL 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 331 CWmctcaidepeELRCHSSGRPL---PGMEMRLIDPETG--KDVPPGMPGEMLFRCY----SVMKGYFEDPEATAAAL-- 399
Cdd:cd05937 261 IR----------RWKFENQVVLVkmdPETDDPIRDPKTGfcVRAPVGEPGEMLGRVPfknrEAFQGYLHNEDATESKLvr 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 400 ----DADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSElVPDILEVAVIGipeprlVEVP------ 469
Cdd:cd05937 331 dvfrKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGA-HPDIAEANVYG------VKVPghdgra 403
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 470 -VAYVVLRPGAAATEESIIAA----CKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRK 524
Cdd:cd05937 404 gCAAITLEESSAVPTEFTKSLlaslARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
21-519 |
8.51e-19 |
|
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: 88.77 E-value: 8.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 21 PEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVV 100
Cdd:cd17645 12 PDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 101 RRGGCKVLIfsgragpidfvalvqrslrsdlergslrtvlvgegvmpgaiswssledavyspaeqralcerraaCKASDL 180
Cdd:cd17645 92 ADSSAKILL-----------------------------------------------------------------TNPDDL 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 181 ALIVFTSGTTGRPKGVMHDHscvrsvrdrgrlwkvqpgETMLNYLPMFHLY-SLSEAVLQCMYSGCrqvvmeTFDAnTAL 259
Cdd:cd17645 107 AYVIYTSGSTGLPKGVMIEH------------------HNLVNLCEWHRPYfGVTPADKSLVYASF------SFDA-SAW 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 260 DLIEqksiNILHGFETHYADLLR----VQAERPRNVGSLRFGTLPSGL-ETSAAIAVQVQRVFCP--------------T 320
Cdd:cd17645 162 EIFP----HLTAGAALHVVPSERrldlDALNDYFNQEGITISFLPTGAaEQFMQLDNQSLRVLLTggdklkkierkgykL 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 321 VTGAGMSESWCWMCTCAIDEPEElrCHSSGRPLPGMEMRLIDpETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALD 400
Cdd:cd17645 238 VNNYGPTENTVVATSFEIDKPYA--NIPIGKPIDNTRVYILD-EALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFI 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 401 ADGWL------HSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVV 474
Cdd:cd17645 315 VHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNH-PLIELAAVLAKEDADGRKYLVAYVT 393
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1828927390 475 lrPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQR 519
Cdd:cd17645 394 --APEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDR 436
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
33-409 |
1.29e-18 |
|
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: 89.05 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 33 MSYAELDARIDRVACGL-MRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLifs 111
Cdd:cd17632 68 ITYAELWERVGAVAAAHdPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLL--- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 112 grAGPIDFVALVQRSLrsdLERGSLRTVLVGEGVMPGAISWSSLEDAVYSPAEQ--------------RALCERRAACKA 177
Cdd:cd17632 145 --AVSAEHLDLAVEAV---LEGGTPPRLVVFDHRPEVDAHRAALESARERLAAVgipvttltliavrgRDLPPAPLFRPE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 178 SD---LALIVFTSGTTGRPKGVMHDHSCVRsvrdrgRLWKV--------QPGETMLNYLPMFHLYSLSEAVLQCMYSGCR 246
Cdd:cd17632 220 PDddpLALLIYTSGSTGTPKGAMYTERLVA------TFWLKvssiqdirPPASITLNFMPMSHIAGRISLYGTLARGGTA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 247 QVV----METFDANTAL-------------DLIEQKSINILHGFETHYADLL----RVQAE-RPRNVGslrfGTLPSGLE 304
Cdd:cd17632 294 YFAaasdMSTLFDDLALvrptelflvprvcDMLFQRYQAELDRRSVAGADAEtlaeRVKAElRERVLG----GRLLAAVC 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 305 TSAAIAVQVQrVFCPTVTGAGMSESWCWMCTCAIDEPEELRchssgRPlPGMEMRLID-PETG---KDVPpgMP-GEMLF 379
Cdd:cd17632 370 GSAPLSAEMK-AFMESLLDLDLHDGYGSTEAGAVILDGVIV-----RP-PVLDYKLVDvPELGyfrTDRP--HPrGELLV 440
|
410 420 430
....*....|....*....|....*....|
gi 1828927390 380 RCYSVMKGYFEDPEATAAALDADGWLHSGD 409
Cdd:cd17632 441 KTDTLFPGYYKRPEVTAEVFDEDGFYRTGD 470
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
21-500 |
1.57e-18 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 88.39 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 21 PEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVV 100
Cdd:PRK09029 17 PQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEELL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 101 RRGGckvlifsgragpIDFVALVQRSLRSDLergsLRTVLVGEGVMPGAISWSSledavyspaeQRalcerraackasdL 180
Cdd:PRK09029 97 PSLT------------LDFALVLEGENTFSA----LTSLHLQLVEGAHAVAWQP----------QR-------------L 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 181 ALIVFTSGTTGRPKGVMHDHSC-VRSVRDRGRLWKVQPGETMLNYLPMFHLySLSEAVLQCMYSGCRQVVMETFDANTAL 259
Cdd:PRK09029 138 ATMTLTSGSTGLPKAAVHTAQAhLASAEGVLSLMPFTAQDSWLLSLPLFHV-SGQGIVWRWLYAGATLVVRDKQPLEQAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 260 DLIeqksinilhgfeTHyADLLRVQAER----PRNVGSLRfGTLPSGLETSAAIAVQVQRVFCPTVTGAGMSESWCWMCT 335
Cdd:PRK09029 217 AGC------------TH-ASLVPTQLWRlldnRSEPLSLK-AVLLGGAAIPVELTEQAEQQGIRCWCGYGLTEMASTVCA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 336 CAIDEpeelrcHSS-GRPLPGMEMRLIDpetgkdvppgmpGEMLFRCYSVMKGYFEDPEATaAALDADGWLHSGDQGVVR 414
Cdd:PRK09029 283 KRADG------LAGvGSPLPGREVKLVD------------GEIWLRGASLALGYWRQGQLV-PLVNDEGWFATRDRGEWQ 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 415 pDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAyvVLRPGAAATEESIIAACKGKI 494
Cdd:PRK09029 344 -NGELTILGRLDNLFFSGGEGIQPEEIERVINQH-PLVQQVFVVPVADAEFGQRPVA--VVESDSEAAVVNLAEWLQDKL 419
|
....*.
gi 1828927390 495 ASFKVP 500
Cdd:PRK09029 420 ARFQQP 425
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
318-528 |
5.29e-18 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 86.59 E-value: 5.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 318 CPTVtgaGMSESWCWMCTCaidEPEELRC--HSSGRPLPGMEMRLIDPETGKdvppgmpgeMLFRCYSVMKGYFedPEAt 395
Cdd:PRK07445 258 APTY---GMTETASQIATL---KPDDFLAgnNSSGQVLPHAQITIPANQTGN---------ITIQAQSLALGYY--PQI- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 396 aaaLDADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQEL--SELVPDileVAVIGIPEPRLVEVPVAYV 473
Cdd:PRK07445 320 ---LDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAIlaTGLVQD---VCVLGLPDPHWGEVVTAIY 393
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1828927390 474 VLRPGAAaTEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRKTALE 528
Cdd:PRK07445 394 VPKDPSI-SLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQ 447
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
17-427 |
1.05e-16 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 83.39 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 17 AAKWPEQKAL-------EWATgaMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNL 89
Cdd:PRK08180 49 AQEAPDRVFLaergadgGWRR--LTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 90 RY--RETDLA------DVVRRGgckvLIFSGRAGPidfvalVQRSLRSDLERGslRTVLVGEGVMPG--AISWSSLEDAV 159
Cdd:PRK08180 127 AYslVSQDFGklrhvlELLTPG----LVFADDGAA------FARALAAVVPAD--VEVVAVRGAVPGraATPFAALLATP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 160 YSPAEQRALcerrAACKASDLALIVFTSGTTGRPKGVMHDHSCVRSVRDRGRLWKVQPGET---MLNYLPMFHlyslsea 236
Cdd:PRK08180 195 PTAAVDAAH----AAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEppvLVDWLPWNH------- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 237 vlqcmysgcrqvvmeTFDANTALDLIeqksiniLHGFETHYADllrvqAERP------RNVGSLR------FGTLPSG-- 302
Cdd:PRK08180 264 ---------------TFGGNHNLGIV-------LYNGGTLYID-----DGKPtpggfdETLRNLReisptvYFNVPKGwe 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 303 -----LETSAA-----------------------------IAVQV--QRVfcPTVTGAGMSES--WCWMCTCAIDEPEEL 344
Cdd:PRK08180 317 mlvpaLERDAAlrrrffsrlkllfyagaalsqdvwdrldrVAEATcgERI--RMMTGLGMTETapSATFTTGPLSRAGNI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 345 rchssGRPLPGMEMRLidpetgkdVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDADGWLHSGDQGVV----RPDGSIR 420
Cdd:PRK08180 395 -----GLPAPGCEVKL--------VPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFvdpaDPERGLM 461
|
....*..
gi 1828927390 421 FTGRYKE 427
Cdd:PRK08180 462 FDGRIAE 468
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
10-430 |
1.56e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 82.79 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 10 GELPTRAAAKWPEQKALEWatGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNL 89
Cdd:PRK12582 60 AEAPDRPWLAQREPGHGQW--RKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSP 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 90 RY--------RETDLADVVRRGgckvLIFsgragpIDFVALVQRSLRSdLERGSLRTVLVGegVMPGAISWSSLEDAVYS 161
Cdd:PRK12582 138 AYslmshdhaKLKHLFDLVKPR----VVF------AQSGAPFARALAA-LDLLDVTVVHVT--GPGEGIASIAFADLAAT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 162 PAEQrALCERRAACKASDLALIVFTSGTTGRPKGVMHDH-------SCVRSVRDRGRlwkVQPGETMLNYLPMFHLYSLS 234
Cdd:PRK12582 205 PPTA-AVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQrmmcaniAMQEQLRPREP---DPPPPVSLDWMPWNHTMGGN 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 235 EAVLQCMYSGcrqvvmETF--DANTAL-DLIEQKSINILHGFETHYAD------LLRVQAERP--------RNVGSLRFG 297
Cdd:PRK12582 281 ANFNGLLWGG------GTLyiDDGKPLpGMFEETIRNLREISPTVYGNvpagyaMLAEAMEKDdalrrsffKNLRLMAYG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 298 --TLPSGL-ETSAAIAVQV--QRVfcPTVTGAGMSESWCWMCTCAIDePEelRCHSSGRPLPGMEMRLidpetgkdVPPG 372
Cdd:PRK12582 355 gaTLSDDLyERMQALAVRTtgHRI--PFYTGYGATETAPTTTGTHWD-TE--RVGLIGLPLPGVELKL--------APVG 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828927390 373 MPGEMLFRCYSVMKGYFEDPEATAAALDADGWLHSGDQGVV----RPDGSIRFTGRYKEMLK 430
Cdd:PRK12582 422 DKYEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFvdpdDPEKGLIFDGRVAEDFK 483
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
3-442 |
1.80e-16 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 82.56 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 3 DKDLPLLGELPTRAAAKWPEQKALEW---ATGAM------SYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEA 73
Cdd:PLN02430 38 DSDITTAWDIFSKSVEKYPDNKMLGWrriVDGKVgpymwkTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 74 IFA----------LW-RIGAAAVPFNLRYRETDLAdVVRRGGCKVLIFSGRAGPIDFVALVQRSLRSDLERGSLRTVlvg 142
Cdd:PLN02430 118 MEAcaahslicvpLYdTLGPGAVDYIVDHAEIDFV-FVQDKKIKELLEPDCKSAKRLKAIVSFTSVTEEESDKASQI--- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 143 eGVMPgaISWSS-LEDAVYSPAEQralcerrAACKASDLALIVFTSGTTGRPKGVMHDH----SCVRSVRdrgrLWKVQP 217
Cdd:PLN02430 194 -GVKT--YSWIDfLHMGKENPSET-------NPPKPLDICTIMYTSGTSGDPKGVVLTHeavaTFVRGVD----LFMEQF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 218 GETM------LNYLPMFH-----------------------LYSLSE--------------AVLQCMYSGCRQVVME--- 251
Cdd:PLN02430 260 EDKMthddvyLSFLPLAHildrmieeyffrkgasvgyyhgdLNALRDdlmelkptllagvpRVFERIHEGIQKALQElnp 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 252 ----TFDAntaldLIEQKSINILHGFETHYA----DLLRVQAERPRNVGSLRFgtLPSGletSAAIAVQVQ---RVFCPT 320
Cdd:PLN02430 340 rrrlIFNA-----LYKYKLAWMNRGYSHKKAspmaDFLAFRKVKAKLGGRLRL--LISG---GAPLSTEIEeflRVTSCA 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 321 --VTGAGMSESwCWMCTCAIdePEELrCH--SSGRPLPGMEMRLID-PETGKDvPPGMP--GEMLFRCYSVMKGYFEDPE 393
Cdd:PLN02430 410 fvVQGYGLTET-LGPTTLGF--PDEM-CMlgTVGAPAVYNELRLEEvPEMGYD-PLGEPprGEICVRGKCLFSGYYKNPE 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1828927390 394 ATAAALdADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVG-GENVSPQGVE 442
Cdd:PLN02430 485 LTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSqGEYVALEYLE 533
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
34-448 |
6.64e-16 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 80.83 E-value: 6.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 34 SYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPfnlryretdLADVVRRGGCKVLIFSGR 113
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVP---------LYDTLGAGAVEFIISHSE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 114 AGpidfVALVQRSLRSDLERGS------LRTVLVGEGVMPGAISWS-SLEDAVYSPAEQRALCERRA----ACKASDLAL 182
Cdd:PLN02614 152 VS----IVFVEEKKISELFKTCpnsteyMKTVVSFGGVSREQKEEAeTFGLVIYAWDEFLKLGEGKQydlpIKKKSDICT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 183 IVFTSGTTGRPKGVM-HDHSCVRSVRDRGRLWK-----VQPGETMLNYLPMFHLY--SLSEAVLQC-----MYSGCRQVV 249
Cdd:PLN02614 228 IMYTSGTTGDPKGVMiSNESIVTLIAGVIRLLKsanaaLTVKDVYLSYLPLAHIFdrVIEECFIQHgaaigFWRGDVKLL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 250 MEtfdantalDLIEQK-SI---------NILHGFETHYADLLRVQAERPRNVGSLRFGTLPSG----------------- 302
Cdd:PLN02614 308 IE--------DLGELKpTIfcavprvldRVYSGLQKKLSDGGFLKKFVFDSAFSYKFGNMKKGqshveasplcdklvfnk 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 303 ------------LETSAAIAVQVQ---RVF--CPTVTGAGMSESwcwmctCA---IDEPEEL-RCHSSGRPLPGMEMRLI 361
Cdd:PLN02614 380 vkqglggnvriiLSGAAPLASHVEsflRVVacCHVLQGYGLTES------CAgtfVSLPDELdMLGTVGPPVPNVDIRLE 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 362 D-PETGKDVPPGMP-GEMLFRCYSVMKGYFEDPEATAAALdADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVG-GENVSP 438
Cdd:PLN02614 454 SvPEMEYDALASTPrGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSqGEYVAV 532
|
490
....*....|
gi 1828927390 439 QGVEQELSEL 448
Cdd:PLN02614 533 ENIENIYGEV 542
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
17-519 |
2.18e-15 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 78.78 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 17 AAKWPEQKALEWATGAMSYAELDARIDRVACGLmrNGVNAGDKVGLLVSNG--PEYVEAIFALWRIGAAAVPFNL---RY 91
Cdd:PRK04813 12 AQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFI--DSLKLPDKSPIIVFGHmsPEMLATFLGAVKAGHAYIPVDVsspAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 92 RETDLADVvrrggckvlifsgrAGPidfvALVQRSLRSDLERGSLRTvlvgegvmpgaISWSSLEDAVYSPAEQralcER 171
Cdd:PRK04813 90 RIEMIIEV--------------AKP----SLIIATEELPLEILGIPV-----------ITLDELKDIFATGNPY----DF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 172 RAACKASDLALIVFTSGTTGRPKGVMHDHSCVRSVRDRG-RLWKVQPGETMLNYLPmfhlYS--LS-EAVLQCMYSGCRQ 247
Cdd:PRK04813 137 DHAVKGDDNYYIIFTSGTTGKPKGVQISHDNLVSFTNWMlEDFALPEGPQFLNQAP----YSfdLSvMDLYPTLASGGTL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 248 VVM---ETFDANTALDLIEQKSINI-------------LHGF-ETHYADL---------LRVQ-AERPRNvgslRFgtlP 300
Cdd:PRK04813 213 VALpkdMTANFKQLFETLPQLPINVwvstpsfadmcllDPSFnEEHLPNLthflfcgeeLPHKtAKKLLE----RF---P 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 301 SGL------ETSAAIAV-QVQrvfcptVTgagmseswcwmctcaidePEELRCHSS---GRPLPGMEMrLIDPETGKDVP 370
Cdd:PRK04813 286 SATiyntygPTEATVAVtSIE------IT------------------DEMLDQYKRlpiGYAKPDSPL-LIIDEEGTKLP 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 371 PGMPGEMLFRCYSVMKGYFEDPEATAAAL-DADGW--LHSGDQGVVrPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSE 447
Cdd:PRK04813 341 DGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGYL-EDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQ 419
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828927390 448 lVPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAATEESIIAACK----GKIASFKVPKRVVVVAELPHTATGKVQR 519
Cdd:PRK04813 420 -SSYVESAVVVPYNKDHKVQYLIAYVVPKEEDFEREFELTKAIKkelkERLMEYMIPRKFIYRDSLPLTPNGKIDR 494
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
33-459 |
4.08e-15 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 78.35 E-value: 4.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 33 MSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFA----------LW-RIGAAAVPFNLRYRETDLADVVR 101
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEAcnsqgityvpLYdTLGANAVEFIINHAEVSIAFVQE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 102 RGGCKVLifsgragpiDFVALVQRSLRSDLERGSLRTVLVGEGVMPGAISWSSLEDAVYSPAEqralCERRAACKaSDLA 181
Cdd:PLN02861 158 SKISSIL---------SCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLD----CELPPKQK-TDIC 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 182 LIVFTSGTTGRPKGV-MHDHSCVRSVRDRGRLWKV-----QPGETMLNYLPMFHLYslsEAVLQ--CMYSGCrQVVMETF 253
Cdd:PLN02861 224 TIMYTSGTTGEPKGViLTNRAIIAEVLSTDHLLKVtdrvaTEEDSYFSYLPLAHVY---DQVIEtyCISKGA-SIGFWQG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 254 DANTALDLIEQKSINILHGFETHYADLLRVQAERPRNVGSLR-----------FGTLPSGLETSAAIAVQVQRVF----- 317
Cdd:PLN02861 300 DIRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRkklfdfaynykLGNLRKGLKQEEASPRLDRLVFdkike 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 318 ----------------------------CPTVT-GAGMSESwCWMCTCAIDEPEELrCHSSGRPLPGMEMRLID-PETGK 367
Cdd:PLN02861 380 glggrvrlllsgaaplprhveeflrvtsCSVLSqGYGLTES-CGGCFTSIANVFSM-VGTVGVPMTTIEARLESvPEMGY 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 368 DVPPGMP-GEMLFRCYSVMKGYFEDPEATAAALdADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVG-GENVSPQGVEQEL 445
Cdd:PLN02861 458 DALSDVPrGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSqGEYVAVENLENTY 536
|
490
....*....|....
gi 1828927390 446 SElVPDILEVAVIG 459
Cdd:PLN02861 537 SR-CPLIASIWVYG 549
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
34-255 |
1.22e-14 |
|
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: 76.56 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 34 SYAELDARIDRVACGLMRN-GVNAGDKVGLLVSNGPEYVEAIFALWRIG--AAAVPFNLRYREtdLADVVRRGGCKVLIf 110
Cdd:cd05938 7 TYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGcpVAFLNTNIRSKS--LLHCFRCCGAKVLV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 111 sgrAGPiDFVALVQRSLRSDLERGSLRTVLVGEGVMPGAISWSSLEDAVYSPAEQRALcerRAACKASDLALIVFTSGTT 190
Cdd:cd05938 84 ---VAP-ELQEAVEEVLPALRADGVSVWYLSHTSNTEGVISLLDKVDAASDEPVPASL---RAHVTIKSPALYIYTSGTT 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828927390 191 GRPKGVMHDHSCVRSVRDRGRLWKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQVVMETFDA 255
Cdd:cd05938 157 GLPKAARISHLRVLQCSGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSA 221
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
176-525 |
2.28e-14 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 75.92 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 176 KASDLALIVFTSGTTGRPKGVMHDH-------SCVRSVrdrgrLWKVQPGETMLNYLPMFHLYSLS-EAVLqcMYSGC-- 245
Cdd:PLN02387 248 SPNDIAVIMYTSGSTGLPKGVMMTHgnivatvAGVMTV-----VPKLGKNDVYLAYLPLAHILELAaESVM--AAVGAai 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 246 --------------------------RQVVMETFDAntALDLIE---QKSINILHG-----FETHYADllRVQA------ 285
Cdd:PLN02387 321 gygspltltdtsnkikkgtkgdasalKPTLMTAVPA--ILDRVRdgvRKKVDAKGGlakklFDIAYKR--RLAAiegswf 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 286 -----ERP-------RNV-----GSLRFgtLPSGletSAAIAVQVQRVF-----CPTVTGAGMSEswcwmcTCA---IDE 340
Cdd:PLN02387 397 gawglEKLlwdalvfKKIravlgGRIRF--MLSG---GAPLSGDTQRFIniclgAPIGQGYGLTE------TCAgatFSE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 341 PEELRCHSSGRPLPGMEMRLIDPETG----KDVPpgMP-GEMLFRCYSVMKGYFEDPEATAAALDADG----WLHSGDQG 411
Cdd:PLN02387 466 WDDTSVGRVGPPLPCCYVKLVSWEEGgyliSDKP--MPrGEIVIGGPSVTLGYFKNQEKTDEVYKVDErgmrWFYTGDIG 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 412 VVRPDGSIRFTGRYKEMLKV-GGENVSPQGVEQEL--SELVPDILE---------VAVIgIPEPRLVE-----VPVAYV- 473
Cdd:PLN02387 544 QFHPDGCLEIIDRKKDIVKLqHGEYVSLGKVEAALsvSPYVDNIMVhadpfhsycVALV-VPSQQALEkwakkAGIDYSn 622
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828927390 474 ---VLRPGAAATE--ESIIAACK-GKIASFKVPKRVVVVAEL--PH----TATGKVQRAVIRKT 525
Cdd:PLN02387 623 faeLCEKEEAVKEvqQSLSKAAKaARLEKFEIPAKIKLLPEPwtPEsglvTAALKLKREQIRKK 686
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
13-532 |
6.44e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 75.20 E-value: 6.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 13 PTRAAAKWPEQKalewatgaMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYR 92
Cdd:PRK05691 3734 PQRIAASCLDQQ--------WSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLP 3805
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 93 ETDLADVVRRGGCKVLIFSG--RAGPIDFVALVQRSLRSDLergslrtvLVGEGVMPGAisWSSLEDAVYSPAEqralce 170
Cdd:PRK05691 3806 AQRLQRIIELSRTPVLVCSAacREQARALLDELGCANRPRL--------LVWEEVQAGE--VASHNPGIYSGPD------ 3869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 171 rraackasDLALIVFTSGTTGRPKGVMhdhscvrsVRDRGRLwkvqpgETMLNYLPMFHL-----------YSLSEAVLQ 239
Cdd:PRK05691 3870 --------NLAYVIYTSGSTGLPKGVM--------VEQRGML------NNQLSKVPYLALseadviaqtasQSFDISVWQ 3927
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 240 CMYS---GCRQVVMET---FDANTALDLIEQKSINILHGFETHYADLLrvqAERPRNVGSLRFgTLPSGLETSAAIAVQ- 312
Cdd:PRK05691 3928 FLAAplfGARVEIVPNaiaHDPQGLLAHVQAQGITVLESVPSLIQGML---AEDRQALDGLRW-MLPTGEAMPPELARQw 4003
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 313 VQRVfcPT---VTGAGMSEswcwmCTcaiDEPEELRCHSS---------GRPLPGMEMRLIDpETGKDVPPGMPGEMLFR 380
Cdd:PRK05691 4004 LQRY--PQiglVNAYGPAE-----CS---DDVAFFRVDLAstrgsylpiGSPTDNNRLYLLD-EALELVPLGAVGELCVA 4072
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 381 CYSVMKGYFEDPEATAAAL-----DADG--WLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSElVPDIL 453
Cdd:PRK05691 4073 GTGVGRGYVGDPLRTALAFvphpfGAPGerLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHE-QAEVR 4151
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 454 EVAViGIPEPRLVEVPVAYVVLRPGAAATE---ESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIrkTALEAG 530
Cdd:PRK05691 4152 EAAV-AVQEGVNGKHLVGYLVPHQTVLAQGallERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL--PALDIG 4228
|
..
gi 1828927390 531 LQ 532
Cdd:PRK05691 4229 QL 4230
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
177-530 |
8.70e-14 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 73.65 E-value: 8.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 177 ASDLALIVFTSGTTGRPK-------GVMHDhscVRSVRDRGRLwkVQPGETMLNYLPMFHLYSLSeAVLQCMYSGcrqvv 249
Cdd:PRK05851 151 SGGPAVLQGTAGSTGTPRtailspgAVLSN---LRGLNARVGL--DAATDVGCSWLPLYHDMGLA-FLLTAALAG----- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 250 METFDANTA---------LDLIEQKSINILHGFETHYaDLLRVQAERPRNV--GSLRF---GTLPSGLETSAAIAVQVQR 315
Cdd:PRK05851 220 APLWLAPTTafsaspfrwLSWLSDSRATLTAAPNFAY-NLIGKYARRVSDVdlGALRValnGGEPVDCDGFERFATAMAP 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 316 V-FCP--TVTGAGMSESwcwmcTCAIDEPE----------------ELRCHSS-GRPLPGMEMRLIDPETGKDVPPGMPG 375
Cdd:PRK05851 299 FgFDAgaAAPSYGLAES-----TCAVTVPVpgiglrvdevttddgsGARRHAVlGNPIPGMEVRISPGDGAAGVAGREIG 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 376 EMLFRCYSVMKGYF-EDPeataaaLDADGWLHSGDQGVVrPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSElVPDILE 454
Cdd:PRK05851 374 EIEIRGASMMSGYLgQAP------IDPDDWFPTGDLGYL-VDGGLVVCGRAKELITVAGRNIFPTEIERVAAQ-VRGVRE 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 455 VAVI------GIPEPRLVevpVAYVVLRPGAAATEESIIAackgKIASF--KVPKRVVVVA--ELPHTATGKVQRAVIRK 524
Cdd:PRK05851 446 GAVVavgtgeGSARPGLV---IAAEFRGPDEAGARSEVVQ----RVASEcgVVPSDVVFVApgSLPRTSSGKLRRLAVKR 518
|
....*.
gi 1828927390 525 TaLEAG 530
Cdd:PRK05851 519 S-LEAA 523
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
33-424 |
1.32e-13 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 72.88 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 33 MSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAaaVPfnlryretdladvvrrggckVLIFSG 112
Cdd:cd05910 3 LSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGA--VP--------------------VLIDPG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 113 ragpidfvalvqrslrsdLERGSLRTVLvgegvmpgaiswssledavySPAEQRALCerrAACKASDLALIVFTSGTTGR 192
Cdd:cd05910 61 ------------------MGRKNLKQCL--------------------QEAEPDAFI---GIPKADEPAAILFTSGSTGT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 193 PKGVMHDHSCVRSVRDRGR-LWKVQPGETMlnyLPMFHLYSLSEAVLqcmysGCRQVVME-------TFDANTALDLIEQ 264
Cdd:cd05910 100 PKGVVYRHGTFAAQIDALRqLYGIRPGEVD---LATFPLFALFGPAL-----GLTSVIPDmdptrpaRADPQKLVGAIRQ 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 265 KSINILHGFETHYADLLRVQAERPRNVGSLRfGTLPSGLETSAAIAVQVQRVFCPTV---TGAGMSESwcwMCTCAIDEP 341
Cdd:cd05910 172 YGVSIVFGSPALLERVARYCAQHGITLPSLR-RVLSAGAPVPIALAARLRKMLSDEAeilTPYGATEA---LPVSSIGSR 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 342 EELRCHSS----------GRPLPGMEMRLID------PETG--KDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDADG 403
Cdd:cd05910 248 ELLATTTAatsggagtcvGRPIPGVRVRIIEiddepiAEWDdtLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN 327
|
410 420
....*....|....*....|....*
gi 1828927390 404 ----WLHSGDQGVVRPDGSIRFTGR 424
Cdd:cd05910 328 segfWHRMGDLGYLDDEGRLWFCGR 352
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
182-519 |
1.56e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 72.38 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 182 LIVFTSGTTGRPKGVMHD-HSCVRSVRDRGRLWKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQVVMETFDANTALD 260
Cdd:PRK08308 105 LLQYSSGTTGEPKLIRRSwTEIDREIEAYNEALNCEQDETPIVACPVTHSYGLICGVLAALTRGSKPVIITNKNPKFALN 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 261 LIEQKSINILHGFETHYADLLRVQAERPRNVGSLRFGT-LPSGLETSaaIAVQVQRVFcptvTGAGMSESWCWMCTCAID 339
Cdd:PRK08308 185 ILRNTPQHILYAVPLMLHILGRLLPGTFQFHAVMTSGTpLPEAWFYK--LRERTTYMM----QQYGCSEAGCVSICPDMK 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 340 EPEELrchssGRPLPGMEMrlidpETGKDvpPGMPGEMLFRCysvmkgyfedpeataaaldADGWLHSGDQGVVRPDGSI 419
Cdd:PRK08308 259 SHLDL-----GNPLPHVSV-----SAGSD--ENAPEEIVVKM-------------------GDKEIFTKDLGYKSERGTL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 420 RFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRPGAAAteESIIAACKGKIASFKV 499
Cdd:PRK08308 308 HFMGRMDDVINVSGLNVYPIEVEDVMLRL-PGVQEAVVYRGKDPVAGERVKAKVISHEEIDP--VQLREWCIQHLAPYQV 384
|
330 340
....*....|....*....|
gi 1828927390 500 PKRVVVVAELPHTATGKVQR 519
Cdd:PRK08308 385 PHEIESVTEIPKNANGKVSR 404
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
177-520 |
2.50e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 69.20 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 177 ASDLALIVFTSGTTGRPKGVMHDHSCVRS---------VRDRGRlwKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQ 247
Cdd:PRK05850 159 LPSTAYLQYTSGSTRTPAGVMVSHRNVIAnfeqlmsdyFGDTGG--VPPPDTTVVSWLPFYHDMGLVLGVCAPILGGCPA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 248 VVM--------------------ETFDA--NTALDLIEQKS-------------INILHGFE-THYADLLRVqAERPRnv 291
Cdd:PRK05850 237 VLTspvaflqrparwmqllasnpHAFSAapNFAFELAVRKTsdddmagldlggvLGIISGSErVHPATLKRF-ADRFA-- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 292 gslRFGTLPSGLETSAAIAVQVqrVFCPTVTGAGMSESWCWmctcaidEPEEL------RCHS-SGRPLPGMEM------ 358
Cdd:PRK05850 314 ---PFNLRETAIRPSYGLAEAT--VYVATREPGQPPESVRF-------DYEKLsaghakRCETgGGTPLVSYGSprsptv 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 359 RLIDPETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAAALDA----------DG-WLHSGDQGVVRpDGSIRFTGRYKE 427
Cdd:PRK05850 382 RIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGAtlvdpspgtpEGpWLRTGDLGFIS-EGELFIVGRIKD 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 428 MLKVGGENVSPQGVEQELSELVPDilEVAVIGIPEPRlVEVPVAYVVLRPGAAATEESI--IAACKGKIASfKVPKR--- 502
Cdd:PRK05850 461 LLIVDGRNHYPDDIEATIQEITGG--RVAAISVPDDG-TEKLVAIIELKKRGDSDEEAMdrLRTVKREVTS-AISKShgl 536
|
410 420
....*....|....*....|....
gi 1828927390 503 ----VVVVA--ELPHTATGKVQRA 520
Cdd:PRK05850 537 svadLVLVApgSIPITTSGKIRRA 560
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
183-434 |
2.03e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 63.58 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 183 IVFTSGTTGRPKGVMHD----HSCVRSVRDRGRLWKVQPgETMLNYLPMFHLYSLSEAVLQCMYSGcrQVVMETFDANT- 257
Cdd:PTZ00342 309 IVYTSGTSGKPKGVMLSnknlYNTVVPLCKHSIFKKYNP-KTHLSYLPISHIYERVIAYLSFMLGG--TINIWSKDINYf 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 258 ALDLIEQKSiNILHG----FETHYADLLRVQAERP-------RNVGSLR-------FGTLPSG---------------LE 304
Cdd:PTZ00342 386 SKDIYNSKG-NILAGvpkvFNRIYTNIMTEINNLPplkrflvKKILSLRksnnnggFSKFLEGithisskikdkvnpnLE 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 305 T----SAAIAVQVQRVFC-----PTVTGAGMSESwcwmcTCAI--DEPEELRCHSSGRPL-PGMEMRLIDPET--GKDVP 370
Cdd:PTZ00342 465 VilngGGKLSPKIAEELSvllnvNYYQGYGLTET-----TGPIfvQHADDNNTESIGGPIsPNTKYKVRTWETykATDTL 539
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828927390 371 PgmPGEMLFRCYSVMKGYFEDPEATAAALDADGWLHSGDQGVVRPDGSIRFTGRYKEMLKVG-GE 434
Cdd:PTZ00342 540 P--KGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSqGE 602
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
34-524 |
2.24e-10 |
|
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: 62.83 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 34 SYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIG--AAAVPFNLRyRETdLADVVRRGGCKVLIFs 111
Cdd:cd05939 5 TFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGveTALINSNLR-LES-LLHCITVSKAKALIF- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 112 gragpidfvalvqrSLRSDLergslrtvlvgegvmpgaiswssLEDAVYSPAEQRALcerraacKASDLALIVFTSGTTG 191
Cdd:cd05939 82 --------------NLLDPL-----------------------LTQSSTEPPSQDDV-------NFRDKLFYIYTSGTTG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 192 RPKGVMHDHScvRSVR---DRGRLWKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQVVMETFDA-NTALDLIEQK-S 266
Cdd:cd05939 118 LPKAAVIVHS--RYYRiaaGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSAsNFWDDCVKYNcT 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 267 INILHGFETHYadLL---RVQAERPRNVgSLRFGtlpSGLETSaaIAVQ-VQRVFCPTVTG-AGMSEswcwmCTCAIDEP 341
Cdd:cd05939 196 IVQYIGEICRY--LLaqpPSEEEQKHNV-RLAVG---NGLRPQ--IWEQfVRRFGIPQIGEfYGATE-----GNSSLVNI 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 342 EEL--RCHSSGRPLPGM-EMRLI--DPETG---KD-----VP--PGMPGEMLFRC-----YSVMKGYFeDPEATAAALDA 401
Cdd:cd05939 263 DNHvgACGFNSRILPSVyPIRLIkvDEDTGeliRDsdglcIPcqPGEPGLLVGKIiqndpLRRFDGYV-NEGATNKKIAR 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 402 DGWLH------SGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELVpDILEVAVIGipeprlVEVP------ 469
Cdd:cd05939 342 DVFKKgdsaflSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVL-GLEDVVVYG------VEVPgvegra 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1828927390 470 -VAYVVlRPGAAATEESIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRK 524
Cdd:cd05939 415 gMAAIV-DPERKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
21-531 |
4.29e-10 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 62.45 E-value: 4.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 21 PEQKALEwatgaMSYAELDARIDRVACGLMRNgVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPfnLRYRE----TDL 96
Cdd:PRK12476 62 AAGCAVE-----LTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVP--LFAPElpghAER 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 97 ADVVRRGG--CKVLIFSGRAGPI-DFVALVQRSLRsdlergslrtvlvgegvmPGAISWSSLEDAV---YSPAEqralce 170
Cdd:PRK12476 134 LDTALRDAepTVVLTTTAAAEAVeGFLRNLPRLRR------------------PRVIAIDAIPDSAgesFVPVE------ 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 171 rraaCKASDLALIVFTSGTTGRPKGV--MHDHSCVRSVRDRGRLWKVQPGETMLNYLPMFHLYSLS----EAV------- 237
Cdd:PRK12476 190 ----LDTDDVSHLQYTSGSTRPPVGVeiTHRAVGTNLVQMILSIDLLDRNTHGVSWLPLYHDMGLSmigfPAVygghstl 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 238 -------------LQCMYSGCRQVVMETFDANTALDLIEQKSINIlHGFETHYADLLRVQAERPRNVGSLR-----FGtl 299
Cdd:PRK12476 266 msptafvrrpqrwIKALSEGSRTGRVVTAAPNFAYEWAAQRGLPA-EGDDIDLSNVVLIIGSEPVSIDAVTtfnkaFA-- 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 300 PSGLETSAaiavqvqrvFCPTVtgaGMSESWCWMCTCAID--------EPEEL-RCH---------------SSGRPLPG 355
Cdd:PRK12476 343 PYGLPRTA---------FKPSY---GIAEATLFVATIAPDaepsvvylDREQLgAGRavrvaadapnavahvSCGQVARS 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 356 MEMRLIDPETGKDVPPGMPGEMLFRCYSVMKGYFEDPEAT-----------------AAALDADG-WLHSGDQGVVRpDG 417
Cdd:PRK12476 411 QWAVIVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETertfgaklqsrlaegshADGAADDGtWLRTGDLGVYL-DG 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 418 SIRFTGRYKEMLKVGGENVSPQGVEQELSELVPDILE--VAVIGIP---EPRLVEVPV-AYVVLRPGAAATEESIIAACK 491
Cdd:PRK12476 490 ELYITGRIADLIVIDGRNHYPQDIEATVAEASPMVRRgyVTAFTVPaedNERLVIVAErAAGTSRADPAPAIDAIRAAVS 569
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1828927390 492 GKIASFKVPKRVVVVAELPHTATGKVQRAVIRKTALEAGL 531
Cdd:PRK12476 570 RRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGRL 609
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
34-532 |
3.19e-09 |
|
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: 59.28 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 34 SYAELDARIDRVACGLM-RNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVrrGGCKV-LIFS 111
Cdd:cd05905 16 TWGKLLSRAEKIAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLL--GTCKVrVALT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 112 GRAGPIDFVALVQRSLRSDLergslrtvlvgegvMPGAISWSSLEDAVYSPAEQRALCERRAA---CKASDLALIVFTSG 188
Cdd:cd05905 94 VEACLKGLPKKLLKSKTAAE--------------IAKKKGWPKILDFVKIPKSKRSKLKKWGPhppTRDGDTAYIEYSFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 189 TTGRPKGVMHDHSCVRSVrdrGRLWKVQ----PGETMLNYLPMFHLYSLSEAVLQCMYSG-----CRQVVMETfDANTAL 259
Cdd:cd05905 160 SDGSLSGVAVSHSSLLAH---CRALKEAcelyESRPLVTVLDFKSGLGLWHGCLLSVYSGhhtilIPPELMKT-NPLLWL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 260 DLIEQKSI-------NILHGFETHYADLLRVQAERPRNVGSLRFGTLPSGLETSAAIAVQVQRVF---------CPTVTG 323
Cdd:cd05905 236 QTLSQYKVrdayvklRTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRISSCDSFLKLFqtlglspraVSTEFG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 324 aGMSESW-CWMCTCAID------EPEELR----------------CHSSGRPLPGMEMRLIDPETGKDVPPGMPGE---- 376
Cdd:cd05905 316 -TRVNPFiCWQGTSGPEpsrvylDMRALRhgvvrlderdkpnslpLQDSGKVLPGAQVAIVNPETKGLCKDGEIGEiwvn 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 377 ------MLFRCYSVMKGYFEDPEAT--AAALDADGWLHSGDQGVVRPDGSIR---------FT-GRYKEMLKVGGENVSP 438
Cdd:cd05905 395 spanasGYFLLDGETNDTFKVFPSTrlSTGITNNSYARTGLLGFLRPTKCTDlnveehdllFVvGSIDETLEVRGLRHHP 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 439 QGVEQELSELVPDILEVAVIGIPEpRLVEVPVAYVVLRPGAAATEESIIAACkgkIASFKVPKRVVVVAE---LPHTATG 515
Cdd:cd05905 475 SDIEATVMRVHPYRGRCAVFSITG-LVVVVAEQPPGSEEEALDLVPLVLNAI---LEEHQVIVDCVALVPpgsLPKNPLG 550
|
570
....*....|....*..
gi 1828927390 516 KVQRAVIRKTALEAGLQ 532
Cdd:cd05905 551 EKQRMEIRQAFLAGKLH 567
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
31-526 |
3.30e-09 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 59.53 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 31 GAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLIF 110
Cdd:PLN02654 119 ASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVIT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 111 SG--RAGP--IDFVALVQRSLRSDLERGslrtVLVGEGVMPGAISWSSLEDAVYSPAE----QRALCERRAACK-----A 177
Cdd:PLN02654 199 CNavKRGPktINLKDIVDAALDESAKNG----VSVGICLTYENQLAMKREDTKWQEGRdvwwQDVVPNYPTKCEvewvdA 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 178 SDLALIVFTSGTTGRPKGVMHDHS--CVRSVRDRGRLWKVQPGETMLNYLPMFHLYSLSEAVLQCMYSGCRQVVMETF-- 253
Cdd:PLN02654 275 EDPLFLLYTSGSTGKPKGVLHTTGgyMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGATVLVFEGApn 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 254 --DANTALDLIEQKSINILHGFETHYADLLRVQAE--RPRNVGSLR-FGTLPSGLETSAaiavqvQRVF--------CPT 320
Cdd:PLN02654 355 ypDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEyvTRHSRKSLRvLGSVGEPINPSA------WRWFfnvvgdsrCPI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 321 VTGAGMSESWCWMCTcAIDEPEELRCHSSGRPLPGMEMRLIDpETGKDVPPGMPGEMLFR-----CYSVMKGYFEDPEAT 395
Cdd:PLN02654 429 SDTWWQTETGGFMIT-PLPGAWPQKPGSATFPFFGVQPVIVD-EKGKEIEGECSGYLCVKkswpgAFRTLYGDHERYETT 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 396 AAALDAdGWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEqelSELV--PDILEVAVIGIPEPRLVEVPVAYV 473
Cdd:PLN02654 507 YFKPFA-GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVE---SALVshPQCAEAAVVGIEHEVKGQGIYAFV 582
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1828927390 474 VLRPGAAATEE---SIIAACKGKIASFKVPKRVVVVAELPHTATGKVQRAVIRKTA 526
Cdd:PLN02654 583 TLVEGVPYSEElrkSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIA 638
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
174-524 |
1.12e-08 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 57.47 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 174 ACKASDLALIVFTSGTTGRPKGVMHDHSCV--------RSVRDRGrlwkVQPGETMLNYLPMfHLYS----LSEAvlqCM 241
Cdd:COG1541 79 AVPLEEIVRIHASSGTTGKPTVVGYTRKDLdrwaelfaRSLRAAG----VRPGDRVQNAFGY-GLFTgglgLHYG---AE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 242 YSGCRQVVMETFDANTALDLIEQKSINILHGFETHYADLLRVQAER---PRNVgSLR---FGTLPSGLETSAAIAvqvQR 315
Cdd:COG1541 151 RLGATVIPAGGGNTERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEEgidPRDL-SLKkgiFGGEPWSEEMRKEIE---ER 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 316 VFCPTVTGAGMSESWCWMCTcaidepeELRCHSsgrplpGMEMR-------LIDPETGKDVPPGMPGEMLFrcysvmkgy 388
Cdd:COG1541 227 WGIKAYDIYGLTEVGPGVAY-------ECEAQD------GLHIWedhflveIIDPETGEPVPEGEEGELVV--------- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 389 fedpeaTAaaLDADGW----LHSGDQGVVRPD------GSIRF---TGRYKEMLKVGGENVSPQGVEQELSElVPDILEV 455
Cdd:COG1541 285 ------TT--LTKEAMplirYRTGDLTRLLPEpcpcgrTHPRIgriLGRADDMLIIRGVNVFPSQIEEVLLR-IPEVGPE 355
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828927390 456 AVIGIP-EPRLVEVPVaYVVLRPGA--AATEESIIAACKGKIasfKVPKRVVVVA--ELPHTaTGKVQRaVIRK 524
Cdd:COG1541 356 YQIVVDrEGGLDELTV-RVELAPGAslEALAEAIAAALKAVL---GLRAEVELVEpgSLPRS-EGKAKR-VIDR 423
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
34-517 |
1.39e-08 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 57.10 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 34 SYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVPFNLRYRETDLADVVRRGGCKVLIFSGR 113
Cdd:cd17654 18 SYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 114 agpidfvalvqrslrsdlergslrtvlvgegvmpgaiswsSLEDAVYSPAEQRALCERRAACkasdLALIVFTSGTTGRP 193
Cdd:cd17654 98 ----------------------------------------LDNAPLSFTPEHRHFNIRTDEC----LAYVIHTSGTTGTP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 194 KGVMHDHSCVRSVRDRGR-LWKVQPGETMLNYLPMFHLYSLSEaVLQCMYSGCRQVVMETfdANTALDLIEQKSINILHG 272
Cdd:cd17654 134 KIVAVPHKCILPNIQHFRsLFNITSEDILFLTSPLTFDPSVVE-IFLSLSSGATLLIVPT--SVKVLPSKLADILFKRHR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 273 FETHYAD--LLR---VQAERPRNVG---SLRFGTL-----PSGLETSAAIAV----QVQRVFCPTvtgagmsESWCWMCT 335
Cdd:cd17654 211 ITVLQATptLFRrfgSQSIKSTVLSatsSLRVLALggepfPSLVILSSWRGKgnrtRIFNIYGIT-------EVSCWALA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 336 CAIDEpEELRCHSsGRPLPGMEMRLIDPETGKDVPPGMPGEMLFRCYsvMKGYFEDPEATaaaldadgWLHSGDQgVVRP 415
Cdd:cd17654 284 YKVPE-EDSPVQL-GSPLLGTVIEVRDQNGSEGTGQVFLGGLNRVCI--LDDEVTVPKGT--------MRATGDF-VTVK 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 416 DGSIRFTGRYKEMLKVGGENVSPQGVEQELSELVPdILEVAVIGIPEPRLVevpvAYVVLRPGAAATEESIIaacKGKIA 495
Cdd:cd17654 351 DGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLG-VESCAVTLSDQQRLI----AFIVGESSSSRIHKELQ---LTLLS 422
|
490 500
....*....|....*....|..
gi 1828927390 496 SFKVPKRVVVVAELPHTATGKV 517
Cdd:cd17654 423 SHAIPDTFVQIDKLPLTSHGKV 444
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
9-109 |
1.47e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 57.80 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 9 LGELPTRAAAKWPEQKALEWATGAMSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGAAAVpfn 88
Cdd:PRK07868 449 LGRIIAEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAV--- 525
|
90 100
....*....|....*....|.
gi 1828927390 89 LRYRETDLADVVRRGGCKVLI 109
Cdd:PRK07868 526 LMPPDTDLAAAVRLGGVTEII 546
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
360-531 |
9.62e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 54.74 E-value: 9.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 360 LIDPETGKDVPPGMPGEMLFRCYSVMKGYFEDPEATAA-----------------ALDADGWLHSGDQGVVRpDGSIRFT 422
Cdd:PRK07769 404 IVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAAtfqnilksrlseshaegAPDDALWVRTGDYGVYF-DGELYIT 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 423 GRYKEMLKVGGENVSPQGVEQELSELVPDILE--VAVIGIPEPRLVEVPV--AYVVLR-----------------PGAAA 481
Cdd:PRK07769 483 GRVKDLVIIDGRNHYPQDLEYTAQEATKALRTgyVAAFSVPANQLPQVVFddSHAGLKfdpedtseqlvivaeraPGAHK 562
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1828927390 482 TE-ESIIAACKGKIAS-FKVPKR---VVVVAELPHTATGKVQRAVIRKTALEAGL 531
Cdd:PRK07769 563 LDpQPIADDIRAAIAVrHGVTVRdvlLVPAGSIPRTSSGKIARRACRAAYLDGSL 617
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
403-534 |
1.39e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 54.36 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 403 GWLHSGDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELvPDILEVAVIGIPEPRLVEVPVAYVVLRpgaAAT 482
Cdd:PTZ00237 492 GYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKH-PLVLECCSIGIYDPDCYNVPIGLLVLK---QDQ 567
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828927390 483 EESIIAACKGK----------IASFKVPKRVVVVAELPHTATGKVQRAVIRKTALEAGLQLK 534
Cdd:PTZ00237 568 SNQSIDLNKLKneinniitqdIESLAVLRKIIIVNQLPKTKTGKIPRQIISKFLNDSNYQLP 629
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
33-200 |
2.05e-07 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 53.65 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 33 MSYAELDARIDRVACGLMRNGVNAGDKVGLLVSNGPEYVEAIFALWRIGA---AAVP-FNLRyretdlaDVVRRGG---C 105
Cdd:PRK03584 115 LSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAiwsSCSPdFGVQ-------GVLDRFGqieP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 106 KVLI------FSGRAgpIDFVALVQRsLRSDLerGSLRTVLV--------GEGVMPGAISWssleDAVYSPAEQRAL-CE 170
Cdd:PRK03584 188 KVLIavdgyrYGGKA--FDRRAKVAE-LRAAL--PSLEHVVVvpylgpaaAAAALPGALLW----EDFLAPAEAAELeFE 258
|
170 180 190
....*....|....*....|....*....|.
gi 1828927390 171 RRAAckasDLAL-IVFTSGTTGRPKGVMHDH 200
Cdd:PRK03584 259 PVPF----DHPLwILYSSGTTGLPKCIVHGH 285
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
408-529 |
3.95e-06 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 49.43 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 408 GDQGVVRPDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELVPDILEVAVIGIPEP-----RLVEVPVAYVVLRPGAAAT 482
Cdd:PLN03051 362 GDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACDRAVAGIAETAAVGVAPPdggpeLLVIFLVLGEEKKGFDQAR 441
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1828927390 483 EESIIAACKGKIAS-----FKVpKRVVVVAELPHTATGKVQRAVIRKTALEA 529
Cdd:PLN03051 442 PEALQKKFQEAIQTnlnplFKV-SRVKIVPELPRNASNKLLRRVLRDQLKKE 492
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
404-524 |
1.68e-05 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 47.48 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 404 WLHsGDQGVVRPDGSIRFTGRYKEMLKvggenvsPQGVEQELSEL------VPDILEVAVIGIPEP-RLVEVPVaYVVLR 476
Cdd:PRK03584 500 WRH-GDWIEITEHGGVVIYGRSDATLN-------RGGVRIGTAEIyrqveaLPEVLDSLVIGQEWPdGDVRMPL-FVVLA 570
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1828927390 477 PGAAATEEsIIAACKGKI---ASFK-VPKRVVVVAELPHTATGKVQRAVIRK 524
Cdd:PRK03584 571 EGVTLDDA-LRARIRTTIrtnLSPRhVPDKIIAVPDIPRTLSGKKVELPVKK 621
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
415-535 |
1.64e-04 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 44.30 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828927390 415 PDGSIRFTGRYKEMLKVGGENVSPQGVEQELSELVPDILEVAVIGIPEPRL-VEVPVAYVVLRPGAAATEE------SII 487
Cdd:PLN03052 601 SGGYYRAHGRADDTMNLGGIKVSSVEIERVCNAADESVLETAAIGVPPPGGgPEQLVIAAVLKDPPGSNPDlnelkkIFN 680
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1828927390 488 AACKGKIAS-FKVpKRVVVVAELPHTATGKVQRAVIRKTALEAGLQLKL 535
Cdd:PLN03052 681 SAIQKKLNPlFKV-SAVVIVPSFPRTASNKVMRRVLRQQLAQELSRSKL 728
|
|
| |
