|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
27-589 |
0e+00 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 798.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 27 SYVHGCSTVPLLFETVGDRLRSAVDQVPDKEFLIFKREGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWT 106
Cdd:PRK08315 3 SYVRGPTDVPLLEQTIGQLLDRTAARYPDREALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 107 TTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITPPGFKKSNYYQSIKDILPEVTLKEPGKsgITSRNFTCFQHL 186
Cdd:PRK08315 83 LTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAADGFKDSDYVAMLYELAPELATCEPGQ--LQSARLPELRRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 187 IMFDEEDkiYPGAWKYTDVMKMGTEEDRHHLSKIERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYS 266
Cdd:PRK08315 161 IFLGDEK--HPGMLNFDELLALGRAVDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 267 EKKTIiCIPNPLYHCFGCVMGVLAALTHLQTCVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSI 346
Cdd:PRK08315 239 EEDRL-CIPVPLYHCFGMVLGNLACVTHGATMVYPGEGFDPLATLAAVEEERCTALYGVPTMFIAELDHPDFARFDLSSL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 347 RSGFIAGAPCPITLCRRLVQDMHMTDMQVCYGTTETSPVSFMSTRDDPPEQRIKSVGHIMDHLEAAIVD-KRNCIVPRGV 425
Cdd:PRK08315 318 RTGIMAGSPCPIEVMKRVIDKMHMSEVTIAYGMTETSPVSTQTRTDDPLEKRVTTVGRALPHLEVKIVDpETGETVPRGE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 426 KGEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVED 505
Cdd:PRK08315 398 QGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQD 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 506 VHIVGVPDERFGEVVCAWVRLHESAEgkTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIREMSKIEL 585
Cdd:PRK08315 478 VQVVGVPDEKYGEEVCAWIILRPGAT--LTEEDVRDFCRGKIAHYKIPRYIRFVD--EFPMTVTGKIQKFKMREMMIEEL 553
|
....
gi 71994694 586 GLQQ 589
Cdd:PRK08315 554 GLQA 557
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
27-588 |
0e+00 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 663.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 27 SYVHGCSTVPLLFETVGDRLRSAVDQVPDKEFLIFKREGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWT 106
Cdd:PRK12583 5 SYYQGGGDKPLLTQTIGDAFDATVARFPDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 107 TTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITPPGFKKSNYYQSIKDILPEVTLKEPGKsgITSRNFTCFQHL 186
Cdd:PRK12583 85 LTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADAFKTSDYHAMLQELLPGLAEGQPGA--LACERLPELRGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 187 IMFDEEDKiyPGAWKYTDVMKMGTEEDRHHLSKIERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYS 266
Cdd:PRK12583 163 VSLAPAPP--PGFLAWHELQARGETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 267 EKKTIiCIPNPLYHCFGCVMGVLAALTHLQTCVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSI 346
Cdd:PRK12583 241 EHDRL-CVPVPLYHCFGMVLANLGCMTVGACLVYPNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 347 RSGFIAGAPCPITLCRRLVQDMHMTDMQVCYGTTETSPVSFMSTRDDPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVK 426
Cdd:PRK12583 320 RTGIMAGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSPVSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 427 GEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDV 506
Cdd:PRK12583 400 GELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 507 HIVGVPDERFGEVVCAWVRLHESAegKTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIREMSKIELG 586
Cdd:PRK12583 480 QVFGVPDEKYGEEIVAWVRLHPGH--AASEEELREFCKARIAHFKVPRYFRFVD--EFPMTVTGKVQKFRMREISIEELA 555
|
..
gi 71994694 587 LQ 588
Cdd:PRK12583 556 LP 557
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
226-578 |
0e+00 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 647.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 226 PDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKkTIICIPNPLYHCFGCVMGVLAALTHLQTCVFPAPSF 305
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQ-DRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSPSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 306 DALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCPITLCRRLVQDMHMTDMQVCYGTTETSPV 385
Cdd:cd05917 80 DPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETSPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 386 SFMSTRDDPPEQRIKSVGHIMDHLEAAIVDKRNCIVP-RGVKGEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAV 464
Cdd:cd05917 160 STQTRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 465 MHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAEgkTTEEDIKAWCK 544
Cdd:cd05917 240 MDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAE--LTEEDIKAYCK 317
|
330 340 350
....*....|....*....|....*....|....
gi 71994694 545 GKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIR 578
Cdd:cd05917 318 GKIAHYKVPRYVFFVD--EFPLTVSGKIQKFKLR 349
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
42-580 |
2.28e-160 |
|
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: 466.21 E-value: 2.28e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 42 VGDRLRSAVDQVPDKEFLIFkrEGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVN 121
Cdd:COG0318 1 LADLLRRAAARHPDRPALVF--GGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 122 INPSYQSEELRYAIEKVGIRALITppgfkksnyyqsikdilpevtlkepgksgitsrnftcfqhlimfdeedkiypgawk 201
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVT-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 202 ytdvmkmgteedrhhlskieretqpddsLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKkTIICIPNPLYHC 281
Cdd:COG0318 103 ----------------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPG-DVVLVALPLFHV 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 282 FGCVMGVLAALTHlQTCVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCPITLC 361
Cdd:COG0318 154 FGLTVGLLAPLLA-GATLVLLPRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELL 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 362 RRLVQDMHMtDMQVCYGTTETSPVSFMsTRDDPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYW 441
Cdd:COG0318 233 ERFEERFGV-RIVEGYGLTETSPVVTV-NPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYW 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 442 NSEEQTKKEItQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVC 521
Cdd:COG0318 311 NDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVV 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 71994694 522 AWVRLHESAEgkTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIREM 580
Cdd:COG0318 390 AFVVLRPGAE--LDAEELRAFLRERLARYKVPRRVEFVD--ELPRTASGKIDRRALRER 444
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
41-580 |
1.22e-133 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 400.05 E-value: 1.22e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 41 TVGDRLRSAVDQVPDKEFLIFkrEGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLV 120
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVF--GDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 121 NINPSYQSEELRYAIEKVGIRALITPPGFKKSNYyqSIKDILPEVtlkepgksgitsrnftcfQHLIMF----DEEDKIY 196
Cdd:PRK07656 84 PLNTRYTADEAAYILARGDAKALFVLGLFLGVDY--SATTRLPAL------------------EHVVICeteeDDPHTEK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 197 PGAWkyTDVMKMGTEEDRhhlskiERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIpN 276
Cdd:PRK07656 144 MKTF--TDFLAAGDPAER------APEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAA-N 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 277 PLYHCFGCVMGVLAALTHLQTcVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPC 356
Cdd:PRK07656 215 PFFHVFGYKAGVNAPLMRGAT-ILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 357 PITLCRRLVQDMHMTDMQVCYGTTETSPVSFMSTRDDPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSV 436
Cdd:PRK07656 294 PVALLERFESELGVDIVLTGYGLSEASGVTTFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 437 MRCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERF 516
Cdd:PRK07656 374 MKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERL 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71994694 517 GEVVCAWVRLHESAEgkTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIREM 580
Cdd:PRK07656 454 GEVGKAYVVLKPGAE--LTEEELIAYCREHLAKYKVPRSIEFLD--ELPKNATGKVLKRALREK 513
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
46-484 |
2.83e-126 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 377.81 E-value: 2.83e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 46 LRSAVDQVPDKEFLIFKrEGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPS 125
Cdd:pfam00501 1 LERQAARTPDKTALEVG-EGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 126 YQSEELRYAIEKVGIRALITPPGFKksnyyqsIKDILPEVTLKEPGKSGITSrnftcfqHLIMFDEEDKIYpgawkytdv 205
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDALK-------LEELLEALGKLEVVKLVLVL-------DRDPVLKEEPLP--------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 206 mkmGTEEDRHHLSKIERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEK---KTIICIPNPLYHCF 282
Cdd:pfam00501 137 ---EEAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGlgpDDRVLSTLPLFHDF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 283 GCVMGVLAALTHLQTCVF--PAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCPITL 360
Cdd:pfam00501 214 GLSLGLLGPLLAGATVVLppGFPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPEL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 361 CRRLVQDMHMTdMQVCYGTTETSPVSFMSTRDDPPEQRIKSVGHIMDHLEAAIVD-KRNCIVPRGVKGEVIVRGYSVMRC 439
Cdd:pfam00501 294 ARRFRELFGGA-LVNGYGLTETTGVVTTPLPLDEDLRSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKG 372
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 71994694 440 YWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRG 484
Cdd:pfam00501 373 YLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
42-578 |
2.91e-115 |
|
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: 351.09 E-value: 2.91e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 42 VGDRLRSAVDQVPDKEFLIFKREGIrkTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVN 121
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKL--TYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 122 INPSYQSEELRYAIEKVGIRALITPPGFkksnyyqsikdilpevtlkepgksgitsrnftcfqhlimfdeedkiypgawk 201
Cdd:cd05936 79 LNPLYTPRELEHILNDSGAKALIVAVSF---------------------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 202 yTDVMKMGTEEDRhhlskiERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAG--YSEKKTIICIPnPLY 279
Cdd:cd05936 107 -TDLLAAGAPLGE------RVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEdlLEGDDVVLAAL-PLF 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 280 HCFGCVMGVLAALtHLQTCVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCPIT 359
Cdd:cd05936 179 HVFGLTVALLLPL-ALGATIVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVE 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 360 LCRRLVQdmhMTDMQVC--YGTTETSPVSFMSTRDDPpeQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVM 437
Cdd:cd05936 258 VAERFEE---LTGVPIVegYGLTETSPVVAVNPLDGP--RKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVM 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 438 RCYWNSEEQTKKEITqDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFG 517
Cdd:cd05936 333 KGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSG 411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71994694 518 EVVCAWVRLHESAegKTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIR 578
Cdd:cd05936 412 EAVKAFVVLKEGA--SLTEEEIIAFCREQLAGYKVPRQVEFRD--ELPKSAVGKILRRELR 468
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
46-574 |
2.29e-108 |
|
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: 332.27 E-value: 2.29e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 46 LRSAVDQVPDKEFLIFkrEGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPS 125
Cdd:cd17631 1 LRRRARRHPDRTALVF--GGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 126 YQSEELRYAIEKVGIRALItppgfkksnyyqsikdilpevtlkepgksgitsrnftcfqhlimfdeedkiypgawkytdv 205
Cdd:cd17631 79 LTPPEVAYILADSGAKVLF------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 206 mkmgteedrhhlskieretqpDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICiPNPLYHCFGCV 285
Cdd:cd17631 98 ---------------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLV-VAPLFHIGGLG 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 286 MGVLAALtHLQTCVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCPITLCRRLv 365
Cdd:cd17631 156 VFTLPTL-LRGGTVVILRKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRAL- 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 366 QDMHmTDMQVCYGTTETSPVSFMSTRDDPpEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEE 445
Cdd:cd17631 234 QARG-VKFVQGYGMTETSPGVTFLSPEDH-RRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPE 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 446 QTKKEItQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVR 525
Cdd:cd17631 312 ATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVV 390
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 71994694 526 LHESAEgkTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKK 574
Cdd:cd17631 391 PRPGAE--LDEDELIAHCRERLARYKIPKSVEFVD--ALPRNATGKILK 435
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
228-573 |
2.53e-107 |
|
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: 326.16 E-value: 2.53e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 228 DSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICiPNPLYHCFGcVMGVLAALTHLQTCVFPaPSFDA 307
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLS-TLPLFHIGG-LFGLLGALLAGGTVVLL-PKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 308 LAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCPITLCRRLVQDMHMTDMQVcYGTTETSPVSF 387
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNG-YGLTETGGTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 388 MSTRDDPPEqRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKkEITQDRWYHTGDIAVMHD 467
Cdd:cd04433 157 TGPPDDDAR-KPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATA-AVDEDGWYRTGDLGRLDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 468 NGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAEGktTEEDIKAWCKGKI 547
Cdd:cd04433 235 DGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADL--DAEELRAHVRERL 312
|
330 340
....*....|....*....|....*.
gi 71994694 548 AHFKIPRYILFKKeyEFPLTVTGKVK 573
Cdd:cd04433 313 APYKVPRRVVFVD--ALPRTASGKID 336
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
41-580 |
1.60e-103 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 322.91 E-value: 1.60e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 41 TVGDRLRSAVDQVPDKEflIFKREGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLV 120
Cdd:PRK06187 7 TIGRILRHGARKHPDKE--AVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 121 NINPSYQSEELRYAIEKVGIRALITPPGFKKSnyYQSIKDILPEVtlkepgksgitsrnftcfQHLIMFDEEDKIYPG-- 198
Cdd:PRK06187 85 PINIRLKPEEIAYILNDAEDRVVLVDSEFVPL--LAAILPQLPTV------------------RTVIVEGDGPAAPLApe 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 199 AWKYTDVMKMGTEEDRHHlskierETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIpNPL 278
Cdd:PRK06187 145 VGEYEELLAAASDTFDFP------DIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVI-VPM 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 279 YHCFG---CVMGVLAALTHlqtcVFPApSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAP 355
Cdd:PRK06187 218 FHVHAwglPYLALMAGAKQ----VIPR-RFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 356 CPITLCRRLVQDMHMTDMQVcYGTTETSPVSFMSTrddPPEQ------RIKSVGHIMDHLEAAIVDKRNCIVPRGVK--G 427
Cdd:PRK06187 293 LPPALLREFKEKFGIDLVQG-YGMTETSPVVSVLP---PEDQlpgqwtKRRSAGRPLPGVEARIVDDDGDELPPDGGevG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 428 EVIVRGYSVMRCYWNSEEQTKKEITQDrWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVH 507
Cdd:PRK06187 369 EIIVRGPWLMQGYWNRPEATAETIDGG-WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVA 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71994694 508 IVGVPDERFGEVVCAWVRLHESAEgkTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIREM 580
Cdd:PRK06187 448 VIGVPDEKWGERPVAVVVLKPGAT--LDAKELRAFLRGRLAKFKLPKRIAFVD--ELPRTSVGKILKRVLREQ 516
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
69-572 |
7.65e-90 |
|
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: 286.03 E-value: 7.65e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 69 TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITPPG 148
Cdd:cd05911 12 TYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDPD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 149 FkksnyYQSIKDILpevtlkepgksgitsRNFTCFQHLIMFDEEDKIYPGAWKYTDVMKMGTEEDRhhlsKIERETQPDD 228
Cdd:cd05911 92 G-----LEKVKEAA---------------KELGPKDKIIVLDDKPDGVLSIEDLLSPTLGEEDEDL----PPPLKDGKDD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 229 SLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYS-EKKTIICIPNPLYHCFGCVMGVLAALthLQTCVFPAPSFDA 307
Cdd:cd05911 148 TAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGNdGSNDVILGFLPLYHIYGLFTTLASLL--NGATVIIMPKFDS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 308 LAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCPITLCRRLVQDMHMTDMQVCYGTTETSPVSF 387
Cdd:cd05911 226 ELFLDLIEKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 388 MSTRDDppeQRIKSVGHIMDHLEAAIVDKR-NCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMH 466
Cdd:cd05911 306 VNPDGD---DKPGSVGRLLPNVEAKIVDDDgKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFD 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 467 DNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAegKTTEEDIKAWCKGK 546
Cdd:cd05911 383 EDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGE--KLTEKEVKDYVAKK 460
|
490 500 510
....*....|....*....|....*....|....
gi 71994694 547 IAHFK--------IPryilfkkeyEFPLTVTGKV 572
Cdd:cd05911 461 VASYKqlrggvvfVD---------EIPKSASGKI 485
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
41-579 |
3.93e-89 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 285.29 E-value: 3.93e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 41 TVGDRLRSAVDQVPDKEFLIFkrEGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLV 120
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALVF--GDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 121 NINPSYQSEELRYAIEKVGIRALITPPGFKKSnyYQSIKDILPEVTLKEPGKSGITSrnftcfqhlimfdeedkiYPGAW 200
Cdd:PRK08316 90 PVNFMLTGEELAYILDHSGARAFLVDPALAPT--AEAALALLPVDTLILSLVLGGRE------------------APGGW 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 201 kyTDVMKMGTEEDRHHLSKIEREtqpDDSLNIQYTSGTTGQPKGATLTHHNVLnnAFFVG--LRAGYS-EKKTIICIPnp 277
Cdd:PRK08316 150 --LDFADWAEAGSVAEPDVELAD---DDLAQILYTSGTESLPKGAMLTHRALI--AEYVSciVAGDMSaDDIPLHALP-- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 278 LYHCFGcvMGVLAaLTHLQ----TCVFPAPSFDALaaLQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAG 353
Cdd:PRK08316 221 LYHCAQ--LDVFL-GPYLYvgatNVILDAPDPELI--LRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 354 APCPITLCRRLVQdmHMTDMQV--CYGTTETSPVSfmsTRDDPPEQ--RIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEV 429
Cdd:PRK08316 296 SIMPVEVLKELRE--RLPGLRFynCYGQTEIAPLA---TVLGPEEHlrRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEI 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 430 IVRGYSVMRCYWNSEEQTKkEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIV 509
Cdd:PRK08316 371 VHRSPQLMLGYWDDPEKTA-EAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVI 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 510 GVPDERFGEVVCAWVRLHESAEgkTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIRE 579
Cdd:PRK08316 450 GLPDPKWIEAVTAVVVPKAGAT--VTEDELIAHCRARLAGFKVPKRVIFVD--ELPRNPSGKILKRELRE 515
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
54-582 |
1.43e-87 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 280.59 E-value: 1.43e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 54 PDKEFLIFKREGIrkTYSQVATDAENLACGLLH-LGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELR 132
Cdd:PRK06839 16 PDRIAIITEEEEM--TYKQLHEYVSKVAAYLIYeLNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 133 YAIEKVGIRALITPPGFkkSNYYQSIKdilpevtlkepGKSGItsrnftcfQHLImfdeedkiypgawKYTDVmkmgTEE 212
Cdd:PRK06839 94 FQLKDSGTTVLFVEKTF--QNMALSMQ-----------KVSYV--------QRVI-------------SITSL----KEI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 213 DRHHLSKIErETQPDDSLNIQYTSGTTGQPKGATLTHHNV----LNNAFFVGLRAgysEKKTIICIPnpLYHCFGCVMGV 288
Cdd:PRK06839 136 EDRKIDNFV-EKNESASFIICYTSGTTGKPKGAVLTQENMfwnaLNNTFAIDLTM---HDRSIVLLP--LFHIGGIGLFA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 289 LAALTHLQTCVFPApSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCPITLCRRLvQDM 368
Cdd:PRK06839 210 FPTLFAGGVIIVPR-KFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREF-IDR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 369 HMTDMQvCYGTTETSPVSFMSTRDDPpEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTK 448
Cdd:PRK06839 288 GFLFGQ-GFGMTETSPTVFMLSEEDA-RRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 449 KEItQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHE 528
Cdd:PRK06839 366 ETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKS 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 71994694 529 SAegKTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIREMSK 582
Cdd:PRK06839 445 SS--VLIEKDVIEHCRLFLAKYKIPKEIVFLK--ELPKNATGKIQKAQLVNQLK 494
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
41-588 |
1.66e-86 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 279.32 E-value: 1.66e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 41 TVGDRLRSAVDQVPDKEFLIFKReGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLV 120
Cdd:PRK06087 24 SLADYWQQTARAMPDKIAVVDNH-GASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 121 NINPSYQSEELRYAIEKVGIRALITPPGFKKSNYyqsIKDILPevtLKEPGKSgitsrnftcFQHLIMFDeedkiypgaw 200
Cdd:PRK06087 103 PLLPSWREAELVWVLNKCQAKMFFAPTLFKQTRP---VDLILP---LQNQLPQ---------LQQIVGVD---------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 201 kytdvmKMGTEEDRHHLSKIERETQP---------DDSLNIQYTSGTTGQPKGATLTHHNVL--NNAFFVGLRAGYSEkk 269
Cdd:PRK06087 158 ------KLAPATSSLSLSQIIADYEPlttaitthgDELAAVLFTSGTEGLPKGVMLTHNNILasERAYCARLNLTWQD-- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 270 tIICIPNPLYHCFGCVMGVLAALTHLQTCVFpAPSFDALAALQAIHEEKCTALYG-TPtmFI-DMINHPEYANYNYDSIR 347
Cdd:PRK06087 230 -VFMMPAPLGHATGFLHGVTAPFLIGARSVL-LDIFTPDACLALLEQQRCTCMLGaTP--FIyDLLNLLEKQPADLSALR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 348 SGFIAGAPCPitlcRRLVQDMHMTDMQVC--YGTTETSPVSFMSTrDDPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGV 425
Cdd:PRK06087 306 FFLCGGTTIP----KKVARECQQRGIKLLsvYGSTESSPHAVVNL-DDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGC 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 426 KGEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVED 505
Cdd:PRK06087 381 EGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 506 VHIVGVPDERFGEVVCAWVRLHESAEGKTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIREMSKIEL 585
Cdd:PRK06087 461 ACVVAMPDERLGERSCAYVVLKAPHHSLTLEEVVAFFSRKRVAKYKYPEHIVVID--KLPRTASGKIQKFLLRKDIMRRL 538
|
...
gi 71994694 586 GLQ 588
Cdd:PRK06087 539 TQD 541
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
228-574 |
4.73e-83 |
|
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: 263.21 E-value: 4.73e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 228 DSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIpNPLYHCFGCVMGVLAALTHLQTcVFPAPSFDA 307
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLII-NPFFHTFGYKAGIVACLLTGAT-VVPVAVFDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 308 LAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCPITLCRRLVQDMHMTDMQVCYGTTETSPVSf 387
Cdd:cd17638 79 DAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGVAT- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 388 MSTRDDPPEQRIKSVGHIMDHLEAAIVDKrncivprgvkGEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHD 467
Cdd:cd17638 158 MCRPGDDAETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 468 NGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLhesAEGKT-TEEDIKAWCKGK 546
Cdd:cd17638 228 RGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVA---RPGVTlTEEDVIAWCRER 304
|
330 340
....*....|....*....|....*...
gi 71994694 547 IAHFKIPRYILFKKeyEFPLTVTGKVKK 574
Cdd:cd17638 305 LANYKVPRFVRFLD--ELPRNASGKVMK 330
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
54-579 |
9.40e-83 |
|
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: 267.64 E-value: 9.40e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 54 PDKEFLIFKREGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRY 133
Cdd:cd05926 1 PDAPALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 134 AIEKVGIRALITPPGfkkSNYYQSIKDILPEVTLKEPGksgitsrnftcfqhlimFDeedkiYPGAWKYTDVMKMGTEED 213
Cdd:cd05926 81 YLADLGSKLVLTPKG---ELGPASRAASKLGLAILELA-----------------LD-----VGVLIRAPSAESLSNLLA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 214 RHHLSKIERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAffVGLRAGY--SEKKTIICIpNPLYHCFGCVMGVLAA 291
Cdd:cd05926 136 DKKNAKSEGVPLPDDLALILHTSGTTGRPKGVPLTHRNLAASA--TNITNTYklTPDDRTLVV-MPLFHVHGLVASLLST 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 292 LTHLQTCVFPaPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDS----IRSgfiAGAPCPITLCRRLVQD 367
Cdd:cd05926 213 LAAGGSVVLP-PRFSASTFWPDVRDYNATWYTAVPTIHQILLNRPEPNPESPPPklrfIRS---CSASLPPAVLEALEAT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 368 MHMTDMQVcYGTTETSPVsfMSTRDDPPEQR-IKSVGhIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQ 446
Cdd:cd05926 289 FGAPVLEA-YGMTEAAHQ--MTSNPLPPGPRkPGSVG-KPVGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 447 TKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRL 526
Cdd:cd05926 365 NAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVL 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 71994694 527 HESAegKTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIRE 579
Cdd:cd05926 445 REGA--SVTEEELRAFCRKHLAAFKVPKKVYFVD--ELPKTATGKIQRRKVAE 493
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
67-579 |
7.16e-81 |
|
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: 261.16 E-value: 7.16e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 67 RKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITP 146
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 147 PGFKKSNYyqsikdilpevtlkepgksgitsrnftcfqhlimfdeedkiypgawkytdvmkmgteedrhhlskierETQP 226
Cdd:cd05903 81 ERFRQFDP--------------------------------------------------------------------AAMP 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 227 DDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIIcIPNPLYHCFGCVMGVLAAL-----THLQTcvfp 301
Cdd:cd05903 93 DAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFL-VASPMAHQTGFVYGFTLPLllgapVVLQD---- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 302 apSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCPITLCRRLVQDMhmtDMQVC--YGT 379
Cdd:cd05903 168 --IWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELL---GAKVCsaYGS 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 380 TETsPVSFMSTRDDPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEItQDRWYHT 459
Cdd:cd05903 243 TEC-PGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAA-PEGWFRT 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 460 GDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAEgkTTEEDI 539
Cdd:cd05903 321 GDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGAL--LTFDEL 398
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 71994694 540 KAWCKGK-IAHFKIPRYILFKKeyEFPLTVTGKVKKFEIRE 579
Cdd:cd05903 399 VAYLDRQgVAKQYWPERLVHVD--DLPRTPSGKVQKFRLRE 437
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
36-579 |
1.55e-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: 253.76 E-value: 1.55e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 36 PLLFetvgdrLRSAVDQVPDKEFLIFkrEGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALA 115
Cdd:cd12118 6 PLSF------LERAAAVYPDRTSIVY--GDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 116 GMVLVNINPSYQSEELRYAIEKVGIRALITppgfkksnyyqsikdilpevtlkepgksgitsrnftcfqhlimfDEEdki 195
Cdd:cd12118 78 GAVLNALNTRLDAEEIAFILRHSEAKVLFV--------------------------------------------DRE--- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 196 ypgaWKYTDVMKMGTEEdrhhlSKIERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIp 275
Cdd:cd12118 111 ----FEYEDLLAEGDPD-----FEWIPPADEWDPIALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWT- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 276 NPLYHCFG-CVMGVLAALTHLQTCVfpaPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGA 354
Cdd:cd12118 181 LPMFHCNGwCFPWTVAAVGGTNVCL---RKVDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGA 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 355 PCPITLCRRlVQDMHMTDMQVcYGTTETS-PVSFMSTRDD----PPEQRIKS-----VGHIMdHLEAAIVDKRNCI-VPR 423
Cdd:cd12118 258 PPPAAVLAK-MEELGFDVTHV-YGLTETYgPATVCAWKPEwdelPTEERARLkarqgVRYVG-LEEVDVLDPETMKpVPR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 424 GVK--GEVIVRGYSVMRCYWNSEEQTKkEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQ 501
Cdd:cd12118 335 DGKtiGEIVFRGNIVMKGYLKNPEATA-EAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHP 413
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71994694 502 SVEDVHIVGVPDERFGEVVCAWVRLHESAegKTTEEDIKAWCKGKIAHFKIPRYILFKkeyEFPLTVTGKVKKFEIRE 579
Cdd:cd12118 414 AVLEAAVVARPDEKWGEVPCAFVELKEGA--KVTEEEIIAFCREHLAGFMVPKTVVFG---ELPKTSTGKIQKFVLRD 486
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
44-572 |
1.42e-76 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 252.96 E-value: 1.42e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 44 DRLRSAVDQVPDKEFLIFKreGIRKTYSQVATDAENLAcGLLH--LGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVN 121
Cdd:PRK08314 14 HNLEVSARRYPDKTAIVFY--GRAISYRELLEEAERLA-GYLQqeCGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 122 INPSYQSEELRYAIEKVGIRALITPpgfkksnyyqsiKDILPEVtLKEPGKSGItsrnftcfQHLI------MFDEEDKI 195
Cdd:PRK08314 91 VNPMNREEELAHYVTDSGARVAIVG------------SELAPKV-APAVGNLRL--------RHVIvaqysdYLPAEPEI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 196 YPGAW----------KYTDVMKMgTEEDRHHLSKIERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGL-RAG 264
Cdd:PRK08314 150 AVPAWlraepplqalAPGGVVAW-KEALAAGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLwSNS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 265 YSEKKTIICIPnpLYHCFGCVMGVLAALTHLQTCVFpAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYD 344
Cdd:PRK08314 229 TPESVVLAVLP--LFHVTGMVHSMNAPIYAGATVVL-MPRWDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 345 SIRSGFIAGAPCPITLCRRLvQDMHMTDMQVCYGTTETSPVSFMSTRDDPPEQ--RIKSVGhimdhLEAAIVDKRNCI-V 421
Cdd:PRK08314 306 SLRYIGGGGAAMPEAVAERL-KELTGLDYVEGYGLTETMAQTHSNPPDRPKLQclGIPTFG-----VDARVIDPETLEeL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 422 PRGVKGEVIVRGYSVMRCYWNSEEQTKK---EITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLF 498
Cdd:PRK08314 380 PPGEVGEIVVHGPQVFKGYWNRPEATAEafiEIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLY 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71994694 499 KHQSVEDVHIVGVPDERFGEVVCAWVRLHESAEGKTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKV 572
Cdd:PRK08314 460 KHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTTEEEIIAWAREHMAAYKYPRIVEFVD--SLPKSGSGKI 531
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
40-580 |
4.24e-76 |
|
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: 251.60 E-value: 4.24e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 40 ETVGDRLRSAVDQVPDKEFLIFkrEGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVL 119
Cdd:COG1021 25 ETLGDLLRRRAERHPDRIAVVD--GERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 120 VNINPSYQSEELRYAIEKVGIRALITP---PGFKKSNYYQSIKDILPEVtlkepgksgitsrnftcfQHLIMFDEEDKIY 196
Cdd:COG1021 103 VFALPAHRRAEISHFAEQSEAVAYIIPdrhRGFDYRALARELQAEVPSL------------------RHVLVVGDAGEFT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 197 PgawkYTDVMkmgteedRHHLSKIERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAffvglRA-----GYSEKKTI 271
Cdd:COG1021 165 S----LDALL-------AAPADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSV-----RAsaeicGLDADTVY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 272 ICIPnPLYHCFG-CVMGVLAALtHLQTCVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGF 350
Cdd:COG1021 229 LAAL-PAAHNFPlSSPGVLGVL-YAGGTVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 351 IAGAPCPITLCRRLVQDMHMTDMQVcYGTTEtSPVSFmsTR-DDPPEQRIKSVGH-IMDHLEAAIVDKRNCIVPRGVKGE 428
Cdd:COG1021 307 VGGAKLSPELARRVRPALGCTLQQV-FGMAE-GLVNY--TRlDDPEEVILTTQGRpISPDDEVRIVDEDGNPVPPGEVGE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 429 VIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHI 508
Cdd:COG1021 383 LLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAV 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71994694 509 VGVPDERFGEVVCAWVRLHESAegkTTEEDIKAWCKGK-IAHFKIPRYILFKKeyEFPLTVTGKVKKFEIREM 580
Cdd:COG1021 463 VAMPDEYLGERSCAFVVPRGEP---LTLAELRRFLRERgLAAFKLPDRLEFVD--ALPLTAVGKIDKKALRAA 530
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
40-572 |
6.01e-76 |
|
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: 250.12 E-value: 6.01e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 40 ETVGDRLRSAVDQVPDKEFLIFKREGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVL 119
Cdd:cd05923 1 QTVFEMLRRAASRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 120 VNINPSYQSEELRYAIEKVGIRALITPPGfkksnyyqsikdilpevtlkepgkSGITSRNFTCFQHLIMFDEEDkiypga 199
Cdd:cd05923 81 ALINPRLKAAELAELIERGEMTAAVIAVD------------------------AQVMDAIFQSGVRVLALSDLV------ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 200 wkytdvmkmGTEEDRHHLSKIE-RETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGY---SEKKTIICIP 275
Cdd:cd05923 131 ---------GLGEPESAGPLIEdPPREPEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLrhgRHNVVLGLMP 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 276 npLYHCFGcVMGVLAALTHLQTCVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAP 355
Cdd:cd05923 202 --LYHVIG-FFAVLVAALALDGTYVVVEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGAT 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 356 CPITLCRRLVQdmHMTDMQV-CYGTTETSPVSFMstRDDPPEQRIKSvGHIMDHLEAAIVDKRNCIVPRGVKGEVIVR-- 432
Cdd:cd05923 279 MPDAVLERVNQ--HLPGEKVnIYGTTEAMNSLYM--RDARTGTEMRP-GFFSEVRIVRIGGSPDEALANGEEGELIVAaa 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 433 GYSVMRCYWNSEEQTKKEItQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVP 512
Cdd:cd05923 354 ADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVA 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71994694 513 DERFGEVVCAWVRLHesaEGKTTEEDIKAWCK-GKIAHFKIPRYILFKKeyEFPLTVTGKV 572
Cdd:cd05923 433 DERWGQSVTACVVPR---EGTLSADELDQFCRaSELADFKRPRRYFFLD--ELPKNAMNKV 488
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
69-578 |
5.39e-74 |
|
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: 242.58 E-value: 5.39e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 69 TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITppg 148
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 149 fkksnyyqsikdilpevtlkepgksgitsrnftcfqhlimfdeedkiypgawkytdvmkmgteedrhhlskieretqpdD 228
Cdd:cd05934 82 -------------------------------------------------------------------------------D 82
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 229 SLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIIcIPNPLYHCFGCVMGVLAALTHLQTCVfPAPSFDAL 308
Cdd:cd05934 83 PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYL-TVLPLFHINAQAVSVLAALSVGATLV-LLPRFSAS 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 309 AALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCPI--TLCRRL-VQdmhmtdMQVCYGTTETSpv 385
Cdd:cd05934 161 RFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRAAYGAPNPPELheEFEERFgVR------LLEGYGMTETI-- 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 386 sFMSTRDDPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVR---GYSVMRCYWNSEEQTKkEITQDRWYHTGDI 462
Cdd:cd05934 233 -VGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRglrGWGFFKGYYNMPEATA-EAMRNGWFHTGDL 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 463 AVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAegKTTEEDIKAW 542
Cdd:cd05934 311 GYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGE--TLDPEELFAF 388
|
490 500 510
....*....|....*....|....*....|....*.
gi 71994694 543 CKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIR 578
Cdd:cd05934 389 CEGQLAYFKVPRYIRFVD--DLPKTPTEKVAKAQLR 422
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
39-582 |
8.87e-74 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 245.94 E-value: 8.87e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 39 FETVGDRLRSAVDQVPDKEflIFKREGIRKTYSQVATDAENLACGLL-HLGLKKGDRIGIWGPNTYEWTTTQFASALAGM 117
Cdd:PRK08751 24 FRTVAEVFATSVAKFADRP--AYHSFGKTITYREADQLVEQFAAYLLgELQLKKGDRVALMMPNCLQYPIATFGVLRAGL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 118 VLVNINPSYQSEELRYAIEKVGIRALITppgfkKSNYYQSIKDILPEVTLKEPGKSGITSR---------NFTcFQHLIM 188
Cdd:PRK08751 102 TVVNVNPLYTPRELKHQLIDSGASVLVV-----IDNFGTTVQQVIADTPVKQVITTGLGDMlgfpkaalvNFV-VKYVKK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 189 FDEEDKIyPGAWKYTDVMKMGTeedRHHLSKIEREtqPDDSLNIQYTSGTTGQPKGATLTHHNVLNN----AFFVGLRAG 264
Cdd:PRK08751 176 LVPEYRI-NGAIRFREALALGR---KHSMPTLQIE--PDDIAFLQYTGGTTGVAKGAMLTHRNLVANmqqaHQWLAGTGK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 265 YSEKKTIICIPNPLYHCF-----GCVMGVLAALTHLQTCVFPAPSFdalaaLQAIHEEKCTALYGTPTMFIDMINHPEYA 339
Cdd:PRK08751 250 LEEGCEVVITALPLYHIFaltanGLVFMKIGGCNHLISNPRDMPGF-----VKELKKTRFTAFTGVNTLFNGLLNTPGFD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 340 NYNYDSIRSGFIAGAPCPITLCRRLVQDMHMTDMQVcYGTTETSPVSFMSTRDDPPEQriKSVGHIMDHLEAAIVDKRNC 419
Cdd:PRK08751 325 QIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEA-YGLTETSPAACINPLTLKEYN--GSIGLPIPSTDACIKDDAGT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 420 IVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFK 499
Cdd:PRK08751 402 VLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAM 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 500 HQSVEDVHIVGVPDERFGEVVCAWVRLHESAegkTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIRE 579
Cdd:PRK08751 482 MPGVLEVAAVGVPDEKSGEIVKVVIVKKDPA---LTAEDVKAHARANLTGYKQPRIIEFRK--ELPKTNVGKILRRELRD 556
|
...
gi 71994694 580 MSK 582
Cdd:PRK08751 557 AAK 559
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
69-572 |
9.98e-74 |
|
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: 242.38 E-value: 9.98e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 69 TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITppg 148
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 149 fkksnyyqsikdilpevtlkepgksgitsrnftcfqhlimfdeedkiypgawkytdvmkmGTEEDrhhlskieretqpdD 228
Cdd:cd05935 80 ------------------------------------------------------------GSELD--------------D 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 229 SLNIQYTSGTTGQPKGATLTHHNVLNNAffVGLRAGYS-EKKTIICIPNPLYHCFGCVMGVLAALTHLQTCVFPApSFDA 307
Cdd:cd05935 86 LALIPYTSGTTGLPKGCMHTHFSAAANA--LQSAVWTGlTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMA-RWDR 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 308 LAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCPITLCRRLVQDMHMTDMQVcYGTTETSPVSF 387
Cdd:cd05935 163 ETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEG-YGLTETMSQTH 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 388 MStrddpPEQRIKS--VGHIMDHLEAAIVDKRNCIV-PRGVKGEVIVRGYSVMRCYWNSEEQTKK---EITQDRWYHTGD 461
Cdd:cd05935 242 TN-----PPLRPKLqcLGIP*FGVDARVIDIETGRElPPNEVGEIVVRGPQIFKGYWNRPEETEEsfiEIKGRRFFRTGD 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 462 IAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAEGKTTEEDIKA 541
Cdd:cd05935 317 LGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEEDIIE 396
|
490 500 510
....*....|....*....|....*....|.
gi 71994694 542 WCKGKIAHFKIPRYILFKKeyEFPLTVTGKV 572
Cdd:cd05935 397 WAREQMAAYKYPREVEFVD--ELPRSASGKI 425
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
46-579 |
1.46e-72 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 241.77 E-value: 1.46e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 46 LRSAVDQVPDKEflIFKREG----IRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVN 121
Cdd:cd12119 2 LEHAARLHGDRE--IVSRTHegevHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 122 INPSYQSEELRYAIEKVGIRALITPPGFKKsnYYQSIKDILPEVtlkepgksgitsrnftcfQHLIMFDEEDKIY----P 197
Cdd:cd12119 80 INPRLFPEQIAYIINHAEDRVVFVDRDFLP--LLEAIAPRLPTV------------------EHVVVMTDDAAMPepagV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 198 GAWKYTDVMkmGTEEDRHHLSKI-ERetqpdDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLR--AGYSEKKTIICI 274
Cdd:cd12119 140 GVLAYEELL--AAESPEYDWPDFdEN-----TAAAICYTSGTTGNPKGVVYSHRSLVLHAMAALLTdgLGLSESDVVLPV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 275 pNPLYHC------FGCVMgVLAALthlqtcVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRS 348
Cdd:cd12119 213 -VPMFHVnawglpYAAAM-VGAKL------VLPGPYLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 349 GFIAGAPCPITLCRRLvQDMHMTDMQVcYGTTETSPVSFMST-----RDDPPEQRIK---SVGHIMDHLEAAIVDKRNCI 420
Cdd:cd12119 285 VVIGGSAVPRSLIEAF-EERGVRVIHA-WGMTETSPLGTVARppsehSNLSEDEQLAlraKQGRPVPGVELRIVDDDGRE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 421 VPR--GVKGEVIVRGYSVMRCYWNSEEQTKkEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLF 498
Cdd:cd12119 363 LPWdgKAVGELQVRGPWVTKSYYKNDEESE-ALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIM 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 499 KHQSVEDVHIVGVPDERFGEVVCAWVRLHESAEgkTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIR 578
Cdd:cd12119 442 AHPAVAEAAVIGVPHPKWGERPLAVVVLKEGAT--VTAEELLEFLADKVAKWWLPDDVVFVD--EIPKTSTGKIDKKALR 517
|
.
gi 71994694 579 E 579
Cdd:cd12119 518 E 518
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
64-582 |
1.68e-72 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 242.16 E-value: 1.68e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 64 EGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRAL 143
Cdd:PRK08162 40 GDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 144 ITPPGFKksnyyQSIKDILPEVtlkePGksgitsrnftcfQHLIMFDEEDKIYPGAwkytdvmkmgteedrHHLSKIERE 223
Cdd:PRK08162 120 IVDTEFA-----EVAREALALL----PG------------PKPLVIDVDDPEYPGG---------------RFIGALDYE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 224 ------------TQPDD-----SLNiqYTSGTTGQPKGaTLTHH-----NVLNNAFFVGL--RAGYSEkkTIicipnPLY 279
Cdd:PRK08162 164 aflasgdpdfawTLPADewdaiALN--YTSGTTGNPKG-VVYHHrgaylNALSNILAWGMpkHPVYLW--TL-----PMF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 280 HCFG-CVMGVLAALTHLQTCVfpaPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCPI 358
Cdd:PRK08162 234 HCNGwCFPWTVAARAGTNVCL---RKVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAGAAPPA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 359 TLCRRlVQDMHMTDMQVcYGTTET-SPVSFMSTRDD----PPEQR--IKSVGHIMDHLEAAI-VDKRNCI--VPRGVK-- 426
Cdd:PRK08162 311 AVIAK-MEEIGFDLTHV-YGLTETyGPATVCAWQPEwdalPLDERaqLKARQGVRYPLQEGVtVLDPDTMqpVPADGEti 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 427 GEVIVRGYSVMRCYWNSEEQTKkEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDV 506
Cdd:PRK08162 389 GEIMFRGNIVMKGYLKNPKATE-EAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVA 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71994694 507 HIVGVPDERFGEVVCAWVRLHESAEgkTTEEDIKAWCKGKIAHFKIPRYILFKkeyEFPLTVTGKVKKFEIREMSK 582
Cdd:PRK08162 468 AVVAKPDPKWGEVPCAFVELKDGAS--ATEEEIIAHCREHLAGFKVPKAVVFG---ELPKTSTGKIQKFVLREQAK 538
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
50-586 |
2.29e-70 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 236.93 E-value: 2.29e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 50 VDQVPDKEFLIFKRE-GIRK--TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSY 126
Cdd:COG0365 19 AEGRGDKVALIWEGEdGEERtlTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 127 QSEELRYAIEKVGIRALITPPGFKKSNYYQSIKDILPEVTLKEPGKsgitsrnftcfQHLIMFD--EEDKIYPGAWKYTD 204
Cdd:COG0365 99 GAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPSL-----------EHVIVVGrtGADVPMEGDLDWDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 205 VMKMGTEEdrhhlskIERE-TQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAffvglragYSEKKTIICI-PNPLYHCF 282
Cdd:COG0365 168 LLAAASAE-------FEPEpTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHA--------ATTAKYVLDLkPGDVFWCT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 283 ---GCVMG----VLAALTHLQTCVF--PAPSF-DALAALQAIHEEKCTALYGTPTMFIDMINHPEY--ANYNYDSIRSGF 350
Cdd:COG0365 233 adiGWATGhsyiVYGPLLNGATVVLyeGRPDFpDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEplKKYDLSSLRLLG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 351 IAGAPCP---ITLCRRLVQdMHMTDMqvcYGTTETSpVSFMSTrddPPEQRIK--SVGHIMDHLEAAIVDKRNCIVPRGV 425
Cdd:COG0365 313 SAGEPLNpevWEWWYEAVG-VPIVDG---WGQTETG-GIFISN---LPGLPVKpgSMGKPVPGYDVAVVDEDGNPVPPGE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 426 KGEVIVRGY--SVMRCYWNSEEQTKKEI--TQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQ 501
Cdd:COG0365 385 EGELVIKGPwpGMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 502 SVEDVHIVGVPDERFGEVVCAWVRLHESAEG-KTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIRem 580
Cdd:COG0365 465 AVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPsDELAKELQAHVREELGPYAYPREIEFVD--ELPKTRSGKIMRRLLR-- 540
|
....*.
gi 71994694 581 sKIELG 586
Cdd:COG0365 541 -KIAEG 545
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
40-580 |
8.95e-70 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 234.95 E-value: 8.95e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 40 ETVGDRLRSAVDQVPDKEFLIFKREGI----RKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALA 115
Cdd:PRK13295 24 RTINDDLDACVASCPDKTAVTAVRLGTgaprRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 116 GMVLVNINPSYQSEELRYAIEKVGIRALITPPGFKKSNYYQSIKDILPEVtlkePGksgitsrnftcFQHLIMFDEEdki 195
Cdd:PRK13295 104 GAVLNPLMPIFRERELSFMLKHAESKVLVVPKTFRGFDHAAMARRLRPEL----PA-----------LRHVVVVGGD--- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 196 ypGAWKYTDVMKMGTEEDRHHLSKI--ERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNN----AFFVGLRAGysekk 269
Cdd:PRK13295 166 --GADSFEALLITPAWEQEPDAPAIlaRLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANivpyAERLGLGAD----- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 270 TIICIPNPLYHCFGCVMGVLAALTHLQTCVFpAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSG 349
Cdd:PRK13295 239 DVILMASPMAHQTGFMYGLMMPVMLGATAVL-QDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 350 FIAGAPCPITLCRRLVQDMHMTdmqVC--YGTTETSPVSfMSTRDDPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKG 427
Cdd:PRK13295 318 LCAGAPIPGALVERARAALGAK---IVsaWGMTENGAVT-LTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 428 EVIVRGYSVMRCYWNSEEQTKKEitQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVH 507
Cdd:PRK13295 394 RLQVRGCSNFGGYLKRPQLNGTD--ADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVA 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71994694 508 IVGVPDERFGEVVCAWVRLHESAEgkTTEEDIKAWCKG-KIAHFKIP-RYILFKkeyEFPLTVTGKVKKFEIREM 580
Cdd:PRK13295 472 IVAYPDERLGERACAFVVPRPGQS--LDFEEMVEFLKAqKVAKQYIPeRLVVRD---ALPRTPSGKIQKFRLREM 541
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
55-579 |
9.83e-69 |
|
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: 229.48 E-value: 9.83e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 55 DKEFLIFKreGIRKTYSQVATDAENLACGLLHLG-LKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRY 133
Cdd:cd05941 1 DRIAIVDD--GDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 134 AIEKVGIRALItppgfkksnyyqsikdilpevtlkepgksgitsrnftcfqhlimfdeedkiypgawkytdvmkmgteed 213
Cdd:cd05941 79 VITDSEPSLVL--------------------------------------------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 214 rhhlskieretqpDDSLnIQYTSGTTGQPKGATLTHHNVLNNaffvgLRA-----GYSEKKTII-CIPnpLYHCFGCVMG 287
Cdd:cd05941 90 -------------DPAL-ILYTSGTTGRPKGVVLTHANLAAN-----VRAlvdawRWTEDDVLLhVLP--LHHVHGLVNA 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 288 VLAALTHLQTCVFpAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSG-------FIAG-APCPIT 359
Cdd:cd05941 149 LLCPLFAGASVEF-LPKFDPKEVAISRLMPSITVFMGVPTIYTRLLQYYEAHFTDPQFARAAaaerlrlMVSGsAALPVP 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 360 LCRRLVQDMHMTDMQVcYGTTETSpvsfMSTRDDPPEQRIK-SVGHIMDHLEAAIVDK-RNCIVPRGVKGEVIVRGYSVM 437
Cdd:cd05941 228 TLEEWEAITGHTLLER-YGMTEIG----MALSNPLDGERRPgTVGMPLPGVQARIVDEeTGEPLPRGEVGEIQVRGPSVF 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 438 RCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIV-RGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERF 516
Cdd:cd05941 303 KEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIkSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDW 382
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71994694 517 GEVVCAWVRLHESAEGKtTEEDIKAWCKGKIAHFKIPRYILFkkEYEFPLTVTGKVKKFEIRE 579
Cdd:cd05941 383 GERVVAVVVLRAGAAAL-SLEELKEWAKQRLAPYKRPRRLIL--VDELPRNAMGKVNKKELRK 442
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
54-579 |
1.81e-68 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 229.85 E-value: 1.81e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 54 PDKEFLIFKREgiRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRY 133
Cdd:PRK03640 16 PDRTAIEFEEK--KVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLW 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 134 AIEKVGIRALITPPGFkksnyyqsikdilpevtlkepgksgitsrnftcfqhlimfdeEDKIYPGA-WKYTDVMKMGTEE 212
Cdd:PRK03640 94 QLDDAEVKCLITDDDF------------------------------------------EAKLIPGIsVKFAELMNGPKEE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 213 drhhlSKIERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICiPNPLYHCFG--CVM-GVL 289
Cdd:PRK03640 132 -----AEIQEEFDLDEVATIMYTSGTTGKPKGVIQTYGNHWWSAVGSALNLGLTEDDCWLA-AVPIFHISGlsILMrSVI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 290 AALThlqtcVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNyDSIRSGFIAGAPCPITL---CRR--- 363
Cdd:PRK03640 206 YGMR-----VVLVEKFDAEKINKLLQTGGVTIISVVSTMLQRLLERLGEGTYP-SSFRCMLLGGGPAPKPLleqCKEkgi 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 364 -LVQDmhmtdmqvcYGTTETSpvSFMSTRddPPE---QRIKSVGHIMDHLEAAIVDKRNcIVPRGVKGEVIVRGYSVMRC 439
Cdd:PRK03640 280 pVYQS---------YGMTETA--SQIVTL--SPEdalTKLGSAGKPLFPCELKIEKDGV-VVPPFEEGEIVVKGPNVTKG 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 440 YWNSEEQTKKEItQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEV 519
Cdd:PRK03640 346 YLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQV 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 520 VCAWVRLHESAegktTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIRE 579
Cdd:PRK03640 425 PVAFVVKSGEV----TEEELRHFCEEKLAKYKVPKRFYFVE--ELPRNASGKLLRHELKQ 478
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
54-572 |
9.68e-68 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 230.30 E-value: 9.68e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 54 PDKEFLIFKREGIrkTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRY 133
Cdd:PRK06710 38 PEKKALHFLGKDI--TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 134 AIEKVGIRALITppgfkksnyyqsIKDILPEVTlkepgksgiTSRNFTCFQHLIMFDEED-------KIYPGAWKYTD-- 204
Cdd:PRK06710 116 QLHDSGAKVILC------------LDLVFPRVT---------NVQSATKIEHVIVTRIADflpfpknLLYPFVQKKQSnl 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 205 VMKMGTEEDRHHLSKIERETQ--------PDDSLNI-QYTSGTTGQPKGATLTHHNVLNNAFfVGLRAGYS--EKKTIIC 273
Cdd:PRK06710 175 VVKVSESETIHLWNSVEKEVNtgvevpcdPENDLALlQYTGGTTGFPKGVMLTHKNLVSNTL-MGVQWLYNckEGEEVVL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 274 IPNPLYHCFGcvMGVLAALTHLQTC-VFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIA 352
Cdd:PRK06710 254 GVLPFFHVYG--MTAVMNLSIMQGYkMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 353 GAPCPITLCRRLvQDMHMTDMQVCYGTTETSPVS---FMSTRDDPpeqriKSVGHIMDHLEAAIVD-KRNCIVPRGVKGE 428
Cdd:PRK06710 332 SAPLPVEVQEKF-ETVTGGKLVEGYGLTESSPVThsnFLWEKRVP-----GSIGVPWPDTEAMIMSlETGEALPPGEIGE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 429 VIVRGYSVMRCYWNSEEQTKKeITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHI 508
Cdd:PRK06710 406 IVVKGPQIMKGYWNKPEETAA-VLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVT 484
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71994694 509 VGVPDERFGEVVCAWVRLHESAEgkTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKV 572
Cdd:PRK06710 485 IGVPDPYRGETVKAFVVLKEGTE--CSEEELNQFARKYLAAYKVPKVYEFRD--ELPKTTVGKI 544
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
39-515 |
1.20e-67 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 230.76 E-value: 1.20e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 39 FETVGDRLRSAVDQVPDKEFLIFKREGIRK--TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAG 116
Cdd:COG1022 10 ADTLPDLLRRRAARFPDRVALREKEDGIWQslTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 117 MVLVNINPSYQSEELRYAIEKVGIRALITppgfkkSNYYQ-----SIKDILPEVtlkepgksgitsrnftcfQHLIMFDE 191
Cdd:COG1022 90 AVTVPIYPTSSAEEVAYILNDSGAKVLFV------EDQEQldkllEVRDELPSL------------------RHIVVLDP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 192 EDKI-YPGAWKYTDVMKMGTE-EDRHHLSKIERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKK 269
Cdd:COG1022 146 RGLRdDPRLLSLDELLALGREvADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 270 TIICIPnPLYHCFGCVMGVlaALTHLQTCVFPAPSFDALAA-LQAIHeekctalygtPTMFI---------------DMI 333
Cdd:COG1022 226 RTLSFL-PLAHVFERTVSY--YALAAGATVAFAESPDTLAEdLREVK----------PTFMLavprvwekvyagiqaKAE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 334 NHP---------------EYANYNYDS-----------------------------IRSGFIAGAPCPITLCrRLVQDMH 369
Cdd:COG1022 293 EAGglkrklfrwalavgrRYARARLAGkspslllrlkhaladklvfsklrealggrLRFAVSGGAALGPELA-RFFRALG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 370 MTDMQVcYGTTETSPVSFMSTRDDPpeqRIKSVGHIMDHLEAAIVDkrncivprgvKGEVIVRGYSVMRCYWNSEEQTKK 449
Cdd:COG1022 372 IPVLEG-YGLTETSPVITVNRPGDN---RIGTVGPPLPGVEVKIAE----------DGEILVRGPNVMKGYYKNPEATAE 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71994694 450 EITQDRWYHTGDIAVMHDNGTISIVGRSKDMIV-RGGENIYPTEVEQFLFKHQSVEDVHIVGvpDER 515
Cdd:COG1022 438 AFDADGWLHTGDIGELDEDGFLRITGRKKDLIVtSGGKNVAPQPIENALKASPLIEQAVVVG--DGR 502
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
40-580 |
1.46e-67 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 229.89 E-value: 1.46e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 40 ETVGDRLRSAVDQVPDKEFLIFKreGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVL 119
Cdd:PRK05605 32 TTLVDLYDNAVARFGDRPALDFF--GATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 120 VNINPSYQSEELRYAIEKVGIRALI---------------TPPgfkKSNYYQSIKDILPEVT---LKEPGKSGITSRnft 181
Cdd:PRK05605 110 VEHNPLYTAHELEHPFEDHGARVAIvwdkvaptverlrrtTPL---ETIVSVNMIAAMPLLQrlaLRLPIPALRKAR--- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 182 cfqhlimfdeeDKIYPGA-----W-KYTDVMKMGTEEDRHHlskieRETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNN 255
Cdd:PRK05605 184 -----------AALTGPApgtvpWeTLVDAAIGGDGSDVSH-----PRPTPDDVALILYTSGTTGKPKGAQLTHRNLFAN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 256 AFfVGlRA---GYSEKKTIICIPNPLYHCFGCVMGV-LAALTHLQTCVFPAPSFDALaaLQAIHEEKCTALYGTPTMFID 331
Cdd:PRK05605 248 AA-QG-KAwvpGLGDGPERVLAALPMFHAYGLTLCLtLAVSIGGELVLLPAPDIDLI--LDAMKKHPPTWLPGVPPLYEK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 332 MINHPEYANYNYDSIRSGFIAGAPCPITLCR--------RLVQDmhmtdmqvcYGTTETSPVSF---MStrddpPEQRIK 400
Cdd:PRK05605 324 IAEAAEERGVDLSGVRNAFSGAMALPVSTVElwekltggLLVEG---------YGLTETSPIIVgnpMS-----DDRRPG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 401 SVGHIMDHLEAAIVDKRNC--IVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEITqDRWYHTGDIAVMHDNGTISIVGRSK 478
Cdd:PRK05605 390 YVGVPFPDTEVRIVDPEDPdeTMPDGEEGELLVRGPQVFKGYWNRPEETAKSFL-DGWFRTGDVVVMEEDGFIRIVDRIK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 479 DMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAEgkTTEEDIKAWCKGKIAHFKIPRyiLF 558
Cdd:PRK05605 469 ELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAA--LDPEGLRAYCREHLTRYKVPR--RF 544
|
570 580
....*....|....*....|..
gi 71994694 559 KKEYEFPLTVTGKVKKFEIREM 580
Cdd:PRK05605 545 YHVDELPRDQLGKVRRREVREE 566
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
61-581 |
7.08e-67 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 227.78 E-value: 7.08e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 61 FKREGIRKTYSQVATDAENLACGLL-HLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVG 139
Cdd:PRK12492 43 FSNLGVTLSYAELERHSAAFAAYLQqHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 140 IRALITPPGFKKSnyyqsIKDILPEvtlkepgksgitsrnfTCFQHLI---MFDEE------------DKI--------Y 196
Cdd:PRK12492 123 ARALVYLNMFGKL-----VQEVLPD----------------TGIEYLIeakMGDLLpaakgwlvntvvDKVkkmvpayhL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 197 PGAWKYTDVMKMGTeedRHHLSKIERETqpDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVglRAGYS---------- 266
Cdd:PRK12492 182 PQAVPFKQALRQGR---GLSLKPVPVGL--DDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQV--RACLSqlgpdgqplm 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 267 -EKKTIICIPNPLYHCFGCVMGVLAALTHLQTCVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDS 345
Cdd:PRK12492 255 kEGQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLITNPRDIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKDLDFSA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 346 IRSGFIAGAPCPITLCRRLVQdmhMTDMQVC--YGTTETSPVSfmSTRDDPPEQRIKSVGHIMDHLEAAIVDKRNCIVPR 423
Cdd:PRK12492 335 LKLTNSGGTALVKATAERWEQ---LTGCTIVegYGLTETSPVA--STNPYGELARLGTVGIPVPGTALKVIDDDGNELPL 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 424 GVKGEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSV 503
Cdd:PRK12492 410 GERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKV 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71994694 504 EDVHIVGVPDERFGEVVCAWVrlhESAEGKTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIREMS 581
Cdd:PRK12492 490 ANCAAIGVPDERSGEAVKLFV---VARDPGLSVEELKAYCKENFTGYKVPKHIVLRD--SLPMTPVGKILRRELRDIA 562
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
67-597 |
5.70e-66 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 225.45 E-value: 5.70e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 67 RKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITP 146
Cdd:PLN02860 32 RRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 147 PGFkkSNYYQSIK-DILPEVTLkepgksgitsrnftcfqHLIMFDEEDKIYPGAWKY--TDVMKmgteedRHHLSKIERE 223
Cdd:PLN02860 112 ETC--SSWYEELQnDRLPSLMW-----------------QVFLESPSSSVFIFLNSFltTEMLK------QRALGTTELD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 224 TQ--PDDSLNIQYTSGTTGQPKGATLTHhnvlnNAFFVGLRA-----GYSEKKTIICIpNPLYHcfgcVMGVLAALTHLQ 296
Cdd:PLN02860 167 YAwaPDDAVLICFTSGTTGRPKGVTISH-----SALIVQSLAkiaivGYGEDDVYLHT-APLCH----IGGLSSALAMLM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 297 T--CVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMI--NHPEYANYNYDSIRSGFIAGAPCPITLCRRLVQDMHMTD 372
Cdd:PLN02860 237 VgaCHVLLPKFDAKAALQAIKQHNVTSMITVPAMMADLIslTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 373 MQVCYGTTET-SPVSFMsTRDDP----PEQRIKSVGHIMD----HLEAAIVDKRNCIVPRGVK-------GEVIVRGYSV 436
Cdd:PLN02860 317 LFSAYGMTEAcSSLTFM-TLHDPtlesPKQTLQTVNQTKSssvhQPQGVCVGKPAPHVELKIGldessrvGRILTRGPHV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 437 MRCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERF 516
Cdd:PLN02860 396 MLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 517 GEVVCAWVRLHE----------SAEGKTT--EEDIKAWCKGK-IAHFKIPRYILFKKEyEFPLTVTGKVKKFEIRemski 583
Cdd:PLN02860 476 TEMVVACVRLRDgwiwsdnekeNAKKNLTlsSETLRHHCREKnLSRFKIPKLFVQWRK-PFPLTTTGKIRRDEVR----- 549
|
570
....*....|....
gi 71994694 584 elglQQVVSHFSEL 597
Cdd:PLN02860 550 ----REVLSHLQSL 559
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
36-582 |
3.76e-65 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 222.97 E-value: 3.76e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 36 PLLFETVGDRLRSAVDQVPDKEFLIFKREGIrkTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALA 115
Cdd:PRK07059 19 ASQYPSLADLLEESFRQYADRPAFICMGKAI--TYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 116 GMVLVNINPSYQSEELRYAIEKVGIRALITppgfkKSNYYQSIKDILPEVTLKEP---------GKSGitsrnftcfqHL 186
Cdd:PRK07059 97 GYVVVNVNPLYTPRELEHQLKDSGAEAIVV-----LENFATTVQQVLAKTAVKHVvvasmgdllGFKG----------HI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 187 IMF--DEEDKIYPgAW------KYTDVMKMGTeedRHHLSKIEreTQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFF 258
Cdd:PRK07059 162 VNFvvRRVKKMVP-AWslpghvRFNDALAEGA---RQTFKPVK--LGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 259 VG--LRAGYSEKK-----TIICIPnPLYHCFG----CVMGVLAALTHLqtcVFPAPSfDALAALQAIHEEKCTALYGTPT 327
Cdd:PRK07059 236 MEawLQPAFEKKPrpdqlNFVCAL-PLYHIFAltvcGLLGMRTGGRNI---LIPNPR-DIPGFIKELKKYQVHIFPAVNT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 328 MFIDMINHPEYANYNYDSIRSGFIAGAPCPITLCRRLVQdmhMTDMQVC--YGTTETSPVSFMSTRDDPpeQRIKSVGHI 405
Cdd:PRK07059 311 LYNALLNNPDFDKLDFSKLIVANGGGMAVQRPVAERWLE---MTGCPITegYGLSETSPVATCNPVDAT--EFSGTIGLP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 406 MDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGG 485
Cdd:PRK07059 386 LPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSG 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 486 ENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAegkTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFP 565
Cdd:PRK07059 466 FNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKDPA---LTEEDVKAFCKERLTNYKRPKFVEFRT--ELP 540
|
570
....*....|....*..
gi 71994694 566 LTVTGKVKKFEIREMSK 582
Cdd:PRK07059 541 KTNVGKILRRELRDGKA 557
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
39-579 |
7.24e-64 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 219.63 E-value: 7.24e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 39 FETVGDRLRSAVDQVPDKEflIFKREGIRKTYSQVATDAENLACGLL-HLGLKKGDRIGIWGPNTYEWTTTQFASALAGM 117
Cdd:PRK05677 23 YPNIQAVLKQSCQRFADKP--AFSNLGKTLTYGELYKLSGAFAAWLQqHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 118 VLVNINPSYQSEELRYAIEKVGIRALITppgfkKSNYYQSIKDILPevtlkepgKSGItsrnftcfQHLIMFDEEDKI-- 195
Cdd:PRK05677 101 IVVNTNPLYTAREMEHQFNDSGAKALVC-----LANMAHLAEKVLP--------KTGV--------KHVIVTEVADMLpp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 196 ---------------------YPGAWKYTDVMKMGTEEdrhhlSKIERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLN 254
Cdd:PRK05677 160 lkrllinavvkhvkkmvpayhLPQAVKFNDALAKGAGQ-----PVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 255 NAFFVG--LRAGYSEKKTIICIPNPLYHCFGCVMGVLAA-LTHLQTCVFPAPSfDALAALQAIHEEKCTALYGTPTMFID 331
Cdd:PRK05677 235 NMLQCRalMGSNLNEGCEILIAPLPLYHIYAFTFHCMAMmLIGNHNILISNPR-DLPAMVKELGKWKFSGFVGLNTLFVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 332 MINHPEYANYNYDSIRSGFIAGAPCPITLCRRLVQdmhMTDMQVC--YGTTETSPVSFMstrdDPPEQ-RIKSVGHIMDH 408
Cdd:PRK05677 314 LCNNEAFRKLDFSALKLTLSGGMALQLATAERWKE---VTGCAICegYGMTETSPVVSV----NPSQAiQVGTIGIPVPS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 409 LEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENI 488
Cdd:PRK05677 387 TLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNV 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 489 YPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVrLHESAEGkTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTV 568
Cdd:PRK05677 467 YPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFV-VVKPGET-LTKEQVMEHMRANLTGYKVPKAVEFRD--ELPTTN 542
|
570
....*....|.
gi 71994694 569 TGKVKKFEIRE 579
Cdd:PRK05677 543 VGKILRRELRD 553
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
49-558 |
2.03e-63 |
|
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: 217.10 E-value: 2.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 49 AVDQVPDKEFLIFKREGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQS 128
Cdd:cd05904 14 FASAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 129 EELRYAIEKVGIRALITppgfkKSNYYQSIKDILPEVTLKEpgksgitsrnfTCFQHLIMFDEEDKIYPGAWKYTDVMKm 208
Cdd:cd05904 94 AEIAKQVKDSGAKLAFT-----TAELAEKLASLALPVVLLD-----------SAEFDSLSFSDLLFEADEAEPPVVVIK- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 209 gteedrhhlskieretqPDDSLNIQYTSGTTGQPKGATLTHHN-VLNNAFFVGLRAGYSEKKTIICIPNPLYHCFGCVMG 287
Cdd:cd05904 157 -----------------QDDVAALLYSSGTTGRSKGVMLTHRNlIAMVAQFVAGEGSNSDSEDVFLCVLPMFHIYGLSSF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 288 VLAALtHLQTCVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCPITLCRRLVQD 367
Cdd:cd05904 220 ALGLL-RLGATVVVMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 368 MHMTDMQVCYGTTETSPVSfmsTRDDPPEQ---RIKSVGHIMDHLEAAIVD-KRNCIVPRGVKGEVIVRGYSVMRCYWNS 443
Cdd:cd05904 299 FPNVDLGQGYGMTESTGVV---AMCFAPEKdraKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 444 EEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAW 523
Cdd:cd05904 376 PEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAF 455
|
490 500 510
....*....|....*....|....*....|....*.
gi 71994694 524 -VRlheSAEGKTTEEDIKAWCKGKIAHFKIPRYILF 558
Cdd:cd05904 456 vVR---KPGSSLTEDEIMDFVAKQVAPYKKVRKVAF 488
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
64-579 |
1.22e-60 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 209.37 E-value: 1.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 64 EGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRAL 143
Cdd:PRK08276 8 SGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 144 ITPPGFKksnyyQSIKDILPEVTLKEPgksgitsrnftcfqHLIMFDEEdkiYPGAWKYTDVMKMGTEEDrhhlskIERE 223
Cdd:PRK08276 88 IVSAALA-----DTAAELAAELPAGVP--------------LLLVVAGP---VPGFRSYEEALAAQPDTP------IADE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 224 TQPDDslnIQYTSGTTGQPKG--ATLTH---HNVLNNAFFVGLRAGYSEKKTIICIPNPLYHC----FGcvMGVLAaLTH 294
Cdd:PRK08276 140 TAGAD---MLYSSGTTGRPKGikRPLPGldpDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTaplrFG--MSALA-LGG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 295 lqTCVFpAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYD--SIRSGFIAGAPCPITLCRRlvqdmhMTD 372
Cdd:PRK08276 214 --TVVV-MEKFDAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYDvsSLRVAIHAAAPCPVEVKRA------MID 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 373 -----MQVCYGTTETSPVSFMStrddpPEQRIK---SVGHIMDHlEAAIVDKRNCIVPRGVKGEVIVR--GYSVMrcYWN 442
Cdd:PRK08276 285 wwgpiIHEYYASSEGGGVTVIT-----SEDWLAhpgSVGKAVLG-EVRILDEDGNELPPGEIGTVYFEmdGYPFE--YHN 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 443 SEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCA 522
Cdd:PRK08276 357 DPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 71994694 523 WVRLHESAE-GKTTEEDIKAWCKGKIAHFKIPRYILFkkEYEFPLTVTGKVKKFEIRE 579
Cdd:PRK08276 437 VVQPADGADaGDALAAELIAWLRGRLAHYKCPRSIDF--EDELPRTPTGKLYKRRLRD 492
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
87-579 |
6.67e-60 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 208.75 E-value: 6.67e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 87 LGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITPPGFKKSnyyqsikdiLPEVT 166
Cdd:PRK08974 69 LGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAHT---------LEKVV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 167 LKEPGKSGITSR-------------NFTCFQHLIMFDEEDkiYPGAWKYTDVMKMGteedrHHLSKIERETQPDDSLNIQ 233
Cdd:PRK08974 140 FKTPVKHVILTRmgdqlstakgtlvNFVVKYIKRLVPKYH--LPDAISFRSALHKG-----RRMQYVKPELVPEDLAFLQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 234 YTSGTTGQPKGATLTHHNVLNNAFFVglRAGYS----EKKTIICIPNPLYHCFGCVMGVLAALtHL--QTCVFPAPSfDA 307
Cdd:PRK08974 213 YTGGTTGVAKGAMLTHRNMLANLEQA--KAAYGpllhPGKELVVTALPLYHIFALTVNCLLFI-ELggQNLLITNPR-DI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 308 LAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCPITLCRRLvQDMHMTDMQVCYGTTETSPVSF 387
Cdd:PRK08974 289 PGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGGMAVQQAVAERW-VKLTGQYLLEGYGLTECSPLVS 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 388 MSTRDdpPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKkEITQDRWYHTGDIAVMHD 467
Cdd:PRK08974 368 VNPYD--LDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATD-EVIKDGWLATGDIAVMDE 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 468 NGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAegkTTEEDIKAWCKGKI 547
Cdd:PRK08974 445 EGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPS---LTEEELITHCRRHL 521
|
490 500 510
....*....|....*....|....*....|..
gi 71994694 548 AHFKIPRYILFKKeyEFPLTVTGKVKKFEIRE 579
Cdd:PRK08974 522 TGYKVPKLVEFRD--ELPKSNVGKILRRELRD 551
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
69-577 |
1.42e-59 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 205.14 E-value: 1.42e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 69 TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITPPg 148
Cdd:cd05907 7 TWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVED- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 149 fkksnyyqsikdilpevtlkepgksgitsrnftcfqhlimfdeedkiypgawkytdvmkmgteedrhhlskieretqPDD 228
Cdd:cd05907 86 -----------------------------------------------------------------------------PDD 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 229 SLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIPnPLYHCFGCVMGVLAALTHLQTCVFPAPSFDAL 308
Cdd:cd05907 89 LATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFL-PLAHVFERRAGLYVPLLAGARIYFASSAETLL 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 309 AALQAIheeKCTALYGTPTMF------IDMINHPE-----YANYNYDSIRSGFIAGAPCPitlcRRLVQDMHMTDMQVC- 376
Cdd:cd05907 168 DDLSEV---RPTVFLAVPRVWekvyaaIKVKAVPGlkrklFDLAVGGRLRFAASGGAPLP----AELLHFFRALGIPVYe 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 377 -YGTTETSPVSFMSTRDDPpeqRIKSVGHIMDHLEAAIVDKrncivprgvkGEVIVRGYSVMRCYWNSEEQTKKEITQDR 455
Cdd:cd05907 241 gYGLTETSAVVTLNPPGDN---RIGTVGKPLPGVEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDADG 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 456 WYHTGDIAVMHDNGTISIVGRSKDMIV-RGGENIYPTEVEQFLFKHQSVEDVHIVG----------VPDErfgEVVCAWV 524
Cdd:cd05907 308 WLHTGDLGEIDEDGFLHITGRKKDLIItSGGKNISPEPIENALKASPLISQAVVIGdgrpflvaliVPDP---EALEAWA 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71994694 525 RLHESAEGKTTE--------EDIKAWCK---GKIAHF-KIPRYILFKKEY---EFPLTVTGKVKKFEI 577
Cdd:cd05907 385 EEHGIAYTDVAElaanpavrAEIEAAVEaanARLSRYeQIKKFLLLPEPFtieNGELTPTLKLKRPVI 452
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
67-579 |
2.07e-57 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 201.08 E-value: 2.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 67 RKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITp 146
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIA- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 147 pgfkKSNYYQSIKDILPE-VT-LKEPGKSGITSRNftcfqhlimfdeedKIYPGAWKytdvMKMGTEEDRHHLSKIERET 224
Cdd:PRK12406 90 ----HADLLHGLASALPAgVTvLSVPTPPEIAAAY--------------RISPALLT----PPAGAIDWEGWLAQQEPYD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 225 QP--DDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRA-GYSEKKTIIC-IPNPLYH----CFGCVMGVLAALTHLQ 296
Cdd:PRK12406 148 GPpvPQPQSMIYTSGTTGHPKGVRRAAPTPEQAAAAEQMRAlIYGLKPGIRAlLTGPLYHsapnAYGLRAGRLGGVLVLQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 297 tcvfpaPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYD--SIRSGFIAGAPCPITLCRRLVqDMHMTDMQ 374
Cdd:PRK12406 228 ------PRFDPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDvsSLRHVIHAAAPCPADVKRAMI-EWWGPVIY 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 375 VCYGTTETSPVSFMStrddpPEQRIK---SVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVR--GYSVMrCYWNSEEQtKK 449
Cdd:PRK12406 301 EYYGSTESGAVTFAT-----SEDALShpgTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRiaGNPDF-TYHNKPEK-RA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 450 EITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHES 529
Cdd:PRK12406 374 EIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPG 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 71994694 530 AEgkTTEEDIKAWCKGKIAHFKIPRYILFkkEYEFPLTVTGKVKKFEIRE 579
Cdd:PRK12406 454 AT--LDEADIRAQLKARLAGYKVPKHIEI--MAELPREDSGKIFKRRLRD 499
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
46-579 |
4.52e-57 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 200.65 E-value: 4.52e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 46 LRSAVDQVPDKEFLIFKREGIrkTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPS 125
Cdd:PRK07470 13 LRQAARRFPDRIALVWGDRSW--TWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 126 YQSEELRYAIEKVGIRALITPPGFKksnyyqsikDILPEVTLKEPGksgitsrnftcFQHLIMFDEEdkiyPGAWKYTDV 205
Cdd:PRK07470 91 QTPDEVAYLAEASGARAMICHADFP---------EHAAAVRAASPD-----------LTHVVAIGGA----RAGLDYEAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 206 MK--MGteeDRHHLSKIERetqpDDSLNIQYTSGTTGQPKGATLTHHN---VLNNaFFVGLRAGYSEKKTIICIPnPLYH 280
Cdd:PRK07470 147 VArhLG---ARVANAAVDH----DDPCWFFFTSGTTGRPKAAVLTHGQmafVITN-HLADLMPGTTEQDASLVVA-PLSH 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 281 CFGC--VMGVLAALThlqTCVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPcpi 358
Cdd:PRK07470 218 GAGIhqLCQVARGAA---TVLLPSERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAP--- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 359 tlcrrlvqdMHMTDMQ----------VCY-------GTTETSPVSFMSTrDDPPEQRIKSVGHIMDHLEAAIVDKRNCIV 421
Cdd:PRK07470 292 ---------MYRADQKralaklgkvlVQYfglgevtGNITVLPPALHDA-EDGPDARIGTCGFERTGMEVQIQDDEGREL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 422 PRGVKGEVIVRGYSVMRCYWNSEEQTKKEItQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQ 501
Cdd:PRK07470 362 PPGETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHP 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71994694 502 SVEDVHIVGVPDERFGEVVCAWVRLHESAegKTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIRE 579
Cdd:PRK07470 441 AVSEVAVLGVPDPVWGEVGVAVCVARDGA--PVDEAELLAWLDGKVARYKLPKRFFFWD--ALPKSGYGKITKKMVRE 514
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
40-574 |
6.27e-57 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 199.09 E-value: 6.27e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 40 ETVGDRLRSAVDQVPDKEFLIfkREGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVL 119
Cdd:cd05920 15 EPLGDLLARSAARHPDRIAVV--DGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 120 VNINPSYQSEELRYAIEKVGIRALITPpgfkksnyyqsikdilpevtlkepgksgitsRNFTCFQHLIMFDEEdkiypga 199
Cdd:cd05920 93 VLALPSHRRSELSAFCAHAEAVAYIVP-------------------------------DRHAGFDHRALAREL------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 200 wkytdvmkmgteedrhhlskieRETQPDDSLnIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIpNPLY 279
Cdd:cd05920 135 ----------------------AESIPEVAL-FLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAV-LPAA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 280 HCFG-CVMGVLAALtHLQTCVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCPI 358
Cdd:cd05920 191 HNFPlACPGVLGTL-LAGGRVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 359 TLCRRLVQDMHMTDMQVcYGTTEtSPVSFmsTR-DDPPEQRIKSVGHIMD-HLEAAIVDKRNCIVPRGVKGEVIVRGYSV 436
Cdd:cd05920 270 ALARRVPPVLGCTLQQV-FGMAE-GLLNY--TRlDDPDEVIIHTQGRPMSpDDEIRVVDEEGNPVPPGEEGELLTRGPYT 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 437 MRCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERF 516
Cdd:cd05920 346 IRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELL 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 71994694 517 GEVVCAWVRLHESAegkTTEEDIKAWCKGK-IAHFKIPRYILFKKeyEFPLTVTGKVKK 574
Cdd:cd05920 426 GERSCAFVVLRDPP---PSAAQLRRFLRERgLAAYKLPDRIEFVD--SLPLTAVGKIDK 479
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
54-579 |
6.47e-57 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 200.39 E-value: 6.47e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 54 PDKEFLIFKreGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRY 133
Cdd:PRK07786 31 PDAPALRFL--GNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 134 AIEKVGIRALITPPgfkksnyyqSIKDILPEVTLKEPGKSGItsrnftcfqhLIMFDEEDKiypGAWKYTDVMKMGTEEd 213
Cdd:PRK07786 109 LVSDCGAHVVVTEA---------ALAPVATAVRDIVPLLSTV----------VVAGGSSDD---SVLGYEDLLAEAGPA- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 214 rHHLSKIeretqPDDSLN-IQYTSGTTGQPKGATLTHHNVLNNAFfVGLRA-GYSEKKTIICIPNPLYHcfgcVMGVLAA 291
Cdd:PRK07786 166 -HAPVDI-----PNDSPAlIMYTSGTTGRPKGAVLTHANLTGQAM-TCLRTnGADINSDVGFVGVPLFH----IAGIGSM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 292 LTHLQ----TCVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYdSIRSGFIAGAPCPITLCRRLVQD 367
Cdd:PRK07786 235 LPGLLlgapTVIYPLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDL-ALRVLSWGAAPASDTLLRQMAAT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 368 MHMTDMQVCYGTTETSPVSFMSTRDDPPeQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQT 447
Cdd:PRK07786 314 FPEAQILAAFGQTEMSPVTCMLLGEDAI-RKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEAT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 448 KkEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLh 527
Cdd:PRK07786 393 A-EAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAV- 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 71994694 528 ESAEGKTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIRE 579
Cdd:PRK07786 471 RNDDAALTLEDLAEFLTDRLARYKHPKALEIVD--ALPRNPAGKVLKTELRE 520
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
216-579 |
5.29e-56 |
|
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: 194.49 E-value: 5.29e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 216 HLSKIERETQPDDS-------LNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIPnPLYHCFG---CV 285
Cdd:cd05912 59 RLTPNELAFQLKDSdvklddiATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCAL-PLFHISGlsiLM 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 286 MGVLAALThlqtcVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMIN-HPEYANYNydsIRSGFIAGAPCPITL---C 361
Cdd:cd05912 138 RSVIYGMT-----VYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRLLEiLGEGYPNN---LRCILLGGGPAPKPLleqC 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 362 RRLVQDMHMTdmqvcYGTTETSPVSFMSTRDDPPEqRIKSVGHIMDHLEAAIVDKRNcivPRGVKGEVIVRGYSVMRCYW 441
Cdd:cd05912 210 KEKGIPVYQS-----YGMTETCSQIVTLSPEDALN-KIGSAGKPLFPVELKIEDDGQ---PPYEVGEILLKGPNVTKGYL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 442 NSEEQTKkEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVC 521
Cdd:cd05912 281 NRPDATE-ESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPV 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 71994694 522 AWVrlheSAEGKTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIRE 579
Cdd:cd05912 360 AFV----VSERPISEEELIAYCSEKLAKYKVPKKIYFVD--ELPRTASGKLLRHELKQ 411
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
30-581 |
1.14e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 196.89 E-value: 1.14e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 30 HGCSTVPLLFETVGDRLRSAvdqvpDKEFLIFKREGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQ 109
Cdd:PRK06164 3 HDAAPRADTLASLLDAHARA-----RPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 110 FASALAGMVLVNINPSYQSEELRYAIEKVGIRALITPPGFKKSNYYQSIKDILPEVTLKEPGksgitsrnftcfqhLIMF 189
Cdd:PRK06164 78 LACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPGFKGIDFAAILAAVPPDALPPLRA--------------IAVV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 190 DEEDKIYPGAWKYTDVMKMGTEEDRHHLSKIERETQPDDSLNIQYTSGTTGQPK-----GATLTHHnvlnnAFFVGLRAG 264
Cdd:PRK06164 144 DDAADATPAPAPGARVQLFALPDPAPPAAAGERAADPDAGALLFTTSGTTSGPKlvlhrQATLLRH-----ARAIARAYG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 265 YSEKKTIICIPnPLYHCFGcVMGVLAALTHLQTCVFpAPSFDALAALQAIHEEKCTALYGTPTMFiDMINHPEYANYNYD 344
Cdd:PRK06164 219 YDPGAVLLAAL-PFCGVFG-FSTLLGALAGGAPLVC-EPVFDAARTARALRRHRVTHTFGNDEML-RRILDTAGERADFP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 345 SIRS-GFIAGAPCPITLCRRL-VQDMHMTDMqvcYGTTETSPVSFMSTRDDPPEQRIKSVGHIMD-HLEAAIVDKRN-CI 420
Cdd:PRK06164 295 SARLfGFASFAPALGELAALArARGVPLTGL---YGSSEVQALVALQPATDPVSVRIEGGGRPASpEARVRARDPQDgAL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 421 VPRGVKGEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKH 500
Cdd:PRK06164 372 LPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEAL 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 501 QSVEDVHIVGVpdERFGEVVC-AWVRLHESAegKTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTG---KVKKFE 576
Cdd:PRK06164 452 PGVAAAQVVGA--TRDGKTVPvAFVIPTDGA--SPDEAGLMAACREALAGFKVPARVQVVE--AFPVTESAngaKIQKHR 525
|
....*
gi 71994694 577 IREMS 581
Cdd:PRK06164 526 LREMA 530
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
44-579 |
1.21e-55 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 198.64 E-value: 1.21e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 44 DRLRSAVDQVPDKEFLIF------KREGIRKTYSQV---ATDAENLacglLH-LGLKKGDRIGIWGPNTYEWTTTQFASA 113
Cdd:PRK07529 29 ELLSRAAARHPDAPALSFlldadpLDRPETWTYAELladVTRTANL----LHsLGVGPGDVVAFLLPNLPETHFALWGGE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 114 LAGMVlVNINPSYQSEELRYAIEKVGIRALITPPGFKKSNYYQSIKDILPEVtlkePGKSGIT----SRNFTCFQHLIMF 189
Cdd:PRK07529 105 AAGIA-NPINPLLEPEQIAELLRAAGAKVLVTLGPFPGTDIWQKVAEVLAAL----PELRTVVevdlARYLPGPKRLAVP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 190 DEEDKIYPGAWKYTDVMKmgTEEDRHHLSkiERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKK 269
Cdd:PRK07529 180 LIRRKAHARILDFDAELA--RQPGDRLFS--GRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 270 TIICiPNPLYHCFGCVMGVLAALTHLQTCVFPAPS-------FDALAALQAIHeeKCTALYGTPTMFIDMINHPeYANYN 342
Cdd:PRK07529 256 TVFC-GLPLFHVNALLVTGLAPLARGAHVVLATPQgyrgpgvIANFWKIVERY--RINFLSGVPTVYAALLQVP-VDGHD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 343 YDSIRSGFIAGAPCPITLCRRLvqdMHMTDMQVC--YGTTETSPVSFMSTRDDPpeQRIKSVGHIMDHLEAAIV------ 414
Cdd:PRK07529 332 ISSLRYALCGAAPLPVEVFRRF---EAATGVRIVegYGLTEATCVSSVNPPDGE--RRIGSVGLRLPYQRVRVVilddag 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 415 -DKRNCivPRGVKGEVIVRGYSVMRCYWNsEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEV 493
Cdd:PRK07529 407 rYLRDC--AVDEVGVLCIAGPNVFSGYLE-AAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAI 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 494 EQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAEgkTTEEDIKAWCKGKIAH-FKIPRYILFKKeyEFPLTVTGKV 572
Cdd:PRK07529 484 EEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGAS--ATEAELLAFARDHIAErAAVPKHVRILD--ALPKTAVGKI 559
|
....*..
gi 71994694 573 KKFEIRE 579
Cdd:PRK07529 560 FKPALRR 566
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
69-578 |
1.65e-55 |
|
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: 195.67 E-value: 1.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 69 TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITPPG 148
Cdd:cd05959 31 TYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 149 FkksnyYQSIKdilPEVTLKEPGKsgitsrnftcfQHLIMFDEEDKIyPGAWKYTDVMkmGTEEDRHHLSKiereTQPDD 228
Cdd:cd05959 111 L-----APVLA---AALTKSEHTL-----------VVLIVSGGAGPE-AGALLLAELV--AAEAEQLKPAA----THADD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 229 SLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIPNPLYHCFGCVMGVLAALTHLQTCV----FPAPS 304
Cdd:cd05959 165 PAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVlmpeRPTPA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 305 fdalAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCPITLCRRLvQDMHMTDMQVCYGTTETSP 384
Cdd:cd05959 245 ----AVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERW-KARFGLDILDGIGSTEMLH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 385 VsFMSTRddPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEItQDRWYHTGDIAV 464
Cdd:cd05959 320 I-FLSNR--PGRVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 465 MHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAEGKTT-EEDIKAWC 543
Cdd:cd05959 396 RDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEAlEEELKEFV 475
|
490 500 510
....*....|....*....|....*....|....*
gi 71994694 544 KGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIR 578
Cdd:cd05959 476 KDRLAPYKYPRWIVFVD--ELPKTATGKIQRFKLR 508
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
41-561 |
3.46e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 195.49 E-value: 3.46e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 41 TVGDRLRSAVDQVPDKEFLIFKREgiRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLV 120
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALVCGDR--RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 121 NINPSYQSEELRYAIEKVGIRALItppgfkksnYYQSIKDILPEVTLKEPGksgitsrnftcFQHLIMFDEE--DKIYPG 198
Cdd:PRK07798 82 NVNYRYVEDELRYLLDDSDAVALV---------YEREFAPRVAEVLPRLPK-----------LRTLVVVEDGsgNDLLPG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 199 AWKYTDVMKMGTEEDRHhlskIERetQPDDsLNIQYTSGTTGQPKGATLTHHNVlnnaFFVGL----------------- 261
Cdd:PRK07798 142 AVDYEDALAAGSPERDF----GER--SPDD-LYLLYTGGTTGMPKGVMWRQEDI----FRVLLggrdfatgepiedeeel 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 262 --RAGYSEKKTIICIPnPLYHCFGcVMGVLAALTHLQTCVF-PAPSFDALAALQAIHEEKCTAL------YGTPtmFIDM 332
Cdd:PRK07798 211 akRAAAGPGMRRFPAP-PLMHGAG-QWAAFAALFSGQTVVLlPDVRFDADEVWRTIEREKVNVItivgdaMARP--LLDA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 333 INHPEyanyNYD-----SIRSGfiaGAPCPITLCRRL---VQDMHMTDmqvCYGTTETSPVSFMSTRDDPPEQRIKSVGh 404
Cdd:PRK07798 287 LEARG----PYDlsslfAIASG---GALFSPSVKEALlelLPNVVLTD---SIGSSETGFGGSGTVAKGAVHTGGPRFT- 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 405 iMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKK---EITQDRWYHTGDIAVMHDNGTISIVGRSKDMI 481
Cdd:PRK07798 356 -IGPRTVVLDEDGNPVEPGSGEIGWIARRGHIPLGYYKDPEKTAEtfpTIDGVRYAIPGDRARVEADGTITLLGRGSVCI 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 482 VRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAEGktTEEDIKAWCKGKIAHFKIPRYILFKKE 561
Cdd:PRK07798 435 NTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARP--DLAELRAHCRSSLAGYKVPRAIWFVDE 512
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
41-579 |
9.56e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 194.05 E-value: 9.56e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 41 TVGDRLRSAVDQVPDKEFLIFkrEGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLV 120
Cdd:PRK06188 13 TYGHLLVSALKRYPDRPALVL--GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 121 NINPSYQSEELRYAIEKVGIRALITPPGfkksNYYQSIKDILPEVtlkePGksgitsrnftcFQHLIMFDEedkiYPGAw 200
Cdd:PRK06188 91 ALHPLGSLDDHAYVLEDAGISTLIVDPA----PFVERALALLARV----PS-----------LKHVLTLGP----VPDG- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 201 kyTDVMKMGTEEDRHHLskiERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLnnAFFVGLRAGYS---EKKTIICipNP 277
Cdd:PRK06188 147 --VDLLAAAAKFGPAPL---VAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIA--TMAQIQLAEWEwpaDPRFLMC--TP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 278 LYHCfgcvmgvlAALTHLQT-----CVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIA 352
Cdd:PRK06188 218 LSHA--------GGAFFLPTllrggTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 353 GAPCPITlcrRLVQDMHMTD---MQVcYGTTET-SPVSFMSTRDDPPEQ--RIKSVGHIMDHLEAAIVDKRNCIVPRGVK 426
Cdd:PRK06188 290 ASPMSPV---RLAEAIERFGpifAQY-YGQTEApMVITYLRKRDHDPDDpkRLTSCGRPTPGLRVALLDEDGREVAQGEV 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 427 GEVIVRGYSVMRCYWNSEEQTKkEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDV 506
Cdd:PRK06188 366 GEICVRGPLVMDGYWNRPEETA-EAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQV 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71994694 507 HIVGVPDERFGEVVCAWVRLHESAEGKTTE--EDIKAWcKGKIAhfkIPRYILFKKeyEFPLTVTGKVKKFEIRE 579
Cdd:PRK06188 445 AVIGVPDEKWGEAVTAVVVLRPGAAVDAAElqAHVKER-KGSVH---APKQVDFVD--SLPLTALGKPDKKALRA 513
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
41-579 |
2.83e-54 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 193.27 E-value: 2.83e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 41 TVGDRLRSAVDQVPDKEFLIFKREGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLV 120
Cdd:PLN02330 29 TLPDFVLQDAELYADKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 121 NINPSYQSEELRYAIEKVGIRALITppgfkKSNYYQSIKDI-LPEVTLKEpgksgitsrnfTCFQhlimfdeedkiypGA 199
Cdd:PLN02330 109 GANPTALESEIKKQAEAAGAKLIVT-----NDTNYGKVKGLgLPVIVLGE-----------EKIE-------------GA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 200 WKYTDVMKMGteeDRHHLSKIERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNA----FFVGLRAgYSEKKTIICIP 275
Cdd:PLN02330 160 VNWKELLEAA---DRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLcsslFSVGPEM-IGQVVTLGLIP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 276 npLYHCFGcVMGVLAALTHLQTCVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSI--RSGFIAG 353
Cdd:PLN02330 236 --FFHIYG-ITGICCATLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLklQAIMTAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 354 APCPITLCRRLVQDMHMTDMQVCYGTTETSPVSFmsTRDDPPE----QRIKSVGHIMDHLEAAIVDKRNCI-VPRGVKGE 428
Cdd:PLN02330 313 APLAPELLTAFEAKFPGVQVQEAYGLTEHSCITL--THGDPEKghgiAKKNSVGFILPNLEVKFIDPDTGRsLPKNTPGE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 429 VIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHI 508
Cdd:PLN02330 391 LCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAV 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71994694 509 VGVPDERFGEVVCAWVRLHESAegKTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIRE 579
Cdd:PLN02330 471 VPLPDEEAGEIPAACVVINPKA--KESEEDILNFVAANVAHYKKVRVVQFVD--SIPKSLSGKIMRRLLKE 537
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
69-581 |
3.62e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 193.22 E-value: 3.62e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 69 TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITppg 148
Cdd:PRK07788 76 TYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVY--- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 149 fkKSNYYQSIKDILPEVTLKepgKSGITSRnftcfqhlimfDEEDKIYPGAWKYTDVMkmgteeDRHHLSKIERETQPDd 228
Cdd:PRK07788 153 --DDEFTDLLSALPPDLGRL---RAWGGNP-----------DDDEPSGSTDETLDDLI------AGSSTAPLPKPPKPG- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 229 SLNIQyTSGTTGQPKGATLTHHNVL--NNAFF--VGLRAGysekkTIICIPNPLYHCFGCVMGVLAaLTHLQTCVFPApS 304
Cdd:PRK07788 210 GIVIL-TSGTTGTPKGAPRPEPSPLapLAGLLsrVPFRAG-----ETTLLPAPMFHATGWAHLTLA-MALGSTVVLRR-R 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 305 FDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYD--SIRSGFIAGAPCPITLCRRlVQDmHMTDMqVC--YGTT 380
Cdd:PRK07788 282 FDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDtsSLKIIFVSGSALSPELATR-ALE-AFGPV-LYnlYGST 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 381 EtspVSFMSTRDdPPEQRI--KSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSeeQTKKEItqDRWYH 458
Cdd:PRK07788 359 E---VAFATIAT-PEDLAEapGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDG--RDKQII--DGLLS 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 459 TGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAEgkTTEED 538
Cdd:PRK07788 431 SGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAA--LDEDA 508
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 71994694 539 IKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIREMS 581
Cdd:PRK07788 509 IKDYVRDNLARYKVPRDVVFLD--ELPRNPTGKVLKRELREMD 549
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
228-572 |
6.29e-53 |
|
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: 184.01 E-value: 6.29e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 228 DSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIPnPLYHcfgcVMGVLAALTHLQT--CVFPAPSF 305
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNML-PLFH----IAGLNLALATFHAggANVVMEKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 306 DALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSgfIAGAPCPITLCRRLVqdmhMTDMQ--VCYGTTETS 383
Cdd:cd17637 76 DPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRH--VLGLDAPETIQRFEE----TTGATfwSLYGQTETS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 384 -PVSFMSTRDDPpeqriKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEiTQDRWYHTGDI 462
Cdd:cd17637 150 gLVTLSPYRERP-----GSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYT-FRNGWHHTGDL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 463 AVMHDNGTISIVGRS--KDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAegKTTEEDIK 540
Cdd:cd17637 224 GRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGA--TLTADELI 301
|
330 340 350
....*....|....*....|....*....|..
gi 71994694 541 AWCKGKIAHFKIPRYILFKKeyEFPLTVTGKV 572
Cdd:cd17637 302 EFVGSRIARYKKPRYVVFVE--ALPKTADGSI 331
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
41-580 |
9.10e-53 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 189.48 E-value: 9.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 41 TVGDRLRSAVDQVPDKEFLIFKreGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLV 120
Cdd:PRK06178 34 PLTEYLRAWARERPQRPAIIFY--GHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 121 NINPSYQSEELRYAIEKVGIRALITPPGFKK------------SNYYQSIKDILP-EVTLKEPGksgitsrnftcfqhli 187
Cdd:PRK06178 112 PVSPLFREHELSYELNDAGAEVLLALDQLAPvveqvraetslrHVIVTSLADVLPaEPTLPLPD---------------- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 188 MFDEEDKIYPGAWKYTDVMKMGTEEDRHHlskierETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSE 267
Cdd:PRK06178 176 SLRAPRLAAAGAIDLLPALRACTAPVPLP------PPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 268 KKTIICIPNPLYHCFGCVMGVLAALTHLQTCVFPApSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIR 347
Cdd:PRK06178 250 EDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLA-RWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 348 SgfiagAPCpITLCRRLVQDMHM--------TDMQVCYGTTETSPV-SF--------MSTRDDP-------PEQRIKsvg 403
Cdd:PRK06178 329 Q-----VRV-VSFVKKLNPDYRQrwraltgsVLAEAAWGMTETHTCdTFtagfqdddFDLLSQPvfvglpvPGTEFK--- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 404 hIMDHLEAAIVdkrncivPRGVKGEVIVRGYSVMRCYWNSEEQTKkEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVR 483
Cdd:PRK06178 400 -ICDFETGELL-------PLGAEGEIVVRTPSLLKGYWNKPEATA-EALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 484 GGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAEgkTTEEDIKAWCKGKIAHFKIPR-YILfkkeY 562
Cdd:PRK06178 471 NGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGAD--LTAAALQAWCRENMAVYKVPEiRIV----D 544
|
570
....*....|....*...
gi 71994694 563 EFPLTVTGKVKKFEIREM 580
Cdd:PRK06178 545 ALPMTATGKVRKQDLQAL 562
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
54-579 |
2.20e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 187.02 E-value: 2.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 54 PDKEFLIFKREGIrkTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRY 133
Cdd:PRK06145 16 PDRAALVYRDQEI--SYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 134 AIEKVGIRalitppgfkksnyyqsikdilpevtlkepgksgitsrnftcfqhLIMFDEEDKIYPGAWKYTDVMKMGTEED 213
Cdd:PRK06145 94 ILGDAGAK--------------------------------------------LLLVDEEFDAIVALETPKIVIDAAAQAD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 214 RHHLSKIERE------TQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSeKKTIICIPNPLYHCFGCVMG 287
Cdd:PRK06145 130 SRRLAQGGLEippqaaVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLT-ASERLLVVGPLYHVGAFDLP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 288 VLAALTHLQT-CVfpAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCPITLCR---R 363
Cdd:PRK06145 209 GIAVLWVGGTlRI--HREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRdftR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 364 LVQDMHMTDmqvCYGTTET-SPVSFMSTRDDPpeQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWN 442
Cdd:PRK06145 287 VFTRARYID---AYGLTETcSGDTLMEAGREI--EKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWK 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 443 SEEQTKKEITQDrWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCA 522
Cdd:PRK06145 362 DPEKTAEAFYGD-WFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITA 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 71994694 523 WVRLhesAEGKTTE-EDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIRE 579
Cdd:PRK06145 441 VVVL---NPGATLTlEALDRHCRQRLASFKVPRQLKVRD--ELPRNPSGKVLKRVLRD 493
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
55-574 |
4.24e-51 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 184.12 E-value: 4.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 55 DKEFLIFK-REGIRKTYSQVATDAE-NLACGL-LHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEEL 131
Cdd:PRK08008 22 HKTALIFEsSGGVVRRYSYLELNEEiNRTANLfYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREES 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 132 RYAIEKVGIRALITPPGFkkSNYYQSIKDILPevtlkepgksgitsrnfTCFQHLIMFDEEDKIYPGAWKYTDVMKMGTE 211
Cdd:PRK08008 102 AWILQNSQASLLVTSAQF--YPMYRQIQQEDA-----------------TPLRHICLTRVALPADDGVSSFTQLKAQQPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 212 EDRHHlskieRETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFF----VGLRAgysekKTIICIPNPLYHC-FGCVm 286
Cdd:PRK08008 163 TLCYA-----PPLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYsawqCALRD-----DDVYLTVMPAFHIdCQCT- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 287 GVLAALTHLQTCVFpAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAgapcpitlcrrlvq 366
Cdd:PRK08008 232 AAMAAFSAGATFVL-LEKYSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHCLREVMFY-------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 367 dMHMTDMQ-------------VCYGTTETspvsFMSTRDDPP--EQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIV 431
Cdd:PRK08008 297 -LNLSDQEkdafeerfgvrllTSYGMTET----IVGIIGDRPgdKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICI 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 432 RGY---SVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHI 508
Cdd:PRK08008 372 KGVpgkTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVV 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71994694 509 VGVPDERFGEVVCAWVRLHESAEgkTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKK 574
Cdd:PRK08008 452 VGIKDSIRDEAIKAFVVLNEGET--LSEEEFFAFCEQNMAKFKVPSYLEIRK--DLPRNCSGKIIK 513
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
16-579 |
4.46e-51 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 184.58 E-value: 4.46e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 16 ANDVMVAPSRKSYVHGCSTVPLLfetvgdrLRSAVDQVPDKEFLIFkrEGIRKTYSQVATDAENLACGLLHLGLKKGDRI 95
Cdd:PRK06155 4 LGAGLAARAVDPLPPSERTLPAM-------LARQAERYPDRPLLVF--GGTRWTYAEAARAAAAAAHALAAAGVKRGDRV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 96 GIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITPPGFkksnyyqsikdiLPEVTLKEPGKSGI 175
Cdd:PRK06155 75 ALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAAL------------LAALEAADPGDLPL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 176 TsrnftcfqHLIMFDEEDKIY-PGAWKYTDVMKMGTEEDrhhlskiERETQPDDSLNIQYTSGTTGQPKGATLTHHNV-- 252
Cdd:PRK06155 143 P--------AVWLLDAPASVSvPAGWSTAPLPPLDAPAP-------AAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFyw 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 253 --LNNAFFVGLRAGysekkTIICIPNPLYHCFGCVMGVLAALTHLQTCVfpAPSFDALAALQAIHEEKCTALYGTPTMFI 330
Cdd:PRK06155 208 wgRNSAEDLEIGAD-----DVLYTTLPLFHTNALNAFFQALLAGATYVL--EPRFSASGFWPAVRRHGATVTYLLGAMVS 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 331 DMINHPEYANYNYDSIRSGFIAGAPCPITLCRRLVQDMHMTDmqvCYGTTETSPVSFmstrDDPPEQRIKSVGHIMDHLE 410
Cdd:PRK06155 281 ILLSQPARESDRAHRVRVALGPGVPAALHAAFRERFGVDLLD---GYGSTETNFVIA----VTHGSQRPGSMGRLAPGFE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 411 AAIVDKRNCIVPRGVKGEVIVRG---YSVMRCYWNSEEQTKkEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGEN 487
Cdd:PRK06155 354 ARVVDEHDQELPDGEPGELLLRAdepFAFATGYFGMPEKTV-EAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGEN 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 488 IYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHesaEGKTTE-EDIKAWCKGKIAHFKIPRYILFKKeyEFPL 566
Cdd:PRK06155 433 ISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLR---DGTALEpVALVRHCEPRLAYFAVPRYVEFVA--ALPK 507
|
570
....*....|...
gi 71994694 567 TVTGKVKKFEIRE 579
Cdd:PRK06155 508 TENGKVQKFVLRE 520
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
65-579 |
4.70e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 183.08 E-value: 4.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 65 GIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVgirali 144
Cdd:PRK09088 20 GRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDA------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 145 tppgfkksnyyqsikdilpevtlkEPgksgitsrnftcfqHLIMFDeeDKIYPGAWKYTDVMKMGTEEDRHHLSkiERET 224
Cdd:PRK09088 94 ------------------------EP--------------RLLLGD--DAVAAGRTDVEDLAAFIASADALEPA--DTPS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 225 QPDDSLN-IQYTSGTTGQPKGATLTHHNVLNNAFFVGlRAGYSEKKTIICIPNPLYHCFGCVMGVLAALTHLQTcVFPAP 303
Cdd:PRK09088 132 IPPERVSlILFTSGTSGQPKGVMLSERNLQQTAHNFG-VLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGS-ILVSN 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 304 SFDALAALQAIHEEK--CTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCPITLCRR-LVQDMHMTDmqvCYGTT 380
Cdd:PRK09088 210 GFEPKRTLGRLGDPAlgITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEDILGwLDDGIPMVD---GFGMS 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 381 ETSPVSFMSTRDDPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTG 460
Cdd:PRK09088 287 EAGTVFGMSVDCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 461 DIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEV-VCAWVrlheSAEGKTTE-ED 538
Cdd:PRK09088 367 DIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVgYLAIV----PADGAPLDlER 442
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 71994694 539 IKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIRE 579
Cdd:PRK09088 443 IRSHLSTRLAKYKVPKHLRLVD--ALPRTASGKLQKARLRD 481
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
64-572 |
3.57e-50 |
|
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: 179.65 E-value: 3.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 64 EGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRAL 143
Cdd:cd05930 9 GDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 144 ITppgfkksnyyqsikdilpevtlkepgksgitsrnftcfqhlimfdeedkiypgawkytdvmkmgteedrhhlskiere 223
Cdd:cd05930 89 LT------------------------------------------------------------------------------ 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 224 tQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIPNPlyhCF-GCVMGVLAALTHLQTCVFPA 302
Cdd:cd05930 91 -DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSF---SFdVSVWEIFGALLAGATLVVLP 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 303 PS--FDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNydSIRSGFIAGAPCPITLCRRLVQdmHMTDMQV--CYG 378
Cdd:cd05930 167 EEvrKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAALP--SLRLVLVGGEALPPDLVRRWRE--LLPGARLvnLYG 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 379 TTETS-PVSFMSTRDDPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEITQD--- 454
Cdd:cd05930 243 PTEATvDATYYRVPPDDEEDGRVPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNpfg 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 455 ---RWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHEsaE 531
Cdd:cd05930 323 pgeRMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDE--G 400
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 71994694 532 GKTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKV 572
Cdd:cd05930 401 GELDEEELRAHLAERLPDYMVPSAFVVLD--ALPLTPNGKV 439
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
220-579 |
1.13e-49 |
|
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: 179.11 E-value: 1.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 220 IERETQPDDslnIQYTSGTTGQPKGATLTHHNVLNNAFFV---GLRAGYSEKKTIICiPNPLYHC--FGCVMGVLAALTH 294
Cdd:cd05929 121 IEDEAAGWK---MLYSGGTTGRPKGIKRGLPGGPPDNDTLmaaALGFGPGADSVYLS-PAPLYHAapFRWSMTALFMGGT 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 295 LQTcvfpAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYD--SIRSGFIAGAPCPITLCRRLVqDMHMTD 372
Cdd:cd05929 197 LVL----MEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDlsSLKRVIHAAAPCPPWVKEQWI-DWGGPI 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 373 MQVCYGTTETSPVSFMSTrddppEQRIK---SVGHIMDHlEAAIVDKRNCIVPRGVKGEVIVR-GYSVMrcYWNSEEQTK 448
Cdd:cd05929 272 IWEYYGGTEGQGLTIING-----EEWLThpgSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFAnGPGFE--YTNDPEKTA 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 449 KEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHE 528
Cdd:cd05929 344 AARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAP 423
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 71994694 529 SAE-GKTTEEDIKAWCKGKIAHFKIPRYILFkkEYEFPLTVTGKVKKFEIRE 579
Cdd:cd05929 424 GADaGTALAEELIAFLRDRLSRYKCPRSIEF--VAELPRDDTGKLYRRLLRD 473
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
64-580 |
1.38e-49 |
|
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: 179.06 E-value: 1.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 64 EGIRKTYSQVATDAENLAcGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRAL 143
Cdd:cd05909 4 LGTSLTYRKLLTGAIALA-RKLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 144 ITPPGF-KKSNYYQ-----------SIKDILPEVTLKEPGKSGITSRnftcfqhlimfdeedkiYPGAWKYTDVMKMGTe 211
Cdd:cd05909 83 LTSKQFiEKLKLHHlfdveydarivYLEDLRAKISKADKCKAFLAGK-----------------FPPKWLLRIFGVAPV- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 212 edrhhlskieretQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAffvglragYSEKKTIICIPN-------PLYHCFGC 284
Cdd:cd05909 145 -------------QPDDPAVILFTSGSEGLPKGVVLSHKNLLANV--------EQITAIFDPNPEdvvfgalPFFHSFGL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 285 VMGVLAALTHLQTCVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEyaNYNYDSIRSGFIAGAPCPITLcRRL 364
Cdd:cd05909 204 TGCLWLPLLSGIKVVFHPNPLDYKKIPELIYDKKATILLGTPTFLRGYARAAH--PEDFSSLRLVVAGAEKLKDTL-RQE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 365 VQDMHMTDMQVCYGTTETSPVSFMSTRDDPpeQRIKSVGHIMDHLEAAIVDKR-NCIVPRGVKGEVIVRGYSVMRCYWNS 443
Cdd:cd05909 281 FQEKFGIRILEGYGTTECSPVISVNTPQSP--NKEGTVGRPLPGMEVKIVSVEtHEEVPIGEGGLLLVRGPNVMLGYLNE 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 444 EEQTKKEItQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVH-IVGVPDERFGEVVCA 522
Cdd:cd05909 359 PELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVaVVSVPDGRKGEKIVL 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 71994694 523 WVRLHEsaegkTTEEDIKAWCK-GKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIREM 580
Cdd:cd05909 438 LTTTTD-----TDPSSLNDILKnAGISNLAKPSYIHQVE--EIPLLGTGKPDYVTLKAL 489
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
65-578 |
1.90e-49 |
|
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: 177.67 E-value: 1.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 65 GIRKTYSQVATDAENLACGLLH-LGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGI-RA 142
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGeLGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARItVA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 143 LItppgfkksnyyqsikdilpevtlkepgksgitsrnftcfqhlimfdeedkiypgawkytdvmkmgteedrhhlskIER 222
Cdd:cd05958 88 LC---------------------------------------------------------------------------AHA 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 223 ETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIPNPLYHCFGcVMGVLAALTHL--QTCVF 300
Cdd:cd05958 93 LTASDDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFG-LGGVLLFPFGVgaSGVLL 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 301 PAPSFDALaaLQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCPITLcRRLVQDMHMTDMQVCYGTT 380
Cdd:cd05958 172 EEATPDLL--LSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAAL-HRAWKEATGIPIIDGIGST 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 381 ETSPVsFMSTRDDppEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVmrcYWNSEEQTKKEITQDRWYHTG 460
Cdd:cd05958 249 EMFHI-FISARPG--DARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGPTG---CRYLADKRQRTYVQGGWNITG 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 461 DIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLH-ESAEGKTTEEDI 539
Cdd:cd05958 323 DTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRpGVIPGPVLAREL 402
|
490 500 510
....*....|....*....|....*....|....*....
gi 71994694 540 KAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIR 578
Cdd:cd05958 403 QDHAKAHIAPYKYPRAIEFVT--ELPRTATGKLQRFALR 439
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
226-578 |
2.52e-49 |
|
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: 174.98 E-value: 2.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 226 PDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICiPNPLYHCFGCVMGVLAALTHLQTCVFPAPS- 304
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLC-GLPLFHVNGSVVTLLTPLASGAHVVLAGPAg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 305 ------FDALAALqaIHEEKCTALYGTPTMFIDMINHPeyANYNYDSIRSGFIAGAPCPITLCRRLvQDMhmTDMQVC-- 376
Cdd:cd05944 80 yrnpglFDNFWKL--VERYRITSLSTVPTVYAALLQVP--VNADISSLRFAMSGAAPLPVELRARF-EDA--TGLPVVeg 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 377 YGTTETSPVSFMSTRDDPpeQRIKSVGHIMDHLEAAIV-------DKRNCIVPRgvKGEVIVRGYSVMRCYWNSEEQtKK 449
Cdd:cd05944 153 YGLTEATCLVAVNPPDGP--KRPGSVGLRLPYARVRIKvldgvgrLLRDCAPDE--VGEICVAGPGVFGGYLYTEGN-KN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 450 EITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHES 529
Cdd:cd05944 228 AFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPG 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 71994694 530 AegKTTEEDIKAWCKGKIAH-FKIPRYILFKKeyEFPLTVTGKVKKFEIR 578
Cdd:cd05944 308 A--VVEEEELLAWARDHVPErAAVPKHIEVLE--ELPVTAVGKVFKPALR 353
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
9-586 |
5.32e-49 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 179.27 E-value: 5.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 9 LEEAALnandvmVAPSRKSYVHGcstvpllfetvgdrlrsavdqvpdkeflifkreGIRKTYSQVATDAENLACGLLHLG 88
Cdd:PLN02479 26 LERAAV------VHPTRKSVVHG---------------------------------SVRYTWAQTYQRCRRLASALAKRS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 89 LKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITPPGFkksnyyqsikdilpeVTLK 168
Cdd:PLN02479 67 IGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQEF---------------FTLA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 169 EPGKSGITSRNFTCFQH-LIMFDEEDKIYPGAWKYTdvMKMGTEEDRHHLSKIERE---TQPDD---SLNIQYTSGTTGQ 241
Cdd:PLN02479 132 EEALKILAEKKKSSFKPpLLIVIGDPTCDPKSLQYA--LGKGAIEYEKFLETGDPEfawKPPADewqSIALGYTSGTTAS 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 242 PKGATLTHHNV----LNNAFFVGLRAGYSEKKTIicipnPLYHCFG-CVMGVLAALTHLQTCVfpaPSFDALAALQAIHE 316
Cdd:PLN02479 210 PKGVVLHHRGAylmaLSNALIWGMNEGAVYLWTL-----PMFHCNGwCFTWTLAALCGTNICL---RQVTAKAIYSAIAN 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 317 EKCTALYGTPTMFIDMINHP-EYANYNYDSIRSGFIAGA-PCPITLCRRLVQDMHMTDMqvcYGTTET---SPVSFMSTR 391
Cdd:PLN02479 282 YGVTHFCAAPVVLNTIVNAPkSETILPLPRVVHVMTAGAaPPPSVLFAMSEKGFRVTHT---YGLSETygpSTVCAWKPE 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 392 DD--PPEQR--------IKSVGhiMDHLEaaIVD-KRNCIVPRGVK--GEVIVRGYSVMRCYWNSEEQTKkEITQDRWYH 458
Cdd:PLN02479 359 WDslPPEEQarlnarqgVRYIG--LEGLD--VVDtKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANE-EAFANGWFH 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 459 TGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAEG---KTT 535
Cdd:PLN02479 434 SGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKsdeAAL 513
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 71994694 536 EEDIKAWCKGKIAHFKIPRYILFKKeyeFPLTVTGKVKKFEIREMSKiELG 586
Cdd:PLN02479 514 AEDIMKFCRERLPAYWVPKSVVFGP---LPKTATGKIQKHVLRAKAK-EMG 560
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
230-572 |
7.11e-49 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 172.59 E-value: 7.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 230 LNIQYTSGTTGQPKGATLTHHNVLnnAFFVGLRAGYSEK-KTIICIPNPLYHCfGCVMGVLAALTHLQTCVFPApSFDAL 308
Cdd:cd17633 3 FYIGFTSGTTGLPKAYYRSERSWI--ESFVCNEDLFNISgEDAILAPGPLSHS-LFLYGAISALYLGGTFIGQR-KFNPK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 309 AALQAIHEEKCTALYGTPTMFIDMINHpeyaNYNYDSIRSGFIAGAPCPITLCRRLVQDMHMTDMQVCYGTTETSPVSFM 388
Cdd:cd17633 79 SWIRKINQYNATVIYLVPTMLQALART----LEPESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 389 STRDdppEQRIKSVGHIMDHLEAAIVDKRNCIVPR-GVKGEVIVRGYSVMRCYwnseeqtkkeiTQDRWYHTGDIAVMHD 467
Cdd:cd17633 155 FNQE---SRPPNSVGRPFPNVEIEIRNADGGEIGKiFVKSEMVFSGYVRGGFS-----------NPDGWMSVGDIGYVDE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 468 NGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVrlhesaEGKT-TEEDIKAWCKGK 546
Cdd:cd17633 221 EGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALY------SGDKlTYKQLKRFLKQK 294
|
330 340
....*....|....*....|....*.
gi 71994694 547 IAHFKIPRYILFKKeyEFPLTVTGKV 572
Cdd:cd17633 295 LSRYEIPKKIIFVD--SLPYTSSGKI 318
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
54-579 |
1.10e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 177.19 E-value: 1.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 54 PDKEFLIFKREGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRY 133
Cdd:PRK13391 11 PDKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 134 AIEKVGIRALITPpgfkksnyyQSIKDILPEVTLKEPGksgitsrnftcFQHLIMFDEEDKIyPGAWKYTDVMKmGTEED 213
Cdd:PRK13391 91 IVDDSGARALITS---------AAKLDVARALLKQCPG-----------VRHRLVLDGDGEL-EGFVGYAEAVA-GLPAT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 214 RhhlskIERETQPDDslnIQYTSGTTGQPKG--ATLTHHNV---LNNAFFVGLRAGYSEKKTIICiPNPLYHC--FGCVM 286
Cdd:PRK13391 149 P-----IADESLGTD---MLYSSGTTGRPKGikRPLPEQPPdtpLPLTAFLQRLWGFRSDMVYLS-PAPLYHSapQRAVM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 287 GVLAalthLQTCVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYD--SIRSGFIAGAPCPITLCRRl 364
Cdd:PRK13391 220 LVIR----LGGTVIVMEHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDlsSLEVAIHAAAPCPPQVKEQ- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 365 vqdmhMTD-----MQVCYGTTETSPVSFMstrdDPPE--QRIKSVGHIMDHlEAAIVDKRNCIVPRGVKGEVIVRGYSVM 437
Cdd:PRK13391 295 -----MIDwwgpiIHEYYAATEGLGFTAC----DSEEwlAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTIWFEGGRPF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 438 RcYWNSEEQTKKEITQDR-WYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERF 516
Cdd:PRK13391 365 E-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDL 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71994694 517 GEVVCAWVRLHESAE-GKTTEEDIKAWCKGKIAHFKIPRYILFkkEYEFPLTVTGKVKKFEIRE 579
Cdd:PRK13391 444 GEEVKAVVQPVDGVDpGPALAAELIAFCRQRLSRQKCPRSIDF--EDELPRLPTGKLYKRLLRD 505
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
235-579 |
1.35e-48 |
|
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: 172.13 E-value: 1.35e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 235 TSGTTGQPKGATLTHHNVLNNAffVGLRAGYSEKKTIICIPN-PLYHCFGCVMGVLAALTHLQTcVFPAPsfdALAALQA 313
Cdd:cd17630 8 TSGSTGTPKAVVHTAANLLASA--AGLHSRLGFGGGDSWLLSlPLYHVGGLAILVRSLLAGAEL-VLLER---NQALAED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 314 IHEEKCTALYGTPTMFIDMINHPEyANYNYDSIRSGFIAGAPCPITLCRRLvQDMHMTDMQVcYGTTETSPvsfMSTRDD 393
Cdd:cd17630 82 LAPPGVTHVSLVPTQLQRLLDSGQ-GPAALKSLRAVLLGGAPIPPELLERA-ADRGIPLYTT-YGMTETAS---QVATKR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 394 PPEQRIKSVGHIMDHLEAAIVDKrncivprgvkGEVIVRGYSVMRCYWNSEEQtkKEITQDRWYHTGDIAVMHDNGTISI 473
Cdd:cd17630 156 PDGFGRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQLV--PEFNEDGWFTTKDLGELHADGRLTV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 474 VGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHesaeGKTTEEDIKAWCKGKIAHFKIP 553
Cdd:cd17630 224 LGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGR----GPADPAELRAWLKDKLARFKLP 299
|
330 340
....*....|....*....|....*.
gi 71994694 554 RYILFKKeyEFPLTVTGKVKKFEIRE 579
Cdd:cd17630 300 KRIYPVP--ELPRTGGGKVDRRALRA 323
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
44-579 |
5.90e-47 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 172.37 E-value: 5.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 44 DRLRSAVDQvPDKEFlIFKREGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNIN 123
Cdd:PRK07514 7 DALRAAFAD-RDAPF-IETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 124 PSYQSEELRYAIEKVGIRALITPPGfkksnyyqsikdilpevtlKEPGKSGITSRNFTcfQHLIMFDEEDKiypgawkyt 203
Cdd:PRK07514 85 TAYTLAELDYFIGDAEPALVVCDPA-------------------NFAWLSKIAAAAGA--PHVETLDADGT--------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 204 dvmkmGTEEDRHHLSKIERET---QPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAffVGLRA--GYSEKKTII-CIPnp 277
Cdd:PRK07514 135 -----GSLLEAAAAAPDDFETvprGADDLAAILYTSGTTGRSKGAMLSHGNLLSNA--LTLVDywRFTPDDVLIhALP-- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 278 LYHCFGCVMGVLAALTHLQTCVFpAPSFDALAALQAIheEKCTALYGTPTMFIDMINHPEYANYNYDSIRSgFIAG-APc 356
Cdd:PRK07514 206 IFHTHGLFVATNVALLAGASMIF-LPKFDPDAVLALM--PRATVMMGVPTFYTRLLQEPRLTREAAAHMRL-FISGsAP- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 357 pitlcrrLVQDMH-----MTDMQVC--YGTTETSpvsfMSTRDdpP---EQRIKSVGHIMDHLEAAIVDKRN-CIVPRGV 425
Cdd:PRK07514 281 -------LLAETHrefqeRTGHAILerYGMTETN----MNTSN--PydgERRAGTVGFPLPGVSLRVTDPETgAELPPGE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 426 KGEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVED 505
Cdd:PRK07514 348 IGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVE 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71994694 506 VHIVGVPDERFGEVVCAWVRLHESAEGktTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIRE 579
Cdd:PRK07514 428 SAVIGVPHPDFGEGVTAVVVPKPGAAL--DEAAILAALKGRLARFKQPKRVFFVD--ELPRNTMGKVQKNLLRE 497
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
69-572 |
7.92e-47 |
|
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: 170.32 E-value: 7.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 69 TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITPPG 148
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 149 FKKSnYYQSikDILPEVTLkepgksgitsrnftcfqhlimfdeedkiypgawkytdvmkmgteEDRHHLSkIERETQPDD 228
Cdd:TIGR01923 81 LEEK-DFQA--DSLDRIEA--------------------------------------------AGRYETS-LSASFNMDQ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 229 SLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIPnPLYHCFGCVMgVLAALTHLQTCVFPAPsFDAL 308
Cdd:TIGR01923 113 IATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWLLSL-PLYHISGLSI-LFRWLIEGATLRIVDK-FNQL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 309 aaLQAIHEEKCTALYGTPTM---FIDMINHPEyanynydSIRSGFIAGAPCPITL---CRRLVQDMHMTdmqvcYGTTET 382
Cdd:TIGR01923 190 --LEMIANERVTHISLVPTQlnrLLDEGGHNE-------NLRKILLGGSAIPAPLieeAQQYGLPIYLS-----YGMTET 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 383 SPVSFMSTRDDPPEQriKSVGHIMDHLEAAI-VDKRNCIvprgvkGEVIVRGYSVMRCYWNSEEQTKKeITQDRWYHTGD 461
Cdd:TIGR01923 256 CSQVTTATPEMLHAR--PDVGRPLAGREIKIkVDNKEGH------GEIMVKGANLMKGYLYQGELTPA-FEQQGWFNTGD 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 462 IAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHeSAEGKTTeedIKA 541
Cdd:TIGR01923 327 IGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSE-SDISQAK---LIA 402
|
490 500 510
....*....|....*....|....*....|.
gi 71994694 542 WCKGKIAHFKIPryILFKKEYEFPLTVTGKV 572
Cdd:TIGR01923 403 YLTEKLAKYKVP--IAFEKLDELPYNASGKI 431
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
41-572 |
4.63e-46 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 169.96 E-value: 4.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 41 TVGDRLRSAVDQVPDKEFLIFKREGIrkTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLV 120
Cdd:TIGR03098 1 LLHHLLEDAAARLPDATALVHHDRTL--TYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 121 NINPSYQSEELRYAIEKVGIRALITPpgfkkSNYYQSIKDILPEVTLkepgksgitsrnftcFQHLIMFDEEDKIYPG-- 198
Cdd:TIGR03098 79 PINPLLKAEQVAHILADCNVRLLVTS-----SERLDLLHPALPGCHD---------------LRTLIIVGDPAHASEGhp 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 199 -----AWKytDVMKMGTEEDRHhlskierETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIIC 273
Cdd:TIGR03098 139 geepaSWP--KLLALGDADPPH-------PVIDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 274 IPnPLyhcfgcvmGVLAALTHLQTCVFPAPS---FDALA---ALQAIHEEKCTALYGTPTMFIDMINH--PEYAnynYDS 345
Cdd:TIGR03098 210 VL-PL--------SFDYGFNQLTTAFYVGATvvlHDYLLprdVLKALEKHGITGLAAVPPLWAQLAQLdwPESA---APS 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 346 IRsgFIA--GAPCPITLCRRLVQDMHMTDMQVCYGTTEtspvSFMSTRDDPPE--QRIKSVGHIMDHLEAAIV--DKRNC 419
Cdd:TIGR03098 278 LR--YLTnsGGAMPRATLSRLRSFLPNARLFLMYGLTE----AFRSTYLPPEEvdRRPDSIGKAIPNAEVLVLreDGSEC 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 420 IVprGVKGEVIVRGYSVMRCYWNSEEQTKKEITQDRWYH-----------TGDIAVMHDNGTISIVGRSKDMIVRGGENI 488
Cdd:TIGR03098 352 AP--GEEGELVHRGALVAMGYWNDPEKTAERFRPLPPFPgelhlpelavwSGDTVRRDEEGFLYFVGRRDEMIKTSGYRV 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 489 YPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRlhESAEGKTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTV 568
Cdd:TIGR03098 430 SPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVT--PPGGEELDRAALLAECRARLPNYMVPALIHVRQ--ALPRNA 505
|
....
gi 71994694 569 TGKV 572
Cdd:TIGR03098 506 NGKI 509
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
69-578 |
6.65e-46 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 167.64 E-value: 6.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 69 TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITppg 148
Cdd:cd05919 12 TYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVT--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 149 fkksnyyqsikdilpevtlkepgksgitsrnftcfqhlimfdeedkiypgawkytdvmkmgteedrhhlskieretQPDD 228
Cdd:cd05919 89 ----------------------------------------------------------------------------SADD 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 229 SLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRA-GYSEKKTIICIPNpLYHCFGCVMGVLAALTHLQTCVFPAPSFDA 307
Cdd:cd05919 93 IAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREAlGLTPGDRVFSSAK-MFFGYGLGNSLWFPLAVGASAVLNPGWPTA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 308 LAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCPITLCRRLvqdMHMTDMQVC--YGTTETSPV 385
Cdd:cd05919 172 ERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERW---MEHFGGPILdgIGATEVGHI 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 386 sFMSTRddPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEItQDRWYHTGDIAVM 465
Cdd:cd05919 249 -FLSNR--PGAWRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCR 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 466 HDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLH-ESAEGKTTEEDIKAWCK 544
Cdd:cd05919 325 DADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKsPAAPQESLARDIHRHLL 404
|
490 500 510
....*....|....*....|....*....|....
gi 71994694 545 GKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIR 578
Cdd:cd05919 405 ERLSAHKVPRRIAFVD--ELPRTATGKLQRFKLR 436
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
52-551 |
3.72e-45 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 167.85 E-value: 3.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 52 QVPDKEFLIFKREGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEEL 131
Cdd:PLN02246 35 EFSDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 132 RYAIEKVGIRALITppgfkKSNYYQSIKDILPE-----VTLKEPGksgitsRNFTCFQHLIMFDEEDkiypgawkytdvm 206
Cdd:PLN02246 115 AKQAKASGAKLIIT-----QSCYVDKLKGLAEDdgvtvVTIDDPP------EGCLHFSELTQADENE------------- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 207 kmgteedrhhLSKIEreTQPDDSLNIQYTSGTTGQPKGATLTHHNVLN-----------NAFFvglragySEKKTIICIP 275
Cdd:PLN02246 171 ----------LPEVE--ISPDDVVALPYSSGTTGLPKGVMLTHKGLVTsvaqqvdgenpNLYF-------HSDDVILCVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 276 nPLYH--CFGCVMgvLAALTHLQTCVFpAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIR---SGf 350
Cdd:PLN02246 232 -PMFHiySLNSVL--LCGLRVGAAILI-MPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRmvlSG- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 351 iaGAPcpitLCRRLvQDMHMTDMQVC-----YGTTETSPVSFMST--RDDPPEQRIKSVGHIMDHLEAAIVD-KRNCIVP 422
Cdd:PLN02246 307 --AAP----LGKEL-EDAFRAKLPNAvlgqgYGMTEAGPVLAMCLafAKEPFPVKSGSCGTVVRNAELKIVDpETGASLP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 423 RGVKGEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQS 502
Cdd:PLN02246 380 RNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPS 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 71994694 503 VEDVHIVGVPDERFGEVVCAWVRlhESAEGKTTEEDIKAWCKGKIAHFK 551
Cdd:PLN02246 460 IADAAVVPMKDEVAGEVPVAFVV--RSNGSEITEDEIKQFVAKQVVFYK 506
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
69-578 |
9.03e-45 |
|
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: 164.43 E-value: 9.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 69 TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITppg 148
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 149 fkksnyyqsikdilpevtlkepgksgitsrnftcfqhlimfDEEDKIYpgawkytdvmkmgteedrhhlskieretqpdd 228
Cdd:cd05972 79 -----------------------------------------DAEDPAL-------------------------------- 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 229 slnIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIPNP--LYHCFGCVMGVLAALTHlqTCVFPAPSFD 306
Cdd:cd05972 86 ---IYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNIADPgwAKGAWSSFFGPWLLGAT--VFVYEGPRFD 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 307 ALAALQAIHEEKCTALYGTPTMFiDMINHPEYANYNYDSIRSGFIAGAPC-PITLcrRLVQDMHMTDMQVCYGTTETSpV 385
Cdd:cd05972 161 AERILELLERYGVTSFCGPPTAY-RMLIKQDLSSYKFSHLRLVVSAGEPLnPEVI--EWWRAATGLPIRDGYGQTETG-L 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 386 SFMSTRDDPPEQriKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVR--GYSVMRCYWNSEEQTKKEITQDrWYHTGDIA 463
Cdd:cd05972 237 TVGNFPDMPVKP--GSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKlpPPGLFLGYVGDPEKTEASIRGD-YYLTGDRA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 464 VMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAEG-KTTEEDIKAW 542
Cdd:cd05972 314 YRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPsEELAEELQGH 393
|
490 500 510
....*....|....*....|....*....|....*.
gi 71994694 543 CKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIR 578
Cdd:cd05972 394 VKKVLAPYKYPREIEFVE--ELPKTISGKIRRVELR 427
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
234-572 |
1.06e-44 |
|
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: 161.70 E-value: 1.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 234 YTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKkTIICIPNPLYHcFGCVMGVLAALTHLQTCVFpAPSFDALAALQA 313
Cdd:cd17636 7 YTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEG-TVFLNSGPLFH-IGTLMFTLATFHAGGTNVF-VRRVDAEEVLEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 314 IHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIA---GAPCPIT---LCRRLVQdmhmtdmqvcYGTTEtspVSF 387
Cdd:cd17636 84 IEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSPAApewNDMATVDtspWGRKPGG----------YGQTE---VMG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 388 MSTRDDPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEiTQDRWYHTGDIAVMHD 467
Cdd:cd17636 151 LATFAALGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARR-TRGGWHHTNDLGRREP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 468 NGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAEgkTTEEDIKAWCKGKI 547
Cdd:cd17636 230 DGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGAS--VTEAELIEHCRARI 307
|
330 340
....*....|....*....|....*
gi 71994694 548 AHFKIPRYILFKKeyEFPLTVTGKV 572
Cdd:cd17636 308 ASYKKPKSVEFAD--ALPRTAGGAD 330
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
69-506 |
1.46e-44 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 163.59 E-value: 1.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 69 TYSQVATDAENLACGLL-HLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITPP 147
Cdd:TIGR01733 1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 148 GFKKSNYYQSIKDILPEVTLKEPGKSGitsrnftcfqhlimfdeedkiypgawkytdvmkmGTEEDRHHLSKieretqPD 227
Cdd:TIGR01733 81 ALASRLAGLVLPVILLDPLELAALDDA----------------------------------PAPPPPDAPSG------PD 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 228 DSLNIQYTSGTTGQPKGATLTHHNVLNnaFFVGLRA--GYSEKKTIICIPNplYHCFGCVMGVLAALTHLQTCVFPAPS- 304
Cdd:TIGR01733 121 DLAYVIYTSGSTGRPKGVVVTHRSLVN--LLAWLARryGLDPDDRVLQFAS--LSFDASVEEIFGALLAGATLVVPPEDe 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 305 --FDALAALQAIHEEKCTALYGTPTMFiDMInhPEYANYNYDSIRSGFIAGAPCPITLCRRLVQDMHMTDMQVCYGTTET 382
Cdd:TIGR01733 197 erDDAALLAALIAEHPVTVLNLTPSLL-ALL--AAALPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTET 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 383 SPVSFMSTRDDPPEQRIKSV--GHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEITQD------ 454
Cdd:TIGR01733 274 TVWSTATLVDPDDAPRESPVpiGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDpfaggd 353
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 71994694 455 --RWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDV 506
Cdd:TIGR01733 354 gaRLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREA 407
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
46-582 |
1.90e-44 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 166.73 E-value: 1.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 46 LRSAVDQVPDKEFLIFKRegIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPS 125
Cdd:PLN03102 20 LKRASECYPNRTSIIYGK--TRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 126 YQSEE----LRYAIEKVgiraLITPPGFKKsnYYQSIKDILP-EVTLKEPGKSGITSRNFTCFQHLIMFDEEDKIYPGAW 200
Cdd:PLN03102 98 LDATSiaaiLRHAKPKI----LFVDRSFEP--LAREVLHLLSsEDSNLNLPVIFIHEIDFPKRPSSEELDYECLIQRGEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 201 KYTDVMKMGTEEDRHhlskieretqpdDSLNIQYTSGTTGQPKGATLTHHNVLNNAF--FVGLRAGYSekkTIICIPNPL 278
Cdd:PLN03102 172 TPSLVARMFRIQDEH------------DPISLNYTSGTTADPKGVVISHRGAYLSTLsaIIGWEMGTC---PVYLWTLPM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 279 YHCFGCVM--GVlAALTHLQTCV--FPAPSFDALAALQAIHEEKCTalygtPTMFIDMINhpeyANYNYDSIRSG----F 350
Cdd:PLN03102 237 FHCNGWTFtwGT-AARGGTSVCMrhVTAPEIYKNIEMHNVTHMCCV-----PTVFNILLK----GNSLDLSPRSGpvhvL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 351 IAGAPCPITLCRRlVQDMHMTDMQvCYGTTE-TSPVSFMSTRDD----PPEQRIK-SVGHIMDHLEAAIVDKRNC----I 420
Cdd:PLN03102 307 TGGSPPPAALVKK-VQRLGFQVMH-AYGLTEaTGPVLFCEWQDEwnrlPENQQMElKARQGVSILGLADVDVKNKetqeS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 421 VPRGVK--GEVIVRGYSVMRCYWNSEEQTKkEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLF 498
Cdd:PLN03102 385 VPRDGKtmGEIVIKGSSIMKGYLKNPKATS-EAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLY 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 499 KHQSVEDVHIVGVPDERFGEVVCAWVRLHESAEGK--------TTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTG 570
Cdd:PLN03102 464 KYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKedrvdklvTRERDLIEYCRENLPHFMCPRKVVFLQ--ELPKNGNG 541
|
570
....*....|..
gi 71994694 571 KVKKFEIREMSK 582
Cdd:PLN03102 542 KILKPKLRDIAK 553
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
69-572 |
9.56e-44 |
|
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: 162.03 E-value: 9.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 69 TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITPPg 148
Cdd:cd05945 18 TYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPALLIADG- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 149 fkKSNYYqsikdilpevtlkepgksgitsrnftcfqhlimfdeedkiypgawkytdvmkmgteedrhhlskieretqpdd 228
Cdd:cd05945 97 --DDNAY------------------------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 229 slnIQYTSGTTGQPKGATLTHHNVLnnAFFVGLRAGY--SEKKTIICipNPLYHCFGCVMGVLAALTHLQTCVfpAPSFD 306
Cdd:cd05945 102 ---IIFTSGSTGRPKGVQISHDNLV--SFTNWMLSDFplGPGDVFLN--QAPFSFDLSVMDLYPALASGATLV--PVPRD 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 307 ALAALQA----IHEEKCTALYGTPTmFIDM-INHPEYANYNYDSIRSGFIAGAPCPITLCRRLVQDMHMTDMQVCYGTTE 381
Cdd:cd05945 173 ATADPKQlfrfLAEHGITVWVSTPS-FAAMcLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTE 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 382 TS-PVSFMSTRDDPPEQ--RIkSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEITQD---R 455
Cdd:cd05945 252 ATvAVTYIEVTPEVLDGydRL-PIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqR 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 456 WYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAEGKTT 535
Cdd:cd05945 331 AYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGLT 410
|
490 500 510
....*....|....*....|....*....|....*..
gi 71994694 536 EEdIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKV 572
Cdd:cd05945 411 KA-IKAELAERLPPYMIPRRFVYLD--ELPLNANGKI 444
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
64-575 |
1.03e-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: 162.23 E-value: 1.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 64 EGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIekvgiral 143
Cdd:cd05914 4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHIL-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 144 itppgfkksnyyqsikdilpevtlkepgksgitsrnftcfqhlimfdeedkiypgawkytdvmkmgteedRHHLSKIERE 223
Cdd:cd05914 76 ----------------------------------------------------------------------NHSEAKAIFV 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 224 TQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIPnPLYHCFGCVMGVLAALTHLQTCVF--- 300
Cdd:cd05914 86 SDEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSIL-PLHHIYPLTFTLLLPLLNGAHVVFldk 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 301 -PAPSFDALAalqaihEEKCTALYGTPTMFI-------DMINHPE--------YANYNYDSIRS--------GF------ 350
Cdd:cd05914 165 iPSAKIIALA------FAQVTPTLGVPVPLViekifkmDIIPKLTlkkfkfklAKKINNRKIRKlafkkvheAFggnike 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 351 --IAGAPCPitlcRRLVQDMHMTDMQVC--YGTTETSP-VSFmstrdDPPEQ-RIKSVGHIMDHLEAAIVDKRncivPRG 424
Cdd:cd05914 239 fvIGGAKIN----PDVEEFLRTIGFPYTigYGMTETAPiISY-----SPPNRiRLGSAGKVIDGVEVRIDSPD----PAT 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 425 VKGEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRG-GENIYPTEVEQFLfkHQSV 503
Cdd:cd05914 306 GEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKI--NNMP 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 504 ED-VHIVGVPDERfgEVVCAWV---RLHESAEGKTTEEDIKAWCKGKIAHFKIPRY--ILFKKEY--EFPLTVTGKVKKF 575
Cdd:cd05914 384 FVlESLVVVQEKK--LVALAYIdpdFLDVKALKQRNIIDAIKWEVRDKVNQKVPNYkkISKVKIVkeEFEKTPKGKIKRF 461
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
36-582 |
6.42e-41 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 156.07 E-value: 6.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 36 PLLFETVGDRlrsAVDQVPDKEFLIFKREG--IRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASA 113
Cdd:PRK06018 9 PLLCHRIIDH---AARIHGNREVVTRSVEGpiVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 114 LAGMVLVNINPSYQSEELRYAIEKVGIRALITPPGF-----KKSNYYQSIK--------DILPEVTLKepgksgitsrNF 180
Cdd:PRK06018 86 GIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLTFvpileKIADKLPSVEryvvltdaAHMPQTTLK----------NA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 181 TCFQHLImfDEEDKIYpgAWKYTDvmkmgteedrhhlskieretqPDDSLNIQYTSGTTGQPKGATLTHH-NVL-----N 254
Cdd:PRK06018 156 VAYEEWI--AEADGDF--AWKTFD---------------------ENTAAGMCYTSGTTGDPKGVLYSHRsNVLhalmaN 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 255 NAFFVGLRAgyseKKTIICIPnPLYHC--FGCVMGVLAALTHLqtcVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDM 332
Cdd:PRK06018 211 NGDALGTSA----ADTMLPVV-PLFHAnsWGIAFSAPSMGTKL---VMPGAKLDGASVYELLDTEKVTFTAGVPTVWLML 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 333 INHPEYANYNYDSIRSGFIAGAPCPitlcRRLVQDMHMTDMQV--CYGTTETSPVSFMST-----RDDPPEQRiksvghi 405
Cdd:PRK06018 283 LQYMEKEGLKLPHLKMVVCGGSAMP----RSMIKAFEDMGVEVrhAWGMTEMSPLGTLAAlkppfSKLPGDAR------- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 406 MDHL----------EAAIVDKRNCIVPRGVK--GEVIVRGYSVMRCYWNSEeqtKKEITQDRWYHTGDIAVMHDNGTISI 473
Cdd:PRK06018 352 LDVLqkqgyppfgvEMKITDDAGKELPWDGKtfGRLKVRGPAVAAAYYRVD---GEILDDDGFFDTGDVATIDAYGYMRI 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 474 VGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLhesAEGKT-TEEDIKAWCKGKIAHFKI 552
Cdd:PRK06018 429 TDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQL---KPGETaTREEILKYMDGKIAKWWM 505
|
570 580 590
....*....|....*....|....*....|
gi 71994694 553 PRYILFKKeyEFPLTVTGKVKKFEIREMSK 582
Cdd:PRK06018 506 PDDVAFVD--AIPHTATGKILKTALREQFK 533
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
80-572 |
6.77e-41 |
|
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: 154.52 E-value: 6.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 80 LACGLLHLGLKKGDRIGIWGPN--TYEWTTTQ--FASALAGMVLVNINPSYQSEELRYAIEKVGIRALITPPGfkksnyy 155
Cdd:cd05922 6 AASALLEAGGVRGERVVLILPNrfTYIELSFAvaYAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAG------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 156 qsikdilpevtlkepgksgitsrnftcfqhliMFDEEDKIYPGAwkYTDVMKMGTEEDRHHLSKIE-RETQPDDSLNIQY 234
Cdd:cd05922 79 --------------------------------AADRLRDALPAS--PDPGTVLDADGIRAARASAPaHEVSHEDLALLLY 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 235 TSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIPnPLYHCFGcvMGVLaaLTHLQ---TCVFPAPSFDALAAL 311
Cdd:cd05922 125 TSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVL-PLSYDYG--LSVL--NTHLLrgaTLVLTNDGVLDDAFW 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 312 QAIHEEKCTALYGTPTMFiDMINHPEYANYNYDSIRSGFIAGAPCPITLCRRLVQDMHMTDMQVCYGTTETSP-VSFMst 390
Cdd:cd05922 200 EDLREHGATGLAGVPSTY-AMLTRLGFDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRrMTYL-- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 391 rddPPEQ---RIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHD 467
Cdd:cd05922 277 ---PPERileKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 468 NGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDErFGEVVCAWVrlheSAEGKTTEEDIKAWCKGKI 547
Cdd:cd05922 354 DGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDP-LGEKLALFV----TAPDKIDPKDVLRSLAERL 428
|
490 500
....*....|....*....|....*
gi 71994694 548 AHFKIPRYILFKKeyEFPLTVTGKV 572
Cdd:cd05922 429 PPYKVPATVRVVD--ELPLTASGKV 451
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
67-582 |
9.57e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 155.63 E-value: 9.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 67 RKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALitp 146
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYV--- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 147 pgFKKSNYYQSIKDILPE-------VTLKEPGKSGITSRNFTCFQHLImfDEEDKIYpgAWKYTDvmkmgteedrhhlsk 219
Cdd:PRK07008 116 --LFDLTFLPLVDALAPQcpnvkgwVAMTDAAHLPAGSTPLLCYETLV--GAQDGDY--DWPRFD--------------- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 220 ierETQPDdslNIQYTSGTTGQPKGATLTHHNVLNNAFFVGL--RAGYSEKKTIICIPnPLYHCFGCVMGVLAALTHLQT 297
Cdd:PRK07008 175 ---ENQAS---SLCYTSGTTGNPKGALYSHRSTVLHAYGAALpdAMGLSARDAVLPVV-PMFHVNAWGLPYSAPLTGAKL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 298 cVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCPITLCRRLVQDMhmtDMQV-- 375
Cdd:PRK07008 248 -VLPGPDLDGKSLYELIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEY---GVEVih 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 376 CYGTTETSPVSFMST-----RDDPPEQRIKSV---GHIMDHLEAAIVDKRNCIVPRGVK--GEVIVRGYSVMRCYWNSEE 445
Cdd:PRK07008 324 AWGMTEMSPLGTLCKlkwkhSQLPLDEQRKLLekqGRVIYGVDMKIVGDDGRELPWDGKafGDLQVRGPWVIDRYFRGDA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 446 QTkkeiTQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVR 525
Cdd:PRK07008 404 SP----LVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVV 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 71994694 526 LHESAEgkTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIREMSK 582
Cdd:PRK07008 480 KRPGAE--VTREELLAFYEGKVAKWWIPDDVVFVD--AIPHTATGKLQKLKLREQFR 532
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
54-578 |
1.01e-40 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 155.77 E-value: 1.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 54 PDKEFLIFKREGIRKTYSQVATDAENLACGLLH-LGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELR 132
Cdd:PLN02574 53 NGDTALIDSSTGFSISYSELQPLVKSMAAGLYHvMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 133 YAIEKVGIRALITPPgfKKSNYYQSIKdiLPEVTLKEPGKSGITSRNFTCFQHLIMFDEEDKIYPgawkytdVMKMgtee 212
Cdd:PLN02574 133 KRVVDCSVGLAFTSP--ENVEKLSPLG--VPVIGVPENYDFDSKRIEFPKFYELIKEDFDFVPKP-------VIKQ---- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 213 drhhlskieretqpDDSLNIQYTSGTTGQPKGATLTHHNVLNNA-FFVGLRAG---YSEKKTIICIPNPLYHCFGC---V 285
Cdd:PLN02574 198 --------------DDVAAIMYSSGTTGASKGVVLTHRNLIAMVeLFVRFEASqyeYPGSDNVYLAALPMFHIYGLslfV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 286 MGVLAalthLQTCVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYN-YDSIRSGFIAGAPcpitLCRRL 364
Cdd:PLN02574 264 VGLLS----LGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEvLKSLKQVSCGAAP----LSGKF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 365 VQDMHMT----DMQVCYGTTETSPVSfmsTRDDPPEQ--RIKSVGHIMDHLEAAIVD-KRNCIVPRGVKGEVIVRGYSVM 437
Cdd:PLN02574 336 IQDFVQTlphvDFIQGYGMTESTAVG---TRGFNTEKlsKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVM 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 438 RCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFG 517
Cdd:PLN02574 413 KGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECG 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71994694 518 EVVCAW-VRLHESAegkTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIR 578
Cdd:PLN02574 493 EIPVAFvVRRQGST---LSQEAVINYVAKQVAPYKKVRKVVFVQ--SIPKSPAGKILRRELK 549
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
41-579 |
1.86e-40 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 154.53 E-value: 1.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 41 TVGdrLRSAVDQVPDKEFLIFKREGIrkTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLV 120
Cdd:PRK13382 46 TSG--FAIAAQRCPDRPGLIDELGTL--TWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADIL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 121 NINPSYQSEELRYAIEKVGIRALItppgfkksnYYQSIKDILPEVTLKEPGKSGITsrnftcfqhlimfdeedkiypgAW 200
Cdd:PRK13382 122 LLNTSFAGPALAEVVTREGVDTVI---------YDEEFSATVDRALADCPQATRIV----------------------AW 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 201 kyTDVMKMGTEE---DRHHLSKIERetQPDDSLNIQYTSGTTGQPKGATLTHhnvlnnaffvglRAGYSEKKTI------ 271
Cdd:PRK13382 171 --TDEDHDLTVEvliAAHAGQRPEP--TGRKGRVILLTSGTTGTPKGARRSG------------PGGIGTLKAIldrtpw 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 272 -----ICIPNPLYHCFGCVMGVLAALthLQTCVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSI 346
Cdd:PRK13382 235 raeepTVIVAPMFHAWGFSQLVLAAS--LACTIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 347 RSGFIA--GAPCPITLCRRLvQDMHMTDMQVCYGTTETSpvsfMSTRDDPPEQR--IKSVGHIMDHLEAAIVDKRNCIVP 422
Cdd:PRK13382 313 SLRFAAasGSRMRPDVVIAF-MDQFGDVIYNNYNATEAG----MIATATPADLRaaPDTAGRPAEGTEIRILDQDFREVP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 423 RGVKGEVIVRGYSVMRCYWNSeeqTKKEItQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQS 502
Cdd:PRK13382 388 TGEVGTIFVRNDTQFDGYTSG---STKDF-HDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPD 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71994694 503 VEDVHIVGVPDERFGEVVCAWVRLheSAEGKTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIRE 579
Cdd:PRK13382 464 VAEAAVIGVDDEQYGQRLAAFVVL--KPGASATPETLKQHVRDNLANYKVPRDIVVLD--ELPRGATGKILRRELQA 536
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
36-580 |
3.36e-40 |
|
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: 153.84 E-value: 3.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 36 PLLFETVGDRLRSAVD---QVPDKEFLIFKREGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFAS 112
Cdd:cd17642 10 PLEDGTAGEQLHKAMKryaSVPGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 113 ALAGMVLVNINPSYQSEELRYAI----------EKVGIRALITPPgfKKSNYYQSIKDILPEVTLKepgksGITSRNFTC 182
Cdd:cd17642 90 LFIGVGVAPTNDIYNERELDHSLniskptivfcSKKGLQKVLNVQ--KKLKIIKTIIILDSKEDYK-----GYQCLYTFI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 183 FQHL-IMFDEEDKIYPGAWKYTDVmkmgteedrhhlskieretqpddSLnIQYTSGTTGQPKGATLTHHNVLnnaffvgL 261
Cdd:cd17642 163 TQNLpPGFNEYDFKPPSFDRDEQV-----------------------AL-IMNSSGSTGLPKGVQLTHKNIV-------A 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 262 RAGYSEKKTIICIPN---------PLYHCFGCvmgvLAALTHLqTCVFPA---PSFDALAALQAIHEEKCTALYGTPTMF 329
Cdd:cd17642 212 RFSHARDPIFGNQIIpdtailtviPFHHGFGM----FTTLGYL-ICGFRVvlmYKFEEELFLRSLQDYKVQSALLVPTLF 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 330 IDMINHPEYANYNYDSIRSGFIAGAPCPITLCRRLVQDMHMTDMQVCYGTTE-TSPVSFMSTRDDPPeqriKSVGHIMDH 408
Cdd:cd17642 287 AFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQGYGLTEtTSAILITPEGDDKP----GAVGKVVPF 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 409 LEAAIVD-KRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGEN 487
Cdd:cd17642 363 FYAKVVDlDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQ 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 488 IYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHesaEGKT-TEEDIKAWCKGKIAHFKIPR-YILFKKeyEFP 565
Cdd:cd17642 443 VPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLE---AGKTmTEKEVMDYVASQVSTAKRLRgGVKFVD--EVP 517
|
570
....*....|....*
gi 71994694 566 LTVTGKVKKFEIREM 580
Cdd:cd17642 518 KGLTGKIDRRKIREI 532
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
226-563 |
3.80e-40 |
|
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: 150.23 E-value: 3.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 226 PDDsLNIQYTSGTTGQPKGATLTHHNVLNNAF--------------FVGLRAGYSEKKTIICIPnPLYHCFGcVMGVLAA 291
Cdd:cd05924 3 ADD-LYILYTGGTTGMPKGVMWRQEDIFRMLMggadfgtgeftpseDAHKAAAAAAGTVMFPAP-PLMHGTG-SWTAFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 292 LTHLQTCVFPAPSFDALAALQAIHEEKCTALygtpTMFIDMINHP------EYANYNYDSIRSGFIAGAPCPITLCRRLV 365
Cdd:cd05924 80 LLGGQTVVLPDDRFDPEEVWRTIEKHKVTSM----TIVGDAMARPlidalrDAGPYDLSSLFAISSGGALLSPEVKQGLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 366 Q---DMHMTDMqvcYGTTETSPVSFMSTRDDPPEQRI-KSVGHimdhlEAAIVDKRNCIVP--RGVKGEVIVRGYsVMRC 439
Cdd:cd05924 156 ElvpNITLVDA---FGSSETGFTGSGHSAGSGPETGPfTRANP-----DTVVLDDDGRVVPpgSGGVGWIARRGH-IPLG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 440 YWNSEEQTKK---EITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERF 516
Cdd:cd05924 227 YYGDEAKTAEtfpEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERW 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 71994694 517 GEVVCAWVRLHESAEgkTTEEDIKAWCKGKIAHFKIPRYILFKKEYE 563
Cdd:cd05924 307 GQEVVAVVQLREGAG--VDLEELREHCRTRIARYKLPKQVVFVDEIE 351
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
66-579 |
5.06e-40 |
|
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: 152.97 E-value: 5.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 66 IRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGiralit 145
Cdd:cd05915 23 HRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAE------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 146 ppgfkksnyyqsikdilPEVTLKEPGKSGITSRNFTCFQHLIMFDEEDKIYPgawKYTDVMKMGTEEdrhhlSKIERETQ 225
Cdd:cd05915 97 -----------------DKVLLFDPNLLPLVEAIRGELKTVQHFVVMDEKAP---EGYLAYEEALGE-----EADPVRVP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 226 PDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIPN-PLYHCFG-CVMGVLAALTHLQTCVFPAP 303
Cdd:cd05915 152 ERAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKDVVLPVvPMFHVNAwCLPYAATLVGAKQVLPGPRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 304 SFDALaaLQAIHEEKCTALYGTPTMfIDMINHPEyanynyDSIRSGF------IAGAPCPITLCRRLvQDMHMTDMQVCY 377
Cdd:cd05915 232 DPASL--VELFDGEGVTFTAGVPTV-WLALADYL------ESTGHRLktlrrlVVGGSAAPRSLIAR-FERMGVEVRQGY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 378 GTTET----SPVSFMSTRDDPPEQ---RIKSVGHIMDHLEAA-IVDKRNCIVPRGVKG--EVIVRGYSVMRCYWNSEEQT 447
Cdd:cd05915 302 GLTETspvvVQNFVKSHLESLSEEeklTLKAKTGLPIPLVRLrVADEEGRPVPKDGKAlgEVQLKGPWITGGYYGNEEAT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 448 KKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLH 527
Cdd:cd05915 382 RSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPR 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 71994694 528 EsAEGKttEEDIKAWCKGKIAHFK-IPRYILFKKeyEFPLTVTGKVKKFEIRE 579
Cdd:cd05915 462 G-EKPT--PEELNEHLLKAGFAKWqLPDAYVFAE--EIPRTSAGKFLKRALRE 509
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
42-579 |
7.12e-40 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 153.12 E-value: 7.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 42 VGDRLRSAVDQVPDKEFLIFKREGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVN 121
Cdd:PRK05852 18 IADLVEVAATRLPEAPALVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 122 INPSYQSEELRYAIEKVGIRALI---TPPGfkksnyyqsikDILPEVTLKEPGKSGITSRNftcfqhlimfdeedkiypG 198
Cdd:PRK05852 98 LDPALPIAEQRVRSQAAGARVVLidaDGPH-----------DRAEPTTRWWPLTVNVGGDS------------------G 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 199 AWKYTDVMKMGTEEDRHHLSKIERETQPDDSLnIQYTSGTTGQPKGATLTHHNVLnnAFFVGLRAGYS---EKKTIICIP 275
Cdd:PRK05852 149 PSGGTLSVHLDAATEPTPATSTPEGLRPDDAM-IMFTGGTTGLPKMVPWTHANIA--SSVRAIITGYRlspRDATVAVMP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 276 npLYHCFGCVMGVLAALTHLQTCVFPAPS-FDALAALQAIHEEKCTALYGTPTMFIDMINHP--EYANYNYDSIRsgFIA 352
Cdd:PRK05852 226 --LYHGHGLIAALLATLASGGAVLLPARGrFSAHTFWDDIKAVGATWYTAVPTIHQILLERAatEPSGRKPAALR--FIR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 353 GAPCPITL-CRRLVQDMHMTDMQVCYGTTE-----TSPVSFMSTRDDPPEQRIKSVGHiMDHLEAAIVDKRNCIVPRGVK 426
Cdd:PRK05852 302 SCSAPLTAeTAQALQTEFAAPVVCAFGMTEathqvTTTQIEGIGQTENPVVSTGLVGR-STGAQIRIVGSDGLPLPAGAV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 427 GEVIVRGYSVMRCYWNSEEQTKKEITqDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDV 506
Cdd:PRK05852 381 GEVWLRGTTVVRGYLGDPTITAANFT-DGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEA 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71994694 507 HIVGVPDERFGEVVCAWVRLHESAEgkTTEEDIKAWCKGKIAHFKIPRYilFKKEYEFPLTVTGKVKKFEIRE 579
Cdd:PRK05852 460 AVFGVPDQLYGEAVAAVIVPRESAP--PTAEELVQFCRERLAAFEIPAS--FQEASGLPHTAKGSLDRRAVAE 528
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
67-516 |
7.63e-40 |
|
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: 151.74 E-value: 7.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 67 RKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITp 146
Cdd:cd17640 5 RITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 147 pgfkksnyyqsikdilpevtlkepgksgitsrnftcfqhlimfdeedkiypgawkytdvmkmgteedrhhlskierETQP 226
Cdd:cd17640 84 ----------------------------------------------------------------------------ENDS 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 227 DDSLNIQYTSGTTGQPKGATLTH----HNVLNNAFFVGLRAGysekKTIICIPnPLYHCFgcvmgvlaalthlqtcvfpA 302
Cdd:cd17640 88 DDLATIIYTSGTTGNPKGVMLTHanllHQIRSLSDIVPPQPG----DRFLSIL-PIWHSY-------------------E 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 303 PSFDALAALQAIhEEKCTALygtPTMFIDMinhpeyANYN----------YDSIRSG-------------FIAGAPCPIT 359
Cdd:cd17640 144 RSAEYFIFACGC-SQAYTSI---RTLKDDL------KRVKphyivsvprlWESLYSGiqkqvsksspikqFLFLFFLSGG 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 360 LCRRLVQD-----MHM--------TDMQVCYGTTETSPVSfmsTRDDPPEQRIKSVGHIMDHLEAAIVD-KRNCIVPRGV 425
Cdd:cd17640 214 IFKFGISGggalpPHVdtffeaigIEVLNGYGLTETSPVV---SARRLKCNVRGSVGRPLPGTEIKIVDpEGNVVLPPGE 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 426 KGEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIV-RGGENIYPTEVEQFLFKHQSVE 504
Cdd:cd17640 291 KGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVlSNGENVEPQPIEEALMRSPFIE 370
|
490
....*....|..
gi 71994694 505 DVHIVGvPDERF 516
Cdd:cd17640 371 QIMVVG-QDQKR 381
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
44-572 |
2.24e-39 |
|
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: 150.43 E-value: 2.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 44 DRLRSAVDQVPDKEFLIFkrEGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNIN 123
Cdd:cd12117 1 ELFEEQAARTPDAVAVVY--GDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 124 PSYQSEELRYAIEKVGIRALITPPGFKksnyyQSIKDILPEVTLKEPGKSGitsrnftcfqhlimfdeedkiypgawkyt 203
Cdd:cd12117 79 PELPAERLAFMLADAGAKVLLTDRSLA-----GRAGGLEVAVVIDEALDAG----------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 204 dvmkmGTEEDRHHLSkieretqPDDSLNIQYTSGTTGQPKGATLTHHNVLN---NAFFVGLRAGysekKTIICIPNP--- 277
Cdd:cd12117 125 -----PAGNPAVPVS-------PDDLAYVMYTSGSTGRPKGVAVTHRGVVRlvkNTNYVTLGPD----DRVLQTSPLafd 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 278 --LYHCFGcvmgvlaALTHLQTCVFPAPSF--DALAALQAIHEEKCTALYGTPTMFIDMIN-HPEYanynYDSIRSGFIA 352
Cdd:cd12117 189 asTFEIWG-------ALLNGARLVLAPKGTllDPDALGALIAEEGVTVLWLTAALFNQLADeDPEC----FAGLRELLTG 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 353 GAPCPITLCRRLVQDMHMTDMQVCYGTTE--TSPVSFMSTRDDPPEQRIkSVGHIMDHLEAAIVDKRNCIVPRGVKGEVI 430
Cdd:cd12117 258 GEVVSPPHVRRVLAACPGLRLVNGYGPTEntTFTTSHVVTELDEVAGSI-PIGRPIANTRVYVLDEDGRPVPPGVPGELY 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 431 VRGYSVMRCYWNSEEQTKKEITQD------RWYHTGDIAVMHDNGTISIVGRSKDMI-VRgGENIYPTEVEQFLFKHQSV 503
Cdd:cd12117 337 VGGDGLALGYLNRPALTAERFVADpfgpgeRLYRTGDLARWLPDGRLEFLGRIDDQVkIR-GFRIELGEIEAALRAHPGV 415
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71994694 504 EDVHIVGVPDERFGEVVCAWVrlheSAEGKTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKV 572
Cdd:cd12117 416 REAVVVVREDAGGDKRLVAYV----VAEGALDAAELRAFLRERLPAYMVPAAFVVLD--ELPLTANGKV 478
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
69-580 |
2.96e-39 |
|
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: 150.76 E-value: 2.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 69 TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALitppg 148
Cdd:TIGR02262 32 SYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVV----- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 149 FKKSNYYQSIKDILPEV-TLKEPGKSGITSRNFTCFQHLIMfDEEDKIYPGAwkytdvmkmgteedrhhlskiereTQPD 227
Cdd:TIGR02262 107 FVSGALLPVIKAALGKSpHLEHRVVVGRPEAGEVQLAELLA-TESEQFKPAA------------------------TQAD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 228 DSLNIQYTSGTTGQPKGATLTHHNVLNNA-FFVGLRAGYSEKKTIICIPNpLYHCFG------CVMGVLAALTHLQTCVF 300
Cdd:TIGR02262 162 DPAFWLYSSGSTGMPKGVVHTHSNPYWTAeLYARNTLGIREDDVCFSAAK-LFFAYGlgnaltFPMSVGATTVLMGERPT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 301 PAPSFDALAALQAiheekcTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCPITLCRRLvQDMHMTDMQVCYGTT 380
Cdd:TIGR02262 241 PDAVFDRLRRHQP------TIFYGVPTLYAAMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRW-QARFGVDIVDGIGST 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 381 ETSPVsFMSTRddPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEItQDRWYHTG 460
Cdd:TIGR02262 314 EMLHI-FLSNL--PGDVRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTF-QGEWTRSG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 461 DIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESaeGKTTEEDIK 540
Cdd:TIGR02262 390 DKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPG--QTALETELK 467
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 71994694 541 AWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIREM 580
Cdd:TIGR02262 468 EHVKDRLAPYKYPRWIVFVD--DLPKTATGKIQRFKLREG 505
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
54-579 |
2.36e-38 |
|
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: 148.93 E-value: 2.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 54 PDKE---FLIFKREGIRK-TYSQVATDAENLACGLLHLGlKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNI---NPSY 126
Cdd:cd05931 7 PDRPaytFLDDEGGREETlTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLpppTPGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 127 QSEELRYAIEKVGIRALITPPGFKksnyyqsikDILPEVTLKEPGKSgitsrnftcfqhlimfdeedkiyPGAWKYTDVM 206
Cdd:cd05931 86 HAERLAAILADAGPRVVLTTAAAL---------AAVRAFAASRPAAG-----------------------TPRLLVVDLL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 207 KMGTEEDRHhlskiERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNafFVGLRAGYSEKKTIICIP-NPLYHCFGCV 285
Cdd:cd05931 134 PDTSAADWP-----PPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLAN--VRQIRRAYGLDPGDVVVSwLPLYHDMGLI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 286 MGVLAALTHLQTCVFPAP-SF--DALAALQAIHEEKCTALYGtPTmF-----IDMINHPEYANYNYDSIRSGFIAGAPC- 356
Cdd:cd05931 207 GGLLTPLYSGGPSVLMSPaAFlrRPLRWLRLISRYRATISAA-PN-FaydlcVRRVRDEDLEGLDLSSWRVALNGAEPVr 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 357 PITLcRRLVQDM-----HMTDMQVCYG-----------TTETSPVS------------FMSTRDDPPEQRIKSVGHIMDH 408
Cdd:cd05931 285 PATL-RRFAEAFapfgfRPEAFRPSYGlaeatlfvsggPPGTGPVVlrvdrdalagraVAVAADDPAARELVSCGRPLPD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 409 LEAAIVDKRNCI-VPRGVKGEVIVRGYSVMRCYWNSEEQTKK------EITQDRWYHTGDIAVMHDnGTISIVGRSKDMI 481
Cdd:cd05931 364 QEVRIVDPETGReLPDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaATDEGGWLRTGDLGFLHD-GELYITGRLKDLI 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 482 VRGGENIYPTEVEQFLFKHQSVEDVHIV---GVPDERFGEVVCawVRLHESAEGKTTEEDIKAWCKGKIA-HFKI-PRYI 556
Cdd:cd05931 443 IVRGRNHYPQDIEATAEEAHPALRPGCVaafSVPDDGEERLVV--VAEVERGADPADLAAIAAAIRAAVArEHGVaPADV 520
|
570 580
....*....|....*....|...
gi 71994694 557 LFKKEYEFPLTVTGKVKKFEIRE 579
Cdd:cd05931 521 VLVRPGSIPRTSSGKIQRRACRA 543
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
64-578 |
5.85e-38 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 145.65 E-value: 5.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 64 EGIRK--TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIR 141
Cdd:cd05971 1 KGTPEkvTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 142 ALITppgfkksnyyqsikdilpevtlkepgksgitsrnftcfqhlimfDEedkiypgawkytdvmkmgteedrhhlskie 221
Cdd:cd05971 81 ALVT--------------------------------------------DG------------------------------ 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 222 retqPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLragysekkTIICIPNPLYhCF----------GCVMGVLAA 291
Cdd:cd05971 87 ----SDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQF--------PFNLFPRDGD-LYwtpadwawigGLLDVLLPS 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 292 LTHLQTCV-FPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPcpitLCRRLVQ---D 367
Cdd:cd05971 154 LYFGVPVLaHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGES----LGEELLGwarE 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 368 MHMTDMQVCYGTTETSPV-----SFMSTRDDPPEQRIKsvGHIMdhleaAIVDKRNCIVPRGVKGEVIVR--GYSVMRCY 440
Cdd:cd05971 230 QFGVEVNEFYGQTECNLVigncsALFPIKPGSMGKPIP--GHRV-----AIVDDNGTPLPPGEVGEIAVElpDPVAFLGY 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 441 WNSEEQTKKEITQDrWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVV 520
Cdd:cd05971 303 WNNPSATEKKMAGD-WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIV 381
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 71994694 521 CAWVRLHESAEGKTT-EEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIR 578
Cdd:cd05971 382 KAFVVLNPGETPSDAlAREIQELVKTRLAAHEYPREIEFVN--ELPRTATGKIRRRELR 438
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
65-572 |
8.33e-38 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 150.07 E-value: 8.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 65 GIRKTYSQVATDAENLAcGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALI 144
Cdd:PRK08633 639 GGELSYGKALTGALALA-RLLKRELKDEENVGILLPPSVAGALANLALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVI 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 145 TPPGF-----KKSNYYQSikDILPEVTLKEPGKSGITSRNFTCFQHLImfdeedKIYPGAWkytdvmkmgteedrhhLSK 219
Cdd:PRK08633 718 TSRKFleklkNKGFDLEL--PENVKVIYLEDLKAKISKVDKLTALLAA------RLLPARL----------------LKR 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 220 IERET-QPDDSLNIQYTSGTTGQPKGATLTHHNVLNN--AFFVGLRAgysEKKTIICIPNPLYHCFGCVMGVLAALTHLQ 296
Cdd:PRK08633 774 LYGPTfKPDDTATIIFSSGSEGEPKGVMLSHHNILSNieQISDVFNL---RNDDVILSSLPFFHSFGLTVTLWLPLLEGI 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 297 TCVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSgFIAGAPcpiTLCRRLVQDMHM---TDM 373
Cdd:PRK08633 851 KVVYHPDPTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRL-VVAGAE---KLKPEVADAFEEkfgIRI 926
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 374 QVCYGTTETSPVSFMSTRD----DPPEQ---RIKSVGHIMDHLEAAIVDKRNC-IVPRGVKGEVIVRGYSVMRCYWNSEE 445
Cdd:PRK08633 927 LEGYGATETSPVASVNLPDvlaaDFKRQtgsKEGSVGMPLPGVAVRIVDPETFeELPPGEDGLILIGGPQVMKGYLGDPE 1006
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 446 QTK---KEITQDRWYHTGDIAVMHDNGTISIVGR----SKdmIvrGGENIYPTEVEQFLFK--HQSVEDVHIVGVPDERF 516
Cdd:PRK08633 1007 KTAeviKDIDGIGWYVTGDKGHLDEDGFLTITDRysrfAK--I--GGEMVPLGAVEEELAKalGGEEVVFAVTAVPDEKK 1082
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 71994694 517 GEVVcawVRLHESAEgKTTEEDIKAWCKGKIAHFKIPRYIlFKKEyEFPLTVTGKV 572
Cdd:PRK08633 1083 GEKL---VVLHTCGA-EDVEELKRAIKESGLPNLWKPSRY-FKVE-ALPLLGSGKL 1132
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
69-572 |
9.30e-38 |
|
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: 145.34 E-value: 9.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 69 TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITppg 148
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 149 fkksnyyqsikdilpevtlkepgksgitsrnftcfqhlimfdeedkiypgawkytdvmkmgTEEdrhhlskIERETQPDD 228
Cdd:cd05969 79 -------------------------------------------------------------TEE-------LYERTDPED 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 229 SLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIPNPLYhCFGCVMGVLAALTHLQTCVFPAPSFDAL 308
Cdd:cd05969 91 PTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYWCTADPGW-VTGTVYGIWAPWLNGVTNVVYEGRFDAE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 309 AALQAIHEEKCTALYGTPTMFIDMINHPEY--ANYNYDSIRSGFIAGAPCPITLCRRLVQDMHMTdMQVCYGTTETSPVS 386
Cdd:cd05969 170 SWYGIIERVKVTVWYTAPTAIRMLMKEGDElaRKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVP-IHDTWWQTETGSIM 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 387 FMSTrddpPEQRIK--SVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVR-GY-SVMRCYWNSEEQTKKEITqDRWYHTGDI 462
Cdd:cd05969 249 IANY----PCMPIKpgSMGKPLPGVKAAVVDENGNELPPGTKGILALKpGWpSMFRGIWNDEERYKNSFI-DGWYLTGDL 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 463 AVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAE-GKTTEEDIKA 541
Cdd:cd05969 324 AYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEpSDELKEEIIN 403
|
490 500 510
....*....|....*....|....*....|.
gi 71994694 542 WCKGKIAHFKIPRYILFKKeyEFPLTVTGKV 572
Cdd:cd05969 404 FVRQKLGAHVAPREIEFVD--NLPKTRSGKI 432
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
68-579 |
2.24e-37 |
|
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: 145.82 E-value: 2.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 68 KTYSQVATDAENLACGLLHLGLK--KGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALIT 145
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 146 PPGFKksnyyqsikdilpevtlkepgksgitsrnftcfqhlimfdeedkiypgAWKYTDVMKMGTEedrhhlsKIERETQ 225
Cdd:cd05927 86 DAGVK------------------------------------------------VYSLEEFEKLGKK-------NKVPPPP 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 226 PD-DSLN-IQYTSGTTGQPKGATLTHHNVLNN--AFFVGLRAGYSEKKTIICIPN-PLYHCFGCVMgVLAALTH------ 294
Cdd:cd05927 111 PKpEDLAtICYTSGTTGNPKGVMLTHGNIVSNvaGVFKILEILNKINPTDVYISYlPLAHIFERVV-EALFLYHgakigf 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 295 -----------LQTC---VFPA-PS-FDAL-AALQAIHEEKctalyGTPTMFIdminhpeyANYNYDSIRSGFIAGAPCP 357
Cdd:cd05927 190 ysgdirlllddIKALkptVFPGvPRvLNRIyDKIFNKVQAK-----GPLKRKL--------FNFALNYKLAELRSGVVRA 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 358 ITLCRRLV----QDMH------------------MTDMQVC--------YGTTETSPVSFMSTRDDppeqriKSVGHI-- 405
Cdd:cd05927 257 SPFWDKLVfnkiKQALggnvrlmltgsaplspevLEFLRVAlgcpvlegYGQTECTAGATLTLPGD------TSVGHVgg 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 406 -MDHLEAAIVDkrnciVP--------RGVKGEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGR 476
Cdd:cd05927 331 pLPCAEVKLVD-----VPemnydakdPNPRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDR 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 477 SKDMI-VRGGENIYPTEVEQFLFKHQSVEDVHIVG-----------VPDErfgEVVCAWVRLHESAEG------------ 532
Cdd:cd05927 406 KKNIFkLSQGEYVAPEKIENIYARSPFVAQIFVYGdslksflvaivVPDP---DVLKEWAASKGGGTGsfeelcknpevk 482
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 71994694 533 KTTEEDIKAWCK-GKIAHFKIPRYILFKKEyEFP-----LTVTGKVKKFEIRE 579
Cdd:cd05927 483 KAILEDLVRLGKeNGLKGFEQVKAIHLEPE-PFSvenglLTPTFKLKRPQLKK 534
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
55-587 |
6.37e-37 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 145.04 E-value: 6.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 55 DKEFLIFK-REGIRK-TYSQVAtDAENLACGLLH-LGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEEL 131
Cdd:PRK04319 59 DKVALRYLdASRKEKyTYKELK-ELSNKFANVLKeLGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 132 RYAIEKVGIRALITPPgfkkSNYYQSIKDILPEVtlkepgksgitsrnftcfQHLIMFDEEDKIYPGAWKYTDVMKMGTE 211
Cdd:PRK04319 138 RDRLEDSEAKVLITTP----ALLERKPADDLPSL------------------KHVLLVGEDVEEGPGTLDFNALMEQASD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 212 EdrhhlSKIErETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNN---AFFV-GLRagysekktiiciPNPLYHCF----- 282
Cdd:PRK04319 196 E-----FDIE-WTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHyqtGKYVlDLH------------EDDVYWCTadpgw 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 283 --GCVMGVLAALTHLQTCVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINH-PEYAN-YNYDSIRsgFIA--GAPC 356
Cdd:PRK04319 258 vtGTSYGIFAPWLNGATNVIDGGRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAgDDLVKkYDLSSLR--HILsvGEPL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 357 -PITLC---RRLVQDMHMTDMQvcygtTETSPVSFMSTrddpPEQRIK--SVGHIMDHLEAAIVDKRNCIVPRGVKGE-V 429
Cdd:PRK04319 336 nPEVVRwgmKVFGLPIHDNWWM-----TETGGIMIANY----PAMDIKpgSMGKPLPGIEAAIVDDQGNELPPNRMGNlA 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 430 IVRGY-SVMRCYWNSEEQTKKEITQDrWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHI 508
Cdd:PRK04319 407 IKKGWpSMMRGIWNNPEKYESYFAGD-WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGV 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 509 VGVPDERFGEVVCAWVRLHESAEGktTEE---DIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVkkfeIREMSKI-E 584
Cdd:PRK04319 486 IGKPDPVRGEIIKAFVALRPGYEP--SEElkeEIRGFVKKGLGAHAAPREIEFKD--KLPKTRSGKI----MRRVLKAwE 557
|
...
gi 71994694 585 LGL 587
Cdd:PRK04319 558 LGL 560
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
54-589 |
7.42e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 143.38 E-value: 7.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 54 PDKEFLIFKREGIrkTYSQVATDAENLAcGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRy 133
Cdd:PRK07638 15 PNKIAIKENDRVL--TYKDWFESVCKVA-NWLNEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELK- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 134 aiEKVGIralitppgfkksnyyqSIKDILpevtlkepgksgITSRNFtcfqhLIMFDEEDKiypGAWKYTDVMKMGTEED 213
Cdd:PRK07638 91 --ERLAI----------------SNADMI------------VTERYK-----LNDLPDEEG---RVIEIDEWKRMIEKYL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 214 RHHLSKIERETQPddsLNIQYTSGTTGQPKGATLTHHNVLNnAFFVGLRAGYSEKKTIICIPNPLYHC-FgcVMGVLAAL 292
Cdd:PRK07638 133 PTYAPIENVQNAP---FYMGFTSGSTGKPKAFLRAQQSWLH-SFDCNVHDFHMKREDSVLIAGTLVHSlF--LYGAISTL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 293 tHLQTCVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANyNYDSIRSgfiAGAPCPITLCRRLVQDMHMTD 372
Cdd:PRK07638 207 -YVGQTVHLMRKFIPNQVLDKLETENISVMYTVPTMLESLYKENRVIE-NKMKIIS---SGAKWEAEAKEKIKNIFPYAK 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 373 MQVCYGTTETSPVSFMSTRDDppEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNsEEQTKKEIT 452
Cdd:PRK07638 282 LYEFYGASELSFVTALVDEES--ERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYII-GGVLARELN 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 453 QDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVrlhesaEG 532
Cdd:PRK07638 359 ADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII------KG 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 71994694 533 KTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIREMSKIELGLQQ 589
Cdd:PRK07638 433 SATKQQLKSFCLQRLSSFKIPKEWHFVD--EIPYTNSGKIARMEAKSWIENQEKIYE 487
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
40-531 |
1.18e-35 |
|
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: 143.46 E-value: 1.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 40 ETVGDRLRSAVDQVPDKEFLIFkrEGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVL 119
Cdd:COG1020 476 ATLHELFEAQAARTPDAVAVVF--GDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAY 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 120 VNINPSYQSEELRYAIEKVGIRALITPpgfkksnyyQSIKDILPEVTLkepgksgitsrnftcfqHLIMFDEEdkiypga 199
Cdd:COG1020 554 VPLDPAYPAERLAYMLEDAGARLVLTQ---------SALAARLPELGV-----------------PVLALDAL------- 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 200 wkytdvmkmgtEEDRHHLSKIERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIicipnPLY 279
Cdd:COG1020 601 -----------ALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRV-----LQF 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 280 H--CF-GCVMGVLAALTHLQTCVFPAPS--FDALAALQAIHEEKCTALYGTPTMFiDMInhPEYANYNYDSIRSGFIAGA 354
Cdd:COG1020 665 AslSFdASVWEIFGALLSGATLVLAPPEarRDPAALAELLARHRVTVLNLTPSLL-RAL--LDAAPEALPSLRLVLVGGE 741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 355 PCPITLCRRLVQDMHMTDMQVCYGTTETS-PVSFMSTRDDPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRG 433
Cdd:COG1020 742 ALPPELVRRWRARLPGARLVNLYGPTETTvDSTYYEVTPPDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGG 821
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 434 YSVMRCYWNSEEQTKK-------EITQDRWYHTGDIAVMHDNGTISIVGRSKDMI-VRGgeniY---PTEVEQFLFKHQS 502
Cdd:COG1020 822 AGLARGYLNRPELTAErfvadpfGFPGARLYRTGDLARWLPDGNLEFLGRADDQVkIRG----FrieLGEIEAALLQHPG 897
|
490 500
....*....|....*....|....*....
gi 71994694 503 VEDVHIVGVPDERFGEVVCAWVRLHESAE 531
Cdd:COG1020 898 VREAVVVAREDAPGDKRLVAYVVPEAGAA 926
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
54-580 |
2.30e-35 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 140.13 E-value: 2.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 54 PDKEFLIfkrEGIRK-TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELR 132
Cdd:PRK10946 37 SDAIAVI---CGERQfSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVAPVNALFSHQRSELN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 133 YAIEKVGIRALITP---PGFKKSNYYQSIKDILP--EVTLKEpGKSGITSrnftcFQHLIMFDEEDKIY-Pgawkytdvm 206
Cdd:PRK10946 114 AYASQIEPALLIADrqhALFSDDDFLNTLVAEHSslRVVLLL-NDDGEHS-----LDDAINHPAEDFTAtP--------- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 207 kmgteedrhhlskiereTQPDDSLNIQYTSGTTGQPKGATLTHhnvlnNAFFVGLRA-----GYSEKKTIIC-IPNPlyH 280
Cdd:PRK10946 179 -----------------SPADEVAFFQLSGGSTGTPKLIPRTH-----NDYYYSVRRsveicGFTPQTRYLCaLPAA--H 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 281 CF-----GcVMGVLAAlthlQTCVFPAPSFDALAALQAIHEEKCTALYGTP---TMFIDMINHPEYaNYNYDSIRSGFIA 352
Cdd:PRK10946 235 NYpmsspG-ALGVFLA----GGTVVLAPDPSATLCFPLIEKHQVNVTALVPpavSLWLQAIAEGGS-RAQLASLKLLQVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 353 GAPCPITLCRR--------LVQDMHMTDMQVCYgttetspvsfmsTR-DDPPEQRIKSVGHIM-DHLEAAIVDKRNCIVP 422
Cdd:PRK10946 309 GARLSETLARRipaelgcqLQQVFGMAEGLVNY------------TRlDDSDERIFTTQGRPMsPDDEVWVADADGNPLP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 423 RGVKGEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQS 502
Cdd:PRK10946 377 QGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPA 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 503 VEDVHIVGVPDERFGEVVCAWVrlhesaegkTTEEDIKA-----WCKGK-IAHFKIP-RYILFKkeyEFPLTVTGKVKKF 575
Cdd:PRK10946 457 VIHAALVSMEDELMGEKSCAFL---------VVKEPLKAvqlrrFLREQgIAEFKLPdRVECVD---SLPLTAVGKVDKK 524
|
....*
gi 71994694 576 EIREM 580
Cdd:PRK10946 525 QLRQW 529
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
54-578 |
3.34e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 138.99 E-value: 3.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 54 PDKEFLIFKREGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRY 133
Cdd:PRK13390 11 PDRPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 134 AIEKVGIRALITPpgfkksnyyQSIKDILPEVTLKEPGKSGITSR--NFTCFqhlimfdeEDKIYPGAWKYTDvmkmgte 211
Cdd:PRK13390 91 IVGDSGARVLVAS---------AALDGLAAKVGADLPLRLSFGGEidGFGSF--------EAALAGAGPRLTE------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 212 edrhhlskieretQPDDSLNIqYTSGTTGQPKG--ATLTHHNV---------LNNAFFvglraGYSEKKtIICIPNPLYH 280
Cdd:PRK13390 147 -------------QPCGAVML-YSSGTTGFPKGiqPDLPGRDVdapgdpivaIARAFY-----DISESD-IYYSSAPIYH 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 281 CFG---CVMgvlaaLTHLQTCVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMI--NHPEYANYNYDSIRSGFIAGAP 355
Cdd:PRK13390 207 AAPlrwCSM-----VHALGGTVVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLLklDADVRTRYDVSSLRAVIHAAAP 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 356 CPITLCRRLVqDMHMTDMQVCYGTTETSPVSFMSTRDDPPEQriKSVGH-IMDHLEaaIVDKRNCIVPRGVKGEVIVRGY 434
Cdd:PRK13390 282 CPVDVKHAMI-DWLGPIVYEYYSSTEAHGMTFIDSPDWLAHP--GSVGRsVLGDLH--ICDDDGNELPAGRIGTVYFERD 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 435 SVMRCYWNSEEQTK--KEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVP 512
Cdd:PRK13390 357 RLPFRYLNDPEKTAaaQHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVP 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71994694 513 DERFGEVVCAWVRLHESAEGktTEE---DIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIR 578
Cdd:PRK13390 437 DPEMGEQVKAVIQLVEGIRG--SDElarELIDYTRSRIAHYKAPRSVEFVD--ELPRTPTGKLVKGLLR 501
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
54-574 |
5.74e-34 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 135.15 E-value: 5.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 54 PDKEFLIFKREGIrkTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRY 133
Cdd:cd17655 11 PDHTAVVFEDQTL--TYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 134 AIEKVGIRALITppgfkksnyyqsikdilpevtlKEPGKSGITsrnftcFQHLIMFDEEDKIYPGawkytdvmkmgteed 213
Cdd:cd17655 89 ILEDSGADILLT----------------------QSHLQPPIA------FIGLIDLLDEDTIYHE--------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 214 rhHLSKIERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIicipnPLYHCF---GCVMGVLA 290
Cdd:cd17655 126 --ESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRV-----ALFASIsfdASVTEIFA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 291 ALTHLQT-CVFPAPS-FDALAALQAIHEEKCTALYGTPTmfidMINHPEYAN-YNYDSIRSGFIAGAPCPITLCRRLVQD 367
Cdd:cd17655 199 SLLSGNTlYIVRKETvLDGQALTQYIRQNRITIIDLTPA----HLKLLDAADdSEGLSLKHLIVGGEALSTELAKKIIEL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 368 MHMT-DMQVCYGTTETSpVSFMSTRDDPPEQRIKSV--GHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSE 444
Cdd:cd17655 275 FGTNpTITNAYGPTETT-VDASIYQYEPETDQQVSVpiGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRP 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 445 EQTKKEITQD------RWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGE 518
Cdd:cd17655 354 ELTAEKFVDDpfvpgeRMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQN 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 71994694 519 VVCAWVrlheSAEGKTTEEDIKAWCKGKIAHFKIPRYilFKKEYEFPLTVTGKVKK 574
Cdd:cd17655 434 YLCAYI----VSEKELPVAQLREFLARELPDYMIPSY--FIKLDEIPLTPNGKVDR 483
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
223-574 |
1.81e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 133.58 E-value: 1.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 223 ETQPDDSLNIQYTSGTTGQPKGATLTHHNV------LNNAF-------FV-GLragysekktiicipnPLYHCFGCVMGV 288
Cdd:PRK07787 124 EPDPDAPALIVYTSGTTGPPKGVVLSRRAIaadldaLAEAWqwtaddvLVhGL---------------PLFHVHGLVLGV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 289 LAAL------THLqtcVFPAPSFDAlAALQAiheeKCTALYGTPTMFIDMINHPEYAnynyDSIRSG--FIAG-APCPIT 359
Cdd:PRK07787 189 LGPLrignrfVHT---GRPTPEAYA-QALSE----GGTLYFGVPTVWSRIAADPEAA----RALRGArlLVSGsAALPVP 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 360 LCRRLVqdmHMTDMQVC--YGTTETspVSFMSTRDDPpEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVK--GEVIVRGYS 435
Cdd:PRK07787 257 VFDRLA---ALTGHRPVerYGMTET--LITLSTRADG-ERRPGWVGLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPT 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 436 VMRCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGR-SKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDE 514
Cdd:PRK07787 331 LFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDD 410
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 515 RFGEVVCAWVrlheSAEGKTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKK 574
Cdd:PRK07787 411 DLGQRIVAYV----VGADDVAADELIDFVAQQLSVHKRPREVRFVD--ALPRNAMGKVLK 464
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
226-579 |
3.07e-33 |
|
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: 133.38 E-value: 3.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 226 PDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIpNPLYHCFGCVMGVLA-ALTHLQTCVFPAPS 304
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSW-MPLTHDMGLIAFHLApLIAGMNQYLMPTRL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 305 F--DALAALQAIHEEKCTALyGTPT----MFIDMINHPEYANYNYDSIRSGFIAGAPCPITLCRRLVQDM-----HMTDM 373
Cdd:cd05908 184 FirRPILWLKKASEHKATIV-SSPNfgykYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMskyglKRNAI 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 374 QVCYGTTETS-PVSF------------------------MSTRDDPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGE 428
Cdd:cd05908 263 LPVYGLAEASvGASLpkaqspfktitlgrrhvthgepepEVDKKDSECLTFVEVGKPIDETDIRICDEDNKILPDGYIGH 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 429 VIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHdNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVE--DV 506
Cdd:cd05908 343 IQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFIR-NGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVElgRV 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 507 HIVGVPDE--RFGEVVCAwvrlhesAEGKTTEEDIKAWCKgkiahfKIPRYILFKKEYE---------FPLTVTGKVKKF 575
Cdd:cd05908 422 VACGVNNSntRNEEIFCF-------IEHRKSEDDFYPLGK------KIKKHLNKRGGWQinevlpirrIPKTTSGKVKRY 488
|
....
gi 71994694 576 EIRE 579
Cdd:cd05908 489 ELAQ 492
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
69-579 |
8.21e-33 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 132.98 E-value: 8.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 69 TYSQVATDAENLAcGLLH--LGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITP 146
Cdd:PRK05620 40 TFAAIGARAAALA-HALHdeLGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVAD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 147 PGFKKSnyyqsIKDILPEVTLKEP----GKSGITS------RNFTCFQHLIMFDEEDKIYPgaWKytdvmkmgteedrhh 216
Cdd:PRK05620 119 PRLAEQ-----LGEILKECPCVRAvvfiGPSDADSaaahmpEGIKVYSYEALLDGRSTVYD--WP--------------- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 217 lskierETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAffVGLRAGYSEKKT-----IICIPnpLYHCFGcvMGV-LA 290
Cdd:PRK05620 177 ------ELDETTAAAICYSTGTTGAPKGVVYSHRSLYLQS--LSLRTTDSLAVThgesfLCCVP--IYHVLS--WGVpLA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 291 ALTHLQTCVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMI-----NHPEYAnynydSIRSGFIAGAPCPITLCRrLV 365
Cdd:PRK05620 245 AFMSGTPLVFPGPDLSAPTLAKIIATAMPRVAHGVPTLWIQLMvhylkNPPERM-----SLQEIYVGGSAVPPILIK-AW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 366 QDMHMTDMQVCYGTTETSPVSfmsTRDDPP-----EQRIK---SVGHIMDHLEAAIVDK--------RNcivprgvKGEV 429
Cdd:PRK05620 319 EERYGVDVVHVWGMTETSPVG---TVARPPsgvsgEARWAyrvSQGRFPASLEYRIVNDgqvmestdRN-------EGEI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 430 IVRGYSVMRCYWNSEEQT----------------KKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEV 493
Cdd:PRK05620 389 QVRGNWVTASYYHSPTEEgggaastfrgedvedaNDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQL 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 494 EQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAE-GKTTEEDIKAWCKGKIAHFKIPRYILFKKEYEfpLTVTGKV 572
Cdd:PRK05620 469 ENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEpTRETAERLRDQLRDRLPNWMLPEYWTFVDEID--KTSVGKF 546
|
....*..
gi 71994694 573 KKFEIRE 579
Cdd:PRK05620 547 DKKDLRQ 553
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
49-572 |
2.18e-32 |
|
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: 130.54 E-value: 2.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 49 AVDQVPDKEFLIFkrEGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQS 128
Cdd:cd17651 4 QAARTPDAPALVA--EGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 129 EELRYAIEKVGIRALITPPGFKksnyyqsikdilpevtlkepgksgitsrnftcfqhlimFDEEDKIYPGAWkyTDVMKM 208
Cdd:cd17651 82 ERLAFMLADAGPVLVLTHPALA--------------------------------------GELAVELVAVTL--LDQPGA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 209 GTEEDRHHlskiERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNnafFVGLRAGYSEKKTiiCIPNPLYHCFG---CV 285
Cdd:cd17651 122 AAGADAEP----DPALDADDLAYVIYTSGSTGRPKGVVMPHRSLAN---LVAWQARASSLGP--GARTLQFAGLGfdvSV 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 286 MGVLAALTHLQTCVFPAP----SFDALAALqaIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCPIT-L 360
Cdd:cd17651 193 QEIFSTLCAGATLVLPPEevrtDPPALAAW--LDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLVLTeD 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 361 CRRLVQDMHMTDMQVCYGTTETSPVSFMSTRDDPPEQ-RIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRC 439
Cdd:cd17651 271 LREFCAGLPGLRLHNHYGPTETHVVTALSLPGDPAAWpAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 440 YWNSEEQTKKEITQD------RWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPD 513
Cdd:cd17651 351 YLNRPELTAERFVPDpfvpgaRMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLARED 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 514 ERFGEVVCAWVRLHESAEGKTteEDIKAWCKGKIAHFKIP-RYILFKkeyEFPLTVTGKV 572
Cdd:cd17651 431 RPGEKRLVAYVVGDPEAPVDA--AELRAALATHLPEYMVPsAFVLLD---ALPLTPNGKL 485
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
88-579 |
8.83e-32 |
|
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: 129.51 E-value: 8.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 88 GLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITppgfkksnyyqsIKDILPEVtl 167
Cdd:cd05928 63 GLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVT------------SDELAPEV-- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 168 kepgkSGITSRNFTCFQHLIMfdeEDKIYPGAWKYTDVMKMGTEEdrHHLSKiereTQPDDSLNIQYTSGTTGQPKGATL 247
Cdd:cd05928 129 -----DSVASECPSLKTKLLV---SEKSRDGWLNFKELLNEASTE--HHCVE----TGSQEPMAIYFTSGTTGSPKMAEH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 248 THHNVlnnaffvGLRAGYSEKKTIICIPNPLYHCFGCVMGVLAALTHL------QTCVF--PAPSFDALAALQAIHEEKC 319
Cdd:cd05928 195 SHSSL-------GLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLfepwiqGACVFvhHLPRFDPLVILKTLSSYPI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 320 TALYGTPTMFiDMINHPEYANYNYDSIRSGFIAGAPC-PITLCRRLVQDMhmTDMQVCYGTTETSPVSfmstrDDPPEQR 398
Cdd:cd05928 268 TTFCGAPTVY-RMLVQQDLSSYKFPSLQHCVTGGEPLnPEVLEKWKAQTG--LDIYEGYGQTETGLIC-----ANFKGMK 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 399 IK--SVGHIMDHLEAAIVDKRNCIVPRGVKGEVIV-----RGYSVMRCYWNSEEQTKKEITQDrWYHTGDIAVMHDNGTI 471
Cdd:cd05928 340 IKpgSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIrvkpiRPFGLFSGYVDNPEKTAATIRGD-FYLTGDRGIMDEDGYF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 472 SIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAEGKTTEE---DIKAWCKGKIA 548
Cdd:cd05928 419 WFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSHDPEQltkELQQHVKSVTA 498
|
490 500 510
....*....|....*....|....*....|.
gi 71994694 549 HFKIPRYILFKKeyEFPLTVTGKVKKFEIRE 579
Cdd:cd05928 499 PYKYPRKVEFVQ--ELPKTVTGKIQRNELRD 527
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
50-574 |
1.24e-31 |
|
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: 127.67 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 50 VDQVPDKEFLIFkrEGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSE 129
Cdd:cd17645 8 VERTPDHVAVVD--RGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 130 ELRYaiekvgiralitppgfkksnyyqsikdilpevtlkepgksgitsrnftcfqhlIMFDEEDKIYPgawkytdvmkmg 209
Cdd:cd17645 86 RIAY-----------------------------------------------------MLADSSAKILL------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 210 teedrhhlskiereTQPDDSLNIQYTSGTTGQPKGATLTHHNVLN------NAFFVGlragySEKKTIIcipnplYHCFG 283
Cdd:cd17645 101 --------------TNPDDLAYVIYTSGSTGLPKGVMIEHHNLVNlcewhrPYFGVT-----PADKSLV------YASFS 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 284 CVMGVLAALTHLQtcvfpapsfdALAALQAIHEEKctalygtpTMFIDMINhpEYANYNYDSIrsGFIagapcPITLCRR 363
Cdd:cd17645 156 FDASAWEIFPHLT----------AGAALHVVPSER--------RLDLDALN--DYFNQEGITI--SFL-----PTGAAEQ 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 364 LVQdMHMTDMQVC--------------------YGTTETSPVSfMSTRDDPPEQRIkSVGHIMDHLEAAIVDKRNCIVPR 423
Cdd:cd17645 209 FMQ-LDNQSLRVLltggdklkkierkgyklvnnYGPTENTVVA-TSFEIDKPYANI-PIGKPIDNTRVYILDEALQLQPI 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 424 GVKGEVIVRGYSVMRCYWNSEEQTKKE------ITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFL 497
Cdd:cd17645 286 GVAGELCIAGEGLARGYLNRPELTAEKfivhpfVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFL 365
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71994694 498 FKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAEgkttEEDIKAWCKGKIAHFKIPRYilFKKEYEFPLTVTGKVKK 574
Cdd:cd17645 366 MNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIP----HEELREWLKNDLPDYMIPTY--FVHLKALPLTANGKVDR 436
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
35-579 |
4.01e-31 |
|
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: 127.61 E-value: 4.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 35 VPLLFETVGDRLRSAVDQVPDKEFLIFKRE-GIRK--TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFA 111
Cdd:cd05970 12 VPENFNFAYDVVDAMAKEYPDKLALVWCDDaGEERifTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 112 SALAGMVLVNINPSYQSEELRYAIEKVGIRALITPPGfkkSNYYQSIKDILPEVtlkePGKSGITSRNFTCFQHLIMFDE 191
Cdd:cd05970 92 LHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAE---DNIPEEIEKAAPEC----PSKPKLVWVGDPVPEGWIDFRK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 192 EdkiypgawkytdVMKMGTEEDRHHlskIERETQPDDSLNIQYTSGTTGQPK----------GATLTH---HNVLNNaff 258
Cdd:cd05970 165 L------------IKNASPDFERPT---ANSYPCGEDILLVYFSSGTTGMPKmvehdftyplGHIVTAkywQNVREG--- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 259 vGLRAGYSEKKTIICIPNPLYHCFGCVMGVLaalthlqtcVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMInHPEY 338
Cdd:cd05970 227 -GLHLTVADTGWGKAVWGKIYGQWIAGAAVF---------VYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLI-REDL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 339 ANYNYDSIRSGFIAGAPCPITLCRRLVQDMHMTDMQvCYGTTETS-PVSFMSTRDDPPeqriKSVGHIMDHLEAAIVDKR 417
Cdd:cd05970 296 SRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLME-GFGQTETTlTIATFPWMEPKP----GSMGKPAPGYEIDLIDRE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 418 NCIVPRGVKGEVIVR-----GYSVMRCYWNSEEQTKkEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTE 492
Cdd:cd05970 371 GRSCEAGEEGEIVIRtskgkPVGLFGGYYKDAEKTA-EVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 493 VEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAE-GKTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGK 571
Cdd:cd05970 450 VESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEpSEELKKELQDHVKKVTAPYKYPRIVEFVD--ELPKTISGK 527
|
....*...
gi 71994694 572 VKKFEIRE 579
Cdd:cd05970 528 IRRVEIRE 535
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
43-572 |
6.81e-31 |
|
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: 126.24 E-value: 6.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 43 GDRLRSAVDQVPDKEFLIFkrEGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNI 122
Cdd:cd17646 1 HALVAEQAARTPDAPAVVD--EGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 123 NPSYQSEELRYAIEKVGIRALITPPgfkksnyyqsikdilpevtlkepgksgitsrnftcfqhlimfDEEDKIYPGAwky 202
Cdd:cd17646 79 DPGYPADRLAYMLADAGPAVVLTTA------------------------------------------DLAARLPAGG--- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 203 TDVMKMGTEEDRHHLSKIERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNafFVGLRAGY-------SEKKTiicip 275
Cdd:cd17646 114 DVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNR--LLWMQDEYplgpgdrVLQKT----- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 276 nPLyhCFG-CVMGVLAALTHLQTCVFPAPSF--DALAALQAIHEEKCTALYGTPTM---FIDMINHPEYAnynydSIRSG 349
Cdd:cd17646 187 -PL--SFDvSVWELFWPLVAGARLVVARPGGhrDPAYLAALIREHGVTTCHFVPSMlrvFLAEPAAGSCA-----SLRRV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 350 FIAGAPCPITLCRRLVQDMHMTdMQVCYGTTETS-PVSFMSTRDDPPEQRIkSVGHIMDHLEAAIVDKRNCIVPRGVKGE 428
Cdd:cd17646 259 FCSGEALPPELAARFLALPGAE-LHNLYGPTEAAiDVTHWPVRGPAETPSV-PIGRPVPNTRLYVLDDALRPVPVGVPGE 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 429 VIVRGYSVMRCYWNSEEQTKKEITQD------RWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQS 502
Cdd:cd17646 337 LYLGGVQLARGYLGRPALTAERFVPDpfgpgsRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPA 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 503 VEDVHIVGVPDERFGEVVCAWVRLHESAEGKTTEEdIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKV 572
Cdd:cd17646 417 VTHAVVVARAAPAGAARLVGYVVPAAGAAGPDTAA-LRAHLAERLPEYMVPAAFVVLD--ALPLTANGKL 483
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
46-578 |
1.00e-30 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 127.22 E-value: 1.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 46 LRSAVDQVPDKEFLIFKRE-GIRK--TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNI 122
Cdd:cd05968 67 LDKWLADTRTRPALRWEGEdGTSRtlTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 123 NPSYQSEELRYAIEKVGIRALITPPGFKKSNYYQSIKDILPEVTLKEPgksgiTSRNFTCFQHLIMFDEEDKIYPGAWky 202
Cdd:cd05968 147 FSGFGKEAAATRLQDAEAKALITADGFTRRGREVNLKEEADKACAQCP-----TVEKVVVVRHLGNDFTPAKGRDLSY-- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 203 tdvmkmgTEEDRHHLSKIEReTQPDDSLNIQYTSGTTGQPKGATLTHhnvlnnaffvglrAGYSEKKTIicipnPLYHCF 282
Cdd:cd05968 220 -------DEEKETAGDGAER-TESEDPLMIIYTSGTTGKPKGTVHVH-------------AGFPLKAAQ-----DMYFQF 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 283 --------------GCVMG---VLAALTHLQTCVF--PAPSFDALAAL-QAIHEEKCTALYGTPTMFIDMINHPEyANYN 342
Cdd:cd05968 274 dlkpgdlltwftdlGWMMGpwlIFGGLILGATMVLydGAPDHPKADRLwRMVEDHEITHLGLSPTLIRALKPRGD-APVN 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 343 YDSIRSGFIAGA------PCPITLCRRLVQDMHMTdmQVCY-GTTETSPVSFMSTRDDPpeqrIKSVGH--IMDHLEAAI 413
Cdd:cd05968 353 AHDLSSLRVLGStgepwnPEPWNWLFETVGKGRNP--IINYsGGTEISGGILGNVLIKP----IKPSSFngPVPGMKADV 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 414 VDKRNCIVPRGVkGEVIVRG--YSVMRCYWNSEE---QTKKEITQDRWYHtGDIAVMHDNGTISIVGRSKDMIVRGGENI 488
Cdd:cd05968 427 LDESGKPARPEV-GELVLLApwPGMTRGFWRDEDrylETYWSRFDNVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRV 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 489 YPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHES-AEGKTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLT 567
Cdd:cd05968 505 GPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGvTPTEALAEELMERVADELGKPLSPERILFVK--DLPKT 582
|
570
....*....|.
gi 71994694 568 VTGKVKKFEIR 578
Cdd:cd05968 583 RNAKVMRRVIR 593
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
224-574 |
6.81e-29 |
|
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: 119.72 E-value: 6.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 224 TQPDDSLNIQYTSGTTGQPKGATLTHHNVLnnAFFVGLRAGYSEkktiicipNP-----LYHCFG---CVMGVLAALTHL 295
Cdd:cd17643 90 TDPDDLAYVIYTSGSTGRPKGVVVSHANVL--ALFAATQRWFGF--------NEddvwtLFHSYAfdfSVWEIWGALLHG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 296 QTCVFP----APSFDALAALqaIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCPITLCRRLVQDM--- 368
Cdd:cd17643 160 GRLVVVpyevARSPEDFARL--LRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFgld 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 369 --HMTDMqvcYGTTETS-PVSFMS-TRDDPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSE 444
Cdd:cd17643 238 rpQLVNM---YGITETTvHVTFRPlDAADLPAAAASPIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 445 EQTKKEITQD-------RWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFG 517
Cdd:cd17643 315 ELTAERFVANpfggpgsRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGD 394
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 71994694 518 EVVCAWVRLHESAEgkTTEEDIKAWCKGKIAHFKIP-RYILFKkeyEFPLTVTGKVKK 574
Cdd:cd17643 395 TRLVAYVVADDGAA--ADIAELRALLKELLPDYMVPaRYVPLD---ALPLTVNGKLDR 447
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
69-494 |
1.08e-28 |
|
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: 120.92 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 69 TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITppg 148
Cdd:cd05933 10 TYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVV--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 149 fkkSNYYQ-----SIKDILPE----VTLKEPGKsgitsrnftcfqhlimfDEEDKIYpgAWKytDVMKMGTEEDRHHLSK 219
Cdd:cd05933 87 ---ENQKQlqkilQIQDKLPHlkaiIQYKEPLK-----------------EKEPNLY--SWD--EFMELGRSIPDEQLDA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 220 IERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSE---KKTIICIPNPLYHCFGCVMGVLAALTHLQ 296
Cdd:cd05933 143 IISSQKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPatvGQESVVSYLPLSHIAAQILDIWLPIKVGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 297 TCVFPAPsfDALAA--LQAIHEEKCTALYGTPTMFIDM-------------------------------------INHPE 337
Cdd:cd05933 223 QVYFAQP--DALKGtlVKTLREVRPTAFMGVPRVWEKIqekmkavgaksgtlkrkiaswakgvgletnlklmggeSPSPL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 338 Y---ANY----------NYDSIRSGFIAGAPCPI-TLCRRLVQDMHMTDmqvCYGTTETSPVSFMSTrddPPEQRIKSVG 403
Cdd:cd05933 301 FyrlAKKlvfkkvrkalGLDRCQKFFTGAAPISReTLEFFLSLNIPIME---LYGMSETSGPHTISN---PQAYRLLSCG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 404 HIMDHLEAAIvDKRNCivpRGVkGEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVR 483
Cdd:cd05933 375 KALPGCKTKI-HNPDA---DGI-GEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIIT 449
|
490
....*....|..
gi 71994694 484 -GGENIYPTEVE 494
Cdd:cd05933 450 aGGENVPPVPIE 461
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
228-574 |
1.83e-28 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 116.59 E-value: 1.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 228 DSLNIQYTSGTTGQPKGATLTHhnvlnNAFFVGLRAGYSEKKTIIC-----IPNPLYHCFGcVMGVLAALTHLQTCVFPA 302
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLAN-----KTFFAVPDILQKEGLNWVVgdvtyLPLPATHIGG-LWWILTCLIHGGLCVTGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 303 PSFDALAALQAIHEEKCTALYGTPTMFIDMINhpEYANYNYDSIRSGFIA-GAPCPITLCRRLVQDMHMTDMQVCYGTTE 381
Cdd:cd17635 76 ENTTYKSLFKILTTNAVTTTCLVPTLLSKLVS--ELKSANATVPSLRLIGyGGSRAIAADVRFIEATGLTNTAQVYGLSE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 382 TSPVSFMSTRDDPPEqrIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEITqDRWYHTGD 461
Cdd:cd17635 154 TGTALCLPTDDDSIE--INAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI-DGWVNTGD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 462 IAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAEgKTTEEDIKA 541
Cdd:cd17635 231 LGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELD-ENAIRALKH 309
|
330 340 350
....*....|....*....|....*....|...
gi 71994694 542 WCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKK 574
Cdd:cd17635 310 TIRRELEPYARPSTIVIVT--DIPRTQSGKVKR 340
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
69-577 |
2.46e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 118.95 E-value: 2.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 69 TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITppg 148
Cdd:PRK13383 62 SYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVA--- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 149 fkKSNYYQSIKDILPEVTLKEPGKSGItsrnftcfqhlimfdEEDKIYPgawkytdvmkmgteedrhhlskierETQPDD 228
Cdd:PRK13383 139 --DNEFAERIAGADDAVAVIDPATAGA---------------EESGGRP-------------------------AVAAPG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 229 SLnIQYTSGTTGQPKGatLTHHNVLNNAFFVG--------LRAGysekkTIICIPNPLYHCFGcvMGVLAALTHLQTCVF 300
Cdd:PRK13383 177 RI-VLLTSGTTGKPKG--VPRAPQLRSAVGVWvtildrtrLRTG-----SRISVAMPMFHGLG--LGMLMLTIALGGTVL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 301 PAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEY--ANYNYDSIRSGFIAGAPCPITLCRRLVqDMHMTDMQVCYG 378
Cdd:PRK13383 247 THRHFDAEAALAQASLHRADAFTAVPVVLARILELPPRvrARNPLPQLRVVMSSGDRLDPTLGQRFM-DTYGDILYNGYG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 379 TTETSPVSFMSTRD--DPPEqrikSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYwnSEEQTKKEItqDRW 456
Cdd:PRK13383 326 STEVGIGALATPADlrDAPE----TVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRY--TDGGGKAVV--DGM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 457 YHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAEgkTTE 536
Cdd:PRK13383 398 TSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSG--VDA 475
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 71994694 537 EDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEI 577
Cdd:PRK13383 476 AQLRDYLKDRVSRFEQPRDINIVS--SIPRNPTGKVLRKEL 514
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
34-509 |
1.13e-27 |
|
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: 117.38 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 34 TVPLLFETVGDRLRSAVDQVPDKeFLIFKRE---GIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQF 110
Cdd:cd05906 4 RPEGAPRTLLELLLRAAERGPTK-GITYIDAdgsEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 111 ASALAGMVLVNINPSYQSEELRYAIEKV-GIRALITPPgfkksnyyqsikDILPEVTLKEPGKsGITSRNFTCFQHLIMF 189
Cdd:cd05906 83 ACVLAGFVPAPLTVPPTYDEPNARLRKLrHIWQLLGSP------------VVLTDAELVAEFA-GLETLSGLPGIRVLSI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 190 DEEDKiypgawkytdvmkmgTEEDrHHLskieRETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKk 269
Cdd:cd05906 150 EELLD---------------TAAD-HDL----PQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQ- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 270 TIICIPNPLYHCFGCVM-GVLAALTHLQTCVFPAPSF--DALAALQAIHEEKCTALYGtPTMFIDMIN----HPEYANYN 342
Cdd:cd05906 209 DVFLNWVPLDHVGGLVElHLRAVYLGCQQVHVPTEEIlaDPLRWLDLIDRYRVTITWA-PNFAFALLNdlleEIEDGTWD 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 343 YDSIRSGFIAGAPCPITLCRRLVQ-----DMHMTDMQVCYGTTETSPVSFMSTR----DDPPEQRIKSVGHIMDHLEAAI 413
Cdd:cd05906 288 LSSLRYLVNAGEAVVAKTIRRLLRllepyGLPPDAIRPAFGMTETCSGVIYSRSfptyDHSQALEFVSLGRPIPGVSMRI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 414 VDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHdNGTISIVGRSKDMIVRGGENIYPTEV 493
Cdd:cd05906 368 VDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEI 446
|
490
....*....|....*.
gi 71994694 494 EqflfkhQSVEDVHIV 509
Cdd:cd05906 447 E------AAVEEVPGV 456
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
69-510 |
3.42e-27 |
|
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: 115.64 E-value: 3.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 69 TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITppg 148
Cdd:cd05932 8 TWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 149 fKKSNYYQSIKDILPEVTLKEPGKSGITSRNFTCFQHLImfdeedkiypgawkytdvmkmgteeDRHHLSKIERETQPDD 228
Cdd:cd05932 85 -GKLDDWKAMAPGVPEGLISISLPPPSAANCQYQWDDLI-------------------------AQHPPLEERPTRFPEQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 229 SLNIQYTSGTTGQPKGATLTHhnvlnNAFFVGLRAGYsekKTIICIPN-------PLYHCFGCVMGVLAALtHLQTCVFP 301
Cdd:cd05932 139 LATLIYTSGTTGQPKGVMLTF-----GSFAWAAQAGI---EHIGTEENdrmlsylPLAHVTERVFVEGGSL-YGGVLVAF 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 302 APSFDALaaLQAIHEEKCTALYGTP---TMF------------------IDMIN----HPEYANYNYDSIRSGFIAGAPC 356
Cdd:cd05932 210 AESLDTF--VEDVQRARPTLFFSVPrlwTKFqqgvqdkipqqklnlllkIPVVNslvkRKVLKGLGLDQCRLAGCGSAPV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 357 PITLC---RRLvqdmhmtDMQVC--YGTTETSPVSFMSTrddPPEQRIKSVGHIMDHLEAAIVDKrncivprgvkGEVIV 431
Cdd:cd05932 288 PPALLewyRSL-------GLNILeaYGMTENFAYSHLNY---PGRDKIGTVGNAGPGVEVRISED----------GEILV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 432 RGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMI-VRGGENIYPTEVEQFLFKHQSVEDVHIVG 510
Cdd:cd05932 348 RSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
69-572 |
5.37e-27 |
|
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: 114.68 E-value: 5.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 69 TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITPPG 148
Cdd:cd12114 14 TYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLTDGP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 149 fkksnyyQSIKDILPEVTLKEPGKSGITSRNFTcfqhlimfdeedkiypgawkytdvmkmgteedrhhlskiERETQPDD 228
Cdd:cd12114 94 -------DAQLDVAVFDVLILDLDALAAPAPPP---------------------------------------PVDVAPDD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 229 SLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIpNPL------YHCFGcVMGVLAALthlqtcVFPA 302
Cdd:cd12114 128 LAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLAL-SSLsfdlsvYDIFG-ALSAGATL------VLPD 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 303 PS--FDALAALQAIHEEKCTALYGTPTMFiDMI-NHPEYANYNYDSIRSGFIAGAPCPITLCRRLVQ---DMHMTDMQvc 376
Cdd:cd12114 200 EArrRDPAHWAELIERHGVTLWNSVPALL-EMLlDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRAlapDARLISLG-- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 377 yGTTETSPVSFMSTRDDPPEQRiKSV--GHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEITQD 454
Cdd:cd12114 277 -GATEASIWSIYHPIDEVPPDW-RSIpyGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTH 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 455 ----RWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVhIVGVPDERFGEVVCAWVRLHESA 530
Cdd:cd12114 355 pdgeRLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARA-VVVVLGDPGGKRLAAFVVPDNDG 433
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 71994694 531 EGkTTEEDIKAWCKGKIAHFKIPRYILFkkEYEFPLTVTGKV 572
Cdd:cd12114 434 TP-IAPDALRAFLAQTLPAYMIPSRVIA--LEALPLTANGKV 472
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
22-589 |
7.47e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 116.98 E-value: 7.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 22 APSRKSYVHGCSTVPLLFETVGDRLRSAVDQV---PDKEFLIFKREgiRKTYSQVATDAENLACGLLHLGLKKGDRIGIW 98
Cdd:PRK12316 490 AEERGQLVEGWNATAAEYPLQRGVHRLFEEQVertPEAPALAFGEE--TLDYAELNRRANRLAHALIERGVGPDVLVGVA 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 99 GPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITPpgfkksnyyQSIKDILPEvtlkepgKSGITsr 178
Cdd:PRK12316 568 MERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQ---------SHLGRKLPL-------AAGVQ-- 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 179 nftcfqhLIMFDEedkiyPGAWKytdvmkmgteeDRHHLSKIERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLN---- 254
Cdd:PRK12316 630 -------VLDLDR-----PAAWL-----------EGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNrlcw 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 255 --NAFFVGLRAGYSEkKTIICIPNPLYHCFGCVMG----VLAAlthlqtcvfPAPSFDALAALQAIHEEKCTALYGTPTM 328
Cdd:PRK12316 687 mqQAYGLGVGDTVLQ-KTPFSFDVSVWEFFWPLMSgarlVVAA---------PGDHRDPAKLVELINREGVDTLHFVPSM 756
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 329 FIDMINHPEYAnyNYDSIRSGFIAGAPCPITLCRRLVQDMHMTDMQVCYGTTETSPVSFMSTRDDPPEQRIkSVGHIMDH 408
Cdd:PRK12316 757 LQAFLQDEDVA--SCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGGDSV-PIGRPIAN 833
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 409 LEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEITQD------RWYHTGDIAVMHDNGTISIVGRSKDMIV 482
Cdd:PRK12316 834 LACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSpfvageRMYRTGDLARYRADGVIEYAGRIDHQVK 913
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 483 RGGENIYPTEVEQFLFKHQSVEDVHIVGVPderfGEVVCAWVRLheSAEGKTTEEDIKAWCKGKIAHFKIPRYILFKKey 562
Cdd:PRK12316 914 LRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVL--ESEGGDWREALKAHLAASLPEYMVPAQWLALE-- 985
|
570 580
....*....|....*....|....*..
gi 71994694 563 EFPLTVTGKVKKfeiREMSKIELGLQQ 589
Cdd:PRK12316 986 RLPLTPNGKLDR---KALPAPEASVAQ 1009
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
63-572 |
1.10e-26 |
|
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: 113.54 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 63 REGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRA 142
Cdd:cd12116 8 DDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 143 LITPPgfkksnyyqsikdilpevTLKEPGKSGITsrnftcfqhLIMFDEEDKIYPGAwkytdvmkmgteedrhhlsKIER 222
Cdd:cd12116 88 VLTDD------------------ALPDRLPAGLP---------VLLLALAAAAAAPA-------------------APRT 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 223 ETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNnaFFVGLRA--GYSEKKTIICIPNPlyhCFGcvMGVLAALTHL---QT 297
Cdd:cd12116 122 PVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVN--FLHSMRErlGLGPGDRLLAVTTY---AFD--ISLLELLLPLlagAR 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 298 CVFpAP---SFDALAALQAIHEEKCTALYGTPT---MFIDminhpeyanyNYDSIRSGFIA---GAPCPITLCRRLV-QD 367
Cdd:cd12116 195 VVI-APretQRDPEALARLIEAHSITVMQATPAtwrMLLD----------AGWQGRAGLTAlcgGEALPPDLAARLLsRV 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 368 MHMTDMqvcYGTTET---SPVSFMSTRDDPPeqrikSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSE 444
Cdd:cd12116 264 GSLWNL---YGPTETtiwSTAARVTAAAGPI-----PIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRP 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 445 EQTKKEITQD-------RWYHTGDIAVMHDNGTISIVGRSKDMI-VRgGENIYPTEVEQFLFKHQSVEDVHIVGVPDERF 516
Cdd:cd12116 336 ALTAERFVPDpfagpgsRLYRTGDLVRRRADGRLEYLGRADGQVkIR-GHRIELGEIEAALAAHPGVAQAAVVVREDGGD 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 71994694 517 GEVVcAWVRLHESAEGktTEEDIKAWCKGKIAHFKIP-RYILFKkeyEFPLTVTGKV 572
Cdd:cd12116 415 RRLV-AYVVLKAGAAP--DAAALRAHLRATLPAYMVPsAFVRLD---ALPLTANGKL 465
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
224-572 |
1.23e-26 |
|
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: 112.95 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 224 TQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFfvGLRAGYSEKKTIICIPNPLYHCFGCVMGVLA-ALTHLQTCVfPA 302
Cdd:cd17650 90 TQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAH--AWRREYELDSFPVRLLQMASFSFDVFAGDFArSLLNGGTLV-IC 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 303 PS---FDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCPI----TLCRRLVQDMHMTDmqv 375
Cdd:cd17650 167 PDevkLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAqdfkTLAARFGQGMRIIN--- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 376 CYGTTETSPVS--FMSTRDDPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEITQ 453
Cdd:cd17650 244 SYGVTEATIDStyYEEGRDPLGDSANVPIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 454 D------RWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVrlh 527
Cdd:cd17650 324 NpfapgeRMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYV--- 400
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 71994694 528 eSAEGKTTEEDIKAWCKGKIAHFKIPRYilFKKEYEFPLTVTGKV 572
Cdd:cd17650 401 -VAAATLNTAELRAFLAKELPSYMIPSY--YVQLDALPLTPNGKV 442
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
54-574 |
1.88e-26 |
|
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: 112.95 E-value: 1.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 54 PDKEFLIFKREGIrkTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRY 133
Cdd:cd17656 2 PDAVAVVFENQKL--TYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 134 AIEKVGIRALITppgfkksnyyqsikdilpEVTLKEPgksgiTSRNFTcfQHLIMFDEEdkiypgawkytdvmkmgTEED 213
Cdd:cd17656 80 IMLDSGVRVVLT------------------QRHLKSK-----LSFNKS--TILLEDPSI-----------------SQED 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 214 RhhlSKIERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLN---------NAFFVGLRAGYSEKKTIICipnplYH---- 280
Cdd:cd17656 118 T---SNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNllhferektNINFSDKVLQFATCSFDVC-----YQeifs 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 281 --CFGCVMGVLAALTHLQtcvfpapsFDALAALQAIHEEKCTALygtPTMFIDMI-NHPEYANYNYDSIRSGFIAGAPCP 357
Cdd:cd17656 190 tlLSGGTLYIIREETKRD--------VEQLFDLVKRHNIEVVFL---PVAFLKFIfSEREFINRFPTCVKHIITAGEQLV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 358 ITlcrRLVQDM---HMTDMQVCYGTTETSPVSFMSTRDDPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGY 434
Cdd:cd17656 259 IT---NEFKEMlheHNVHLHNHYGPSETHVVTTYTINPEAEIPELPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGA 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 435 SVMRCYWNSEEQTKKEITQD------RWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHI 508
Cdd:cd17656 336 SVARGYLNRQELTAEKFFPDpfdpneRMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVV 415
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71994694 509 VGVPDERFGEVVCAWVrlheSAEGKTTEEDIKAWCKGKIAHFKIPRYilFKKEYEFPLTVTGKVKK 574
Cdd:cd17656 416 LDKADDKGEKYLCAYF----VMEQELNISQLREYLAKQLPEYMIPSF--FVPLDQLPLTPNGKVDR 475
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
15-572 |
3.99e-26 |
|
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: 113.06 E-value: 3.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 15 NANDVMVAPSRKSYVHGcsTVPLLFETVGDRLRSAvdqvPDKEFLIFKRE---GIRK-TYSQVATDAENLACGLLHLGLK 90
Cdd:cd17634 34 NTSFAPGAPSIKWFEDA--TLNLAANALDRHLREN----GDRTAIIYEGDdtsQSRTiSYRELHREVCRFAGTLLDLGVK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 91 KGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITPPGFKKSNYYQSIKDILPEVTlkEP 170
Cdd:cd17634 108 KGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGVRAGRSVPLKKNVDDAL--NP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 171 gksgitsrNFTCFQHLIMFDEEDKIY---PGAWKYTDVMkMGTEEDRHHLSKIEretqPDDSLNIQYTSGTTGQPKGATL 247
Cdd:cd17634 186 --------NVTSVEHVIVLKRTGSDIdwqEGRDLWWRDL-IAKASPEHQPEAMN----AEDPLFILYTSGTTGKPKGVLH 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 248 THHNVLnnaffvgLRAGYSEKKTIICIPNPLYHCF---GCVMG---------VLAALTHLQTCVFPAPSFDALaaLQAIH 315
Cdd:cd17634 253 TTGGYL-------VYAATTMKYVFDYGPGDIYWCTadvGWVTGhsyllygplACGATTLLYEGVPNWPTPARM--WQVVD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 316 EEKCTALYGTPTMFIDMINHPEYANYNYD--SIRSGFIAGAPCPITLCRRLVQDMHMTDMQVC--YGTTETSpvSFM-ST 390
Cdd:cd17634 324 KHGVNILYTAPTAIRALMAAGDDAIEGTDrsSLRILGSVGEPINPEAYEWYWKKIGKEKCPVVdtWWQTETG--GFMiTP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 391 RDDPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIV--------RGYsvmrcYWNSEEQTKKEI-TQDRWYHTGD 461
Cdd:cd17634 402 LPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVItdpwpgqtRTL-----FGDHERFEQTYFsTFKGMYFSGD 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 462 IAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRL-HESAEGKTTEEDIK 540
Cdd:cd17634 477 GARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLnHGVEPSPELYAELR 556
|
570 580 590
....*....|....*....|....*....|..
gi 71994694 541 AWCKGKIAHFKIPRYILFKKeyEFPLTVTGKV 572
Cdd:cd17634 557 NWVRKEIGPLATPDVVHWVD--SLPKTRSGKI 586
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
225-582 |
4.41e-26 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 113.91 E-value: 4.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 225 QPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIPnPLYHCFGCVMG-VLAALTHLQTCVFPAP 303
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNAL-PVFHSFGLTGGlVLPLLSGVKVFLYPSP 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 304 sFDALAALQAIHEEKCTALYGTPTmFIDmiNHPEYAN-YNYDSIRSGFiAGAPCPITLCRRLVQDMHMTDMQVCYGTTET 382
Cdd:PRK06814 870 -LHYRIIPELIYDTNATILFGTDT-FLN--GYARYAHpYDFRSLRYVF-AGAEKVKEETRQTWMEKFGIRILEGYGVTET 944
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 383 SPVSFMSTrddPPEQRIKSVGHIMDHLEAAIVDkrnciVPrGVK--GEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTG 460
Cdd:PRK06814 945 APVIALNT---PMHNKAGTVGRLLPGIEYRLEP-----VP-GIDegGRLFVRGPNVMLGYLRAENPGVLEPPADGWYDTG 1015
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 461 DIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFK----HQSVedvhIVGVPDERFGEVVcawVRLHESAEGktTE 536
Cdd:PRK06814 1016 DIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAElwpdALHA----AVSIPDARKGERI---ILLTTASDA--TR 1086
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 71994694 537 EDIKAWCKGK-IAHFKIPRYILFKKeyEFPLTVTGKVKKFEIREMSK 582
Cdd:PRK06814 1087 AAFLAHAKAAgASELMVPAEIITID--EIPLLGTGKIDYVAVTKLAE 1131
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
33-574 |
5.90e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 114.10 E-value: 5.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 33 STVPLLFEtvgdrlrSAVDQVPDKEFLIFKREgiRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFAS 112
Cdd:PRK12467 1574 RLVHQLIE-------DQAAATPEAVALVFGEQ--ELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAI 1644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 113 ALAGMVLVNINPSYQSEELRYAIEKVGIRALITppgfkksnyyQSikDILPEVTLKEpgksGITSrnftcfqhlIMFDEE 192
Cdd:PRK12467 1645 LKAGGAYVPLDPEYPRERLAYMIEDSGIELLLT----------QS--HLQARLPLPD----GLRS---------LVLDQE 1699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 193 DkiypgAWKYTDVMkmgteedrhhlSKIERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTII 272
Cdd:PRK12467 1700 D-----DWLEGYSD-----------SNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVL 1763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 273 cipnpLYHCF---GCVMGVLAALTHLQTCVFPAP--SFDALAALQAIHEEKCTALYGTPTMFIDMINHPEyANYNYDSIR 347
Cdd:PRK12467 1764 -----QFTSFafdVSVWELFWPLINGARLVIAPPgaHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDE-QVEHPLSLR 1837
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 348 SGFIAGAPCPITLCRRLVQDMHMTDMQVCYGTTETS--PVSFMSTRDDPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGV 425
Cdd:PRK12467 1838 RVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAvdVTHWTCRRKDLEGRDSVPIGQPIANLSTYILDASLNPVPIGV 1917
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 426 KGEVIVRGYSVMRCYWNSEEQTKKEITQD-------RWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLF 498
Cdd:PRK12467 1918 AGELYLGGVGLARGYLNRPALTAERFVADpfgtvgsRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLR 1997
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 499 KHQSVEDVHIVGVpDERFGEVVCAWV------RLHESAEGKTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKV 572
Cdd:PRK12467 1998 EQGGVREAVVIAQ-DGANGKQLVAYVvptdpgLVDDDEAQVALRAILKNHLKASLPEYMVPAHLVFLA--RMPLTPNGKL 2074
|
..
gi 71994694 573 KK 574
Cdd:PRK12467 2075 DR 2076
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
64-572 |
9.59e-26 |
|
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: 110.09 E-value: 9.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 64 EGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRAL 143
Cdd:cd17653 19 LGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 144 ITPPGfkksnyyqsikdilpevtlkepgksgitsrnftcfqhlimfdeedkiypgawkytdvmkmgteedrhhlskiere 223
Cdd:cd17653 99 LTTDS--------------------------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 224 tqPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFV--GLRAGYSEKKTIICipNPLYHCfgCVMGVLAALTHLQTCVFP 301
Cdd:cd17653 104 --PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPpaRLDVGPGSRVAQVL--SIAFDA--CIGEIFSTLCNGGTLVLA 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 302 APSfDALAALQAiheeKCTALYGTPTmFIDMINhPEyanyNYDSIRSGFIAGAPCPITLCRRLVQDMHMTDmqvCYGTTE 381
Cdd:cd17653 178 DPS-DPFAHVAR----TVDALMSTPS-ILSTLS-PQ----DFPNLKTIFLGGEAVPPSLLDRWSPGRRLYN---AYGPTE 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 382 TSPVSFM-STRddpPEQRIkSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEITQDRWYH-- 458
Cdd:cd17653 244 CTISSTMtELL---PGQPV-TIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPgs 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 459 ----TGDIAVMHDNGTISIVGRSKDMI-VRGGE-NIYptEVEQFLFKHQS-VEDVHIVGVpderfGEVVCAWVrlhesae 531
Cdd:cd17653 320 rmyrTGDYGRWTEDGGLEFLGREDNQVkVRGFRiNLE--EIEEVVLQSQPeVTQAAAIVV-----NGRLVAFV------- 385
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 71994694 532 gkTTE----EDIKAWCKGKIAHFKIPRYILfkKEYEFPLTVTGKV 572
Cdd:cd17653 386 --TPEtvdvDGLRSELAKHLPSYAVPDRII--ALDSFPLTANGKV 426
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
69-572 |
5.59e-25 |
|
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: 108.17 E-value: 5.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 69 TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITppg 148
Cdd:cd12115 26 TYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 149 fkksnyyqsikdilpevtlkepgksgitsrnftcfqhlimfdeedkiypgawkytdvmkmgteedrhhlskieretQPDD 228
Cdd:cd12115 103 ----------------------------------------------------------------------------DPDD 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 229 SLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKK-----TIICIPNPLYHCFG--CVMGvlaalthlqtCVFP 301
Cdd:cd12115 107 LAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEELAgvlasTSICFDLSVFELFGplATGG----------KVVL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 302 APSFDALAALQAIHEekcTALYGT-PTMFIDMINH---PEyanynydSIRSGFIAGAPCPITLCRRLVQDMHMTDMQVCY 377
Cdd:cd12115 177 ADNVLALPDLPAAAE---VTLINTvPSAAAELLRHdalPA-------SVRVVNLAGEPLPRDLVQRLYARLQVERVVNLY 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 378 GTTETSPVSFMSTRDdPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEITQD--- 454
Cdd:cd12115 247 GPSEDTTYSTVAPVP-PGASGEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDpfg 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 455 ---RWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLheSAE 531
Cdd:cd12115 326 pgaRLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVA--EPG 403
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 71994694 532 GKTTEEDIKAWCKGKIAHFKIP-RYILFKkeyEFPLTVTGKV 572
Cdd:cd12115 404 AAGLVEDLRRHLGTRLPAYMVPsRFVRLD---ALPLTPNGKI 442
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
68-577 |
1.50e-24 |
|
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: 107.30 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 68 KTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITPP 147
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIFTDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 148 GfkksnyyqsikdilpevtlkepgksgitsrnftcfqhlimfdeedkiypgawkytdvmkmgteedrhhlskieretqPD 227
Cdd:cd17639 86 K-----------------------------------------------------------------------------PD 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 228 DSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAG--YSEKKTIICIPnPLYHCF-----------GCVMGVLAALTh 294
Cdd:cd17639 89 DLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPelLGPDDRYLAYL-PLAHIFelaaenvclyrGGTIGYGSPRT- 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 295 LQTCVFPAPSFDalaalqaIHEEKCTALYGTPTMF-------IDMINHPEY-------ANYN---------YDS------ 345
Cdd:cd17639 167 LTDKSKRGCKGD-------LTEFKPTLMVGVPAIWdtirkgvLAKLNPMGGlkrtlfwTAYQsklkalkegPGTplldel 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 346 ------------IRSGFIAGAPCPI-------TLCRRLVQDmhmtdmqvcYGTTETSPVSFMStrdDPPEQRIKSVGHIM 406
Cdd:cd17639 240 vfkkvraalggrLRYMLSGGAPLSAdtqeflnIVLCPVIQG---------YGLTETCAGGTVQ---DPGDLETGRVGPPL 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 407 DHLEAAIVD--------KRNCivPRGvkgEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSK 478
Cdd:cd17639 308 PCCEIKLVDweeggystDKPP--PRG---EILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKK 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 479 DMI-VRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFgevVCAWV-----RLHESAEGKTTEED-----------IKA 541
Cdd:cd17639 383 DLVkLQNGEYIALEKLESIYRSNPLVNNICVYADPDKSY---PVAIVvpnekHLTKLAEKHGVINSeweelcedkklQKA 459
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 71994694 542 WCK-----GKIAHFK---IPRYILFKKEYEFP----LTVTGKVKKFEI 577
Cdd:cd17639 460 VLKslaetARAAGLEkfeIPQGVVLLDEEWTPenglVTAAQKLKRKEI 507
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
227-578 |
5.66e-24 |
|
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: 104.91 E-value: 5.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 227 DDSLNIQYTSGTTGQPKG------ATLTHHNVLNNAffVGLRAGYSekktIICIPNPLYhCFGCVMGVLAALTHLQTCVF 300
Cdd:cd05973 88 SDPFVMMFTSGTTGLPKGvpvplrALAAFGAYLRDA--VDLRPEDS----FWNAADPGW-AYGLYYAITGPLALGHPTIL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 301 PAPSFDALAALQAIHEEKCTALYGTPTMF-IDMINHPEYANYNYDSIRSGFIAGAPCPITLCR-------RLVQDmHmtd 372
Cdd:cd05973 161 LEGGFSVESTWRVIERLGVTNLAGSPTAYrLLMAAGAEVPARPKGRLRRVSSAGEPLTPEVIRwfdaalgVPIHD-H--- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 373 mqvcYGTTETSPVsFMSTRDDPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVI--VRGYSVM--RCYWNSEEQTk 448
Cdd:cd05973 237 ----YGQTELGMV-LANHHALEHPVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAidIANSPLMwfRGYQLPDTPA- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 449 keiTQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHE 528
Cdd:cd05973 311 ---IDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRG 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 71994694 529 SAEGKTT-EEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIR 578
Cdd:cd05973 388 GHEGTPAlADELQLHVKKRLSAHAYPRTIHFVD--ELPKTPSGKIQRFLLR 436
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
49-572 |
2.02e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 106.01 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 49 AVDQVPDKEFLIFKREgiRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQS 128
Cdd:PRK12467 521 QARQHPERPALVFGEQ--VLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQ 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 129 EELRYAIEKVGIRALITPPgfkksnyyqsikdilpEVTLKEPGKSGITSrnftcfqhLIMFDEEDKI--YPGAWKYTDVm 206
Cdd:PRK12467 599 DRLAYMLDDSGVRLLLTQS----------------HLLAQLPVPAGLRS--------LCLDEPADLLcgYSGHNPEVAL- 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 207 kmgteedrhhlskieretQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIPNPLYHCFGCVM 286
Cdd:PRK12467 654 ------------------DPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTEL 715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 287 gvLAALTHLQTCVFPAP--SFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNydSIRSGFIAGAPCPITLCRRL 364
Cdd:PRK12467 716 --FGALASGATLHLLPPdcARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPR--PQRALVCGGEALQVDLLARV 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 365 VQDMHMTDMQVCYGTTETS-PVSFMSTRDDPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNS 443
Cdd:PRK12467 792 RALGPGARLINHYGPTETTvGVSTYELSDEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRR 871
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 444 EEQTKKEITQD-------RWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERF 516
Cdd:PRK12467 872 PALTAERFVPDpfgadggRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAG 951
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 71994694 517 GEVV--CAWVRLHESAEGKTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKV 572
Cdd:PRK12467 952 LQLVayLVPAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLD--SLPLTPNGKL 1007
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
70-494 |
2.89e-23 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 103.93 E-value: 2.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 70 YSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNI--------NPSYqSEELRYAIEKVGIR 141
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLplpmgfggRESY-IAQLRGMLASAQPA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 142 ALITPPGfkksnyyqsIKDILPEVTLKEPGKSGITSRNFtcfqhlimfdeedkiypgawkytdvmkMGTEEDRHHLSKIe 221
Cdd:PRK09192 131 AIITPDE---------LLPWVNEATHGNPLLHVLSHAWF---------------------------KALPEADVALPRP- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 222 retQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGlRAGYSEKKTIICIP-NPLYHCFGCVMGVLAALT------H 294
Cdd:PRK09192 174 ---TPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAIS-HDGLKVRPGDRCVSwLPFYHDMGLVGFLLTPVAtqlsvdY 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 295 LQTCVF---PapsfdaLAALQAIHEEKCTALYgTPTMFIDM----INHPEYANYNYDSIRSGFIAGAPCPITLCRRLVQ- 366
Cdd:PRK09192 250 LPTRDFarrP------LQWLDLISRNRGTISY-SPPFGYELcarrVNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEa 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 367 --DMHMTD--MQVCYGTTE-TSPVSFM---------------------STRDDPPEQRIKSV---GHIMDHLEAAIVDKR 417
Cdd:PRK09192 323 faPAGFDDkaFMPSYGLAEaTLAVSFSplgsgivveevdrdrleyqgkAVAPGAETRRVRTFvncGKALPGHEIEIRNEA 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71994694 418 NCIVPRGVKGEVIVRGYSVMRCYWNSEEqTKKEITQDRWYHTGDIAVMHDnGTISIVGRSKDMIVRGGENIYPTEVE 494
Cdd:PRK09192 403 GMPLPERVVGHICVRGPSLMSGYFRDEE-SQDVLAADGWLDTGDLGYLLD-GYLYITGRAKDLIIINGRNIWPQDIE 477
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
232-582 |
3.13e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 102.42 E-value: 3.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 232 IQYTSGTTGQPKGATLTHHNVLN--NAFFVGLRAGYSEKKTIICipnPLYHCFGCVMGVLAALTHLQTCVF---PAPSFd 306
Cdd:PRK08308 106 LQYSSGTTGEPKLIRRSWTEIDReiEAYNEALNCEQDETPIVAC---PVTHSYGLICGVLAALTRGSKPVIitnKNPKF- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 307 ALAALQAIHEEkctALYGTPTMFIDMINHPEyANYNYDSIRSgfiAGAPCPITLCRRLvQDMHMTDMQVcYGTTETSPVS 386
Cdd:PRK08308 182 ALNILRNTPQH---ILYAVPLMLHILGRLLP-GTFQFHAVMT---SGTPLPEAWFYKL-RERTTYMMQQ-YGCSEAGCVS 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 387 F---MSTRDDppeqriksVGHIMDHLEAAIVDKRNciVPRgvkgEVIVRgysvmrcywnseeqtkkeiTQDRWYHTGDIA 463
Cdd:PRK08308 253 IcpdMKSHLD--------LGNPLPHVSVSAGSDEN--APE----EIVVK-------------------MGDKEIFTKDLG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 464 VMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVrlheSAEGKTTEEDIKAWC 543
Cdd:PRK08308 300 YKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKV----ISHEEIDPVQLREWC 375
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 71994694 544 KGKIAHFKIPRYILFKKeyEFPLTVTGKV--KKFEIREMSK 582
Cdd:PRK08308 376 IQHLAPYQVPHEIESVT--EIPKNANGKVsrKLLELGEVTA 414
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
32-512 |
4.26e-23 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 103.44 E-value: 4.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 32 CSTVPLLFETVGDRLrsAVdQVPDKEFLIFKREGIRKTYSQVATDAENLACGLLHLGLKKGDRigiwgpntyewtttqfa 111
Cdd:PRK09274 9 ARHLPRAAQERPDQL--AV-AVPGGRGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMR----------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 112 salagmVLVNINPSYQSEELRYAIEKVGIRALITPPGFKKSNYYQSIKDILPEVTLKEP-----------GKSGITsRNF 180
Cdd:PRK09274 69 ------AVLMVTPSLEFFALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIGIPkahlarrlfgwGKPSVR-RLV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 181 TCFQHLIMfdeedkiypGAWKYTDVMKMGTEEdrhhlSKIERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLnnAFFVG 260
Cdd:PRK09274 142 TVGGRLLW---------GGTTLATLLRDGAAA-----PFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFE--AQIEA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 261 LRAGYSEKKTIICIPN-PLYHCFGCVMGVlaalthlqTCVFPA--PSFDALA----ALQAIHEEKCTALYGTPTMFIDMI 333
Cdd:PRK09274 206 LREDYGIEPGEIDLPTfPLFALFGPALGM--------TSVIPDmdPTRPATVdpakLFAAIERYGVTNLFGSPALLERLG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 334 NHPEYANYNYDSIRSGFIAGAPCPITLCRRLVQDM-HMTDMQVCYGTTETSPVSFMSTRDDPPEQRIKS-------VGHI 405
Cdd:PRK09274 278 RYGEANGIKLPSLRRVISAGAPVPIAVIERFRAMLpPDAEILTPYGATEALPISSIESREILFATRAATdngagicVGRP 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 406 MDHLEAAIV------------DKRnciVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEITQDR----WYHTGDIAVMHDNG 469
Cdd:PRK09274 358 VDGVEVRIIaisdapipewddALR---LATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDGqgdvWHRMGDLGYLDAQG 434
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 71994694 470 TISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVP 512
Cdd:PRK09274 435 RLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVG 477
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
36-589 |
1.01e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 103.88 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 36 PLLFETVGDRLRSAvdqvPDKEFLIFKREgiRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALA 115
Cdd:PRK12316 4551 RCVHQLVAERARMT----PDAVAVVFDEE--KLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKA 4624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 116 GMVLVNINPSYQSEELRYAIEKVGIRALITppgfkksnyyQSikDILPEVtlkePGKSGITSrnftcfqhliMFDEEDKI 195
Cdd:PRK12316 4625 GGAYVPLDPEYPRERLAYMMEDSGAALLLT----------QS--HLLQRL----PIPDGLAS----------LALDRDED 4678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 196 YPGAwkytdvmkmgTEEDRhhlskiERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIP 275
Cdd:PRK12316 4679 WEGF----------PAHDP------AVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFM 4742
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 276 NplYHCFGCVMGVLAALTHLQTCVFPAPSF-DALAALQAIHEEKCTALYGTPTMFIDMINHPEyANYNYDSIRSGFIAGA 354
Cdd:PRK12316 4743 S--FSFDGSHEGLYHPLINGASVVIRDDSLwDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAE-RDGEPPSLRVYCFGGE 4819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 355 PCPITLCRRLVQDMHMTDMQVCYGTTETS-PVSFMSTRD-DPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVR 432
Cdd:PRK12316 4820 AVAQASYDLAWRALKPVYLFNGYGPTETTvTVLLWKARDgDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLG 4899
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 433 GYSVMRCYWNSEEQTKKEITQD-------RWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVED 505
Cdd:PRK12316 4900 GEGVARGYLERPALTAERFVPDpfgapggRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVRE 4979
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 506 VHIVGVP----DERFGEVVCAWVRLHESAEGKTTEED-IKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKfeiREM 580
Cdd:PRK12316 4980 AVVIAQEgavgKQLVGYVVPQDPALADADEAQAELRDeLKAALRERLPEYMVPAHLVFLA--RMPLTPNGKLDR---KAL 5054
|
....*....
gi 71994694 581 SKIELGLQQ 589
Cdd:PRK12316 5055 PQPDASLLQ 5063
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
224-572 |
1.35e-22 |
|
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: 100.94 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 224 TQPDDSLNIQYTSGTTGQPKGATLTHHNVLNnaFFVGLRAGY----SEKKTIICIPNPLYHCFgcVMGVLAALTHLQTCV 299
Cdd:cd17648 91 TNSTDLAYAIYTSGTTGKPKGVLVEHGSVVN--LRTSLSERYfgrdNGDEAVLFFSNYVFDFF--VEQMTLALLNGQKLV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 300 FPAPSF----DALAALqaIHEEKCTALYGTPTmfidMINHPEYANYN----------------YDSIRSGFiagaPCPIT 359
Cdd:cd17648 167 VPPDEMrfdpDRFYAY--INREKVTYLSGTPS----VLQQYDLARLPhlkrvdaageeftapvFEKLRSRF----AGLII 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 360 lcrrlvqdmhmtdmqVCYGTTETSpVSFMSTRDDPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRC 439
Cdd:cd17648 237 ---------------NAYGPTETT-VTNHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 440 YWNSEE-----------QTKKEI---TQDRWYHTGDIAVMHDNGTISIVGRSkDMIVR-GGENIYPTEVEQFLFKHQSVE 504
Cdd:cd17648 301 YLNRPEltaerflpnpfQTEQERargRNARLYKTGDLVRWLPSGELEYLGRN-DFQVKiRGQRIEPGEVEAALASYPGVR 379
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 505 DVHIVG--VPDERFGEVVCAWVRLHESAEGKTTEEDIKAWCKGKIAHFKIPRYILfkKEYEFPLTVTGKV 572
Cdd:cd17648 380 ECAVVAkeDASQAQSRIQKYLVGYYLPEPGHVPESDLLSFLRAKLPRYMVPARLV--RLEGIPVTINGKL 447
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
62-480 |
1.47e-22 |
|
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: 101.73 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 62 KREGIRK--TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVG 139
Cdd:cd17641 4 KDFGIWQefTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 140 IRALITppgfkkSNYYQSIK--DILPEVTLKEpgksgitsrnftcfqHLIMFDEEdkiypGAWKYTD--------VMKMG 209
Cdd:cd17641 84 ARVVIA------EDEEQVDKllEIADRIPSVR---------------YVIYCDPR-----GMRKYDDprlisfedVVALG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 210 TEEDRHHLSKIER---ETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFfVGLRAGYSEKKTIICIPNPLYHCFGCVM 286
Cdd:cd17641 138 RALDRRDPGLYERevaAGKGEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCA-AYLAADPLGPGDEYVSVLPLPWIGEQMY 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 287 GVLAALTHLQTCVFP-------------APSF--------------------DALAALQAIHEEKCTALY--------GT 325
Cdd:cd17641 217 SVGQALVCGFIVNFPeepetmmedlreiGPTFvllpprvwegiaadvrarmmDATPFKRFMFELGMKLGLraldrgkrGR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 326 PTMFIDMINH---------PEYANYNYDSIRSGFIAGAPC-PITLcrRLVQDMHMTDMQVcYGTTETSPVSFMSTRDDPP 395
Cdd:cd17641 297 PVSLWLRLASwladallfrPLRDRLGFSRLRSAATGGAALgPDTF--RFFHAIGVPLKQL-YGQTELAGAYTVHRDGDVD 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 396 EQrikSVGHIMDHLEAAIVDKrncivprgvkGEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVG 475
Cdd:cd17641 374 PD---TVGVPFPGTEVRIDEV----------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVID 440
|
....*
gi 71994694 476 RSKDM 480
Cdd:cd17641 441 RAKDV 445
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
92-521 |
4.07e-22 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 100.28 E-value: 4.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 92 GDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITPPGFkksnyyqsikdilpevtlkepg 171
Cdd:PRK06334 67 DQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTSKQL---------------------- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 172 ksgitsrnftcFQHLIMFDEEDKIYPgawkyTDVMKMgtEEDRHHLSKIER---------------------ETQPDDSL 230
Cdd:PRK06334 125 -----------MQHLAQTHGEDAEYP-----FSLIYM--EEVRKELSFWEKcrigiymsipfewlmrwfgvsDKDPEDVA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 231 NIQYTSGTTGQPKGATLTHHNVLNNA-----FFvglragySEKKTIICIPN-PLYHCFG---CVMGVLAALTHLqtcVFP 301
Cdd:PRK06334 187 VILFTSGTEKLPKGVPLTHANLLANQraclkFF-------SPKEDDVMMSFlPPFHAYGfnsCTLFPLLSGVPV---VFA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 302 APSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCPITLCRRLVQDMHMTDMQVCYGTTE 381
Cdd:PRK06334 257 YNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTTE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 382 TSPVSFMSTRDDPPEQRikSVGHIMDHLEAAIVDKRNCI-VPRGVKGEVIVRGYSVMRCYW-NSEEQTKKEITQDRWYHT 459
Cdd:PRK06334 337 CSPVITINTVNSPKHES--CVGMPIRGMDVLIVSEETKVpVSSGETGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVT 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71994694 460 GDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHqsvedvhiVGVPDERFGE--VVC 521
Cdd:PRK06334 415 GDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG--------FGQNAADHAGplVVC 470
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
376-555 |
5.13e-22 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 99.30 E-value: 5.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 376 CYGTTETSpvSFMSTRDdpPEQRIK---SVGHIMDHLEAAIVdkrncivpRGVKGEVIVRGYSVMRCYWNSEEQTKKEIT 452
Cdd:PRK07445 260 TYGMTETA--SQIATLK--PDDFLAgnnSSGQVLPHAQITIP--------ANQTGNITIQAQSLALGYYPQILDSQGIFE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 453 qdrwyhTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAwvrLHESAEG 532
Cdd:PRK07445 328 ------TDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTA---IYVPKDP 398
|
170 180
....*....|....*....|...
gi 71994694 533 KTTEEDIKAWCKGKIAHFKIPRY 555
Cdd:PRK07445 399 SISLEELKTAIKDQLSPFKQPKH 421
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
41-544 |
7.61e-22 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 99.79 E-value: 7.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 41 TVGDRLRSAVDQVPDKEFLifkreGIR------------KTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTT 108
Cdd:PLN02736 45 TLHDNFVYAVETFRDYKYL-----GTRirvdgtvgeykwMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 109 QFASALAGMVLVNINPSYQSEELRYAIEKVGIRAL-ITP-------------PGFKKSNYYQSIKDILPEVtlkePGKSG 174
Cdd:PLN02736 120 DHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIfCVPqtlntllsclseiPSVRLIVVVGGADEPLPSL----PSGTG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 175 ItsrnftcfqhlimfdeedKIYPgawkYTDVMKMGTEEDRHHlskieRETQPDDSLNIQYTSGTTGQPKGATLTHHNVLN 254
Cdd:PLN02736 196 V------------------EIVT----YSKLLAQGRSSPQPF-----RPPKPEDVATICYTSGTTGTPKGVVLTHGNLIA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 255 NAffvglrAGYSEkkTIICIPN-------PLYHCFGCVMGVL-----AALTHLQTCVFPApsFDALAALQaiheekctal 322
Cdd:PLN02736 249 NV------AGSSL--STKFYPSdvhisylPLAHIYERVNQIVmlhygVAVGFYQGDNLKL--MDDLAALR---------- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 323 ygtPTMFIDMinhPEYANYNYDSI-----RSGFIA-----------------GAPcPITLCRRLV--------------- 365
Cdd:PLN02736 309 ---PTIFCSV---PRLYNRIYDGItnavkESGGLKerlfnaaynakkqalenGKN-PSPMWDRLVfnkikaklggrvrfm 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 366 --------QDMhMTDMQVC--------YGTTETS-PVSFMSTRDdppeqriKSVGHI---MDHLEAAIVD-------KRN 418
Cdd:PLN02736 382 ssgasplsPDV-MEFLRICfggrvlegYGMTETScVISGMDEGD-------NLSGHVgspNPACEVKLVDvpemnytSED 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 419 CIVPRGvkgEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMI-VRGGENIYPTEVEQFL 497
Cdd:PLN02736 454 QPYPRG---EICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVY 530
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 71994694 498 FKHQSVEDVHIVG-----------VPDErfgEVVCAWvrlheSAEGKTTEEDIKAWCK 544
Cdd:PLN02736 531 AKCKFVAQCFVYGdslnsslvavvVVDP---EVLKAW-----AASEGIKYEDLKQLCN 580
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
54-572 |
1.45e-21 |
|
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: 97.71 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 54 PDKEFLIFKreGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRY 133
Cdd:cd17652 1 PDAPAVVFG--DETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 134 AIEKVGIRALITppgfkksnyyqsikdilpevtlkepgksgitsrnftcfqhlimfdeedkiypgawkytdvmkmgteed 213
Cdd:cd17652 79 MLADARPALLLT-------------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 214 rhhlskieretQPDDSLNIQYTSGTTGQPKGATLTHHNVLNnaffvgLRAGYSEKktiicipnplyhcfgcvMGVLAALT 293
Cdd:cd17652 91 -----------TPDNLAYVIYTSGSTGRPKGVVVTHRGLAN------LAAAQIAA-----------------FDVGPGSR 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 294 HLQtcvFPAPSFDA-----LAAL---------------------QAIHEEKCTALYGTPTMFIDMinhPEYanyNYDSIR 347
Cdd:cd17652 137 VLQ---FASPSFDAsvwelLMALlagatlvlapaeellpgeplaDLLREHRITHVTLPPAALAAL---PPD---DLPDLR 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 348 SGFIAGAPCPITLCRRLVQDMHMTDmqvCYGTTETSPVSFMS----TRDDPPeqriksVGHIMDHLEAAIVDKRNCIVPR 423
Cdd:cd17652 208 TLVVAGEACPAELVDRWAPGRRMIN---AYGPTETTVCATMAgplpGGGVPP------IGRPVPGTRVYVLDARLRPVPP 278
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 424 GVKGEVIVRGYSVMRCYWNSEEQTKKEITQD-------RWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQF 496
Cdd:cd17652 279 GVPGELYIAGAGLARGYLNRPGLTAERFVADpfgapgsRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAA 358
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71994694 497 LFKHQSVEDVhIVGVPDERFGEV-VCAWVRlhESAEGKTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKV 572
Cdd:cd17652 359 LTEHPGVAEA-VVVVRDDRPGDKrLVAYVV--PAPGAAPTAAELRAHLAERLPGYMVPAAFVVLD--ALPLTPNGKL 430
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
66-511 |
2.16e-21 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 97.15 E-value: 2.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 66 IRKTYSQVATDAENLACGLLHLGLKKGDRigiwgpntyewtttqfasalagmVLVNINPSYQSEELRYAIEKVGIRALIT 145
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRGMR-----------------------AVLMVPPGPDFFALTFALFKAGAVPVLI 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 146 PPGFKKSNYYQSIKDILPEVTLKEPgksgitsrnftcfqhlimfdeedkiypgawkytdvmkmgteedrhhlskieretQ 225
Cdd:cd05910 58 DPGMGRKNLKQCLQEAEPDAFIGIP------------------------------------------------------K 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 226 PDDSLNIQYTSGTTGQPKGATLTHHNvlnnafFVG----LRAGYSEKKTIICIPN-PLYHCFGCVMGVLAALTHLQ-TCv 299
Cdd:cd05910 84 ADEPAAILFTSGSTGTPKGVVYRHGT------FAAqidaLRQLYGIRPGEVDLATfPLFALFGPALGLTSVIPDMDpTR- 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 300 fPApSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCPITLCRRLVQDMH-MTDMQVCYG 378
Cdd:cd05910 157 -PA-RADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLSdEAEILTPYG 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 379 TTETSPVSFMSTRD------DPPEQ-RIKSVGHIMDHLEAAIV----------DKRNCiVPRGVKGEVIVRGYSVMRCYW 441
Cdd:cd05910 235 ATEALPVSSIGSREllatttAATSGgAGTCVGRPIPGVRVRIIeiddepiaewDDTLE-LPRGEIGEITVTGPTVTPTYV 313
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71994694 442 NSEEQTK----KEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGV 511
Cdd:cd05910 314 NRPVATAlakiDDNSEGFWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV 387
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
69-581 |
3.56e-21 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 97.79 E-value: 3.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 69 TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAiEKVGIRALITPPG 148
Cdd:PRK06060 32 THGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALA-ARNTEPALVVTSD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 149 fkksnyyqSIKDILPEVTLKEPGKsgitsrnftcfqhliMFDEEDKIYPGawkytdvmkmgteeDRHHLSKieretqpDD 228
Cdd:PRK06060 111 --------ALRDRFQPSRVAEAAE---------------LMSEAARVAPG--------------GYEPMGG-------DA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 229 SLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIPNPLYHCFGCVMGVLAAL-THLQTCVFPAP-SFD 306
Cdd:PRK06060 147 LAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLaTGGSAVINSAPvTPE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 307 ALAALQAIHEEkcTALYGTPTMFIDMIN--HPEyanyNYDSIRSGFIAGAPCPITLCRRLVQDMHMTDMQVCYGTTETSP 384
Cdd:PRK06060 227 AAAILSARFGP--SVLYGVPNFFARVIDscSPD----SFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQ 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 385 vSFMSTRDDppEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTkkeITQDRWYHTGDIAV 464
Cdd:PRK06060 301 -TFVSNRVD--EWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDSP---VANEGWLDTRDRVC 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 465 MHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVrLHESAEG--KTTEEDIKAW 542
Cdd:PRK06060 375 IDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFL-VATSGATidGSVMRDLHRG 453
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 71994694 543 CKGKIAHFKIP-RYILFKKeyeFPLTVTGKVKKFEIREMS 581
Cdd:PRK06060 454 LLNRLSAFKVPhRFAVVDR---LPRTPNGKLVRGALRKQS 490
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
225-580 |
3.77e-21 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 96.84 E-value: 3.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 225 QPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIPNplyHCFG-CVMGVLAALTHlQTCVFPAP 303
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQFAS---YTFDvSILEIFTTLAA-GGCLCIPS 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 304 SFDALAALQ-AIHEEKCTALYGTPTmFIDMInHPEyanyNYDSIRSGFIAGAPCPITLCRRLVQDMHMTdmqVCYGTTET 382
Cdd:cd05918 180 EEDRLNDLAgFINRLRVTWAFLTPS-VARLL-DPE----DVPSLRTLVLGGEALTQSDVDTWADRVRLI---NAYGPAEC 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 383 SPVSfmSTRDDPPEQRIKSVGHIMDhleAA--IVDKRNC--IVPRGVKGEVIVRGYSVMRCYWNSEEQTKKE-ITQDRW- 456
Cdd:cd05918 251 TIAA--TVSPVVPSTDPRNIGRPLG---ATcwVVDPDNHdrLVPIGAVGELLIEGPILARGYLNDPEKTAAAfIEDPAWl 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 457 -----------YHTGDIAVMHDNGTISIVGRsKDMIVR-GGENIYPTEVEQFLfkHQSVEDVHIVGV-----PDERFGEV 519
Cdd:cd05918 326 kqegsgrgrrlYRTGDLVRYNPDGSLEYVGR-KDTQVKiRGQRVELGEIEHHL--RQSLPGAKEVVVevvkpKDGSSSPQ 402
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71994694 520 VCAWVRLHESAEGKTTEED---------------IKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIREM 580
Cdd:cd05918 403 LVAFVVLDGSSSGSGDGDSlflepsdefralvaeLRSKLRQRLPSYMVPSVFLPLS--HLPLTASGKIDRRALREL 476
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
211-579 |
7.10e-21 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 95.33 E-value: 7.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 211 EEDRHHLSKIERETQPDDSLNIQYTSGTTGQPKGATLTHHNV----LNNAFFVGLRAGysEKKTIICIPNPLYHCFGCVM 286
Cdd:cd05974 69 DRGGAVYAAVDENTHADDPMLLYFTSGTTSKPKLVEHTHRSYpvghLSTMYWIGLKPG--DVHWNISSPGWAKHAWSCFF 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 287 GVLAAlthlQTCVF--PAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPeYANYNYdSIRSGFIAGAPCPITLCRRl 364
Cdd:cd05974 147 APWNA----GATVFlfNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQD-LASFDV-KLREVVGAGEPLNPEVIEQ- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 365 VQDMHMTDMQVCYGTTETSPVSFMStrddpPEQRIK--SVGHIMDHLEAAIVDkrncivPRG---VKGEVIV-----RGY 434
Cdd:cd05974 220 VRRAWGLTIRDGYGQTETTALVGNS-----PGQPVKagSMGRPLPGYRVALLD------PDGapaTEGEVALdlgdtRPV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 435 SVMRCYWNSEEQTKkEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDE 514
Cdd:cd05974 289 GLMKGYAGDPDKTA-HAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDP 367
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71994694 515 RFGEVVCAWVRLHESAE-GKTTEEDIKAWCKGKIAHFKIPRYILFKkeyEFPLTVTGKVKKFEIRE 579
Cdd:cd05974 368 VRLSVPKAFIVLRAGYEpSPETALEIFRFSRERLAPYKRIRRLEFA---ELPKTISGKIRRVELRR 430
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
31-508 |
1.37e-20 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 95.95 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 31 GCSTVPLLFEtvgdrlrSAVDQVPDKEFL----IFKREGI-----RK------------TYSQVATDAENLACGLLHLGL 89
Cdd:PLN02387 56 GATTLAALFE-------QSCKKYSDKRLLgtrkLISREFEtssdgRKfeklhlgeyewiTYGQVFERVCNFASGLVALGH 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 90 KKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITppgfkKSNYYQSIKDIlpevtlke 169
Cdd:PLN02387 129 NKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVIC-----DSKQLKKLIDI-------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 170 pgksgitSRNFTCFQHLIMFDEEDKIYP------GAWK---YTDVMKMGTEedrhhlSKIE-RETQPDDSLNIQYTSGTT 239
Cdd:PLN02387 196 -------SSQLETVKRVIYMDDEGVDSDsslsgsSNWTvssFSEVEKLGKE------NPVDpDLPSPNDIAVIMYTSGST 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 240 GQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIPNPLYHCF-----------GCVMGVLAALT--------------- 293
Cdd:PLN02387 263 GLPKGVMMTHGNIVATVAGVMTVVPKLGKNDVYLAYLPLAHILelaaesvmaavGAAIGYGSPLTltdtsnkikkgtkgd 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 294 ------HLQTCVfPA---------------------PSFD-ALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDS 345
Cdd:PLN02387 343 asalkpTLMTAV-PAildrvrdgvrkkvdakgglakKLFDiAYKRRLAAIEGSWFGAWGLEKLLWDALVFKKIRAVLGGR 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 346 IRSGFIAGAPcpitlcrrLVQDMHMTdMQVC--------YGTTETSPVSFMSTRDDPpeqrikSVGHIMDHLEAAIV--- 414
Cdd:PLN02387 422 IRFMLSGGAP--------LSGDTQRF-INIClgapigqgYGLTETCAGATFSEWDDT------SVGRVGPPLPCCYVklv 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 415 ----------DKRnciVPRgvkGEVIVRGYSVMRCYWNSEEQTKKEITQD----RWYHTGDIAVMHDNGTISIVGRSKDM 480
Cdd:PLN02387 487 sweeggylisDKP---MPR---GEIVIGGPSVTLGYFKNQEKTDEVYKVDergmRWFYTGDIGQFHPDGCLEIIDRKKDI 560
|
570 580
....*....|....*....|....*....
gi 71994694 481 I-VRGGENIYPTEVEQFLFKHQSVEDVHI 508
Cdd:PLN02387 561 VkLQHGEYVSLGKVEAALSVSPYVDNIMV 589
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
54-575 |
1.52e-20 |
|
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: 94.74 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 54 PDKEFLIFkrEGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRY 133
Cdd:cd17649 1 PDAVALVF--GDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 134 AIEKVGIRALITppgfkksnyyqsikdilpevtlkepgksgitsrnftcfqhlimfdeedkiypgawkytdvmkmgteed 213
Cdd:cd17649 79 MLEDSGAGLLLT-------------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 214 rHHlskieretqPDDSLNIQYTSGTTGQPKG-----ATLTHHNVLNNAFFvGLRAGYsekktiiCIPNPLYHCF-GCVMG 287
Cdd:cd17649 91 -HH---------PRQLAYVIYTSGSTGTPKGvavshGPLAAHCQATAERY-GLTPGD-------RELQFASFNFdGAHEQ 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 288 VLAALTHLQTCVFPAPS--FDALAALQAIHEEKCTALYGTPT---MFIDMINHPEYANYNydSIRSGFIAGAPCPITLCR 362
Cdd:cd17649 153 LLPPLICGACVVLRPDElwASADELAEMVRELGVTVLDLPPAylqQLAEEADRTGDGRPP--SLRLYIFGGEALSPELLR 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 363 RLVqdmhMTDMQVC--YGTTET--SPVSFMSTRDDPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMR 438
Cdd:cd17649 231 RWL----KAPVRLFnaYGPTEAtvTPLVWKCEAGAARAGASMPIGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLAR 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 439 CYWNSEEQTKKEITQD-------RWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGV 511
Cdd:cd17649 307 GYLGRPELTAERFVPDpfgapgsRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVAL 386
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71994694 512 PDERfGEVVCAWVRLHESAEGKTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKF 575
Cdd:cd17649 387 DGAG-GKQLVAYVVLRAAAAQPELRAQLRTALRASLPDYMVPAHLVFLA--RLPLTPNGKLDRK 447
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
41-512 |
1.85e-20 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 95.33 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 41 TVGDRLRSAVDQVPDKEFLIFKREGIrkTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLV 120
Cdd:PRK08279 38 SLGDVFEEAAARHPDRPALLFEDQSI--SYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 121 NINPSYQSEELRYAIEKVGIRALITPPGFKKSnyYQSIKdilPEVTLKEPgksgitsrnftcfqhLIMFDEEDKIYPGAW 200
Cdd:PRK08279 116 LLNTQQRGAVLAHSLNLVDAKHLIVGEELVEA--FEEAR---ADLARPPR---------------LWVAGGDTLDDPEGY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 201 KytDVMKMGTEEDRHHLSKIERETQPDDSLNIqYTSGTTGQPKGATLTHHNVLN--NAFFVGLRAGysEKKTIICiPNPL 278
Cdd:PRK08279 176 E--DLAAAAAGAPTTNPASRSGVTAKDTAFYI-YTSGTTGLPKAAVMSHMRWLKamGGFGGLLRLT--PDDVLYC-CLPL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 279 YH------CFGCVM--GVLAALthlqtcvfpAPSFDALAALQAIHEEKCTALygtptMFID-----MINHPEYANYNYDS 345
Cdd:PRK08279 250 YHntggtvAWSSVLaaGATLAL---------RRKFSASRFWDDVRRYRATAF-----QYIGelcryLLNQPPKPTDRDHR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 346 IRSGFIAGApcpitlcRRLVQDmHMTD----MQVC--YGTTEtSPVSFMSTrddppEQRIKSVGHIMDHLE--AAIV--- 414
Cdd:PRK08279 316 LRLMIGNGL-------RPDIWD-EFQQrfgiPRILefYAASE-GNVGFINV-----FNFDGTVGRVPLWLAhpYAIVkyd 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 415 ---------DKRNCI-VPRGVKGEVIVR--------GYsvmrcywNSEEQTKKEITQ------DRWYHTGDIAVMHDNGT 470
Cdd:PRK08279 382 vdtgepvrdADGRCIkVKPGEVGLLIGRitdrgpfdGY-------TDPEASEKKILRdvfkkgDAWFNTGDLMRDDGFGH 454
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 71994694 471 ISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVP 512
Cdd:PRK08279 455 AQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVE 496
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
222-541 |
1.92e-20 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 94.06 E-value: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 222 RETQPDDSLN--------IQYTSGTTGQPKGATLTHHNVLNNAFFV--GLRAGYSEKKTIICIPNPlYHCF--GcvMGVL 289
Cdd:COG1541 70 RDNYPFGLFAvpleeivrIHASSGTTGKPTVVGYTRKDLDRWAELFarSLRAAGVRPGDRVQNAFG-YGLFtgG--LGLH 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 290 AALTHLQTCVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYD--SIRSGFIAGAPCPITLCRRLVQD 367
Cdd:COG1541 147 YGAERLGATVIPAGGGNTERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEEGIDPRdlSLKKGIFGGEPWSEEMRKEIEER 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 368 MHMTDMQvCYGTTETSPVSFMSTRDdppeqriKSVGHIM-DHLEAAIVDKRNC-IVPRGVKGEVIV-----RGYSVMRcy 440
Cdd:COG1541 227 WGIKAYD-IYGLTEVGPGVAYECEA-------QDGLHIWeDHFLVEIIDPETGePVPEGEEGELVVttltkEAMPLIR-- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 441 wnseeqtkkeitqdrwYHTGDIAVMHD--------NGTIS-IVGRSKDM-IVRGGeNIYPTEVEQFLFKHQSVEDVHIVG 510
Cdd:COG1541 297 ----------------YRTGDLTRLLPepcpcgrtHPRIGrILGRADDMlIIRGV-NVFPSQIEEVLLRIPEVGPEYQIV 359
|
330 340 350
....*....|....*....|....*....|.
gi 71994694 511 VPDERFGEVVCAWVRLHESAEGKTTEEDIKA 541
Cdd:COG1541 360 VDREGGLDELTVRVELAPGASLEALAEAIAA 390
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
69-580 |
3.11e-20 |
|
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: 94.69 E-value: 3.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 69 TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITP-- 146
Cdd:cd05967 84 TYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLIVTAsc 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 147 ---PGfKKSNYyqsiKDILPEvTLKEPGKSGItsrnftcfqHLIMFDEEDK----IYPGAW-KYTDVMKMGTeedRHHLS 218
Cdd:cd05967 164 giePG-KVVPY----KPLLDK-ALELSGHKPH---------HVLVLNRPQVpadlTKPGRDlDWSELLAKAE---PVDCV 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 219 KIEretqPDDSLNIQYTSGTTGQPKGATLThhnvlNNAFFVGLRagYSEKKTIICIPNPLYHC---FGCVMG----VLAA 291
Cdd:cd05967 226 PVA----ATDPLYILYTSGTTGKPKGVVRD-----NGGHAVALN--WSMRNIYGIKPGDVWWAasdVGWVVGhsyiVYGP 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 292 LTHLQTCVF----PAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANY--NYD--SIRSGFIAGAPC-PITL-- 360
Cdd:cd05967 295 LLHGATTVLyegkPVGTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPDGKYikKYDlsSLRTLFLAGERLdPPTLew 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 361 ----CRRLVQDmHmtdmqvcYGTTET-SPVSF----MSTRDDPPEQRIKSV-GHIMDhleaaIVDKRNCIVPRGVKGEVI 430
Cdd:cd05967 375 aentLGVPVID-H-------WWQTETgWPITAnpvgLEPLPIKAGSPGKPVpGYQVQ-----VLDEDGEPVGPNELGNIV 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 431 VRGY---SVMRCYWNSEEQTKKEITQDR--WYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVED 505
Cdd:cd05967 442 IKLPlppGCLLTLWKNDERFKKLYLSKFpgYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAE 521
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71994694 506 VHIVGVPDERFGEVVCAWVRLHESAE--GKTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIREM 580
Cdd:cd05967 522 CAVVGVRDELKGQVPLGLVVLKEGVKitAEELEKELVALVREQIGPVAAFRLVIFVK--RLPKTRSGKILRRTLRKI 596
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
90-580 |
3.11e-20 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 94.78 E-value: 3.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 90 KKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALIT-------------PPGFKKSN--Y 154
Cdd:PRK08043 253 VEGERIGLMLPNATISAAVIFGASLRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTsrqfldkgklwhlPEQLTQVRwvY 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 155 YQSIKDilpEVTLKEpgKSGItsrnftcFQHLIMfdeedkiyPgawkytdvmkmgteedrhHLSKIERetQPDDSLNIQY 234
Cdd:PRK08043 333 LEDLKD---DVTTAD--KLWI-------FAHLLM--------P------------------RLAQVKQ--QPEDAALILF 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 235 TSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICiPNPLYHCFGCVMGVLAAL-THLQTCVFPAP-SFDALAALq 312
Cdd:PRK08043 373 TSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMS-ALPLFHSFGLTVGLFTPLlTGAEVFLYPSPlHYRIVPEL- 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 313 aIHEEKCTALYGTPTmFIDmiNHPEYAN-YNYDSIRSgFIAGAPCPITLCRRLVQDMHMTDMQVCYGTTETSPVSFMSTr 391
Cdd:PRK08043 451 -VYDRNCTVLFGTST-FLG--NYARFANpYDFARLRY-VVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINV- 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 392 ddPPEQRIKSVGHIMDHLEAAIVDkrnciVPrGVK--GEVIVRGYSVMRCYWNSE-----EQTKKE----ITQDRWYHTG 460
Cdd:PRK08043 525 --PMAAKPGTVGRILPGMDARLLS-----VP-GIEqgGRLQLKGPNIMNGYLRVEkpgvlEVPTAEnargEMERGWYDTG 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 461 DIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKhQSVEDVHIVGV-PDERFGEvvcAWVrLHESAEGKTTEEDI 539
Cdd:PRK08043 597 DIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALG-VSPDKQHATAIkSDASKGE---ALV-LFTTDSELTREKLQ 671
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 71994694 540 KAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIREM 580
Cdd:PRK08043 672 QYAREHGVPELAVPRDIRYLK--QLPLLGSGKPDFVTLKSM 710
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
42-574 |
3.59e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 95.79 E-value: 3.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 42 VGDRLRSAVDQVPDKEFLIFKREgiRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVN 121
Cdd:PRK12316 2005 VHQRIAEQAARAPEAIAVVFGDQ--HLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVP 2082
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 122 INPSYQSEELRYAIEKVGIRALITPpgfkksnyyQSIKDILPevtlkepgksgitsrnftCFQHLIMFDEEDkiyPGAWK 201
Cdd:PRK12316 2083 LDPNYPAERLAYMLEDSGAALLLTQ---------RHLLERLP------------------LPAGVARLPLDR---DAEWA 2132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 202 ytdvmkmgtEEDRHHlskIERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRagySEKKTIICIPNPLYHC 281
Cdd:PRK12316 2133 ---------DYPDTA---PAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGER---YELSPADCELQFMSFS 2197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 282 F-GCVMGVLAALTH-LQTCVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANyNYDSIRSGFIAGAPCPIT 359
Cdd:PRK12316 2198 FdGAHEQWFHPLLNgARVLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDG-RPPAVRVYCFGGEAVPAA 2276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 360 LCRRLVQDMHMTDMQVCYGTTET--SPVSFMSTRDDPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVM 437
Cdd:PRK12316 2277 SLRLAWEALRPVYLFNGYGPTEAvvTPLLWKCRPQDPCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLA 2356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 438 RCYWNSEEQTKKEITQD-------RWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVG 510
Cdd:PRK12316 2357 RGYLNRPGLTAERFVPDpfsasgeRLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVA 2436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71994694 511 VpDERFGEVVCAWVRLHESAEGktTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKK 574
Cdd:PRK12316 2437 Q-DGASGKQLVAYVVPDDAAED--LLAELRAWLAARLPAYMVPAHWVVLE--RLPLNPNGKLDR 2495
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
50-572 |
5.49e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 95.02 E-value: 5.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 50 VDQVPDKEFLIFKREgiRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSE 129
Cdd:PRK12316 3067 VERTPDAVALAFGEQ--RLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEE 3144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 130 ELRYAIEKVGIRALITPPgfkksnyyqsikdilpevTLKEPGKSGItsrnftcfqHLIMFDEEDKIYPGAWKYTDVMkmg 209
Cdd:PRK12316 3145 RLAYMLEDSGAQLLLSQS------------------HLRLPLAQGV---------QVLDLDRGDENYAEANPAIRTM--- 3194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 210 teedrhhlskieretqPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIPNPLYHCFgcVMGVL 289
Cdd:PRK12316 3195 ----------------PENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVF--VEELF 3256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 290 AALTHLQTCVFPAPSF--DALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNydSIRSGFIAGAPCPITLCRRLVQD 367
Cdd:PRK12316 3257 WPLMSGARVVLAGPEDwrDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCT--SLKRIVCGGEALPADLQQQVFAG 3334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 368 MHMTDMqvcYGTTETSPVSFMSTRDDPPEQRIkSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQT 447
Cdd:PRK12316 3335 LPLYNL---YGPTEATITVTHWQCVEEGKDAV-PIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLT 3410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 448 KKEITQD------RWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVc 521
Cdd:PRK12316 3411 AERFVPDpfvpgeRLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQLVAYV- 3489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 71994694 522 awvrLHESAEGKTTEEdIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKV 572
Cdd:PRK12316 3490 ----VPEDEAGDLREA-LKAHLKASLPEYMVPAHLLFLE--RMPLTPNGKL 3533
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
224-580 |
7.15e-20 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 93.29 E-value: 7.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 224 TQPDDS--LNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIPNPLYHCFGCVMGVLAALTHLQTCVFP 301
Cdd:PRK05851 147 TPPDSGgpAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDVGCSWLPLYHDMGLAFLLTAALAGAPLWLAP 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 302 APSFDA--LAALQAIHEEKCTaLYGTPTMFIDMINhpEYANYNYD----SIRSGFIAGAPCPITLCRRLVQDMHMTDMQV 375
Cdd:PRK05851 227 TTAFSAspFRWLSWLSDSRAT-LTAAPNFAYNLIG--KYARRVSDvdlgALRVALNGGEPVDCDGFERFATAMAPFGFDA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 376 -----CYGTTE-----TSP-------VSFMSTRDDPPEQRIKSVGHIMDHLEAAIV--DKRNCIVPRGVkGEVIVRGYSV 436
Cdd:PRK05851 304 gaaapSYGLAEstcavTVPvpgiglrVDEVTTDDGSGARRHAVLGNPIPGMEVRISpgDGAAGVAGREI-GEIEIRGASM 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 437 MRCYWNSEEqtkkeITQDRWYHTGDIAVMHDNGTIsIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGV-PDER 515
Cdd:PRK05851 383 MSGYLGQAP-----IDPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVgTGEG 456
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71994694 516 fgevvCAWVRLHESAEGKTTEED---------IKAWCKgkiahfKIPRYILFKKEYEFPLTVTGKVKKFEIREM 580
Cdd:PRK05851 457 -----SARPGLVIAAEFRGPDEAgarsevvqrVASECG------VVPSDVVFVAPGSLPRTSSGKLRRLAVKRS 519
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
62-580 |
7.78e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 93.17 E-value: 7.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 62 KREGIRKTYSQVATDAENLACGLLhlGLKKGDR---IGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKV 138
Cdd:PRK13388 21 RYGDRTWTWREVLAEAAARAAALI--ALADPDRplhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 139 GIRALITPPGfkksnYYQSIKDI-LPEVTLkepgksgitsrnftcfqhlimFDEEDKIYPGAWkytdvmkmgteeDRHHL 217
Cdd:PRK13388 99 DCQLLVTDAE-----HRPLLDGLdLPGVRV---------------------LDVDTPAYAELV------------AAAGA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 218 SKIERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICiPNPLYHCFGCVMGVLAALTHLQT 297
Cdd:PRK13388 141 LTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYV-SMPLFHSNAVMAGWAPAVASGAA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 298 CVFPaPSFDALAALQAIHEEKCTAL-Y-GTPTMFIdmINHPEYANYNYDSIRSGF-IAGAPCPIT-LCRRLvqDMHMTDm 373
Cdd:PRK13388 220 VALP-AKFSASGFLDDVRRYGATYFnYvGKPLAYI--LATPERPDDADNPLRVAFgNEASPRDIAeFSRRF--GCQVED- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 374 qvCYGTTETSpvsFMSTRDD--PPeqriKSVGHIMDHLeaAIVD---KRNCIV-----------PRGVKGEVIVR-GYSV 436
Cdd:PRK13388 294 --GYGSSEGA---VIVVREPgtPP----GSIGRGAPGV--AIYNpetLTECAVarfdahgallnADEAIGELVNTaGAGF 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 437 MRCYWNSEEQTKKEItQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERF 516
Cdd:PRK13388 363 FEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERV 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71994694 517 GEVVCAWVRLHESAEGKTTE--------EDI--KAWckgkiahfkiPRYIlfKKEYEFPLTVTGKVKKFEIREM 580
Cdd:PRK13388 442 GDQVMAALVLRDGATFDPDAfaaflaaqPDLgtKAW----------PRYV--RIAADLPSTATNKVLKRELIAQ 503
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
64-579 |
1.78e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 92.05 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 64 EGIRKTYSQVATDAENLACGLLhlGLKKGDR---IGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGI 140
Cdd:PRK07867 25 EDSFTSWREHIRGSAARAAALR--ARLDPTRpphVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADC 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 141 RALITppgfkKSNYYQSIKDILPEVtlkepgksgitsrnftcfqHLIMFDEEdkiypgAWKYTDVMKMGTEEDRhhlski 220
Cdd:PRK07867 103 QLVLT-----ESAHAELLDGLDPGV-------------------RVINVDSP------AWADELAAHRDAEPPF------ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 221 eRETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSeKKTIICIPNPLYHCfGCVMGVLAALTHLQTCVF 300
Cdd:PRK07867 147 -RVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLG-PDDVCYVSMPLFHS-NAVMAGWAVALAAGASIA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 301 PAPSFDALAALQAIHEEKCT-ALY-GTPTMFIdmINHPEYANYNYDSIRSGF--IAGAPCPITLCRRLvqDMHMTDmqvC 376
Cdd:PRK07867 224 LRRKFSASGFLPDVRRYGATyANYvGKPLSYV--LATPERPDDADNPLRIVYgnEGAPGDIARFARRF--GCVVVD---G 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 377 YGTTETSpVSFMSTRDDPPeqriKSVGHIMDHLeaAIVD---KRNCivPRGVK------------GE-VIVRGYSVMRCY 440
Cdd:PRK07867 297 FGSTEGG-VAITRTPDTPP----GALGPLPPGV--AIVDpdtGTEC--PPAEDadgrllnadeaiGElVNTAGPGGFEGY 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 441 WNSEEQTKKEItQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVV 520
Cdd:PRK07867 368 YNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQV 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71994694 521 CAWVRLHESAE---GKTTE-----EDI--KAWckgkiahfkiPRYILFKKeyEFPLTVTGKVKKFEIRE 579
Cdd:PRK07867 447 MAALVLAPGAKfdpDAFAEflaaqPDLgpKQW----------PSYVRVCA--ELPRTATFKVLKRQLSA 503
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
234-579 |
2.19e-19 |
|
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: 91.26 E-value: 2.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 234 YTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTI-ICIPnpLYHCFGCVMGVLAALTHLQTCVFpAPSFDALAALQ 312
Cdd:cd05940 88 YTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLyTCLP--LYHSTALIVGWSACLASGATLVI-RKKFSASNFWD 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 313 AIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGapcpitlcrrLVQDM------HMTDMQVC--YGTTE--T 382
Cdd:cd05940 165 DIRKYQATIFQYIGELCRYLLNQPPKPTERKHKVRMIFGNG----------LRPDIweefkeRFGVPRIAefYAATEgnS 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 383 SPVSFMSTRD----DPPEQRIKSVGHIM--DH-LEAAIVDKRN-CI-VPRGVKGEVIVR--GYSVMRCYWNSEEQTKKEI 451
Cdd:cd05940 235 GFINFFGKPGaigrNPSLLRKVAPLALVkyDLeSGEPIRDAEGrCIkVPRGEPGLLISRinPLEPFDGYTDPAATEKKIL 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 452 TQ-----DRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVP----DERFGevvCA 522
Cdd:cd05940 315 RDvfkkgDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvpgtDGRAG---MA 391
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 523 WVRLHESaegktTEEDIKAWCK---GKIAHFKIPRYILFKKEYEfpLTVTGKVKKFEIRE 579
Cdd:cd05940 392 AIVLQPN-----EEFDLSALAAhleKNLPGYARPLFLRLQPEME--ITGTFKQQKVDLRN 444
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
209-520 |
4.25e-19 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 90.84 E-value: 4.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 209 GTEEDRHHLSKIERETQP----DDSLNIQYTSGTTGQPKGATLThhnvlNNAFFV--------GLR-AGYSEKKTIICiP 275
Cdd:PRK05857 147 VTRESEHSLDAASLAGNAdqgsEDPLAMIFTSGTTGEPKAVLLA-----NRTFFAvpdilqkeGLNwVTWVVGETTYS-P 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 276 NPLYHcFGCVMGVLAALTHLQTCVFPAPSFDALAALQAIHEEKCTALygTPTMFIDMINHPEYANYNYDSIRsgFIA-GA 354
Cdd:PRK05857 221 LPATH-IGGLWWILTCLMHGGLCVTGGENTTSLLEILTTNAVATTCL--VPTLLSKLVSELKSANATVPSLR--LVGyGG 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 355 PCPITLCRRLVQDMHMTDMQVcYGTTETSPVSFMSTRDDPPEQRIK--SVGHIMDHLEAAIVDKRNC--IVPRGVK---- 426
Cdd:PRK05857 296 SRAIAADVRFIEATGVRTAQV-YGLSETGCTALCLPTDDGSIVKIEagAVGRPYPGVDVYLAATDGIgpTAPGAGPsasf 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 427 GEVIVRGYSVMRCYWNSEEQTKkEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDV 506
Cdd:PRK05857 375 GTLWIKSPANMLGYWNNPERTA-EVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREA 453
|
330
....*....|....
gi 71994694 507 HIVGVPDERFGEVV 520
Cdd:PRK05857 454 ACYEIPDEEFGALV 467
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
223-494 |
6.63e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 90.06 E-value: 6.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 223 ETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIPNPLYHcfgcVMGVLAALTHLQTCvfpa 302
Cdd:PRK07768 148 ETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSWLPLFH----DMGMVGFLTVPMYF---- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 303 psfdalaalqaiheeKCTALYGTPTMFI-------DMINH-----------------------PEYANYNYDSIRSGFIA 352
Cdd:PRK07768 220 ---------------GAELVKVTPMDFLrdpllwaELISKyrgtmtaapnfayallarrlrrqAKPGAFDLSSLRFALNG 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 353 GAPCPITLCRRLVQD-----MHMTDMQVCYGTTETS-PVSFmSTRDDPPE-----------------------QRIKSVG 403
Cdd:PRK07768 285 AEPIDPADVEDLLDAgarfgLRPEAILPAYGMAEATlAVSF-SPCGAGLVvdevdadllaalrravpatkgntRRLATLG 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 404 HIMDHLEAAIVDK-RNCIVPRGVkGEVIVRGYSVMRCYWNSEeqtKKEITQDR--WYHTGDIAVMHDNGTISIVGRSKDM 480
Cdd:PRK07768 364 PPLPGLEVRVVDEdGQVLPPRGV-GVIELRGESVTPGYLTMD---GFIPAQDAdgWLDTGDLGYLTEEGEVVVCGRVKDV 439
|
330
....*....|....
gi 71994694 481 IVRGGENIYPTEVE 494
Cdd:PRK07768 440 IIMAGRNIYPTDIE 453
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
38-572 |
6.94e-19 |
|
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: 89.80 E-value: 6.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 38 LFETVGDRLRSAVDQVPDKEFLifkregirkTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGM 117
Cdd:cd17644 5 LFEEQVERTPDAVAVVFEDQQL---------TYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 118 VLVNINPSYQSEELRYAIEKVGIRALITppgfkksnyyqsikdilpevtlkepgksgitsrnftcfqhlimfdeedkiyp 197
Cdd:cd17644 76 AYVPLDPNYPQERLTYILEDAQISVLLT---------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 198 gawkytdvmkmgteedrhhlskieretQPDDSLNIQYTSGTTGQPKGATLTHHNVLNnaFFVGLRAGYSekktiicIPNP 277
Cdd:cd17644 104 ---------------------------QPENLAYVIYTSGSTGKPKGVMIEHQSLVN--LSHGLIKEYG-------ITSS 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 278 LYHCFGCVMGVLAALTHLQTCVFPAPS---------FDALAALQAIHEEKCTALYGTPTMFIDMINH--PEYANYNyDSI 346
Cdd:cd17644 148 DRVLQFASIAFDVAAEEIYVTLLSGATlvlrpeemrSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLEllLSTIDLP-SSL 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 347 RSGFIAG-APCPITLcrRLVQDMHMTDMQV--CYGTTETSPVSFMSTRDDPPEQRIKSV--GHIMDHLEAAIVDKRNCIV 421
Cdd:cd17644 227 RLVIVGGeAVQPELV--RQWQKNVGNFIQLinVYGPTEATIAATVCRLTQLTERNITSVpiGRPIANTQVYILDENLQPV 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 422 PRGVKGEVIVRGYSVMRCYWNSEEQTKKEITQD--------RWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEV 493
Cdd:cd17644 305 PVGVPGELHIGGVGLARGYLNRPELTAEKFISHpfnsseseRLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEI 384
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71994694 494 EQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAEGKTTEedIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKV 572
Cdd:cd17644 385 EAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVE--LRQFLKAKLPDYMIPSAFVVLE--ELPLTPNGKI 459
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
50-574 |
7.70e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 91.38 E-value: 7.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 50 VDQVPDKEFLIFkrEGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSE 129
Cdd:PRK12467 3105 VARTPEAPALVF--GDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRE 3182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 130 ELRYAIEKVGIRALITppgfkksnyYQSIKDILPEVTlkepgksGITSrnftcfqhlIMFDEEDkiypgAWKYTDvmkmg 209
Cdd:PRK12467 3183 RLAYMIEDSGVKLLLT---------QAHLLEQLPAPA-------GDTA---------LTLDRLD-----LNGYSE----- 3227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 210 teedrhhlSKIERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIIcipnpLYHCF---GCVM 286
Cdd:PRK12467 3228 --------NNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVL-----LFMSFsfdGAQE 3294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 287 GVLAAL-THLQTCVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANY-NYDSIRSGFIAGAPCPITLCRRL 364
Cdd:PRK12467 3295 RFLWTLiCGGCLVVRDNDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGADCaSLDIYVFGGEAVPPAAFEQVKRK 3374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 365 VQDMHMTDMqvcYGTTET--SPVSFMSTRDDPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWN 442
Cdd:PRK12467 3375 LKPRGLTNG---YGPTEAvvTVTLWKCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQ 3451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 443 SEEQTKKEITQD-------RWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDER 515
Cdd:PRK12467 3452 RPSLTAERFVADpfsgsggRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAG 3531
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 71994694 516 fGEVVCAWVRLHesAEGKTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKK 574
Cdd:PRK12467 3532 -GKQLVAYVVPA--DPQGDWRETLRDHLAASLPDYMVPAQLLVLA--AMPLGPNGKVDR 3585
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
54-572 |
1.39e-18 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 89.61 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 54 PDKEFLIFKREG---IRK-TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSE 129
Cdd:TIGR02188 71 PDKVAIIWEGDEpgeVRKiTYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 130 ELRYAIEKVGIRALITPPGFKKSNYYQSIKDILPEVTLKEPGksgiTSRNFTCFQHL-----IMFDEEDKiypgaWkYTD 204
Cdd:TIGR02188 151 ALADRINDAGAKLVITADEGLRGGKVIPLKAIVDEALEKCPV----SVEHVLVVRRTgnpvvPWVEGRDV-----W-WHD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 205 VMKmgTEEDRHHLSKIEREtqpdDSLNIQYTSGTTGQPKG-----------ATLTHHNVL----NNAFF----VGLRAGY 265
Cdd:TIGR02188 221 LMA--KASAYCEPEPMDSE----DPLFILYTSGSTGKPKGvlhttggyllyAAMTMKYVFdikdGDIFWctadVGWITGH 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 266 SekktiicipnplYHCFGCVMGVLAALTHLQTCVFPAPS-FdalaaLQAIHEEKCTALYGTPT---MFIDMINHPeYANY 341
Cdd:TIGR02188 295 S------------YIVYGPLANGATTVMFEGVPTYPDPGrF-----WEIIEKHKVTIFYTAPTairALMRLGDEW-VKKH 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 342 NYDSIRSGFIAGAP-----------------CPI--TlcrrlvqdmhmtdmqvcYGTTETSpvsfmstrddppeqriksv 402
Cdd:TIGR02188 357 DLSSLRLLGSVGEPinpeawmwyykvvgkerCPIvdT-----------------WWQTETG------------------- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 403 GHIMDHL------------------EAAIVDKRNCIVPRGVKGE--VIVRGY-SVMRCYWNSEEQTKKEITQD--RWYHT 459
Cdd:TIGR02188 401 GIMITPLpgatptkpgsatlpffgiEPAVVDEEGNPVEGPGEGGylVIKQPWpGMLRTIYGDHERFVDTYFSPfpGYYFT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 460 GDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAE-GKTTEED 538
Cdd:TIGR02188 481 GDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEpDDELRKE 560
|
570 580 590
....*....|....*....|....*....|....
gi 71994694 539 IKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKV 572
Cdd:TIGR02188 561 LRKHVRKEIGPIAKPDKIRFVP--GLPKTRSGKI 592
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
69-478 |
2.48e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 88.88 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 69 TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWtttqFASALA----GMVLVNINPSYQSEELRYAIEKVGIRALI 144
Cdd:PTZ00216 123 TYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEW----LASIYGiwsqSMVAATVYANLGEDALAYALRETECKAIV 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 145 TPPgfkksnyyQSIKDILPEVTLKEpgksgitsrnftcFQH--LIMFD--------EEDKIYpgAWkyTDVMKMGTEEDR 214
Cdd:PTZ00216 199 CNG--------KNVPNLLRLMKSGG-------------MPNttIIYLDslpasvdtEGCRLV--AW--TDVVAKGHSAGS 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 215 HHLSKIEreTQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRA----GYSEKKTIICIPNPLYHC--FGCVMGV 288
Cdd:PTZ00216 254 HHPLNIP--ENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLndliGPPEEDETYCSYLPLAHImeFGVTNIF 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 289 LAalthlqtcvfpapsfdalaalqaiheEKCTALYGTPTMFIDMINHP--EYANYN----------YDSIRSGFIAGAPC 356
Cdd:PTZ00216 332 LA--------------------------RGALIGFGSPRTLTDTFARPhgDLTEFRpvfligvpriFDTIKKAVEAKLPP 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 357 PITLCRRL--------------------------------------------------VQDMhmtdMQVC-------YGT 379
Cdd:PTZ00216 386 VGSLKRRVfdhayqsrlralkegkdtpywnekvfsapravlggrvramlsgggplsaaTQEF----VNVVfgmviqgWGL 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 380 TETSPV-SFMSTRDDPPEqrikSVGHIMDHLEAAIVDkrnciV----------PRGvkgEVIVRGYSVMRCYWNSEEQTK 448
Cdd:PTZ00216 462 TETVCCgGIQRTGDLEPN----AVGQLLKGVEMKLLD-----TeeykhtdtpePRG---EILLRGPFLFKGYYKQEELTR 529
|
490 500 510
....*....|....*....|....*....|
gi 71994694 449 KEITQDRWYHTGDIAVMHDNGTISIVGRSK 478
Cdd:PTZ00216 530 EVLDEDGWFHTGDVGSIAANGTLRIIGRVK 559
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
41-544 |
8.52e-18 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 87.18 E-value: 8.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 41 TVGDRLRSAVDQVPDKEFLIFKR--EG-----IRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASA 113
Cdd:PLN02430 43 TAWDIFSKSVEKYPDNKMLGWRRivDGkvgpyMWKTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 114 LAGMVLVNINPSYQSEELRYAIEKVGIRALITPPgfKKsnyyqsIKDILpevtlkEPG-KSGITSRNFTCFQHLIMfDEE 192
Cdd:PLN02430 123 AHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQD--KK------IKELL------EPDcKSAKRLKAIVSFTSVTE-EES 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 193 DK-----IYPGAWKytDVMKMGTEEdrhhlskiERET---QPDDSLNIQYTSGTTGQPKGATLTHHNVLnnAFFVGL--- 261
Cdd:PLN02430 188 DKasqigVKTYSWI--DFLHMGKEN--------PSETnppKPLDICTIMYTSGTSGDPKGVVLTHEAVA--TFVRGVdlf 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 262 RAGYSEKKT---IICIPNPLYHCF---------------GCVMGVLAALTH-LQ----TCVFPAPS-FD--------ALA 309
Cdd:PLN02430 256 MEQFEDKMThddVYLSFLPLAHILdrmieeyffrkgasvGYYHGDLNALRDdLMelkpTLLAGVPRvFErihegiqkALQ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 310 ALQAIHEEKCTALY-------------GTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCP--------ITLCRRLVQDm 368
Cdd:PLN02430 336 ELNPRRRLIFNALYkyklawmnrgyshKKASPMADFLAFRKVKAKLGGRLRLLISGGAPLSteieeflrVTSCAFVVQG- 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 369 hmtdmqvcYGTTETSPVSFMSTRDDppEQRIKSVGHIMDHLEAAIVDkrnciVPR--------GVKGEVIVRGYSVMRCY 440
Cdd:PLN02430 415 --------YGLTETLGPTTLGFPDE--MCMLGTVGAPAVYNELRLEE-----VPEmgydplgePPRGEICVRGKCLFSGY 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 441 WNSEEQTkKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMI-VRGGENIYPTEVEQFLFKHQSVEDVHIVGvpdERFGEV 519
Cdd:PLN02430 480 YKNPELT-EEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEYLENVYGQNPIVEDIWVYG---DSFKSM 555
|
570 580
....*....|....*....|....*
gi 71994694 520 VCAWVRLHesaegkttEEDIKAWCK 544
Cdd:PLN02430 556 LVAVVVPN--------EENTNKWAK 572
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
492-571 |
1.84e-17 |
|
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: 77.20 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 492 EVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAEgkTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGK 571
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVE--LLEEELVAHVREELGPYAVPKEVVFVD--ELPKTRSGK 76
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
63-512 |
2.24e-17 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 85.42 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 63 REGIRKTYSQVATDAENLACGLL-HLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIR 141
Cdd:cd05938 1 FEGETYTYRDVDRRSNQAARALLaHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 142 ALITPPGFKKSnyyqsIKDILPEvtLKEPGKS------GITSRNFTCFQHLIMfDEEDKIYPGAWKYTDVMKmgteedrh 215
Cdd:cd05938 81 VLVVAPELQEA-----VEEVLPA--LRADGVSvwylshTSNTEGVISLLDKVD-AASDEPVPASLRAHVTIK-------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 216 hlskieretqpDDSLNIqYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKktIICIPNPLYHCFGCVMGVLAALTHL 295
Cdd:cd05938 145 -----------SPALYI-YTSGTTGLPKAARISHLRVLQCSGFLSLCGVTADD--VIYITLPLYHSSGFLLGIGGCIELG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 296 QTCVFpAPSFDA-----------LAALQAIHEekcTALYgtptmfidMINHPEYANYNYDSIR----SGFIAgapcpiTL 360
Cdd:cd05938 211 ATCVL-KPKFSAsqfwddcrkhnVTVIQYIGE---LLRY--------LCNQPQSPNDRDHKVRlaigNGLRA------DV 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 361 CRRLVQdmHMTDMQVC--YGTTETSpVSFMSTRDdppeqRIKSVG-----HIMDHLEAAI---VDK----RN----CI-V 421
Cdd:cd05938 273 WREFLR--RFGPIRIRefYGSTEGN-IGFFNYTG-----KIGAVGrvsylYKLLFPFELIkfdVEKeepvRDaqgfCIpV 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 422 PRGVKGEVI--VRGYSVMRCYWNSEEQTKKEI------TQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEV 493
Cdd:cd05938 345 AKGEPGLLVakITQQSPFLGYAGDKEQTEKKLlrdvfkKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEV 424
|
490
....*....|....*....
gi 71994694 494 EQFLFKHQSVEDVHIVGVP 512
Cdd:cd05938 425 ADVLGLLDFLQEVNVYGVT 443
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
57-572 |
2.50e-17 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 84.95 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 57 EFLIFKREGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIE 136
Cdd:PRK04813 17 DFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIEMIIE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 137 KVGIRALITPPGFKksnyyQSIKDIlPEVTLKEpgksgitsrnftcfqhlimfdeedkiypgawkYTDVMKMGTEEDRHH 216
Cdd:PRK04813 97 VAKPSLIIATEELP-----LEILGI-PVITLDE--------------------------------LKDIFATGNPYDFDH 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 217 LSKieretqPDDSLNIQYTSGTTGQPKGATLTHHNVL------NNAFFVGLR------AGYSEKKTIICIpnplYHCFgC 284
Cdd:PRK04813 139 AVK------GDDNYYIIFTSGTTGKPKGVQISHDNLVsftnwmLEDFALPEGpqflnqAPYSFDLSVMDL----YPTL-A 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 285 VMGVLAALTHLQTCVFpAPSFDALAALQAiheekcTALYGTPTmFIDM-INHPEYANYNYDSIRSGFIAGAPCPITLCRR 363
Cdd:PRK04813 208 SGGTLVALPKDMTANF-KQLFETLPQLPI------NVWVSTPS-FADMcLLDPSFNEEHLPNLTHFLFCGEELPHKTAKK 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 364 LVQ---DMHMTDMqvcYGTTE-TSPVSFMSTRDDPPEQ--RIkSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVM 437
Cdd:PRK04813 280 LLErfpSATIYNT---YGPTEaTVAVTSIEITDEMLDQykRL-PIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVS 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 438 RCYWNSEEQTKKEITQD---RWYHTGDIAVMhDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEdvHIVGVPDE 514
Cdd:PRK04813 356 KGYLNNPEKTAEAFFTFdgqPAYHTGDAGYL-EDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVE--SAVVVPYN 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71994694 515 RFGEVV--CAWVRLHE---SAEGKTTEEdIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKV 572
Cdd:PRK04813 433 KDHKVQylIAYVVPKEedfEREFELTKA-IKKELKERLMEYMIPRKFIYRD--SLPLTPNGKI 492
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
54-590 |
7.32e-16 |
|
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: 80.68 E-value: 7.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 54 PDKEFLIFKRE----GIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSE 129
Cdd:cd05966 67 GDKVAIIWEGDepdqSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 130 ELRYAIEKVGIRALITPPGFKKSNYYQSIKDILPEVtLKEPgksgitsrnfTCFQHLIMF---DEEDKIYPG--AWkYTD 204
Cdd:cd05966 147 SLADRINDAQCKLVITADGGYRGGKVIPLKEIVDEA-LEKC----------PSVEKVLVVkrtGGEVPMTEGrdLW-WHD 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 205 VMKmgteedrhhlsKIERETQP-----DDSLNIQYTSGTTGQPKG-----------ATLTHHNVLNNAffvglragysek 268
Cdd:cd05966 215 LMA-----------KQSPECEPewmdsEDPLFILYTSGSTGKPKGvvhttggyllyAATTFKYVFDYH------------ 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 269 ktiiciPNPLYHC---FGCVMG----VLAALTHLQTCV-------FPAPS-FdalaaLQAIHEEKCTALYGTPT---MFI 330
Cdd:cd05966 272 ------PDDIYWCtadIGWITGhsyiVYGPLANGATTVmfegtptYPDPGrY-----WDIVEKHKVTIFYTAPTairALM 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 331 DMINHPEYAnYNYDSIR-----------------SGFIAGAPCPI--TlcrrlvqdmhmtdmqvcYGTTETSpvSFMSTr 391
Cdd:cd05966 341 KFGDEWVKK-HDLSSLRvlgsvgepinpeawmwyYEVIGKERCPIvdT-----------------WWQTETG--GIMIT- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 392 DDPPEQRIK--SVGHIMDHLEAAIVDKRNCIVPRGVKGE-VIVRGY-SVMRCYWNSEEQTKKEITQD--RWYHTGDIAVM 465
Cdd:cd05966 400 PLPGATPLKpgSATRPFFGIEPAILDEEGNEVEGEVEGYlVIKRPWpGMARTIYGDHERYEDTYFSKfpGYYFTGDGARR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 466 HDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAEGKT-TEEDIKAWCK 544
Cdd:cd05966 480 DEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDeLRKELRKHVR 559
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 71994694 545 GKIAHFKIPRYILFKKeyEFPLTVTGKVKKfeiREMSKIELGLQQV 590
Cdd:cd05966 560 KEIGPIATPDKIQFVP--GLPKTRSGKIMR---RILRKIAAGEEEL 600
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
212-580 |
5.13e-15 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 76.62 E-value: 5.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 212 EDRHH---LSKIERETQP--DDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGySEKKTIICIPNplYHCFG--- 283
Cdd:PRK07824 15 QDERRaalLRDALRVGEPidDDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLG-GPGQWLLALPA--HHIAGlqv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 284 CVMGVLAALTHLQTCV---FPAPSF-DALAALQAihEEKCTALygTPTMFIDMINHPE--YANYNYDSIrsgFIAGAPCP 357
Cdd:PRK07824 92 LVRSVIAGSEPVELDVsagFDPTALpRAVAELGG--GRRYTSL--VPMQLAKALDDPAatAALAELDAV---LVGGGPAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 358 ITLCRRLVQdmhmTDMQVC--YGTTETSPvsfmstrddppeqriksvGHIMDH--LEAAIVdkrncivpRGVKGEVIVRG 433
Cdd:PRK07824 165 APVLDAAAA----AGINVVrtYGMSETSG------------------GCVYDGvpLDGVRV--------RVEDGRIALGG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 434 YSVMRCYWNSEEQtkKEITQDRWYHTGDIAVMHDnGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPD 513
Cdd:PRK07824 215 PTLAKGYRNPVDP--DPFAEPGWFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPD 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71994694 514 ERFGE-VVCAWVRLHESAEgktTEEDIKAWCKGKIAHFKIPRYIlfKKEYEFPLTVTGKVKKFEIREM 580
Cdd:PRK07824 292 DRLGQrVVAAVVGDGGPAP---TLEALRAHVARTLDRTAAPREL--HVVDELPRRGIGKVDRRALVRR 354
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
425-557 |
5.76e-15 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 77.60 E-value: 5.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 425 VKGEVIVRGYSVMRCYWNSeeqtkKEIT----QDRWYHTGDIAVMhDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKH 500
Cdd:PRK09029 303 VDGEIWLRGASLALGYWRQ-----GQLVplvnDEGWFATRDRGEW-QNGELTILGRLDNLFFSGGEGIQPEEIERVINQH 376
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 71994694 501 QSVEDVHIVGVPDERFGEVVCAWVRLHEsaegKTTEEDIKAWCKGKIAHFKIP-RYIL 557
Cdd:PRK09029 377 PLVQQVFVVPVADAEFGQRPVAVVESDS----EAAVVNLAEWLQDKLARFQQPvAYYL 430
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
225-495 |
7.24e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 78.67 E-value: 7.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 225 QPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVglRAGYSekktIICIPN-------PLYHCFGCVMGVLAALTHLQT 297
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLI--RHGFG----IDLNPDdvivswlPLYHDMGLIGGLLQPIFSGVP 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 298 CVFPAPSF---DALAALQAIHEEKCTaLYGTPT----MFIDMINHPEYANYNYDSIRSGFIAGAPCPITLCRRLVQDMHM 370
Cdd:PRK05691 238 CVLMSPAYfleRPLRWLEAISEYGGT-ISGGPDfayrLCSERVSESALERLDLSRWRVAYSGSEPIRQDSLERFAEKFAA 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 371 TDMQ-----VCYGTTE-TSPVS-----------------FMSTRDDPPE-QRIKSVGHIMDHLEAAIVDKRNCIV-PRGV 425
Cdd:PRK05691 317 CGFDpdsffASYGLAEaTLFVSggrrgqgipaleldaeaLARNRAEPGTgSVLMSCGRSQPGHAVLIVDPQSLEVlGDNR 396
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71994694 426 KGEVIVRGYSVMRCYWNSEEQTKKEITQ---DRWYHTGDIAVMHDnGTISIVGRSKDMIVRGGENIYPTEVEQ 495
Cdd:PRK05691 397 VGEIWASGPSIAHGYWRNPEASAKTFVEhdgRTWLRTGDLGFLRD-GELFVTGRLKDMLIVRGHNLYPQDIEK 468
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
69-582 |
3.60e-14 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 75.65 E-value: 3.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 69 TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRAlitppG 148
Cdd:PLN02861 79 TYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSI-----A 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 149 FKKSNYYQSIKDILPEVTLKEpgKSGITSRNFTCFQHlimfDEEDKIYPGAWKYTDVMKMGTEEdrhhlSKIEREtQPDD 228
Cdd:PLN02861 154 FVQESKISSILSCLPKCSSNL--KTIVSFGDVSSEQK----EEAEELGVSCFSWEEFSLMGSLD-----CELPPK-QKTD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 229 SLNIQYTSGTTGQPKGATLTHHNVL------NNAFFVGLRAGYSEKKTIICIPnpLYHCFGCVMGVLaalthlqtCVFPA 302
Cdd:PLN02861 222 ICTIMYTSGTTGEPKGVILTNRAIIaevlstDHLLKVTDRVATEEDSYFSYLP--LAHVYDQVIETY--------CISKG 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 303 PSF-----DALAALQAIHEEKCTALYGTPTMFIDM---INHP------------EYAnYNY------------------- 343
Cdd:PLN02861 292 ASIgfwqgDIRYLMEDVQALKPTIFCGVPRVYDRIytgIMQKissggmlrkklfDFA-YNYklgnlrkglkqeeasprld 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 344 ----DSIRSGF-------IAGA-PCP--------ITLCRRLVQDmhmtdmqvcYGTTETSPVSFMSTRDDPPeqRIKSVG 403
Cdd:PLN02861 371 rlvfDKIKEGLggrvrllLSGAaPLPrhveeflrVTSCSVLSQG---------YGLTESCGGCFTSIANVFS--MVGTVG 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 404 HIMDHLEAAIVDKRN------CIVPRGvkgEVIVRGYSVMRCYWNSEEQTKkEITQDRWYHTGDIAVMHDNGTISIVGRS 477
Cdd:PLN02861 440 VPMTTIEARLESVPEmgydalSDVPRG---EICLRGNTLFSGYHKRQDLTE-EVLIDGWFHTGDIGEWQPNGAMKIIDRK 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 478 KDMI-VRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERF--GEVVCAWVRLHESAEGKTTEEDIKAWCKgkiaHFKIPR 554
Cdd:PLN02861 516 KNIFkLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFlvAVVVPDRQALEDWAANNNKTGDFKSLCK----NLKARK 591
|
570 580
....*....|....*....|....*...
gi 71994694 555 YILFKkeyefpLTVTGKVKKFEIREMSK 582
Cdd:PLN02861 592 YILDE------LNSTGKKLQLRGFEMLK 613
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
35-511 |
6.44e-14 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 75.47 E-value: 6.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 35 VPLLFETVGDRLRSAVDQVPDKEFLIFkrEGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASAL 114
Cdd:PRK10252 453 VEIPETTLSALVAQQAAKTPDAPALAD--ARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVE 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 115 AGMVLVNINPSYQSEELRYAIEKVGIRALITPPGFKKsnyyqsikdilpevtlKEPGKSGITSRNftcfqhlimfdeedk 194
Cdd:PRK10252 531 AGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLP----------------RFADVPDLTSLC--------------- 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 195 iYPGAWKYTDVmkmgteedrhhlsKIERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEK-----K 269
Cdd:PRK10252 580 -YNAPLAPQGA-------------APLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADdvvlqK 645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 270 TIICIPNPLYHCFGCVMG----VLAAlthlqtcvfPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINH--PEYANYNY 343
Cdd:PRK10252 646 TPCSFDVSVWEFFWPFIAgaklVMAE---------PEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASltPEGARQSC 716
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 344 DSIRSGFIAGAPCPITLCRRLVQDMHmTDMQVCYGTTETS-PVSFM-STRDDPPEQRIKSV--GHIMDHLEAAIVDKRNC 419
Cdd:PRK10252 717 ASLRQVFCSGEALPADLCREWQQLTG-APLHNLYGPTEAAvDVSWYpAFGEELAAVRGSSVpiGYPVWNTGLRILDARMR 795
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 420 IVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEITQD------RWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEV 493
Cdd:PRK10252 796 PVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADpfapgeRMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEI 875
|
490
....*....|....*...
gi 71994694 494 EQFLFKHQSVEDVHIVGV 511
Cdd:PRK10252 876 DRAMQALPDVEQAVTHAC 893
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
234-572 |
5.99e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 72.51 E-value: 5.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 234 YTSGTTGQPKGATLTHHNVLNNAFFvgLRAGYS-------EKKTIICIPNPLYHCF-----GCVMgVLAAlthlqtcvfP 301
Cdd:PRK05691 1280 YTSGSTGQPKGVGNTHAALAERLQW--MQATYAlddsdvlMQKAPISFDVSVWECFwplitGCRL-VLAG---------P 1347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 302 APSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNydSIRSGFIAGAPCPITLCRRLVQDMHMTDMQVCYGTTE 381
Cdd:PRK05691 1348 GEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACT--SLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTE 1425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 382 TS-PVSFMSTRDDPPEQriKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEITQD------ 454
Cdd:PRK05691 1426 TAiNVTHWQCQAEDGER--SPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDplgedg 1503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 455 -RWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVhIVGVPDERFGEVVCAWVRLHESAEGK 533
Cdd:PRK05691 1504 aRLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQA-AVLVREGAAGAQLVGYYTGEAGQEAE 1582
|
330 340 350
....*....|....*....|....*....|....*....
gi 71994694 534 TteEDIKAWCKGKIAHFKIPRYILfkKEYEFPLTVTGKV 572
Cdd:PRK05691 1583 A--ERLKAALAAELPEYMVPAQLI--RLDQMPLGPSGKL 1617
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
222-494 |
6.48e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 71.51 E-value: 6.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 222 RETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNafFVGLRAGYSEKKTIICIPN-------PLYHCFGCVMGVLAALTH 294
Cdd:PRK05850 155 RPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIAN--FEQLMSDYFGDTGGVPPPDttvvswlPFYHDMGLVLGVCAPILG 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 295 LQTCVFPAPsfdaLAALQ---------AIHEEKCTA-------LYGTPTMFIDMinhpeyANYNYDSIRsGFIAGAP--C 356
Cdd:PRK05850 233 GCPAVLTSP----VAFLQrparwmqllASNPHAFSAapnfafeLAVRKTSDDDM------AGLDLGGVL-GIISGSErvH 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 357 PITLcRRLVQ-----DMHMTDMQVCYGTTETspVSFMSTRD--DPPE------QRIkSVGH------------IMDHLEA 411
Cdd:PRK05850 302 PATL-KRFADrfapfNLRETAIRPSYGLAEA--TVYVATREpgQPPEsvrfdyEKL-SAGHakrcetgggtplVSYGSPR 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 412 A----IVDKRNCI-VPRGVKGEVIVRGYSVMRCYWNSEEQTKK----EIT-------QDRWYHTGDIAVMHDnGTISIVG 475
Cdd:PRK05850 378 SptvrIVDPDTCIeCPAGTVGEIWVHGDNVAAGYWQKPEETERtfgaTLVdpspgtpEGPWLRTGDLGFISE-GELFIVG 456
|
330
....*....|....*....
gi 71994694 476 RSKDMIVRGGENIYPTEVE 494
Cdd:PRK05850 457 RIKDLLIVDGRNHYPDDIE 475
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
44-516 |
1.38e-12 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 70.43 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 44 DRLRSAVDQVPDKEFLiFKRE--------GIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALA 115
Cdd:PLN02614 49 DVFRMSVEKYPNNPML-GRREivdgkpgkYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 116 GMVLVNINPSYQSEELRYAIEKVGIRALIT-----PPGFKK-SNYYQSIKDILPEVTLKEPGKsgitsrnftcfqhlimf 189
Cdd:PLN02614 128 GLYCVPLYDTLGAGAVEFIISHSEVSIVFVeekkiSELFKTcPNSTEYMKTVVSFGGVSREQK----------------- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 190 DEEDKIYPGAWKYTDVMKMGteEDRHHLSKIERetqPDDSLNIQYTSGTTGQPKGATLTHHNVLNNA-----FFVGLRAG 264
Cdd:PLN02614 191 EEAETFGLVIYAWDEFLKLG--EGKQYDLPIKK---KSDICTIMYTSGTTGDPKGVMISNESIVTLIagvirLLKSANAA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 265 YSEKKTIICIPnPLYHCFG-----CVMGVLAALTHLQTcvfpapsfDALAALQAIHEEKCTALYGTPTM----------- 328
Cdd:PLN02614 266 LTVKDVYLSYL-PLAHIFDrvieeCFIQHGAAIGFWRG--------DVKLLIEDLGELKPTIFCAVPRVldrvysglqkk 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 329 -----FIDMINHPEYANYNYDSIRSG--FIAGAPcpitLCRRLV-----QDM----------------HMTD----MQVC 376
Cdd:PLN02614 337 lsdggFLKKFVFDSAFSYKFGNMKKGqsHVEASP----LCDKLVfnkvkQGLggnvriilsgaaplasHVESflrvVACC 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 377 -----YGTTETSPVSFMSTRDD--------PP----EQRIKSVGHI-MDHLEAAivdkrncivPRGvkgEVIVRGYSVMR 438
Cdd:PLN02614 413 hvlqgYGLTESCAGTFVSLPDEldmlgtvgPPvpnvDIRLESVPEMeYDALAST---------PRG---EICIRGKTLFS 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71994694 439 CYWNSEEQTKkEITQDRWYHTGDIAVMHDNGTISIVGRSKDMI-VRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERF 516
Cdd:PLN02614 481 GYYKREDLTK-EVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFkLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESF 558
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
52-467 |
4.82e-12 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 68.61 E-value: 4.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 52 QVPDKEFLIFK--REGIRK-TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQS 128
Cdd:cd05921 7 QAPDRTWLAERegNGGWRRvTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 129 -----EELRYAIEKVGIRALITPPGFKksnYYQSIKDILPevtlkePGKSGITSRNFTCFQHLIMFDEEDKIYPGAwkyt 203
Cdd:cd05921 87 msqdlAKLKHLFELLKPGLVFAQDAAP---FARALAAIFP------LGTPLVVSRNAVAGRGAISFAELAATPPTA---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 204 dvmkmgtEEDRHHlskieRETQPDDSLNIQYTSGTTGQPKGATLTHHNV-LNNAFFVGLRAGYSEKKTIICIPNPLYHCF 282
Cdd:cd05921 154 -------AVDAAF-----AAVGPDTVAKFLFTSGSTGLPKAVINTQRMLcANQAMLEQTYPFFGEEPPVLVDWLPWNHTF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 283 GCVMGVLAALTHLQTCVF----PAPSF--DALAALQAIHEekcTALYGTP---TMFID-MINHPEYANYNYDSIRSGFIA 352
Cdd:cd05921 222 GGNHNFNLVLYNGGTLYIddgkPMPGGfeETLRNLREISP---TVYFNVPagwEMLVAaLEKDEALRRRFFKRLKLMFYA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 353 GAPCPITLCRRL----VQDM-HMTDMQVCYGTTETSPVSFMSTRddpPEQRIKSVGhimdhLEAAIVDKRncIVPRGVKG 427
Cdd:cd05921 299 GAGLSQDVWDRLqalaVATVgERIPMMAGLGATETAPTATFTHW---PTERSGLIG-----LPAPGTELK--LVPSGGKY 368
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 71994694 428 EVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHD 467
Cdd:cd05921 369 EVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAD 408
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
235-577 |
6.16e-12 |
|
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: 67.88 E-value: 6.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 235 TSGTTGQPKGATLTHHNVLNNafFVGLRAGYSEKKTIICIPNPLYHCFGCVMGVLAAL--------THLQTCVFPAPSFD 306
Cdd:cd17654 126 TSGTTGTPKIVAVPHKCILPN--IQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLssgatlliVPTSVKVLPSKLAD 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 307 ALAALQaiheeKCTALYGTPTMFiDMINHPEYANYN---YDSIRSGFIAGAPCPI-TLCRRLVQDMHMTdmQVC--YGTT 380
Cdd:cd17654 204 ILFKRH-----RITVLQATPTLF-RRFGSQSIKSTVlsaTSSLRVLALGGEPFPSlVILSSWRGKGNRT--RIFniYGIT 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 381 ETSpvSFMSTRDDPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYsVMRCYWNSEEQTkkeitqdrWYHTG 460
Cdd:cd17654 276 EVS--CWALAYKVPEEDSPVQLGSPLLGTVIEVRDQNGSEGTGQVFLGGLNRVC-ILDDEVTVPKGT--------MRATG 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 461 DIaVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERfgeVVCAWVRLHESAEgktTEEDIK 540
Cdd:cd17654 345 DF-VTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQR---LIAFIVGESSSSR---IHKELQ 417
|
330 340 350
....*....|....*....|....*....|....*..
gi 71994694 541 awcKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEI 577
Cdd:cd17654 418 ---LTLLSSHAIPDTFVQID--KLPLTSHGKVDKSEL 449
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
69-578 |
1.09e-11 |
|
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: 67.45 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 69 TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITppg 148
Cdd:cd05939 5 TFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 149 fkksnyyqSIKDILPEVTLKEPGKsgITSRNFTcfqhlimfdeedkiypgawkytdvmkmgteedrhhlskieretqpdD 228
Cdd:cd05939 82 --------NLLDPLLTQSSTEPPS--QDDVNFR----------------------------------------------D 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 229 SLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKtIICIPNPLYHCFGCVMGVLAALTHLQTCV----FPAPS 304
Cdd:cd05939 106 KLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPED-VVYDCLPLYHSAGGIMGVGQALLHGSTVVirkkFSASN 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 305 F--DAL----AALQAIHeEKCTALYGTPTMfidminhPEYANYNydsIRSGFIAGAPCPItlCRRLVQDMHMTDMQVCYG 378
Cdd:cd05939 185 FwdDCVkyncTIVQYIG-EICRYLLAQPPS-------EEEQKHN---VRLAVGNGLRPQI--WEQFVRRFGIPQIGEFYG 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 379 TTE-----------TSPVSFMStRDDP---PEQRIKSVGHIMDhleaAIVDKRNCIVP--RGVKGE---VIVRGYSVMRC 439
Cdd:cd05939 252 ATEgnsslvnidnhVGACGFNS-RILPsvyPIRLIKVDEDTGE----LIRDSDGLCIPcqPGEPGLlvgKIIQNDPLRRF 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 440 --YWNsEEQTKKEITQ------DRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGV 511
Cdd:cd05939 327 dgYVN-EGATNKKIARdvfkkgDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGV 405
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71994694 512 P-DERFGEVVCAWVrlhESAEGKTTEEDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIR 578
Cdd:cd05939 406 EvPGVEGRAGMAAI---VDPERKVDLDRFSAVLAKSLPPYARPQFIRLLP--EVDKTGTFKLQKTDLQ 468
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
226-589 |
2.12e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 67.50 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 226 PDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIiciPNPLYHCFG-CVMGVLAA-LTHLQTCVFP-A 302
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVI---AQTASQSFDiSVWQFLAApLFGARVEIVPnA 3944
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 303 PSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYAnynYDSIRSGFIAGAPCPITLCRRLVQDMHMTDMQVCYGTTET 382
Cdd:PRK05691 3945 IAHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQA---LDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAEC 4021
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 383 S------PVSFMSTRDD--PpeqriksVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEITQ- 453
Cdd:PRK05691 4022 SddvaffRVDLASTRGSylP-------IGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPh 4094
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 454 ------DRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVhIVGVPDERFGEVVCAWVRLH 527
Cdd:PRK05691 4095 pfgapgERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREA-AVAVQEGVNGKHLVGYLVPH 4173
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71994694 528 ESAEGKTTE-EDIKAWCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKfeiREMSKIELGLQQ 589
Cdd:PRK05691 4174 QTVLAQGALlERIKQRLRAELPDYMVPLHWLWLD--RLPLNANGKLDR---KALPALDIGQLQ 4231
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
216-579 |
3.01e-11 |
|
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: 65.92 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 216 HLSKIERETQ----PDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYS-EKKTIICIPnpLYHCFGCVMGVLA 290
Cdd:cd05937 72 HCLKLSGSRFvivdPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKnGDRTYTCMP--LYHGTAAFLGACN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 291 ALTHLQTCVFpAPSFDALAALQAIHE----------EKCTALYGTP-----------------------TMFIDMINHPE 337
Cdd:cd05937 150 CLMSGGTLAL-SRKFSASQFWKDVRDsgatiiqyvgELCRYLLSTPpspydrdhkvrvawgnglrpdiwERFRERFNVPE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 338 ----YA---------NYNydsiRSGFIAGApcpitlCRRlvqdmHMTDMQVCYGTTETsPVSfMSTRDDPPeqriksvgh 404
Cdd:cd05937 229 igefYAategvfaltNHN----VGDFGAGA------IGH-----HGLIRRWKFENQVV-LVK-MDPETDDP--------- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 405 imdhleaaIVDKRN--CI-VPRGVKGEVIVRGYSVMRC----YWNSEEQTKKEITQ------DRWYHTGDIAVMHDNGTI 471
Cdd:cd05937 283 --------IRDPKTgfCVrAPVGEPGEMLGRVPFKNREafqgYLHNEDATESKLVRdvfrkgDIYFRTGDLLRQDADGRW 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 472 SIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERF-GEVVCAWVRLHESAEGKTTE--EDIKAWCKGKIA 548
Cdd:cd05937 355 YFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHdGRAGCAAITLEESSAVPTEFtkSLLASLARKNLP 434
|
410 420 430
....*....|....*....|....*....|.
gi 71994694 549 HFKIPRYILFKKEYEFplTVTGKVKKFEIRE 579
Cdd:cd05937 435 SYAVPLFLRLTEEVAT--TDNHKQQKGVLRD 463
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
54-597 |
2.40e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 64.03 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 54 PDKEFLIFKREGIrkTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRY 133
Cdd:PRK05691 2202 PQAPALTFAGQTL--SYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHY 2279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 134 AIEKVGIRALITppgfkksnyYQSIKDILPEVtlkepgKSGItsrNFTCFqhlimfdEEDKiyPGAWKYTDvmkmgteed 213
Cdd:PRK05691 2280 MIEDSGIGLLLS---------DRALFEALGEL------PAGV---ARWCL-------EDDA--AALAAYSD--------- 2323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 214 rhhlSKIERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFV----GLRAGYSEkktiicipnplYHCF-----GC 284
Cdd:PRK05691 2324 ----APLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVierfGMRADDCE-----------LHFYsinfdAA 2388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 285 VMGVLAALTHLQTCVFPAP-SFDALAALQAIHEEKCTALYGTPTmfidminhpeyanynYDSIRSGFIA--GAPCPITLC 361
Cdd:PRK05691 2389 SERLLVPLLCGARVVLRAQgQWGAEEICQLIREQQVSILGFTPS---------------YGSQLAQWLAgqGEQLPVRMC 2453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 362 ------------RRLVQDMHMTDMQVCYGTTETSPVSFMSTRDDPPEQRIKSV--GHIMDHLEAAIVDKRNCIVPRGVKG 427
Cdd:PRK05691 2454 itggealtgehlQRIRQAFAPQLFFNAYGPTETVVMPLACLAPEQLEEGAASVpiGRVVGARVAYILDADLALVPQGATG 2533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 428 EVIVRGYSVMRCYWNSEEQTKKEITQD-------RWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKH 500
Cdd:PRK05691 2534 ELYVGGAGLAQGYHDRPGLTAERFVADpfaadggRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEH 2613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 501 QSVED--VHIVGVPDER--FGEVVCAwVRLHESAEGKTTEEDIKAWCKGKIAHFKIPRY-ILFKKeyeFPLTVTGKVKKF 575
Cdd:PRK05691 2614 PAVREavVLALDTPSGKqlAGYLVSA-VAGQDDEAQAALREALKAHLKQQLPDYMVPAHlILLDS---LPLTANGKLDRR 2689
|
570 580
....*....|....*....|..
gi 71994694 576 EIrEMSKIELGLQQVVSHFSEL 597
Cdd:PRK05691 2690 AL-PAPDPELNRQAYQAPRSEL 2710
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
223-494 |
3.47e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 62.82 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 223 ETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVgLRAGYSEKKTIICIPNPLYHCFGCVMGVLAALT-HLQTCVFP 301
Cdd:PRK07769 176 EANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQV-IDALEGQEGDRGVSWLPFFHDMGLITVLLPALLgHYITFMSP 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 302 ---------------------------APSFD-ALAALQAIHEEkctalyGTPTM----FIDMINHPEYANYNydSIRSG 349
Cdd:PRK07769 255 aafvrrpgrwirelarkpggtggtfsaAPNFAfEHAAARGLPKD------GEPPLdlsnVKGLLNGSEPVSPA--SMRKF 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 350 FIAGAPcpitlcrrlvQDMHMTDMQVCYGTTETSpvSFMST-------------RDDPPEQRI-------------KSVG 403
Cdd:PRK07769 327 NEAFAP----------YGLPPTAIKPSYGMAEAT--LFVSTtpmdeeptviyvdRDELNAGRFvevpadapnavaqVSAG 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 404 HIMDHLEAAIVDKRNCI-VPRGVKGEVIVRGYSVMRCYWNSEEQT--------KKEITQ---------DRWYHTGDIAVM 465
Cdd:PRK07769 395 KVGVSEWAVIVDPETASeLPDGQIGEIWLHGNNIGTGYWGKPEETaatfqnilKSRLSEshaegapddALWVRTGDYGVY 474
|
330 340
....*....|....*....|....*....
gi 71994694 466 HDnGTISIVGRSKDMIVRGGENIYPTEVE 494
Cdd:PRK07769 475 FD-GELYITGRVKDLVIIDGRNHYPQDLE 502
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
410-571 |
9.50e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 61.31 E-value: 9.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 410 EAAIVDKRNCIVPRGVKGE-VIVRGY-SVMRCYWNSEEQTKKEI--TQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGG 485
Cdd:PRK00174 434 QPAVVDEEGNPLEGGEGGNlVIKDPWpGMMRTIYGDHERFVKTYfsTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSG 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 486 ENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAEG-KTTEEDIKAWCK---GKIAhfkIPRYILFKKe 561
Cdd:PRK00174 514 HRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPsDELRKELRNWVRkeiGPIA---KPDVIQFAP- 589
|
170
....*....|
gi 71994694 562 yEFPLTVTGK 571
Cdd:PRK00174 590 -GLPKTRSGK 598
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
223-481 |
4.19e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 59.35 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 223 ETQPDDSLNIQYTSGTTGQPKGATLTH------------HNVLNN-----------------------AFFVGLRAGYSE 267
Cdd:PTZ00342 300 NEDPDFITSIVYTSGTSGKPKGVMLSNknlyntvvplckHSIFKKynpkthlsylpishiyerviaylSFMLGGTINIWS 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 268 KKtIICIPNPLYHCFGCVM-GVLAALTHLQTCVFPapSFDALAALQAIHEEKCTAL-----YGTPTMFIDMINH-----P 336
Cdd:PTZ00342 380 KD-INYFSKDIYNSKGNILaGVPKVFNRIYTNIMT--EINNLPPLKRFLVKKILSLrksnnNGGFSKFLEGITHisskiK 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 337 EYANYNYDSIRSGfiaGAPCPITLCRRLVQDMHMTDMQVcYGTTETS-PVSFMSTRDDPPEqrikSVG-HIMDHLEAAIV 414
Cdd:PTZ00342 457 DKVNPNLEVILNG---GGKLSPKIAEELSVLLNVNYYQG-YGLTETTgPIFVQHADDNNTE----SIGgPISPNTKYKVR 528
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71994694 415 D----KRNCIVPrgvKGEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMI 481
Cdd:PTZ00342 529 TwetyKATDTLP---KGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLV 596
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
69-585 |
4.61e-09 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 59.14 E-value: 4.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 69 TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITPPG 148
Cdd:PLN02654 122 TYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITCNA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 149 FKKSNYYQSIKDILpEVTLKEPGKSGITSRNFTCFQHLIMFDEED-KIYPG--AWkYTDVMKmgteedrHHLSKIERE-T 224
Cdd:PLN02654 202 VKRGPKTINLKDIV-DAALDESAKNGVSVGICLTYENQLAMKREDtKWQEGrdVW-WQDVVP-------NYPTKCEVEwV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 225 QPDDSLNIQYTSGTTGQPKGatlthhnVLNNAFFVGLRAGYSEKKTIICIPNPLYHCF---GCVMG--------VLAALT 293
Cdd:PLN02654 273 DAEDPLFLLYTSGSTGKPKG-------VLHTTGGYMVYTATTFKYAFDYKPTDVYWCTadcGWITGhsyvtygpMLNGAT 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 294 HLqtcVFP-APSF-DALAALQAIHEEKCTALYGTPTMFID-MINHPEY-ANYNYDSIRSGFIAGAPCPITLCR---RLVQ 366
Cdd:PLN02654 346 VL---VFEgAPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSlMRDGDEYvTRHSRKSLRVLGSVGEPINPSAWRwffNVVG 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 367 DMH--MTDMqvcYGTTETSpvSFMSTrddpP-----EQRIKSVGHIMDHLEAAIVDKrncivpRGVKGEVIVRGYSVMRC 439
Cdd:PLN02654 423 DSRcpISDT---WWQTETG--GFMIT----PlpgawPQKPGSATFPFFGVQPVIVDE------KGKEIEGECSGYLCVKK 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 440 YWNSEEQT------KKEITQDR----WYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIV 509
Cdd:PLN02654 488 SWPGAFRTlygdheRYETTYFKpfagYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVV 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 510 GVPDERFGEVVCAWVRLhesAEGKTTEEDIKA----WCKGKIAHFKIPRYILFKKeyEFPLTVTGKVKKFEIREMSKIEL 585
Cdd:PLN02654 568 GIEHEVKGQGIYAFVTL---VEGVPYSEELRKslilTVRNQIGAFAAPDKIHWAP--GLPKTRSGKIMRRILRKIASRQL 642
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
223-494 |
7.54e-09 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 58.60 E-value: 7.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 223 ETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIPNPLYHCFGCVMGVLAALT--HLqTCVF 300
Cdd:PRK12476 189 ELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLLDRNTHGVSWLPLYHDMGLSMIGFPAVYggHS-TLMS 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 301 P--------------------------APSFD-ALAALQAIHEEKCTalygtptmfID-----MINHPEYANYnyDSIRS 348
Cdd:PRK12476 268 PtafvrrpqrwikalsegsrtgrvvtaAPNFAyEWAAQRGLPAEGDD---------IDlsnvvLIIGSEPVSI--DAVTT 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 349 gFIAgAPCPITLCRRLVQDMH-MTDMQVCYGTT----ETSPVSF--------MSTRDDPPEQRIK---SVGHIMDHLEAA 412
Cdd:PRK12476 337 -FNK-AFAPYGLPRTAFKPSYgIAEATLFVATIapdaEPSVVYLdreqlgagRAVRVAADAPNAVahvSCGQVARSQWAV 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 413 IVD-KRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEI------------------TQDRWYHTGDIAVMHDnGTISI 473
Cdd:PRK12476 415 IVDpDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegshadgaaDDGTWLRTGDLGVYLD-GELYI 493
|
330 340
....*....|....*....|.
gi 71994694 474 VGRSKDMIVRGGENIYPTEVE 494
Cdd:PRK12476 494 TGRIADLIVIDGRNHYPQDIE 514
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
232-504 |
1.05e-08 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 57.63 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 232 IQYTSGTTGQPKGATLTHHNVLNNAFFVG--LRAGYSEKKTIICIpNPLYHCFGCVMGVLAALTHLQTCVFPAPSFDALA 309
Cdd:cd05913 83 IHASSGTTGKPTVVGYTKNDLDVWAELVArcLDAAGVTPGDRVQN-AYGYGLFTGGLGFHYGAERLGALVIPAGGGNTER 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 310 ALQAIHEEKCTALYGTPTMFIDMInhpEYANYN-YD----SIRSGFIAGAP-CPITlcRRLVQDMHMTDMQVCYGTTEts 383
Cdd:cd05913 162 QLQLIKDFGPTVLCCTPSYALYLA---EEAEEEgIDprelSLKVGIFGAEPwTEEM--RKRIERRLGIKAYDIYGLTE-- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 384 pVSFMSTRDDPPEQRiksVGHIM-DHLEAAIVD-KRNCIVPRGVKGEVIV-----RGYSVMRcywnseeqtkkeitqdrw 456
Cdd:cd05913 235 -IIGPGVAFECEEKD---GLHIWeDHFIPEIIDpETGEPVPPGEVGELVFttltkEAMPLIR------------------ 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 71994694 457 YHTGDIAVMHDnGTIS----------IVGRSKDMIVRGGENIYPTEVEQFLFKHQSVE 504
Cdd:cd05913 293 YRTRDITRLLP-GPCPcgrthrridrITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLG 349
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
69-325 |
5.06e-08 |
|
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: 55.82 E-value: 5.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 69 TYSQVATDAENLACGLL-HLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIR-ALITp 146
Cdd:cd05905 16 TWGKLLSRAEKIAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRvALTV- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 147 pgfkksnyyqsikdilpEVTLKEPGKSGITSRNFTCfqhlimfdeedKIYPGAW-KYTDVMKMGTEEDRHHLSKIERE-T 224
Cdd:cd05905 95 -----------------EACLKGLPKKLLKSKTAAE-----------IAKKKGWpKILDFVKIPKSKRSKLKKWGPHPpT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 225 QPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIPNP-----LYHcfGCVMGVLAALThlqTCV 299
Cdd:cd05905 147 RDGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFksglgLWH--GCLLSVYSGHH---TIL 221
|
250 260
....*....|....*....|....*...
gi 71994694 300 FPAPSF--DALAALQAIHEEKCTALYGT 325
Cdd:cd05905 222 IPPELMktNPLLWLQTLSQYKVRDAYVK 249
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
40-467 |
1.16e-07 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 54.88 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 40 ETVGDRLRSAVDQVPDKEFLIfKREG----IRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALA 115
Cdd:PRK08180 39 RRLTDRLVHWAQEAPDRVFLA-ERGAdggwRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 116 GMVLVNINPSYqS------EELRYAIEkvgiraLITP------PGFKksnYYQSIKDILPevtlkePGKSGITSRNFTCF 183
Cdd:PRK08180 118 GVPYAPVSPAY-SlvsqdfGKLRHVLE------LLTPglvfadDGAA---FARALAAVVP------ADVEVVAVRGAVPG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 184 QHLIMFDEEDKIYPGAwkytdvmkmgtEEDRHHLSkiereTQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAffVGLRA 263
Cdd:PRK08180 182 RAATPFAALLATPPTA-----------AVDAAHAA-----VGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQ--QMLAQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 264 GY---SEKKTIICIPNPLYHCFGCVMGVLAALTHLQTCVF----PAPS-FDAlaALQAIHEEKCTALYGTPTMFIDMINH 335
Cdd:PRK08180 244 TFpflAEEPPVLVDWLPWNHTFGGNHNLGIVLYNGGTLYIddgkPTPGgFDE--TLRNLREISPTVYFNVPKGWEMLVPA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 336 ----PEYANYNYDSIRSGFIAGAPCPITLCRRLvqdmHMTDMQVC---------YGTTETSPVSFMSTrddPPEQRIKSV 402
Cdd:PRK08180 322 lerdAALRRRFFSRLKLLFYAGAALSQDVWDRL----DRVAEATCgerirmmtgLGMTETAPSATFTT---GPLSRAGNI 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71994694 403 GHIMDHLEAaivdkrnCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHD 467
Cdd:PRK08180 395 GLPAPGCEV-------KLVPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVD 452
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
40-467 |
2.24e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 53.90 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 40 ETVGDRLRSAVDQVPDKEFLIfKREGIRK-----TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASAL 114
Cdd:PRK12582 49 RSIPHLLAKWAAEAPDRPWLA-QREPGHGqwrkvTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 115 AGMVLVNINPSYQS-----EELRYAIEKVGIRALITPPGFKKSNYYQSIKDILPEVTLKEPGKSGITSrnftcfqhlIMF 189
Cdd:PRK12582 128 AGVPAAPVSPAYSLmshdhAKLKHLFDLVKPRVVFAQSGAPFARALAALDLLDVTVVHVTGPGEGIAS---------IAF 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 190 DEedkiypgaWKYTDVmkmgTEEDRHHLSKIeretQPDDSLNIQYTSGTTGQPKGATLTHHNVLNN-AFFVGLRAGYSEK 268
Cdd:PRK12582 199 AD--------LAATPP----TAAVAAAIAAI----TPDTVAKYLFTSGSTGMPKAVINTQRMMCANiAMQEQLRPREPDP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 269 KtiicIPN-----PLYHCFGCVMGVLAALTHLQTCVF----PAPS-FDAlaALQAIHEEKCTALYGTPTMFIDMINHPEy 338
Cdd:PRK12582 263 P----PPVsldwmPWNHTMGGNANFNGLLWGGGTLYIddgkPLPGmFEE--TIRNLREISPTVYGNVPAGYAMLAEAME- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 339 anyNYDSIRSGFI--------AGAPCPITLCRRLvQDM------HMTDMQVCYGTTETSPVSfMSTRDDPpeQRIKSVGh 404
Cdd:PRK12582 336 ---KDDALRRSFFknlrlmayGGATLSDDLYERM-QALavrttgHRIPFYTGYGATETAPTT-TGTHWDT--ERVGLIG- 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71994694 405 imdhLEAAIVDKRncIVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHD 467
Cdd:PRK12582 408 ----LPLPGVELK--LAPVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVD 464
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
69-592 |
1.01e-04 |
|
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: 45.34 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 69 TYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEEL--RYA-IE-KVgiraLI 144
Cdd:cd05943 100 TWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVldRFGqIEpKV----LF 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 145 TPPGFKksnYYQSIKDILPEVTLKEPGKSGITsrnftcfQHLIMFDEEDKIYPGAWKYTDVMKMGTEEDRHHLSKIERET 224
Cdd:cd05943 176 AVDAYT---YNGKRHDVREKVAELVKGLPSLL-------AVVVVPYTVAAGQPDLSKIAKALTLEDFLATGAAGELEFEP 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 225 QP-DDSLNIQYTSGTTGQPK------GATLTHHnvLNNaffVGLRAGYSEKKTIICipnplYHCFGCVM--GVLAALTHL 295
Cdd:cd05943 246 LPfDHPLYILYSSGTTGLPKcivhgaGGTLLQH--LKE---HILHCDLRPGDRLFY-----YTTCGWMMwnWLVSGLAVG 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 296 QTCVF----P-APSFDALAALqaIHEEKCTaLYGTPTMFIDMIN----HPEyANYNYDSIRSGFIAGAPCPITlCRRLVQ 366
Cdd:cd05943 316 ATIVLydgsPfYPDTNALWDL--ADEEGIT-VFGTSAKYLDALEkaglKPA-ETHDLSSLRTILSTGSPLKPE-SFDYVY 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 367 DMHMTDMQVCYGTTETSPVS-FMSTRDDPPEQR--IKSVGHIMDhLEAAIVDKRNCIvprGVKGE-VIVRGYSVMRCY-W 441
Cdd:cd05943 391 DHIKPDVLLASISGGTDIIScFVGGNPLLPVYRgeIQCRGLGMA-VEAFDEEGKPVW---GEKGElVCTKPFPSMPVGfW 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 442 NSEEQTK-KEITQDR----WYHtGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERF 516
Cdd:cd05943 467 NDPDGSRyRAAYFAKypgvWAH-GDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDG 545
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71994694 517 GEVVCAWVRLhesAEGKTTEEDIKAWCKGKIAHFKIPRYI--LFKKEYEFPLTVTGKvkkfeiremsKIELGLQQVVS 592
Cdd:cd05943 546 DERVILFVKL---REGVELDDELRKRIRSTIRSALSPRHVpaKIIAVPDIPRTLSGK----------KVEVAVKKIIA 610
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
457-537 |
2.63e-04 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 43.78 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 457 YHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAEGKTTE 536
Cdd:PRK10524 475 YSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADRE 554
|
.
gi 71994694 537 E 537
Cdd:PRK10524 555 A 555
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
229-503 |
1.94e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 41.27 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 229 SLNIQYTSGTTGQPKGATLThhnvlNNAFFVGLRagYSEKKTIICIPNPLYHCFGCV------MGVLAALTHLQTCV--- 299
Cdd:PTZ00237 256 PLYILYTSGTTGNSKAVVRS-----NGPHLVGLK--YYWRSIIEKDIPTVVFSHSSIgwvsfhGFLYGSLSLGNTFVmfe 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 300 --FPAPSFDALAALQAIHEEKCTALYGTPTMFIDMI-NHPE----YANYNYDSIRSGFIAGAPCPITLCRRLVQDMHMTD 372
Cdd:PTZ00237 329 ggIIKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIkTDPEatiiRSKYDLSNLKEIWCGGEVIEESIPEYIENKLKIKS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994694 373 MQVcYGTTETSPVSFMSTrdDPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVR---GYSVMRCYWNSEEQTKK 449
Cdd:PTZ00237 409 SRG-YGQTEIGITYLYCY--GHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmPPSFATTFYKNDEKFKQ 485
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 71994694 450 EITQ-DRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSV 503
Cdd:PTZ00237 486 LFSKfPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLV 540
|
|
| |
