|
Name |
Accession |
Description |
Interval |
E-value |
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
96-673 |
0e+00 |
|
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: 899.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 96 QPYKWISYKQVSDRAEYLGSCLLHKGYKPSQDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADI 175
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 176 SVVICDTpqkatmlienvekdltpglktvilmdpfdddlmkrgekcGIEMLSLHDAENLGKENFKKPVPPNPEDLSVICF 255
Cdd:cd05927 81 SIVFCDA---------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 256 TSGTTGDPKGAMLTHQNIVSNMAAFLKFLEPIFQPTPEDVTISYLPLAHMFERLVQGVIFSCGGKIGFFQGDIRLLPDDM 335
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 336 KALKPTVFPTVPRLLNRVYDKVQN--EAKTPLKKFLLNLAIISKFNEVRNGIIRRNSLWDKLVFSKIQSSLGGKVRLMIT 413
Cdd:cd05927 202 KALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 414 GAAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCSITSPGDWTAGHVGTPVSCNFVKLEDVADMNYFS--VNNEGEICIK 491
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAkdPNPRGEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 492 GNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAQGEYIAPEKIENVYSRSRPILQVFVHGE 571
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 572 SLRSFLIGVVVPDPESLPSFAA-KIGVKGSFEELCQNQCVKKAILEDLQKVGKEGGLKSFEQVKSIFVHPEPFSIENGLL 650
Cdd:cd05927 442 SLKSFLVAIVVPDPDVLKEWAAsKGGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLL 521
|
570 580
....*....|....*....|...
gi 1958650325 651 TPTLKAKRVELAKFFQTQIKSLY 673
Cdd:cd05927 522 TPTFKLKRPQLKKYYKKQIDEMY 544
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
66-676 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 700.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 66 FSDAKTLYEVFQRGLAVSDNGPCLGYRKPNQ----PYKWISYKQVSDRAEYLGSCLLHKGYKPSQDqfIGIFAQNRPEWV 141
Cdd:PLN02736 40 HPEIGTLHDNFVYAVETFRDYKYLGTRIRVDgtvgEYKWMTYGEAGTARTAIGSGLVQHGIPKGAC--VGLYFINRPEWL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 142 ISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVICdTPQKATMLIENVEKdlTPGLKTVILMDPFDDDLMKRGEKC 221
Cdd:PLN02736 118 IVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCLSE--IPSVRLIVVVGGADEPLPSLPSGT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 222 GIEMLSLHDAENLGKENFKKPVPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAF---LKFLepifqptPEDVTIS 298
Cdd:PLN02736 195 GVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSslsTKFY-------PSDVHIS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 299 YLPLAHMFERLVQGVIFSCGGKIGFFQGDIRLLPDDMKALKPTVFPTVPRLLNRVYDKVQNEAKT--PLKKFLLNLAIIS 376
Cdd:PLN02736 268 YLPLAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKEsgGLKERLFNAAYNA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 377 KFNEVRNGiirRN--SLWDKLVFSKIQSSLGGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCSITSPGD 454
Cdd:PLN02736 348 KKQALENG---KNpsPMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGD 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 455 WTAGHVGTPVSCNFVKLEDVADMNYFSVNN---EGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLK 531
Cdd:PLN02736 425 NLSGHVGSPNPACEVKLVDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLK 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 532 IIDRKKNIFKLAQGEYIAPEKIENVYSRSRPILQVFVHGESLRSFLIGVVVPDPESLPSFAAKIGVK-GSFEELCQNQCV 610
Cdd:PLN02736 505 IIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRV 584
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958650325 611 KKAILEDLQKVGKEGGLKSFEQVKSIFVHPEPFSIENGLLTPTLKAKRVELAKFFQTQIKSLYESI 676
Cdd:PLN02736 585 RAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYAEL 650
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
67-674 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 543.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 67 SDAKTLYEVFQRGLAVSDNGPCLGYrKPNQPYKWISYKQVSDRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEWVISELA 146
Cdd:COG1022 8 PPADTLPDLLRRRAARFPDRVALRE-KEDGIWQSLTWAEFAERVRALAAGLLALGVKP--GDRVAILSDNRPEWVIADLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 147 CYTYSMVAVPLYDTLGAEAIIYVINRADISVVICDTPQKATMLIEnVEKDLtPGLKTVILMDPfdddlmkRGEKCGIEML 226
Cdd:COG1022 85 ILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLE-VRDEL-PSLRHIVVLDP-------RGLRDDPRLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 227 SLHDAENLGKENF------KKPVPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFlepiFQPTPEDVTISYL 300
Cdd:COG1022 156 SLDELLALGREVAdpaeleARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLER----LPLGPGDRTLSFL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 301 PLAHMFERLVQGVIFSCGGKIGFfQGDIRLLPDDMKALKPTVFPTVPRLLNRVYDKVQN--EAKTPLKKFLLNLAI---I 375
Cdd:COG1022 232 PLAHVFERTVSYYALAAGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAkaEEAGGLKRKLFRWALavgR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 376 SKFNEVRNGiiRRNSLW--------DKLVFSKIQSSLGGKVRLMITGAAPISTPVLTFFRAaMGCWVFEAYGQTECTAGC 447
Cdd:COG1022 311 RYARARLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPVI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 448 SITSPGDWTAGHVGTPVSCNFVKLEDvadmnyfsvnnEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPN 527
Cdd:COG1022 388 TVNRPGDNRIGTVGPPLPGVEVKIAE-----------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDED 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 528 GTLKIIDRKKNIFKLAQGEYIAPEKIENVYSRSRPILQVFVHGESlRSFLIGVVVPDPESLPSFAAKIGVK-GSFEELCQ 606
Cdd:COG1022 457 GFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGLPyTSYAELAQ 535
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958650325 607 NQCVKKAILEDLQKVGKegGLKSFEQVKSIFVHPEPFSIENGLLTPTLKAKRVELAKFFQTQIKSLYE 674
Cdd:COG1022 536 DPEVRALIQEEVDRANA--GLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYA 601
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
96-658 |
4.50e-166 |
|
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: 483.64 E-value: 4.50e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 96 QPYKWISYKQVSDRAEYLGSCLLHKGYKPSQDqfIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADI 175
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDR--VAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 176 SVVICDtpqkatmlienvekdltpglktvilmdpfdddlmkrgekcgiemlslhdaenlgkenfkkpvppNPEDLSVICF 255
Cdd:cd05907 79 KALFVE----------------------------------------------------------------DPDDLATIIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 256 TSGTTGDPKGAMLTHQNIVSNMAAFLKFLEPifqpTPEDVTISYLPLAHMFE-RLVQGVIFSCGGKIGFFQgDIRLLPDD 334
Cdd:cd05907 95 TSGTTGRPKGVMLSHRNILSNALALAERLPA----TEGDRHLSFLPLAHVFErRAGLYVPLLAGARIYFAS-SAETLLDD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 335 MKALKPTVFPTVPRLLNRVYDKVQNEAKTPLKKFLLNLAIiskfnevrngiirrnslwdklvfskiqsslGGKVRLMITG 414
Cdd:cd05907 170 LSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV------------------------------GGRLRFAASG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 415 AAPISTPVLTFFRAAmGCWVFEAYGQTECTAGCSITSPGDWTAGHVGTPVSCNFVKLEDvadmnyfsvnnEGEICIKGNN 494
Cdd:cd05907 220 GAPLPAELLHFFRAL-GIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPN 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 495 VFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAQGEYIAPEKIENVYSRSRPILQVFVHGESlR 574
Cdd:cd05907 288 VMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDG-R 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 575 SFLIGVVVPDPESLPSFAAKIGVKG-SFEELCQNQCVKKAILEDLQKVGKEggLKSFEQVKSIFVHPEPFSIENGLLTPT 653
Cdd:cd05907 367 PFLVALIVPDPEALEAWAEEHGIAYtDVAELAANPAVRAEIEAAVEAANAR--LSRYEQIKKFLLLPEPFTIENGELTPT 444
|
....*
gi 1958650325 654 LKAKR 658
Cdd:cd05907 445 LKLKR 449
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
67-678 |
5.89e-165 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 488.56 E-value: 5.89e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 67 SDAKTLYEVFQRGLAVSDNGPCLGYRKPNQ----PYKWISYKQVSDRAEYLGSCLLHKGYKPSQDqfIGIFAQNRPEWVI 142
Cdd:PLN02430 39 SDITTAWDIFSKSVEKYPDNKMLGWRRIVDgkvgPYMWKTYKEVYEEVLQIGSALRASGAEPGSR--VGIYGSNCPQWIV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 143 SELACYTYSMVAVPLYDTLGAEAIIYVINRADISVV-ICDTPQKatmliENVEKDLTPG--LKTVILMDPFDDDLMKRGE 219
Cdd:PLN02430 117 AMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVfVQDKKIK-----ELLEPDCKSAkrLKAIVSFTSVTEEESDKAS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 220 KCGIEMLSLHDAENLGKENFKKPVPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFLEPiFQP--TPEDVTI 297
Cdd:PLN02430 192 QIGVKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVDLFMEQ-FEDkmTHDDVYL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 298 SYLPLAHMFERLVQGVIFSCGGKIGFFQGDIRLLPDDMKALKPTVFPTVPRLLNRVYDKVQN--EAKTPLKKFLLNLAII 375
Cdd:PLN02430 271 SFLPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYK 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 376 SKFNEVRNGIIRRNS--LWDKLVFSKIQSSLGGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCSITSPG 453
Cdd:PLN02430 351 YKLAWMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPD 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 454 DWTA-GHVGTPVSCNFVKLEDVADMNY--FSVNNEGEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTL 530
Cdd:PLN02430 431 EMCMlGTVGAPAVYNELRLEEVPEMGYdpLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVL 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 531 KIIDRKKNIFKLAQGEYIAPEKIENVYSRSrPILQ-VFVHGESLRSFLIGVVVPDPESLPSFAAKIGVKGSFEELCQNQC 609
Cdd:PLN02430 510 KIIDRKKNLIKLSQGEYVALEYLENVYGQN-PIVEdIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPE 588
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958650325 610 VKKAILEDLQKVGKEGGLKSFEQVKSIFVHPEPFSIENGLLTPTLKAKRVELAKFFQTQIKSLYESIEE 678
Cdd:PLN02430 589 LKEHILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMYRKLAE 657
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
70-678 |
3.82e-163 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 484.14 E-value: 3.82e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 70 KTLYEVFQRGLAVSDNGPCLGYR-----KPNQpYKWISYKQVSDRAEYLGSCLLHKGYKpsQDQFIGIFAQNRPEWVISE 144
Cdd:PLN02614 45 DSCWDVFRMSVEKYPNNPMLGRReivdgKPGK-YVWQTYQEVYDIVIKLGNSLRSVGVK--DEAKCGIYGANSPEWIISM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 145 LACYTYSMVAVPLYDTLGAEAIIYVINRADISVVICDTpQKATMLIENVEKDlTPGLKTVILMDPFDDDLMKRGEKCGIE 224
Cdd:PLN02614 122 EACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEE-KKISELFKTCPNS-TEYMKTVVSFGGVSREQKEEAETFGLV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 225 MLSLHDAENLGK-ENFKKPVPpNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFLEPIFQP-TPEDVTISYLPL 302
Cdd:PLN02614 200 IYAWDEFLKLGEgKQYDLPIK-KKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANAAlTVKDVYLSYLPL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 303 AHMFERLVQGVIFSCGGKIGFFQGDIRLLPDDMKALKPTVFPTVPRLLNRVYDKVQNEAKTP--LKKFLLNLAIISKFNE 380
Cdd:PLN02614 279 AHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGgfLKKFVFDSAFSYKFGN 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 381 VRNGI--IRRNSLWDKLVFSKIQSSLGGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCSITSPGDW-TA 457
Cdd:PLN02614 359 MKKGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELdML 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 458 GHVGTPVSCNFVKLEDVADMNYFSVNN--EGEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIIDR 535
Cdd:PLN02614 439 GTVGPPVPNVDIRLESVPEMEYDALAStpRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDR 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 536 KKNIFKLAQGEYIAPEKIENVYSRSRPILQVFVHGESLRSFLIGVVVPDPESLPSFAAKIGVKGSFEELCQNQCVKKAIL 615
Cdd:PLN02614 518 KKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEFIL 597
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958650325 616 EDLQKVGKEGGLKSFEQVKSIFVHPEPFSIENGLLTPTLKAKRVELAKFFQTQIKSLYESIEE 678
Cdd:PLN02614 598 GELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYKTTNE 660
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
97-661 |
1.54e-159 |
|
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: 469.00 E-value: 1.54e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 97 PYKWISYKQVSDRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADIS 176
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLVELGLKP--GDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 177 VVICDtpqkatmlienvekdltpglktvilmdpfdddlmkrgekcgiemlslhdaenlgkenfkkpvpPNPEDLSVICFT 256
Cdd:cd17639 80 AIFTD---------------------------------------------------------------GKPDDLACIMYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 257 SGTTGDPKGAMLTHQNIVSNMAAFLKFLePIFqPTPEDVTISYLPLAHMFERLVQGVIFSCGGKIGFfqGDIRLLPD--- 333
Cdd:cd17639 97 SGSTGNPKGVMLTHGNLVAGIAGLGDRV-PEL-LGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDksk 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 334 -----DMKALKPTVFPTVPRLLNRVYDKVQNE--AKTPLKKFLLNLAIISKFNEVRNGIirRNSLWDKLVFSKIQSSLGG 406
Cdd:cd17639 173 rgckgDLTEFKPTLMVGVPAIWDTIRKGVLAKlnPMGGLKRTLFWTAYQSKLKALKEGP--GTPLLDELVFKKVRAALGG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 407 KVRLMITGAAPISTPVLTFFrAAMGCWVFEAYGQTECTAGCSITSPGDWTAGHVGTPVSCNFVKLEDVADMNYFSVNNE- 485
Cdd:cd17639 251 RLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDKPPp 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 486 -GEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAQGEYIAPEKIENVYSRSRPIL 564
Cdd:cd17639 330 rGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVN 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 565 QVFVHGESLRSFLIGVVVPDPESLPSFAAKIGVKGS-FEELCQNQCVKKAILEDLQKVGKEGGLKSFEQVKSIFVHPEPF 643
Cdd:cd17639 410 NICVYADPDKSYPVAIVVPNEKHLTKLAEKHGVINSeWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEW 489
|
570
....*....|....*...
gi 1958650325 644 SIENGLLTPTLKAKRVEL 661
Cdd:cd17639 490 TPENGLVTAAQKLKRKEI 507
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
97-673 |
1.14e-156 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 467.40 E-value: 1.14e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 97 PYKWISYKQVSDRAEYLGSCLLHKGYKPSQDqfIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADIS 176
Cdd:PLN02861 74 PYVWLTYKEVYDAAIRIGSAIRSRGVNPGDR--CGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 177 VVICDTPQKATMLieNVEKDLTPGLKTVILMDPFDDDLMKRGEKCGIEMLSLHDAENLGKENFKKPvPPNPEDLSVICFT 256
Cdd:PLN02861 152 IAFVQESKISSIL--SCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLDCELP-PKQKTDICTIMYT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 257 SGTTGDPKGAMLTHQNIVSNMAAFLKFLEPIFQ-PTPEDVTISYLPLAHMFERLVQGVIFSCGGKIGFFQGDIRLLPDDM 335
Cdd:PLN02861 229 SGTTGEPKGVILTNRAIIAEVLSTDHLLKVTDRvATEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQGDIRYLMEDV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 336 KALKPTVFPTVPRLLNRVY----DKVQneAKTPLKKFLLNLAIISKFNEVRNGIIRRNS--LWDKLVFSKIQSSLGGKVR 409
Cdd:PLN02861 309 QALKPTIFCGVPRVYDRIYtgimQKIS--SGGMLRKKLFDFAYNYKLGNLRKGLKQEEAspRLDRLVFDKIKEGLGGRVR 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 410 LMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCsITSPGDW--TAGHVGTPVSCNFVKLEDVADMNYFSVNN--E 485
Cdd:PLN02861 387 LLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGC-FTSIANVfsMVGTVGVPMTTIEARLESVPEMGYDALSDvpR 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 486 GEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAQGEYIAPEKIENVYSRSRPILQ 565
Cdd:PLN02861 466 GEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIAS 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 566 VFVHGESLRSFLIGVVVPDPESLPSFAAKIGVKGSFEELCQNQCVKKAILEDLQKVGKEGGLKSFEQVKSIFVHPEPFSI 645
Cdd:PLN02861 545 IWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDI 624
|
570 580
....*....|....*....|....*...
gi 1958650325 646 ENGLLTPTLKAKRVELAKFFQTQIKSLY 673
Cdd:PLN02861 625 ERDLITPTFKLKRPQLLKYYKDCIDQLY 652
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
97-674 |
5.81e-136 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 415.28 E-value: 5.81e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 97 PYKWISYKQVSDRAEYLGSCLLHKGYKpsQDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADIS 176
Cdd:PLN02387 103 EYEWITYGQVFERVCNFASGLVALGHN--KEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVT 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 177 VVICDTPQKATMLienvekDLTPGLKT---VILMDPFDDDLMKRGEK-CGIEMLSLHDAENLGKENFKKPVPPNPEDLSV 252
Cdd:PLN02387 181 TVICDSKQLKKLI------DISSQLETvkrVIYMDDEGVDSDSSLSGsSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAV 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 253 ICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFLEPIfqpTPEDVTISYLPLAHMFERLVQGVIFSCGGKIGFfqGDIRLLP 332
Cdd:PLN02387 255 IMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKL---GKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLT 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 333 D-----------DMKALKPTVFPTVPRLLNRVYDKVQN--EAKTPLKKFLLNLAIISKFNEVRN------GIIRrnSLWD 393
Cdd:PLN02387 330 DtsnkikkgtkgDASALKPTLMTAVPAILDRVRDGVRKkvDAKGGLAKKLFDIAYKRRLAAIEGswfgawGLEK--LLWD 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 394 KLVFSKIQSSLGGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCSITSPGDWTAGHVGTPVSCNFVKLED 473
Cdd:PLN02387 408 ALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVS 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 474 VADMNYFSVNN---EGEICIKGNNVFKGYLKDPEKTQEV--LDKDG--WLHTGDIGRWLPNGTLKIIDRKKNIFKLAQGE 546
Cdd:PLN02387 488 WEEGGYLISDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGE 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 547 YIAPEKIENVYSRSRPILQVFVHGESLRSFLIGVVVPDPESLPSFAAKIGVK-GSFEELCQNQCVKKAILEDLQKVGKEG 625
Cdd:PLN02387 568 YVSLGKVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAA 647
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1958650325 626 GLKSFEQVKSIFVHPEPFSIENGLLTPTLKAKRVELAKFFQTQIKSLYE 674
Cdd:PLN02387 648 RLEKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
97-543 |
8.85e-128 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 384.36 E-value: 8.85e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 97 PYKWISYKQVSDRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADIS 176
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRALGVGK--GDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 177 VVICDTPQKATMLIENVEKDLTPGLKTVILMDPFDDDLMkrgekcgiemlsLHDAENLGKENFKKPVPPNPEDLSVICFT 256
Cdd:pfam00501 96 VLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEP------------LPEEAKPADVPPPPPPPPDPDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 257 SGTTGDPKGAMLTHQNIVSNMAAFLKFLEPIFQPTPEDVTISYLPLAHMFER-LVQGVIFSCGGKIGFFQGDIRLLP--- 332
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDPaal 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 333 -DDMKALKPTVFPTVPRLLNRvydkvqneaktplkkfLLNLAIISKFnevrngiirrnslwdklvfskIQSSLggkvRLM 411
Cdd:pfam00501 244 lELIERYKVTVLYGVPTLLNM----------------LLEAGAPKRA---------------------LLSSL----RLV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 412 ITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCSITSPGDW---TAGHVGTPVSCNFVKLEDVADMNYFSVNNEGEI 488
Cdd:pfam00501 283 LSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGEL 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1958650325 489 CIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLA 543
Cdd:pfam00501 363 CVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
99-674 |
2.45e-102 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 327.70 E-value: 2.45e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 99 KWISYKQVSDRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVV 178
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLAELGLTK--GSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 179 ICDTpQKATMLIENVEKDLTPGLkTVILMDPFDDDLmkrgEKCGIEMLSLHDAENLGKE---NFKKPVPPNPEDLSVICF 255
Cdd:PTZ00216 198 VCNG-KNVPNLLRLMKSGGMPNT-TIIYLDSLPASV----DTEGCRLVAWTDVVAKGHSagsHHPLNIPENNDDLALIMY 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 256 TSGTTGDPKGAMLTHQNIVSNMAAF-LKFLEPIFQPTPEDVTISYLPLAHMFERLVQGVIFSCGGKIGFfqGDIRLLPD- 333
Cdd:PTZ00216 272 TSGTTGDPKGVMHTHGSLTAGILALeDRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRTLTDt 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 334 ------DMKALKPTVFPTVPRllnrVYDKVQN--EAKTP----LKKFLLNLAIISKFNEVRNGiiRRNSLWDKLVFSKIQ 401
Cdd:PTZ00216 350 farphgDLTEFRPVFLIGVPR----IFDTIKKavEAKLPpvgsLKRRVFDHAYQSRLRALKEG--KDTPYWNEKVFSAPR 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 402 SSLGGKVRLMITGAAPISTPVLTFFRAAMGCwVFEAYGQTEcTAGC-SITSPGDWTAGHVGTPVSCNFVKLEDVADmnYF 480
Cdd:PTZ00216 424 AVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTE-TVCCgGIQRTGDLEPNAVGQLLKGVEMKLLDTEE--YK 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 481 SVNN---EGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAQGEYIAPEKIENVY 557
Cdd:PTZ00216 500 HTDTpepRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEALY 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 558 SrSRPILQ-----VFVHgeSLRSFLIGVVVPDPESLPSFAAKIGVKGSFEELCQNQCVKKAILEDLQKVGKEGGLKSFEQ 632
Cdd:PTZ00216 580 G-QNELVVpngvcVLVH--PARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFEI 656
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1958650325 633 VKSIFVHPEPFSIENGLLTPTLKAKRVELAKFFQTQIKSLYE 674
Cdd:PTZ00216 657 VRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELFA 698
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
96-658 |
1.02e-90 |
|
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: 290.03 E-value: 1.02e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 96 QPYKWISYKQVSDRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADI 175
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKA--GEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 176 SVVIcdtpqkatmlIENvekdltpglktvilmdpfdddlmkrgekcgiemlslhdaenlgkenfkkpvppNPEDLSVICF 255
Cdd:cd17640 79 VALV----------VEN-----------------------------------------------------DSDDLATIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 256 TSGTTGDPKGAMLTHQNIVSNMAAFLKFlepiFQPTPEDVTISYLPLAHMFERLVQGVIFSCGGKIGFfqGDIRLLPDDM 335
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLLHQIRSLSDI----VPPQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDDL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 336 KALKPTVFPTVPRLLNRVYDKVQNE--AKTPLKKFLLNLAIiskfnevrngiirrnslwdklvfskiqssLGGKVRLMIT 413
Cdd:cd17640 170 KRVKPHYIVSVPRLWESLYSGIQKQvsKSSPIKQFLFLFFL-----------------------------SGGIFKFGIS 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 414 GAAPISTPVLTFFRAAmGCWVFEAYGQTECTAGCSITSPGDWTAGHVGTPVSCNFVKLEDVADMNYFSVNNEGEICIKGN 493
Cdd:cd17640 221 GGGALPPHVDTFFEAI-GIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGP 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 494 NVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAQGEYIAPEKIENVYSRSRPILQVFVHGESL 573
Cdd:cd17640 300 QVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQ 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 574 RsFLIGVVVPDPESLPSFAAKIGVKGSFEE---LCQNQCVKKAILEDLQKVGKEGGLKSFEQVKSIFVHPEPFsIENGLL 650
Cdd:cd17640 380 K-RLGALIVPNFEELEKWAKESGVKLANDRsqlLASKKVLKLYKNEIKDEISNRPGFKSFEQIAPFALLEEPF-IENGEM 457
|
....*...
gi 1958650325 651 TPTLKAKR 658
Cdd:cd17640 458 TQTMKIKR 465
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
102-665 |
8.56e-84 |
|
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: 273.19 E-value: 8.56e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 102 SYKQVSDRAEYLGSCLLHKGYKPSQDqfIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIC- 180
Cdd:cd05932 8 TWGEVADKARRLAAALRALGLEPGSK--IALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 ---DTPQKATMLIENVEKDLTPGLKTVILMDPFdDDLMKRGEKCGIEMlslhdaenlgkenfkkpvPPNPEDLSVICFTS 257
Cdd:cd05932 86 kldDWKAMAPGVPEGLISISLPPPSAANCQYQW-DDLIAQHPPLEERP------------------TRFPEQLATLIYTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 258 GTTGDPKGAMLTHqnivSNMAAFLKFLEPIFQPTPEDVTISYLPLAHMFER-LVQGVIFScGGKIGFFQGDIRLLPDDMK 336
Cdd:cd05932 147 GTTGQPKGVMLTF----GSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERvFVEGGSLY-GGVLVAFAESLDTFVEDVQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 337 ALKPTVFPTVPRLL----NRVYDKVqneaktPLKKF--LLNLAIISKfnevrngIIRRnslwdklvfsKIQSSLG-GKVR 409
Cdd:cd05932 222 RARPTLFFSVPRLWtkfqQGVQDKI------PQQKLnlLLKIPVVNS-------LVKR----------KVLKGLGlDQCR 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 410 LMITGAAPISTPVLTFFRaAMGCWVFEAYGQTECTAGCSITSPGDWTAGHVGTPVSCNFVKLEDvadmnyfsvnnEGEIC 489
Cdd:cd05932 279 LAGCGSAPVPPALLEWYR-SLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEIL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 490 IKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAQGEYIAPEKIENVYSRSRPILQVFVH 569
Cdd:cd05932 347 VRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVI 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 570 GESLrSFLIGVVVPDPESLPSfaAKIGVKGSFEELCQnqcvkkailEDLQKVGKEggLKSFEQVKSIFVHPEPFSIENGL 649
Cdd:cd05932 427 GSGL-PAPLALVVLSEEARLR--ADAFARAELEASLR---------AHLARVNST--LDSHEQLAGIVVVKDPWSIDNGI 492
|
570
....*....|....*.
gi 1958650325 650 LTPTLKAKRVELAKFF 665
Cdd:cd05932 493 LTPTLKIKRNVLEKAY 508
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
93-673 |
1.78e-70 |
|
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: 240.34 E-value: 1.78e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 93 KPNQPYKWISYKQVSDRAEYLGSCLLHKGYkpsqDQF--IGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVI 170
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLKLGL----ERFhgVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 171 NRADISVVICDTpQKATMLIENVEKDLtPGLKTVI-LMDPFD---------DDLMKRGEkcGIEMLSLHDAENLGKenfk 240
Cdd:cd05933 77 ETSEANILVVEN-QKQLQKILQIQDKL-PHLKAIIqYKEPLKekepnlyswDEFMELGR--SIPDEQLDAIISSQK---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 241 kpvppnPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFLEPIFQPTPEDVTISYLPLAHMFERLVQgvIFSC--- 317
Cdd:cd05933 149 ------PNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILD--IWLPikv 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 318 GGKIGFFQGDIR--LLPDDMKALKPTVFPTVPRLLNRVYDKVQ-NEAK-TPLKKFLLNLA--IISKFNEV----RNGIIR 387
Cdd:cd05933 221 GGQVYFAQPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMKaVGAKsGTLKRKIASWAkgVGLETNLKlmggESPSPL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 388 RNSLWDKLVFSKIQSSLG-GKVRLMITGAAPISTPVLTFFrAAMGCWVFEAYGQTECTAGCSITSPGDWTAGHVGTPVSC 466
Cdd:cd05933 301 FYRLAKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 467 NFVKLEDVADmnyfsvNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAQGE 546
Cdd:cd05933 380 CKTKIHNPDA------DGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGE 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 547 YIAPEKIENVYSRSRPILQ-VFVHGESlRSFLIGVVV----PDPES------LPS----FAAKIGVKGS-FEELCQNQC- 609
Cdd:cd05933 454 NVPPVPIEDAVKKELPIISnAMLIGDK-RKFLSMLLTlkceVNPETgepldeLTEeaieFCRKLGSQATrVSEIAGGKDp 532
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958650325 610 -VKKAILEDLQKVGKEgGLKSFEQVKSIFVHPEPFSIENGLLTPTLKAKRVELAKFFQTQIKSLY 673
Cdd:cd05933 533 kVYEAIEEGIKRVNKK-AISNAQKIQKWVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
101-658 |
4.56e-70 |
|
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: 238.48 E-value: 4.56e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPSQdqFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIC 180
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGD--VVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 DTPQKATMLIENveKDLTPGLKTVILMDP-----FDDDLMKRGEKCgIEMLSLHDAENLGKenFKKPVPP-NPEDLSVIC 254
Cdd:cd17641 90 EDEEQVDKLLEI--ADRIPSVRYVIYCDPrgmrkYDDPRLISFEDV-VALGRALDRRDPGL--YEREVAAgKGEDVAVLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 255 FTSGTTGDPKGAMLTHQNIVSNMAAFLKFlEPIfqpTPEDVTISYLPLAHMFER---LVQGVIfsCGGKIGFFQGDIRLL 331
Cdd:cd17641 165 TTSGTTGKPKLAMLSHGNFLGHCAAYLAA-DPL---GPGDEYVSVLPLPWIGEQmysVGQALV--CGFIVNFPEEPETMM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 332 PDdMKALKPTVFPTVPRLLNRVYDKVQN--EAKTPLKKFLLNLAIiSKFNEVRNGIIR--RNSLW--------DKLVFSK 399
Cdd:cd17641 239 ED-LREIGPTFVLLPPRVWEGIAADVRArmMDATPFKRFMFELGM-KLGLRALDRGKRgrPVSLWlrlaswlaDALLFRP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 400 IQSSLG-GKVRLMITGAAPISTPVLTFFRAaMGCWVFEAYGQTECTAGCSITSPGDWTAGHVGTPVSCNFVKledvadmn 478
Cdd:cd17641 317 LRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVR-------- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 479 yfsVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAQGEYIAPEKIENVYS 558
Cdd:cd17641 388 ---IDEVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 559 RSRPILQVFVHGESlRSFLIGVVVPDPESLPSFAAKIGVK-GSFEELCQNQCVKKAILEDLQKVGKEggLKSFEQVKSIF 637
Cdd:cd17641 465 FSPYIAEAVVLGAG-RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKVNAS--LPEAQRIRRFL 541
|
570 580
....*....|....*....|.
gi 1958650325 638 VHPEPFSIENGLLTPTLKAKR 658
Cdd:cd17641 542 LLYKELDADDGELTRTRKVRR 562
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
101-658 |
1.57e-68 |
|
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: 231.56 E-value: 1.57e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPSQDqfIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIC 180
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDR--VALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 DtpqkatmlienvekdltpglktvilmdpfdddlmkrgekcgiemlslhdaenlgkenfkkpvppNPEDLSVICFTSGTT 260
Cdd:cd05914 86 S----------------------------------------------------------------DEDDVALINYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 261 GDPKGAMLTHQNIVSNMAaFLKFLEPIfqpTPEDVTISYLPLAHMFERLVQGVI-FSCGGKIgFFQGDI---RLLPDDMK 336
Cdd:cd05914 102 GNSKGVMLTYRNIVSNVD-GVKEVVLL---GKGDKILSILPLHHIYPLTFTLLLpLLNGAHV-VFLDKIpsaKIIALAFA 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 337 ALKPTVFPTVPRLLNRVYDKVQNEAKTpLKKFLLNLAIISKFNEVRngiirrnslwdKLVFSKIQSSLGGKVRLMITGAA 416
Cdd:cd05914 177 QVTPTLGVPVPLVIEKIFKMDIIPKLT-LKKFKFKLAKKINNRKIR-----------KLAFKKVHEAFGGNIKEFVIGGA 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 417 PISTPVLTFFRAaMGCWVFEAYGQTECTAGCSITSPGDWTAGHVGTPVSCNFVKLEDVAdmnyfSVNNEGEICIKGNNVF 496
Cdd:cd05914 245 KINPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPD-----PATGEGEIIVRGPNVM 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 497 KGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAQGEYIAPEKIENVYSRSRPILQ--VFV-HGEsl 573
Cdd:cd05914 319 KGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLEslVVVqEKK-- 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 574 rsfLIGVVVPDPESLPSFAAKIgvkgsfeelcqnQCVKKAILED-LQKVGKEggLKSFEQVKSIFVHPEPFSienglLTP 652
Cdd:cd05914 397 ---LVALAYIDPDFLDVKALKQ------------RNIIDAIKWEvRDKVNQK--VPNYKKISKVKIVKEEFE-----KTP 454
|
....*.
gi 1958650325 653 TLKAKR 658
Cdd:cd05914 455 KGKIKR 460
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
101-593 |
2.51e-68 |
|
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: 230.47 E-value: 2.51e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIC 180
Cdd:COG0318 25 LTYAELDARARRLAAALRALGVGP--GDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 dtpqkatmlienvekdltpglktvilmdpfdddlmkrgekcgiemlslhdaenlgkenfkkpvppnpedlSVICFTSGTT 260
Cdd:COG0318 103 ----------------------------------------------------------------------ALILYTSGTT 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 261 GDPKGAMLTHQNIVSNMAAFLKflepIFQPTPEDVTISYLPLAHMFErLVQGVIFS--CGGKI----GFfqgDIRLLPDD 334
Cdd:COG0318 113 GRPKGVMLTHRNLLANAAAIAA----ALGLTPGDVVLVALPLFHVFG-LTVGLLAPllAGATLvllpRF---DPERVLEL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 335 MKALKPTVFPTVPRLLNRvydkvqneaktplkkfLLNLAiiskfnevrngiirrnsLWDKLVFSkiqsSLggkvRLMITG 414
Cdd:COG0318 185 IERERVTVLFGVPTMLAR----------------LLRHP-----------------EFARYDLS----SL----RLVVSG 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 415 AAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCSITSPGDWTA--GHVGTPVSCNFVKLEDvADMNYFSVNNEGEICIKG 492
Cdd:COG0318 224 GAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGRPLPGVEVRIVD-EDGRELPPGEVGEIVVRG 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 493 NNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENVYSRSRPILQVFV---- 568
Cdd:COG0318 303 PNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEVLAAHPGVAEAAVvgvp 380
|
490 500
....*....|....*....|....*...
gi 1958650325 569 ---HGESlrsfLIGVVVPDPESLPSFAA 593
Cdd:COG0318 381 dekWGER----VVAFVVLRPGAELDAEE 404
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
242-651 |
1.12e-64 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 224.26 E-value: 1.12e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 242 PVPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSnmaAFLKFlEPIFQPTPED-VTISYLPLAHMFERlvqGVIFS--CG 318
Cdd:cd17632 217 RPEPDDDPLALLIYTSGSTGTPKGAMYTERLVAT---FWLKV-SSIQDIRPPAsITLNFMPMSHIAGR---ISLYGtlAR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 319 GKIGFFQG--DIRLLPDDMKALKPTVFPTVPRLLNRVYDKVQNEaktplkkflLNLAIISKFNEVRNGIIRRNSLWDKLv 396
Cdd:cd17632 290 GGTAYFAAasDMSTLFDDLALVRPTELFLVPRVCDMLFQRYQAE---------LDRRSVAGADAETLAERVKAELRERV- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 397 fskiqssLGGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTEctAGCSITSpgdwtaGHVGTPVSCNFvKLEDVAD 476
Cdd:cd17632 360 -------LGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE--AGAVILD------GVIVRPPVLDY-KLVDVPE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 477 MNYFSVNN---EGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAQGEYIAPEKI 553
Cdd:cd17632 424 LGYFRTDRphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARL 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 554 ENVYSRSRPILQVFVHGESLRSFLIGVVVPDPESLpsfaakigVKGSFEELcqnqcvKKAILEDLQKVGKEGGLKSFEQV 633
Cdd:cd17632 504 EAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDAL--------AGEDTARL------RAALAESLQRIAREAGLQSYEIP 569
|
410
....*....|....*...
gi 1958650325 634 KSIFVHPEPFSIENGLLT 651
Cdd:cd17632 570 RDFLIETEPFTIANGLLS 587
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
249-593 |
1.09e-63 |
|
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: 214.46 E-value: 1.09e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 249 DLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKflepIFQPTPEDVTISYLPLAHMFerlVQGVIFSC---GGKIGFFQ 325
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAA----SGGLTEGDVFLSTLPLFHIG---GLFGLLGAllaGGTVVLLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 326 G-DIRLLPDDMKALKPTVFPTVPRLLNRVyDKVQNEAKTPLkkfllnlaiiskfnevrngiirrnslwdklvfskiqSSL 404
Cdd:cd04433 74 KfDPEAALELIEREKVTILLGVPTLLARL-LKAPESAGYDL------------------------------------SSL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 405 ggkvRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCSITSPGDWT--AGHVGTPVSCNFVKLEDVADmNYFSV 482
Cdd:cd04433 117 ----RALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDPDG-GELPP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 483 NNEGEICIKGNNVFKGYLKDPEKTQEVlDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKlAQGEYIAPEKIENVYSRSRP 562
Cdd:cd04433 192 GEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPG 269
|
330 340 350
....*....|....*....|....*....|....
gi 1958650325 563 ILQVFVHG---ESLRSFLIGVVVPDPESLPSFAA 593
Cdd:cd04433 270 VAEAAVVGvpdPEWGERVVAVVVLRPGADLDAEE 303
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
72-588 |
2.31e-60 |
|
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: 209.73 E-value: 2.31e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 72 LYEVFQRGLAvsdngpclgyRKPNQPY-----KWISYKQVSDRAEYLGSCLLHKGYKPSqDQfIGIFAQNRPEWVISELA 146
Cdd:cd05936 1 LADLLEEAAR----------RFPDKTAlifmgRKLTYRELDALAEAFAAGLQNLGVQPG-DR-VALMLPNCPQFPIAYFG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 147 CYTYSMVAVPLYDTLGAEAIIYVINRADISVVICDTPqkatmLIENVEKDLTPGLktvilmdpfdddlmkrgekcgieml 226
Cdd:cd05936 69 ALKAGAVVVPLNPLYTPRELEHILNDSGAKALIVAVS-----FTDLLAAGAPLGE------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 227 slhdaenlgkenfkkPVPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFLEPIFqpTPEDVTISYLPLAHMF 306
Cdd:cd05936 119 ---------------RVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLL--EGDDVVLAALPLFHVF 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 307 ERLVQGVIFSC-GGKIGFFQG--DIRLLpDDMKALKPTVFPTVPRLLNRvydkvqneaktplkkfLLNLAIISKFNevrn 383
Cdd:cd05936 182 GLTVALLLPLAlGATIVLIPRfrPIGVL-KEIRKHRVTIFPGVPTMYIA----------------LLNAPEFKKRD---- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 384 giirrnslwdklvFSKIqsslggkvRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTEC---TAGCSITspGDWTAGHV 460
Cdd:cd05936 241 -------------FSSL--------RLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETspvVAVNPLD--GPRKPGSI 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 461 GTPVSCNFVKLEDvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIIDRKKNIF 540
Cdd:cd05936 298 GIPLPGTEVKIVD-DDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAF-VDGWLRTGDIGYMDEDGYFFIVDRKKDMI 375
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1958650325 541 kLAQGEYIAPEKIENVYSRSRPILQVFV-------HGESLRSFligVVVPDPESL 588
Cdd:cd05936 376 -IVGGFNVYPREVEEVLYEHPAVAEAAVvgvpdpySGEAVKAF---VVLKEGASL 426
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
101-586 |
8.66e-56 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 198.20 E-value: 8.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPSqDQfIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIC 180
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGKG-DR-VAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 dtpQKATMLIENVEKDLTPGLKTVILMDPFDDDLMKRGEKCGIEMLSLHDAEnlgkenfKKPVPPNPEDLSVICFTSGTT 260
Cdd:PRK07656 109 ---LGLFLGVDYSATTRLPALEHVVICETEEDDPHTEKMKTFTDFLAAGDPA-------ERAPEVDPDDVADILFTSGTT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 261 GDPKGAMLTHQNIVSNMAAFLKFLepifQPTPEDVTISYLPLAHMFErLVQGVI--FSCGGKIgffqgdIRLL---PDDM 335
Cdd:PRK07656 179 GRPKGAMLTHRQLLSNAADWAEYL----GLTEGDRYLAANPFFHVFG-YKAGVNapLMRGATI------LPLPvfdPDEV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 336 KAL----KPTVFPTVPRLLNrvydkvqneaktplkkFLLNLAIISKFNevrngiirrnslwdklvfskiQSSLggkvRLM 411
Cdd:PRK07656 248 FRLieteRITVLPGPPTMYN----------------SLLQHPDRSAED---------------------LSSL----RLA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 412 ITGAAPISTPVLTFFRAAMGCW-VFEAYGQTECTAGCSITSPGD---WTAGHVGTPvsCNFVKLEDVADMNYFSVNNE-G 486
Cdd:PRK07656 287 VTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTA--IAGVENKIVNELGEEVPVGEvG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 487 EICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENVYSRSRPILQV 566
Cdd:PRK07656 365 ELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IVGGFNVYPAEVEEVLYEHPAVAEA 443
|
490 500
....*....|....*....|
gi 1958650325 567 FVhgeslrsflIGvvVPDPE 586
Cdd:PRK07656 444 AV---------IG--VPDER 452
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
101-556 |
1.05e-55 |
|
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: 197.44 E-value: 1.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKpsQDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIC 180
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLK--KGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 DTPQKATMLieNVEKDLTPGLKtVILMDPfdddlmkRGEKCGIEMLSLHDAENLGKENFKKPVPPNPEDLSVICFTSGTT 260
Cdd:cd05911 89 DPDGLEKVK--EAAKELGPKDK-IIVLDD-------KPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 261 GDPKGAMLTHQNIVSNMAAFLKFLEPIFQPtpEDVTISYLPLAHMF------ERLVQG---VIFSCggkigFFqgdirll 331
Cdd:cd05911 159 GLPKGVCLSHRNLIANLSQVQTFLYGNDGS--NDVILGFLPLYHIYglfttlASLLNGatvIIMPK-----FD------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 332 PDDMKAL----KPTVFPTVPRLLNRVydkvqneAKTPLkkfllnlaiiskfnevrngiirrnslwdkLVFSKIQSslggk 407
Cdd:cd05911 225 SELFLDLiekyKITFLYLVPPIAAAL-------AKSPL-----------------------------LDKYDLSS----- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 408 VRLMITGAAPISTPVLTFFRAAMGCWVF-EAYGQTECTAGCSITSPGDWTAGHVGTPVScNF-VKLEDVADMNYFSVNNE 485
Cdd:cd05911 264 LRVILSGGAPLSKELQELLAKRFPNATIkQGYGMTETGGILTVNPDGDDKPGSVGRLLP-NVeAKIVDDDGKDSLGPNEP 342
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958650325 486 GEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIENV 556
Cdd:cd05911 343 GEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAV 412
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
101-585 |
7.68e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 173.45 E-value: 7.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEWVISELACytySM---VAVPLYDTLGAEAIIYVINRADISV 177
Cdd:PRK06187 32 TTYAELDERVNRLANALRALGVKK--GDRVAVFDWNSHEYLEAYFAV---PKigaVLHPINIRLKPEEIAYILNDAEDRV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 178 VICDT---PqkatmLIENVeKDLTPGLKTVILMDPFDDdlmkrgEKCGIEMLSLHDAENLGKENFKKPvPPNPEDLSVIC 254
Cdd:PRK06187 107 VLVDSefvP-----LLAAI-LPQLPTVRTVIVEGDGPA------APLAPEVGEYEELLAAASDTFDFP-DIDENDAAAML 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 255 FTSGTTGDPKGAMLTHQNIVSN---MAAFLKFlepifqpTPEDVTISYLPLAHMFERLVQGVIFSCGGKI---GFFqgDI 328
Cdd:PRK06187 174 YTSGTTGHPKGVVLSHRNLFLHslaVCAWLKL-------SRDDVYLVIVPMFHVHAWGLPYLALMAGAKQvipRRF--DP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 329 RLLPDDMKALKPTVFPTVPRLLNrvydkvqneaktplkkFLLNLAIISKFNevrngiirrnslwdklvFSKIqsslggkv 408
Cdd:PRK06187 245 ENLLDLIETERVTFFFAVPTIWQ----------------MLLKAPRAYFVD-----------------FSSL-------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 409 RLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCSITSP-----GDWT-AGHVGTPVSCNFVKLEDvADMNYFSV 482
Cdd:PRK06187 284 RLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVLPPedqlpGQWTkRRSAGRPLPGVEARIVD-DDGDELPP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 483 NNE--GEICIKGNNVFKGYLKDPEKTQEVLDkDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENVYSRS 560
Cdd:PRK06187 363 DGGevGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIKDVIISG-GENIYPRELEDALYGH 440
|
490 500
....*....|....*....|....*
gi 1958650325 561 RPILQVFVhgeslrsflIGvvVPDP 585
Cdd:PRK06187 441 PAVAEVAV---------IG--VPDE 454
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
213-675 |
2.37e-44 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 169.90 E-value: 2.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 213 DLMKRGEKCGIEMLSLHDAENLGKENFKKPvPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKflEPIFQPTP 292
Cdd:PTZ00342 270 DLKEKAKKLGISIILFDDMTKNKTTNYKIQ-NEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCK--HSIFKKYN 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 293 EDVTISYLPLAHMFERLVQGVIFSCGGKIGFFQGDIRLLPDDMKALKPTVFPTVPRLLNRVYDKVQNEAK--TPLKKFLL 370
Cdd:PTZ00342 347 PKTHLSYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINnlPPLKRFLV 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 371 NlAIISKFNEVRNGIIRRnsLWDKL--VFSKIQSSLGGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCS 448
Cdd:PTZ00342 427 K-KILSLRKSNNNGGFSK--FLEGIthISSKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTGPIF 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 449 ITSPGDWTAGHVGTPVSCNfVKLEDVADMNYFSVNN--EGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLP 526
Cdd:PTZ00342 504 VQHADDNNTESIGGPISPN-TKYKVRTWETYKATDTlpKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINK 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 527 NGTLKIIDRKKNIFKLAQGEYIAPEKIENVYSRSRPILQVFVHGESLRSFLIGVVVPDPESLPSFAAKIGV--------- 597
Cdd:PTZ00342 583 NGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGDDSMDGPLAIISVDKYLLFKCLKDDNMlestginek 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 598 ----KGSFEELCQN---QCVKKAILEdlqkVGKEGGLKSFEQVKSIFVHPEPFSIENgLLTPTLKAKRVELAK---FFQT 667
Cdd:PTZ00342 663 nyleKLTDETINNNiyvDYVKGKMLE----VYKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKRFYVFKdyaFFID 737
|
....*...
gi 1958650325 668 QIKSLYES 675
Cdd:PTZ00342 738 QVKKIYKN 745
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
101-597 |
5.24e-44 |
|
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: 164.81 E-value: 5.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLlHKGYKPsqDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIC 180
Cdd:cd05909 8 LTYRKLLTGAIALARKL-AKMTKE--GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 DTP--QKATML-IENVEKDltpglKTVILMDpfddDLMKR---GEKC----GIEMLSLHDAENLGKENFKkpvppnPEDL 250
Cdd:cd05909 85 SKQfiEKLKLHhLFDVEYD-----ARIVYLE----DLRAKiskADKCkaflAGKFPPKWLLRIFGVAPVQ------PDDP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 251 SVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKflepIFQPTPEDVTISYLPLAHMFErLVQGVIFS--CGGKIGFFqgdi 328
Cdd:cd05909 150 AVILFTSGSEGLPKGVVLSHKNLLANVEQITA----IFDPNPEDVVFGALPFFHSFG-LTGCLWLPllSGIKVVFH---- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 329 rllPDdmkalkPTVFPTVPRLlnrVYD-KVQNEAKTPLkkFLlnlaiiskfnevrNGIIRRnslWDKLVFSKIqsslggk 407
Cdd:cd05909 221 ---PN------PLDYKKIPEL---IYDkKATILLGTPT--FL-------------RGYARA---AHPEDFSSL------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 408 vRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCSITSPG-DWTAGHVGTPVSCNFVKLEDVADMNYFSVNNEG 486
Cdd:cd05909 264 -RLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGG 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 487 EICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENVYSRSRPIlQV 566
Cdd:cd05909 343 LLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDILSEILPE-DN 419
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1958650325 567 FV---------HGESLRSFLIGvVVPDPESLPSFAAKIGV 597
Cdd:cd05909 420 EVavvsvpdgrKGEKIVLLTTT-TDTDPSSLNDILKNAGI 458
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
101-585 |
2.24e-42 |
|
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: 158.93 E-value: 2.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPsQDQfIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIc 180
Cdd:cd17631 21 LTYAELDERVNRLAHALRALGVAK-GDR-VAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 dtpqkatmlienvekdltpglktvilmdpfdddlmkrgekcgiemlslhdaenlgkenfkkpvppnpEDLSVICFTSGTT 260
Cdd:cd17631 98 -------------------------------------------------------------------DDLALLMYTSGTT 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 261 GDPKGAMLTHQNIVSNMAAFLKFLEPifqpTPEDVTISYLPLAHMFERLV-QGVIFSCGGKI----GFfqgDIRLLPDDM 335
Cdd:cd17631 111 GRPKGAMLTHRNLLWNAVNALAALDL----GPDDVLLVVAPLFHIGGLGVfTLPTLLRGGTVvilrKF---DPETVLDLI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 336 KALKPTVFPTVPRLLNrvydkvqneaktplkkFLLNLaiiSKFNEVRngiirrnslwdklvfskiQSSLggkvRLMITGA 415
Cdd:cd17631 184 ERHRVTSFFLVPTMIQ----------------ALLQH---PRFATTD------------------LSSL----RAVIYGG 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 416 APISTPVLTFFRAAmGCWVFEAYGQTECTAGCSITSPGDW--TAGHVGTPVSCNFVKLEDvADMNYFSVNNEGEICIKGN 493
Cdd:cd17631 223 APMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHrrKLGSAGRPVFFVEVRIVD-PDGREVPPGEVGEIVVRGP 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 494 NVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKlAQGEYIAPEKIENVYSRSRPILQVFVhgesl 573
Cdd:cd17631 301 HVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDVLYEHPAVAEVAV----- 373
|
490
....*....|..
gi 1958650325 574 rsflIGvvVPDP 585
Cdd:cd17631 374 ----IG--VPDE 379
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
191-556 |
5.74e-42 |
|
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: 159.32 E-value: 5.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 191 ENVEKdLTPGLKTVILMD--PFDDDLMKRGEKCGiemlslhdaenlgKENFKKPVPPNPEDLSVICFTSGTTGDPKGAML 268
Cdd:cd05904 113 ELAEK-LASLALPVVLLDsaEFDSLSFSDLLFEA-------------DEAEPPVVVIKQDDVAALLYSSGTTGRSKGVML 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 269 THQNIVSNMAAFLKFLEPifQPTPEDVTISYLPLAHM--FERLVQGVIfSCGGKI----GFfqgDIRLLPDDMKALKPTV 342
Cdd:cd05904 179 THRNLIAMVAQFVAGEGS--NSDSEDVFLCVLPMFHIygLSSFALGLL-RLGATVvvmpRF---DLEELLAAIERYKVTH 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 343 FPTVPrllnrvydkvqneaktPLkkfLLNLAiiskfnevrngiirRNSLWDKLVFSKIQSslggkvrlMITGAAPISTPV 422
Cdd:cd05904 253 LPVVP----------------PI---VLALV--------------KSPIVDKYDLSSLRQ--------IMSGAAPLGKEL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 423 LTFFRAAM-GCWVFEAYGQTECTAGCSITSPGDWTAGHVGtpvSCNFV------KLEDVADMNYFSVNNEGEICIKGNNV 495
Cdd:cd05904 292 IEAFRAKFpNVDLGQGYGMTESTGVVAMCFAPEKDRAKYG---SVGRLvpnveaKIVDPETGESLPPNQTGELWIRGPSI 368
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958650325 496 FKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIENV 556
Cdd:cd05904 369 MKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEAL 428
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
101-589 |
6.51e-42 |
|
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: 160.00 E-value: 6.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLlhKGYKPSQDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIC 180
Cdd:cd17642 45 YSYAEYLEMSVRLAEAL--KKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFC 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 DtpQKATMLIENVEKDLtPGLKTVILMDPFDDdlmKRGEKCGIEMLSLHDAENLGKENFKKPVPPNPEDLSVICFTSGTT 260
Cdd:cd17642 123 S--KKGLQKVLNVQKKL-KIIKTIIILDSKED---YKGYQCLYTFITQNLPPGFNEYDFKPPSFDRDEQVALIMNSSGST 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 261 GDPKGAMLTHQNIVsnmAAFLKFLEPIF--QPTPEDVTISYLPLAHMFERLVQGVIFSCGGKIGFfqgdirllpddMKAL 338
Cdd:cd17642 197 GLPKGVQLTHKNIV---ARFSHARDPIFgnQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVL-----------MYKF 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 339 KPTVFptvprlLNRVYD-KVQNEAKTP-LKKFLLNLAIISKFNevrngiirrnslwdklvfskiQSSLggkvRLMITGAA 416
Cdd:cd17642 263 EEELF------LRSLQDyKVQSALLVPtLFAFFAKSTLVDKYD---------------------LSNL----HEIASGGA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 417 PISTPV---------LTFFRaamgcwvfEAYGQTECTAGCSITSPGDWTAGHVGTPVSCNFVKLEDVADMNYFSVNNEGE 487
Cdd:cd17642 312 PLSKEVgeavakrfkLPGIR--------QGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 488 ICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIENVYSRSRPILQVF 567
Cdd:cd17642 384 LCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQHPKIFDAG 462
|
490 500
....*....|....*....|....
gi 1958650325 568 VHGeslrsfligvvVPDPES--LP 589
Cdd:cd17642 463 VAG-----------IPDEDAgeLP 475
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
99-585 |
9.26e-42 |
|
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: 158.63 E-value: 9.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 99 KWISYKQVSDRAEYLGSCLLHKGYKPsQDQfIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVV 178
Cdd:cd05926 13 PALTYADLAELVDDLARQLAALGIKK-GDR-VAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 179 IcdTPQKATMLIENVEKDLTPGLKTVILmDPFDDDLMKRGEKcgiemLSLHDAenlGKENFKKPVPPNPEDLSVICFTSG 258
Cdd:cd05926 91 L--TPKGELGPASRAASKLGLAILELAL-DVGVLIRAPSAES-----LSNLLA---DKKNAKSEGVPLPDDLALILHTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 259 TTGDPKGAMLTHQNIVSNMAAFLKflepIFQPTPEDVTISYLPLAHmferlVQGVI------FSCGGKIgffqgdirLLP 332
Cdd:cd05926 160 TTGRPKGVPLTHRNLAASATNITN----TYKLTPDDRTLVVMPLFH-----VHGLVasllstLAAGGSV--------VLP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 333 ---------DDMKALKPTVFPTVPRLLnrvydkvqneaktplkKFLLNlaiiskfNEVRNGIIRRNSLwdklvfskiqss 403
Cdd:cd05926 223 prfsastfwPDVRDYNATWYTAVPTIH----------------QILLN-------RPEPNPESPPPKL------------ 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 404 lggkvRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAgcSITS----PGDWTAGHVGTPVSCNFVKLEDvaDMNY 479
Cdd:cd05926 268 -----RFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAH--QMTSnplpPGPRKPGSVGKPVGVEVRILDE--DGEI 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 480 FSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENVYSR 559
Cdd:cd05926 339 LPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVLLS 417
|
490 500
....*....|....*....|....*.
gi 1958650325 560 SRPILQVFVHGeslrsfligvvVPDP 585
Cdd:cd05926 418 HPAVLEAVAFG-----------VPDE 432
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
101-586 |
1.80e-41 |
|
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: 156.68 E-value: 1.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQ-VSDRAEYlgSCLLHKGYKPSQDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVI 179
Cdd:cd05941 12 ITYADlVARAARL--ANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 180 cdtpqkatmlienvekdltpglktvilmdpfdddlmkrgekcgiemlslhdaenlgkenfkkpvppnpeDLSVICFTSGT 259
Cdd:cd05941 90 ---------------------------------------------------------------------DPALILYTSGT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 260 TGDPKGAMLTHQNIVSNMAAFLKFlepiFQPTPEDVTISYLPLAHmferlVQGVIFS------CGGKI---GFFQGDIRL 330
Cdd:cd05941 101 TGRPKGVVLTHANLAANVRALVDA----WRWTEDDVLLHVLPLHH-----VHGLVNAllcplfAGASVeflPKFDPKEVA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 331 LPDDMKALkpTVFPTVPRLLNRVYDkvQNEAKTPLKKFllnlaiiskfnevrngiIRRNSLwdklvfskiqsslgGKVRL 410
Cdd:cd05941 172 ISRLMPSI--TVFMGVPTIYTRLLQ--YYEAHFTDPQF-----------------ARAAAA--------------ERLRL 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 411 MITGAAPISTPVLTFFRAAMGCWVFEAYGQTEctAGCSITSP--GDWTAGHVGTPVSCNFVKLEDVADMNYFSVNNEGEI 488
Cdd:cd05941 217 MVSGSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEI 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 489 CIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKK-NIFKlAQGEYIAPEKIENVYSRSRPILQVF 567
Cdd:cd05941 295 QVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEIERVLLAHPGVSECA 373
|
490 500
....*....|....*....|..
gi 1958650325 568 VHGESLRSF---LIGVVVPDPE 586
Cdd:cd05941 374 VIGVPDPDWgerVVAVVVLRAG 395
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
230-587 |
7.71e-39 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 151.57 E-value: 7.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 230 DAENLGKENFKKPVPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFLEPIFQPTP-EDVTISYLPLAHMFER 308
Cdd:PRK08751 190 EALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKLEEgCEVVITALPLYHIFAL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 309 LVQGVIFSCGGKIGFFQGDIRLLPDDMKALKPTVFpTVPRLLNRVYDKVQNeakTPLkkfllnlaiiskfnevrngiirr 388
Cdd:PRK08751 270 TANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRF-TAFTGVNTLFNGLLN---TPG----------------------- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 389 nslWDKLVFSKIQSSLGGkvrlmitGAApISTPVLTFFRAAMGCWVFEAYGQTECTAGCSItSPGDWTA--GHVGTPVSC 466
Cdd:PRK08751 323 ---FDQIDFSSLKMTLGG-------GMA-VQRSVAERWKQVTGLTLVEAYGLTETSPAACI-NPLTLKEynGSIGLPIPS 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 467 NFVKLEDVADmNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGE 546
Cdd:PRK08751 391 TDACIKDDAG-TVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-LVSGF 468
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1958650325 547 YIAPEKIENVYSRSRPILQVfvhgeslrsflIGVVVPDPES 587
Cdd:PRK08751 469 NVYPNEIEDVIAMMPGVLEV-----------AAVGVPDEKS 498
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
226-588 |
1.33e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 147.99 E-value: 1.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 226 LSLHDAENLGKENFKKPVPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFLEPIFQPTPEdVTISYLPLAHM 305
Cdd:PRK05677 185 VKFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEGCE-ILIAPLPLYHI 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 306 FerlvqGVIFSCGGKigffqgdirllpddMKALKPTVFPTVPRLLNRVydkVQNEAKTPLKKFL-LNLAIISKFNevrng 384
Cdd:PRK05677 264 Y-----AFTFHCMAM--------------MLIGNHNILISNPRDLPAM---VKELGKWKFSGFVgLNTLFVALCN----- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 385 iirrNSLWDKLVFSKIQSSLGGKVRLMITGAApistpvltFFRAAMGCWVFEAYGQTECTAGCSITSPGDWTAGHVGTPV 464
Cdd:PRK05677 317 ----NEAFRKLDFSALKLTLSGGMALQLATAE--------RWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPV 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 465 SCNFVKLEDvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQ 544
Cdd:PRK05677 385 PSTLCKVID-DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVS 462
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1958650325 545 GEYIAPEKIENVYSRSRPILQVFV-------HGESLRSFligVVVPDPESL 588
Cdd:PRK05677 463 GFNVYPNELEDVLAALPGVLQCAAigvpdekSGEAIKVF---VVVKPGETL 510
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
241-587 |
1.05e-36 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 145.16 E-value: 1.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 241 KPVPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFLEPIFQPTPED---VTISYLPLAHMFERLVQGVI-FS 316
Cdd:PRK07059 197 KPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAFEKKPRPdqlNFVCALPLYHIFALTVCGLLgMR 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 317 CGGkIGFFQGDIRLLPDDMKALKP---TVFPTVPRLLNRvydkvqneaktplkkfLLNlaiiskfnevrngiirrNSLWD 393
Cdd:PRK07059 277 TGG-RNILIPNPRDIPGFIKELKKyqvHIFPAVNTLYNA----------------LLN-----------------NPDFD 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 394 KLVFSKIQSSLGGkvrlmitGAApISTPVLTFFRAAMGCWVFEAYG--QTECTAGCSITSPGDWTaGHVGTPVSCNFVKL 471
Cdd:PRK07059 323 KLDFSKLIVANGG-------GMA-VQRPVAERWLEMTGCPITEGYGlsETSPVATCNPVDATEFS-GTIGLPLPSTEVSI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 472 EDvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPE 551
Cdd:PRK07059 394 RD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMI-LVSGFNVYPN 471
|
330 340 350
....*....|....*....|....*....|....*.
gi 1958650325 552 KIENVYSRSRPILQVFVHGeslrsfligvvVPDPES 587
Cdd:PRK07059 472 EIEEVVASHPGVLEVAAVG-----------VPDEHS 496
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
246-588 |
4.85e-36 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 143.27 E-value: 4.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 246 NPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFLEPIFQPTPEDVTISyLPLAHMFERLVQGVIFSCGGKIGFFQ 325
Cdd:PRK08974 204 VPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGPLLHPGKELVVTA-LPLYHIFALTVNCLLFIELGGQNLLI 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 326 GDIRLLPDDMKALKP---TVFPTVPRLLNRvydkvqneaktplkkfLLNlaiiskfnevrngiirrNSLWDKLVFSKIqs 402
Cdd:PRK08974 283 TNPRDIPGFVKELKKypfTAITGVNTLFNA----------------LLN-----------------NEEFQELDFSSL-- 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 403 slggkvRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECT---AGCSITSPGdwTAGHVGTPVSCNFVKLEDvADMNY 479
Cdd:PRK08974 328 ------KLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVNPYDLDY--YSGSIGLPVPSTEIKLVD-DDGNE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 480 FSVNNEGEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENVYSR 559
Cdd:PRK08974 399 VPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMI-LVSGFNVYPNEIEDVVML 476
|
330 340 350
....*....|....*....|....*....|....*.
gi 1958650325 560 SRPILQVF-------VHGESLRSFligvVVPDPESL 588
Cdd:PRK08974 477 HPKVLEVAavgvpseVSGEAVKIF----VVKKDPSL 508
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
227-539 |
1.23e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 139.36 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 227 SLHDAENLGKENFKKPVPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFLePIFQPTPEdVTISYLPLAHMF 306
Cdd:PRK05605 198 TLVDAAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWV-PGLGDGPE-RVLAALPMFHAY 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 307 E-RLVQGVIFSCGGKIGFF-QGDIRLLPDDMKALKPTVFPTVPRLlnrvYDKVQNEAKtplkkfllnlaiiskfnevRNG 384
Cdd:PRK05605 276 GlTLCLTLAVSIGGELVLLpAPDIDLILDAMKKHPPTWLPGVPPL----YEKIAEAAE-------------------ERG 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 385 IirrnslwdklvfskiqsSLGGkVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTEC---TAGCSITSpgDWTAGHVG 461
Cdd:PRK05605 333 V-----------------DLSG-VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETspiIVGNPMSD--DRRPGYVG 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 462 TPVSCNFVKledVADMNYFSVN----NEGEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIIDRKK 537
Cdd:PRK05605 393 VPFPDTEVR---IVDPEDPDETmpdgEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIK 468
|
..
gi 1958650325 538 NI 539
Cdd:PRK05605 469 EL 470
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
73-556 |
2.91e-34 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 137.94 E-value: 2.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 73 YEVFQRGLAVSDNGPCLGYRKPNQPYKWISYKQVSDRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEWVISELACYTYSM 152
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRALGVKK--GDRVAIYLPNIPEAVIAMLACARIGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 153 VAVPLYDTLGAEAIIYVINRADISVVICDT----PQKATMLIENVEK--DLTPGLKTVILMDPFDDDLMKRGEkcgiemL 226
Cdd:COG0365 90 VHSPVFPGFGAEALADRIEDAEAKVLITADgglrGGKVIDLKEKVDEalEELPSLEHVIVVGRTGADVPMEGD------L 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 227 SLHDAENLGKENFKkPVPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFlepIFQPTPEDV--TIS------ 298
Cdd:COG0365 164 DWDELLAAASAEFE-PEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKY---VLDLKPGDVfwCTAdigwat 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 299 ------YLPLAH-----MFErlvqgvifscgGKIGFFQGDiRLLpDDMKALKPTVF---PTVPRLLNRVYDKvqneaktP 364
Cdd:COG0365 240 ghsyivYGPLLNgatvvLYE-----------GRPDFPDPG-RLW-ELIEKYGVTVFftaPTAIRALMKAGDE-------P 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 365 LKKFLLnlaiiskfnevrngiirrnslwdklvfskiqSSLggkvRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTEcT 444
Cdd:COG0365 300 LKKYDL-------------------------------SSL----RLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTE-T 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 445 AGCSITSPGDWT--AGHVGTPVSCNFVKLEDvADMNYFSVNNEGEICIKGNN--VFKGYLKDPEKTQEVL--DKDGWLHT 518
Cdd:COG0365 344 GGIFISNLPGLPvkPGSMGKPVPGYDVAVVD-EDGNPVPPGEEGELVIKGPWpgMFRGYWNDPERYRETYfgRFPGWYRT 422
|
490 500 510
....*....|....*....|....*....|....*...
gi 1958650325 519 GDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENV 556
Cdd:COG0365 423 GDGARRDEDGYFWILGRSDDVINVS-GHRIGTAEIESA 459
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
91-554 |
8.73e-34 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 136.42 E-value: 8.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 91 YRKPNQPYKWiSYKQVSDRAEYLGSCLLHKGYKPSQdqfigIFAQNRPEW---VISELACYTYSMVAVPLYDTLGAEAII 167
Cdd:PRK06087 41 AVVDNHGASY-TYSALDHAASRLANWLLAKGIEPGD-----RVAFQLPGWcefTIIYLACLKVGAVSVPLLPSWREAELV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 168 YVINRADISVVICDTPQKAT---MLIENVEKDLtPGLKTVILMDpfdddlmKRGEKCGIEMLS--LHDAENLgkenfKKP 242
Cdd:PRK06087 115 WVLNKCQAKMFFAPTLFKQTrpvDLILPLQNQL-PQLQQIVGVD-------KLAPATSSLSLSqiIADYEPL-----TTA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 243 VPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFLEpifqPTPEDVTISYLPLAHmferlvqgvifscggKIG 322
Cdd:PRK06087 182 ITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLN----LTWQDVFMMPAPLGH---------------ATG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 323 FFQGDI--------RLLPDDMKAlkptvfPTVPRLLNRvyDKVQ-NEAKTPlkkFLLNLaiiskFNEVRNGIIRRNSLwd 393
Cdd:PRK06087 243 FLHGVTapfligarSVLLDIFTP------DACLALLEQ--QRCTcMLGATP---FIYDL-----LNLLEKQPADLSAL-- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 394 klvfskiqsslggkvRLMITGAAPISTPVLtffRAAM--GCWVFEAYGQTECT--AGCSITSPGDWTAGHVGTPVSCNFV 469
Cdd:PRK06087 305 ---------------RFFLCGGTTIPKKVA---RECQqrGIKLLSVYGSTESSphAVVNLDDPLSRFMHTDGYAAAGVEI 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 470 KLEDvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIA 549
Cdd:PRK06087 367 KVVD-EARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENIS 444
|
....*
gi 1958650325 550 PEKIE 554
Cdd:PRK06087 445 SREVE 449
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
103-568 |
1.02e-33 |
|
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: 134.11 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 103 YKQVSDRAEYLgscllhKGYKPSQDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLgaeaiiyvinradisvvicdT 182
Cdd:TIGR01923 6 DCEAAHLAKAL------KAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRL--------------------T 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 183 PQKATMLIENVEKDLTpglktvilmdpFDDDLMkrgEKCGIEMLSLHDAENLGKENFKKPVPPNPEDLSVICFTSGTTGD 262
Cdd:TIGR01923 60 ENERTNQLEDLDVQLL-----------LTDSLL---EEKDFQADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 263 PKGAMLTHQNI-VSNMAAFLKFlePIfqpTPEDVTISYLPLAHMFErlvQGVIFSC---GGKIGFFQGDIRLLpDDMKAL 338
Cdd:TIGR01923 126 PKAVPHTFRNHyASAVGSKENL--GF---TEDDNWLLSLPLYHISG---LSILFRWlieGATLRIVDKFNQLL-EMIANE 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 339 KPTVFPTVPRLLNRVYDKVQNEakTPLKKFLLnlaiiskfnevrngiirrnslwdklvfskiqsslggkvrlmitGAAPI 418
Cdd:TIGR01923 197 RVTHISLVPTQLNRLLDEGGHN--ENLRKILL-------------------------------------------GGSAI 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 419 STPVLtffRAAM--GCWVFEAYGQTE-CTAGCSITSPGDWTAGHVGTPVSCNFVKLEdVADMNyfsvnNEGEICIKGNNV 495
Cdd:TIGR01923 232 PAPLI---EEAQqyGLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIK-VDNKE-----GHGEIMVKGANL 302
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958650325 496 FKGYLkDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENVYSRSRPILQVFV 568
Cdd:TIGR01923 303 MKGYL-YQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVV 373
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
247-570 |
2.27e-32 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 128.55 E-value: 2.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 247 PEDLSVICFTSGTTGDPKGAMLTHQNIVSNmAAF----LKFlepifqpTPEDVTISYLPLAHMFErLVQGVIfSC---GG 319
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNN-GYFigerLGL-------TEQDRLCIPVPLFHCFG-SVLGVL-AClthGA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 320 KIgffqgdirllpddmkalkptVFPTvprllnRVYD------KVQNEAKTPL----KKF--LLNLAIISKFN--EVRNGI 385
Cdd:cd05917 71 TM--------------------VFPS------PSFDplavleAIEKEKCTALhgvpTMFiaELEHPDFDKFDlsSLRTGI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 386 IrrnslwdklvfskiqsslggkvrlmitGAAPISTPVLTFFRAAMGCW-VFEAYGQTECTAGCSITSPGD---WTAGHVG 461
Cdd:cd05917 125 M---------------------------AGAPCPPELMKRVIEVMNMKdVTIAYGMTETSPVSTQTRTDDsieKRVNTVG 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 462 TPVSCNFVKLEDVADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFk 541
Cdd:cd05917 178 RIMPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI- 256
|
330 340
....*....|....*....|....*....
gi 1958650325 542 LAQGEYIAPEKIENVYSRSRPILQVFVHG 570
Cdd:cd05917 257 IRGGENIYPREIEEFLHTHPKVSDVQVVG 285
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
138-537 |
2.35e-32 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 131.54 E-value: 2.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 138 PEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVICDtPQKATMLIENVEKDLTPGLKTVilmdpfDDDlmKR 217
Cdd:PRK07514 64 PEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCD-PANFAWLSKIAAAAGAPHVETL------DAD--GT 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 218 GekcgiemlSLHDAENLGKENFKkPVPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAflkfLEPIFQPTPEDVTI 297
Cdd:PRK07514 135 G--------SLLEAAAAAPDDFE-TVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALT----LVDYWRFTPDDVLI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 298 SYLPLAHMFERLV--QGVIFScGGKIGFFQgdiRLLPDDMKALKP--TVFPTVP----RLLnrvydkvQNEAKTPlkkfl 369
Cdd:PRK07514 202 HALPIFHTHGLFVatNVALLA-GASMIFLP---KFDPDAVLALMPraTVMMGVPtfytRLL-------QEPRLTR----- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 370 lnlaiiskfnevrngiirrnslwdklvfskiqsSLGGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTEctaGCSI 449
Cdd:PRK07514 266 ---------------------------------EAAAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTE---TNMN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 450 TS-P--GDWTAGHVGTP---VScnfVKLEDVADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGR 523
Cdd:PRK07514 310 TSnPydGERRAGTVGFPlpgVS---LRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGK 386
|
410
....*....|....
gi 1958650325 524 WLPNGTLKIIDRKK 537
Cdd:PRK07514 387 IDERGYVHIVGRGK 400
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
70-570 |
2.88e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 131.82 E-value: 2.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 70 KTLYEVFQRGLAVSDNGPCLGYRKPNQPYkwiSYKQVSDRAEYLGSCLLHKGYKPSQDqfIGIFAQNRPEWVISELACYT 149
Cdd:PRK12583 18 QTIGDAFDATVARFPDREALVVRHQALRY---TWRQLADAVDRLARGLLALGVQPGDR--VGIWAPNCAEWLLTQFATAR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 150 YSMVAVPLYDTLGAEAIIYVINRADISVVICDTPQKAT----MLIEnVEKDLT------------PGLKTVILMDPFD-- 211
Cdd:PRK12583 93 IGAILVNINPAYRASELEYALGQSGVRWVICADAFKTSdyhaMLQE-LLPGLAegqpgalacerlPELRGVVSLAPAPpp 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 212 -----DDLMKRGEkcGIEMLSLHDAEnlgkenfkkpVPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAaflkFLEP 286
Cdd:PRK12583 172 gflawHELQARGE--TVSREALAERQ----------ASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGY----FVAE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 287 IFQPTPEDVTISYLPLAHMFerlvqGVIFSCGGKIGffQGDIRLLPDDmkALKPTVfptvprllnrVYDKVQNEAKTPLk 366
Cdd:PRK12583 236 SLGLTEHDRLCVPVPLYHCF-----GMVLANLGCMT--VGACLVYPNE--AFDPLA----------TLQAVEEERCTAL- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 367 kFLLNLAIISKFNEVRNGIIRRNSLwdklvfskiqsslggkvRLMITGAAPISTPVLTFFRAAMGCW-VFEAYGQTECTA 445
Cdd:PRK12583 296 -YGVPTMFIAELDHPQRGNFDLSSL-----------------RTGIMAGAPCPIEVMRRVMDEMHMAeVQIAYGMTETSP 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 446 GCSITSPGD------WTAGHVGTPVSCNFVKledvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTG 519
Cdd:PRK12583 358 VSLQTTAADdlerrvETVGRTQPHLEVKVVD----PDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTG 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1958650325 520 DIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENVYSRSRPILQVFVHG 570
Cdd:PRK12583 434 DLATMDEQGYVRIVGRSKDMI-IRGGENIYPREIEEFLFTHPAVADVQVFG 483
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
226-587 |
1.78e-31 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 129.56 E-value: 1.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 226 LSLHDAENLGKENFKKPVPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMA---AFLKFLEPIFQPTPED---VTISY 299
Cdd:PRK12492 185 VPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLqvrACLSQLGPDGQPLMKEgqeVMIAP 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 300 LPLAHMFERLVQGVIFSCGGKIGFFQGDIRLLPDDMKALKPTVFPTvprLLNrvydkvqneaktplkkflLNLAIISKFN 379
Cdd:PRK12492 265 LPLYHIYAFTANCMCMMVSGNHNVLITNPRDIPGFIKELGKWRFSA---LLG------------------LNTLFVALMD 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 380 evrngiirrNSLWDKLVFSKIQSSLGGKVRLMITGAAPistpvltfFRAAMGCWVFEAYGQTECTAGCSITSPGDWTA-G 458
Cdd:PRK12492 324 ---------HPGFKDLDFSALKLTNSGGTALVKATAER--------WEQLTGCTIVEGYGLTETSPVASTNPYGELARlG 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 459 HVGTPVSCNFVKLEDvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKN 538
Cdd:PRK12492 387 TVGIPVPGTALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKD 465
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1958650325 539 IFkLAQGEYIAPEKIENVysrsrpilqVFVHGESLRSFLIGvvVPDPES 587
Cdd:PRK12492 466 LI-IVSGFNVYPNEIEDV---------VMAHPKVANCAAIG--VPDERS 502
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
101-587 |
1.91e-31 |
|
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: 127.41 E-value: 1.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPSQdqFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIC 180
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRPGD--RVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 DTpqkATMLienvekdltpglktvilmdpfdddlmkrgekcgiemlslhdaenlgkenfkkpvppnpedlsvicFTSGTT 260
Cdd:cd05934 82 DP---ASIL-----------------------------------------------------------------YTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 261 GDPKGAMLTHQNIVSNMAAFLKFlepiFQPTPEDVTISYLPLAHMfERLVQGVI--FSCGGKIGffqgdirLLP------ 332
Cdd:cd05934 94 GPPKGVVITHANLTFAGYYSARR----FGLGEDDVYLTVLPLFHI-NAQAVSVLaaLSVGATLV-------LLPrfsasr 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 333 --DDMKALKPTVFPTVPRLLNRVYdkVQNEAKTPlkkfllnlaiiskfnevrngiiRRNslwdklvfskiqsslggKVRL 410
Cdd:cd05934 162 fwSDVRRYGATVTNYLGAMLSYLL--AQPPSPDD----------------------RAH-----------------RLRA 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 411 miTGAAPISTPVLTFFRAAMGCWVFEAYGQTEctAGCSITSPGDWTA--GHVGTPVSCNFVKLEDvADMNYFSVNNEGEI 488
Cdd:cd05934 201 --AYGAPNPPELHEEFEERFGVRLLEGYGMTE--TIVGVIGPRDEPRrpGSIGRPAPGYEVRIVD-DDGQELPAGEPGEL 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 489 CIKGNN---VFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKlAQGEYIAPEKIENVYSRSRPILQ 565
Cdd:cd05934 276 VIRGLRgwgFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVERAILRHPAVRE 353
|
490 500
....*....|....*....|..
gi 1958650325 566 VFVHGeslrsfligvvVPDPES 587
Cdd:cd05934 354 AAVVA-----------VPDEVG 364
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
75-554 |
3.53e-31 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 128.56 E-value: 3.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 75 VFQRGLAVSDNgPCLGYRKPNQPYkwiSYKQVSDRAEYLGSCLLHKGYKpsQDQFIGIFAQNRPEWVISELACytySMV- 153
Cdd:PLN02246 29 CFERLSEFSDR-PCLIDGATGRVY---TYADVELLSRRVAAGLHKLGIR--QGDVVMLLLPNCPEFVLAFLGA---SRRg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 154 -----AVPLYDTlgAEaiiyVINRADISvvicdtpqKATMLIEN---VEK----DLTPGLKTVILMDPFDDDLMkrgekc 221
Cdd:PLN02246 100 avtttANPFYTP--AE----IAKQAKAS--------GAKLIITQscyVDKlkglAEDDGVTVVTIDDPPEGCLH------ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 222 gIEMLSLHDAENLGKENFkkpvppNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFLEPIFQPTPEDVTISYLP 301
Cdd:PLN02246 160 -FSELTQADENELPEVEI------SPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYFHSDDVILCVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 302 LAHMFErlvQGVIFSCGGKIG--------FfqgDIRLLPDDMKALKPTVFPTVPRLLnrvydkvqneaktplkkfllnLA 373
Cdd:PLN02246 233 MFHIYS---LNSVLLCGLRVGaailimpkF---EIGALLELIQRHKVTIAPFVPPIV---------------------LA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 374 IIskfnevRNGIIRRNSLwdklvfskiqSSlggkVRLMITGAAPISTPVLTFFRAAMGCWVF-EAYGQTEctAGCSIT-- 450
Cdd:PLN02246 286 IA------KSPVVEKYDL----------SS----IRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMTE--AGPVLAmc 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 451 -----SPGDWTAGHVGTPVSCNFVKLEDVADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWL 525
Cdd:PLN02246 344 lafakEPFPVKSGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYID 423
|
490 500
....*....|....*....|....*....
gi 1958650325 526 PNGTLKIIDRKKNIFKLaQGEYIAPEKIE 554
Cdd:PLN02246 424 DDDELFIVDRLKELIKY-KGFQVAPAELE 451
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
101-586 |
9.71e-31 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 126.51 E-value: 9.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHK-GYKPSQDqfIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVI 179
Cdd:PRK06839 28 MTYKQLHEYVSKVAAYLIYElNVKKGER--IAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 180 CDtPQKATMLIEnvekdltpgLKTVILMDPFdddlmkrgekcgIEMLSLHDAENLGKENFkkpVPPNPEDLSVICFTSGT 259
Cdd:PRK06839 106 VE-KTFQNMALS---------MQKVSYVQRV------------ISITSLKEIEDRKIDNF---VEKNESASFIICYTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 260 TGDPKGAMLTHQNI----VSNMAAFlkflepifQPTPEDVTISYLPLAHMferlvqgvifscgGKIGFFqgdirllpddm 335
Cdd:PRK06839 161 TGKPKGAVLTQENMfwnaLNNTFAI--------DLTMHDRSIVLLPLFHI-------------GGIGLF----------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 336 kALkPTVFPTVPRLLNRVYDKVQNEAKTPLKKFLLNLAIISKFNEVRNGIIRRNSLWDKlvfskiqsslggkVRLMITGA 415
Cdd:PRK06839 209 -AF-PTLFAGGVIIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQS-------------VRWFYNGG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 416 APISTPVLTFFRAaMGCWVFEAYGQTECTAGCSITSPGDW--TAGHVGTPVSCNFVKLEDvADMNYFSVNNEGEICIKGN 493
Cdd:PRK06839 274 APCPEELMREFID-RGFLFGQGFGMTETSPTVFMLSEEDArrKVGSIGKPVLFCDYELID-ENKNKVEVGEVGELLIRGP 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 494 NVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENVYSRSRPILQVFVHGesl 573
Cdd:PRK06839 352 NVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQVINKLSDVYEVAVVG--- 426
|
490
....*....|...
gi 1958650325 574 rsfligvvVPDPE 586
Cdd:PRK06839 427 --------RQHVK 431
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
94-605 |
1.14e-30 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 127.23 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 94 PNQPYKWiSYKQVSDRAEYLGSCLLHKGYKPSQDqfIGIFAQNRPEWVISELACYTYSMVAV---PLYDTlgAEaIIYVI 170
Cdd:PRK08315 38 RDQGLRW-TYREFNEEVDALAKGLLALGIEKGDR--VGIWAPNVPEWVLTQFATAKIGAILVtinPAYRL--SE-LEYAL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 171 NRADISVVIC-----DT----------PQKATMLIENVEKDLTPGLKTVIL--------MDPFDDdLMKRGEKCGIE--- 224
Cdd:PRK08315 112 NQSGCKALIAadgfkDSdyvamlyelaPELATCEPGQLQSARLPELRRVIFlgdekhpgMLNFDE-LLALGRAVDDAela 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 225 ----MLSLHDAENlgkenfkkpvppnpedlsvICFTSGTTGDPKGAMLTHQNIVSN---MAAFLKFlepifqpTPED-VT 296
Cdd:PRK08315 191 arqaTLDPDDPIN-------------------IQYTSGTTGFPKGATLTHRNILNNgyfIGEAMKL-------TEEDrLC 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 297 ISyLPLAHMFErLVQGV--IFSCGGKIgffqgdirllpddmkalkptVFPtvprllNRVYD------KVQNEAKTPL--- 365
Cdd:PRK08315 245 IP-VPLYHCFG-MVLGNlaCVTHGATM--------------------VYP------GEGFDplatlaAVEEERCTALygv 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 366 -KKFL--LNLAIISKFNevrngiirrnslwdklvfskiQSSLggkvRLMITGAAPISTPVLTFFRAAMGC-WVFEAYGQT 441
Cdd:PRK08315 297 pTMFIaeLDHPDFARFD---------------------LSSL----RTGIMAGSPCPIEVMKRVIDKMHMsEVTIAYGMT 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 442 ECTAGCSITSPGD------WTAGHVGTPVScnfVKLEDVADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGW 515
Cdd:PRK08315 352 ETSPVSTQTRTDDplekrvTTVGRALPHLE---VKIVDPETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGW 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 516 LHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENVYSRSRPILQVFVHGeslrsfligvvVPDPeslpsfaaKI 595
Cdd:PRK08315 429 MHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEFLYTHPKIQDVQVVG-----------VPDE--------KY 488
|
570
....*....|
gi 1958650325 596 GvkgsfEELC 605
Cdd:PRK08315 489 G-----EEVC 493
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
102-593 |
3.51e-30 |
|
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: 124.03 E-value: 3.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 102 SYKQVSDRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRAdisvvicd 181
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGP--GDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRA-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 182 tpqKATMLIenvekdlTPGLktvilmdpfdddlmkrgekcgiemlslhdaenlgkenFKKPVP-PNPEDLSVICFTSGTT 260
Cdd:cd05903 73 ---KAKVFV-------VPER-------------------------------------FRQFDPaAMPDAVALLLFTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 261 GDPKGAMLTHQNIVSNMAAFLKFLEPifqpTPEDVTISYLPLAHMferlvqgvifscggkIGFFQGdirllpddmkALKP 340
Cdd:cd05903 106 GEPKGVMHSHNTLSASIRQYAERLGL----GPGDVFLVASPMAHQ---------------TGFVYG----------FTLP 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 341 TVFPTvPRLLNRVYD-----KVQNE-------AKTPLKKFLLNLAiiskfnevrngiirrnslwdklvfsKIQSSLGGKV 408
Cdd:cd05903 157 LLLGA-PVVLQDIWDpdkalALMREhgvtfmmGATPFLTDLLNAV-------------------------EEAGEPLSRL 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 409 RLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTEC-TAGCSITSPGDWTAGHV-GTPVSCNFVKLEDvADMNYFSVNNEG 486
Cdd:cd05903 211 RTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECpGAVTSITPAPEDRRLYTdGRPLPGVEIKVVD-DTGATLAPGVEG 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 487 EICIKGNNVFKGYLKDPEKTQEVLDkDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENVYSRSRPILQV 566
Cdd:cd05903 290 ELLSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEA 367
|
490 500 510
....*....|....*....|....*....|
gi 1958650325 567 FVHG---ESLRSFLIGVVVPDPESLPSFAA 593
Cdd:cd05903 368 AVVAlpdERLGERACAVVVTKSGALLTFDE 397
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
130-585 |
5.24e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 124.71 E-value: 5.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 130 IGIFAQNRPEWVISELACYTYSMVAVPLYdTLGAEA-IIYVINRADISVVICDT---PQKATMLIENVekdltPGLKTVI 205
Cdd:PRK06188 65 VALLSLNRPEVLMAIGAAQLAGLRRTALH-PLGSLDdHAYVLEDAGISTLIVDPapfVERALALLARV-----PSLKHVL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 206 LMDPFDD--DLMKRGEKCGIEMLSLHDAenlgkenfkkpvppnPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKF 283
Cdd:PRK06188 139 TLGPVPDgvDLLAAAAKFGPAPLVAAAL---------------PPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 284 LEpifqpTPEDvtISYL---PLAHMFERLVQGVIFScGGKIGFFQG-DIRLLPDDMKALKPTVFPTVPRLLNRVYDkvqn 359
Cdd:PRK06188 204 WE-----WPAD--PRFLmctPLSHAGGAFFLPTLLR-GGTVIVLAKfDPAEVLRAIEEQRITATFLVPTMIYALLD---- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 360 eaktplkkfllnlaiiskfnevrNGIIRRNSLwdklvfskiqSSLggkvRLMITGAAPISTPVLTFFRAAMGCWVFEAYG 439
Cdd:PRK06188 272 -----------------------HPDLRTRDL----------SSL----ETVYYGASPMSPVRLAEAIERFGPIFAQYYG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 440 QTECTAGCSITSPGDWTAGHVGTPVSCNF------VKLEDvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLdKD 513
Cdd:PRK06188 315 QTEAPMVITYLRKRDHDPDDPKRLTSCGRptpglrVALLD-EDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-RD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 514 GWLHTGDIGRWLPNGTLKIIDRKK--------NIFklaqgeyiaPEKIENVYSRSRPILQVFVHGeslrsfligvvVPDP 585
Cdd:PRK06188 393 GWLHTGDVAREDEDGFYYIVDRKKdmivtggfNVF---------PREVEDVLAEHPAVAQVAVIG-----------VPDE 452
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
249-556 |
1.04e-29 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 123.94 E-value: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 249 DLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLkflepiFQPTPEDV----TISYLPLAHMFErlVQGVIFSC----GGK 320
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTHRNLVANLCSSL------FSVGPEMIgqvvTLGLIPFFHIYG--ITGICCATlrnkGKV 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 321 IGFFQGDIRLLPDDMKALKPTVFPTVPrllnrvydkvqneaktPLkkfLLNLaiiskfneVRNGIIrrnslwDKLVFSKI 400
Cdd:PLN02330 257 VVMSRFELRTFLNALITQEVSFAPIVP----------------PI---ILNL--------VKNPIV------EEFDLSKL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 401 qsslggKVRLMITGAAPISTPVLTFFRAAM-GCWVFEAYGQTECTagCSITSPGDWTAGH-VGTPVSCNF------VKLE 472
Cdd:PLN02330 304 ------KLQAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEHS--CITLTHGDPEKGHgIAKKNSVGFilpnleVKFI 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 473 DVADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEK 552
Cdd:PLN02330 376 DPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAE 454
|
....
gi 1958650325 553 IENV 556
Cdd:PLN02330 455 LEAI 458
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
153-555 |
2.55e-29 |
|
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: 121.78 E-value: 2.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 153 VAVPLYDTLGAEAIIYVINRADISVVICDTPqkatmlienvekdltpglktviLMDPFDDDLMKrgekCGIEMLSLhDAE 232
Cdd:cd05922 48 VFVPLNPTLKESVLRYLVADAGGRIVLADAG----------------------AADRLRDALPA----SPDPGTVL-DAD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 233 NL-GKENFKKPVPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFLEPifqpTPEDVTISYLPLAHMFERLVQ 311
Cdd:cd05922 101 GIrAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGI----TADDRALTVLPLSYDYGLSVL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 312 GVIFSCGGKIgFFQGDIRL---LPDDMKALKPTVFPTVP---RLLNRV-YDKvqneAKTPLKKFLLNLAiiSKFNEVRng 384
Cdd:cd05922 177 NTHLLRGATL-VLTNDGVLddaFWEDLREHGATGLAGVPstyAMLTRLgFDP----AKLPSLRYLTQAG--GRLPQET-- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 385 iIRRnsLWDKLVfskiqsslGGKVRLMitgaapistpvltffraamgcwvfeaYGQTECTAGCSITSPG--DWTAGHVGT 462
Cdd:cd05922 248 -IAR--LRELLP--------GAQVYVM--------------------------YGQTEATRRMTYLPPEriLEKPGSIGL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 463 PV-SCNFVKLEDvaDMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFK 541
Cdd:cd05922 291 AIpGGEFEILDD--DGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIK 368
|
410
....*....|....
gi 1958650325 542 LAqGEYIAPEKIEN 555
Cdd:cd05922 369 LF-GNRISPTEIEA 381
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
101-593 |
3.26e-29 |
|
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: 121.10 E-value: 3.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEWVISELACY----TYsmvaVPLYDTLGAEAIIYVINRADIS 176
Cdd:cd05930 13 LTYAELDARANRLARYLRERGVGP--GDLVAVLLERSLEMVVAILAVLkagaAY----VPLDPSYPAERLAYILEDSGAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 177 VVICDtpqkatmlienvekdltpglktvilmdpfdddlmkrgekcgiemlslhdaenlgkenfkkpvppnPEDLSVICFT 256
Cdd:cd05930 87 LVLTD-----------------------------------------------------------------PDDLAYVIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 257 SGTTGDPKGAMLTHQNIVSnmaaFLKFLEPIFQPTPEDVTISYLPLAH------MFERLVQG---VIFSCGGKigffqGD 327
Cdd:cd05930 102 SGSTGKPKGVMVEHRGLVN----LLLWMQEAYPLTPGDRVLQFTSFSFdvsvweIFGALLAGatlVVLPEEVR-----KD 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 328 IRLLPDDMKALKPTVFPTVPRLLNRVYDKVQNEAKTPLkkfllnlaiiskfnevrngiirrnslwdklvfskiqsslggk 407
Cdd:cd05930 173 PEALADLLAEEGITVLHLTPSLLRLLLQELELAALPSL------------------------------------------ 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 408 vRLMITGAAPISTPVLT-FFRAAMGCWVFEAYGQTECTAGCSIT--SPGDWTAGHV--GTPVSCNFVKLEDvADMNYFSV 482
Cdd:cd05930 211 -RLVLVGGEALPPDLVRrWRELLPGARLVNLYGPTEATVDATYYrvPPDDEEDGRVpiGRPIPNTRVYVLD-ENLRPVPP 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 483 NNEGEICIKGNNVFKGYLKDPEKTQEV-----LDKDGWLH-TGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENV 556
Cdd:cd05930 289 GVPGELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIELGEIEAA 367
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1958650325 557 YSRSRPILQVFV---HGESLRSFLIGVVVPDPESLPSFAA 593
Cdd:cd05930 368 LLAHPGVREAAVvarEDGDGEKRLVAYVVPDEGGELDEEE 407
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
141-584 |
2.13e-28 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 121.95 E-value: 2.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 141 VISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIcdTPQKATMLIENVEKDLT-PGLKTVILMDpfddDLMKR-G 218
Cdd:PRK08633 679 ALANLALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVI--TSRKFLEKLKNKGFDLElPENVKVIYLE----DLKAKiS 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 219 EKCGIEML---SLHDAENLGKENFKkpvPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAflkfLEPIFQPTPEDV 295
Cdd:PRK08633 753 KVDKLTALlaaRLLPARLLKRLYGP---TFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQ----ISDVFNLRNDDV 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 296 TISYLPLAHMFERLVQGVIFSCGGKIGFFQGDirllPDDMKALKPTVFptvprllnrvydkvQNEAK----TPlkKFLln 371
Cdd:PRK08633 826 ILSSLPFFHSFGLTVTLWLPLLEGIKVVYHPD----PTDALGIAKLVA--------------KHRATillgTP--TFL-- 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 372 laiiskfnevrnGIIRRNSLWDKLVFSKIqsslggkvRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECT--AGCSI 449
Cdd:PRK08633 884 ------------RLYLRNKKLHPLMFASL--------RLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSpvASVNL 943
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 450 TS---PGDWT-----AGHVGTPVSCNFVKLEDVADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVL---DKDGWLHT 518
Cdd:PRK08633 944 PDvlaADFKRqtgskEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVT 1023
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958650325 519 GDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENVysrsrpiLQVFVHGESLRsfLIGVVVPD 584
Cdd:PRK08633 1024 GDKGHLDEDGFLTITDRYSRFAKIG-GEMVPLGAVEEE-------LAKALGGEEVV--FAVTAVPD 1079
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
153-537 |
2.75e-28 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 120.45 E-value: 2.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 153 VAVPLYDTLGAEAIIYVINRADISVVICDTPQKATMLIENVEK--DLTPGLKTVILMDPFDDdlmKRGEKCGIEMLSLHD 230
Cdd:PRK07529 108 IANPINPLLEPEQIAELLRAAGAKVLVTLGPFPGTDIWQKVAEvlAALPELRTVVEVDLARY---LPGPKRLAVPLIRRK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 231 AE----NLGKENFKKPV-------PPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSN---MAAFLKFlepifqpTPEDVT 296
Cdd:PRK07529 185 AHarilDFDAELARQPGdrlfsgrPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANawlGALLLGL-------GPGDTV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 297 ISYLPLAHMFERLVQGVI-FSCGGKIGFF--QG--DIRLLPDDMK---ALKPTVFPTVPRLLNrvydkvqneaktplkkf 368
Cdd:PRK07529 258 FCGLPLFHVNALLVTGLApLARGAHVVLAtpQGyrGPGVIANFWKiveRYRINFLSGVPTVYA----------------- 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 369 llnlaiiskfnevrngiirrnSLWDKLVFSKIQSSLggkvRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCS 448
Cdd:PRK07529 321 ---------------------ALLQVPVDGHDISSL----RYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSS 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 449 ITSP-GDWTAGHVGTPV---SCNFVKLEDvaDMNYFS---VNNEGEICIKGNNVFKGYLkDPEKTQEVLDKDGWLHTGDI 521
Cdd:PRK07529 376 VNPPdGERRIGSVGLRLpyqRVRVVILDD--AGRYLRdcaVDEVGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDL 452
|
410
....*....|....*.
gi 1958650325 522 GRWLPNGTLKIIDRKK 537
Cdd:PRK07529 453 GRIDADGYFWLTGRAK 468
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
102-585 |
6.62e-28 |
|
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: 118.12 E-value: 6.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 102 SYKQVSDRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEwvisELACYtysmVAVPLydtLGA-----------EAIIYVI 170
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKP--GDRVATLAWNTHR----HLELY----YAVPG---MGAvlhtinprlfpEQIAYII 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 171 NRADISVVICDtpqkATM--LIENVEKDLtPGLKTVILMDPFDDDLMKRGEKcgiemlsLHDAENL-GKENfkkPVPPNP 247
Cdd:cd12119 94 NHAEDRVVFVD----RDFlpLLEAIAPRL-PTVEHVVVMTDDAAMPEPAGVG-------VLAYEELlAAES---PEYDWP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 248 E----DLSVICFTSGTTGDPKGAMLTHQNIVSN-MAAFLKFLEPIfqpTPEDVtisYLPLAHMFERLVQGVIFSCggkig 322
Cdd:cd12119 159 DfdenTAAAICYTSGTTGNPKGVVYSHRSLVLHaMAALLTDGLGL---SESDV---VLPVVPMFHVNAWGLPYAA----- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 323 FFQGDIRLLPDD----------MKALKPTV---FPTVPRLLnrvydkvqneaktplkkfllnlaiiskFNEVRNGIIRRN 389
Cdd:cd12119 228 AMVGAKLVLPGPyldpaslaelIEREGVTFaagVPTVWQGL---------------------------LDHLEANGRDLS 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 390 SLWdklvfskiqsslggkvRLMITGAAPISTPVLTFfrAAMGCWVFEAYGQTE-CTAGCSITSPGDWTAGHV-------- 460
Cdd:cd12119 281 SLR----------------RVVIGGSAVPRSLIEAF--EERGVRVIHAWGMTEtSPLGTVARPPSEHSNLSEdeqlalra 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 461 --GTPVSCNFVKLED----VADMNYFSVnneGEICIKGNNVFKGYLKDPEKTQEvLDKDGWLHTGDIGRWLPNGTLKIID 534
Cdd:cd12119 343 kqGRPVPGVELRIVDddgrELPWDGKAV---GELQVRGPWVTKSYYKNDEESEA-LTEDGWLRTGDVATIDEDGYLTITD 418
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1958650325 535 RKKNIFKLAqGEYIAPEKIENVYSRSRPILQVFVhgeslrsflIGvvVPDP 585
Cdd:cd12119 419 RSKDVIKSG-GEWISSVELENAIMAHPAVAEAAV---------IG--VPHP 457
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
249-570 |
1.02e-27 |
|
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: 114.52 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 249 DLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKflepIFQPTPEDVTISYLPLAHMFerlvqgvifscGGKIGFFQGDI 328
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWAD----CADLTEDDRYLIINPFFHTF-----------GYKAGIVACLL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 329 R---LLP----DDMKALKP------TVFPTVPRLLNRVYDKvqneakTPLKKFLLnlaiiskfnevrngiirrnslwdkl 395
Cdd:cd17638 66 TgatVVPvavfDVDAILEAiereriTVLPGPPTLFQSLLDH------PGRKKFDL------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 396 vfskiqSSLggkvRLMITGAAPISTPVLTFFRAAMGC-WVFEAYGQTECTAGcSITSPGD---WTAGHVGTPVSCNFVKL 471
Cdd:cd17638 115 ------SSL----RAAVTGAATVPVELVRRMRSELGFeTVLTAYGLTEAGVA-TMCRPGDdaeTVATTCGRACPGFEVRI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 472 EDvadmnyfsvnnEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPE 551
Cdd:cd17638 184 AD-----------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPA 251
|
330
....*....|....*....
gi 1958650325 552 KIENVYSRSRPILQVFVHG 570
Cdd:cd17638 252 EVEGALAEHPGVAQVAVIG 270
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
69-677 |
7.33e-27 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 117.26 E-value: 7.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 69 AKTLYEVFQRGLAVSDNGPCLGYRKPNQPYKWISYKQVSDRAEYLGSCLLHKGYKPSqdQFIGIFAQNRPEWVISELACY 148
Cdd:PTZ00297 426 VRSLGEMWERSVTRHSTFRCLGQTSESGESEWLTYGTVDARARELGSGLLALGVRPG--DVIGVDCEASRNIVILEVACA 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 149 TYSMVAVPLYDTlgAEAIIYVINRADISVVICDTPQKATMLIENVEKdltpgLKTVILMDPF---DDDLMKRgeKCGIEM 225
Cdd:PTZ00297 504 LYGFTTLPLVGK--GSTMRTLIDEHKIKVVFADRNSVAAILTCRSRK-----LETVVYTHSFydeDDHAVAR--DLNITL 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 226 LSLHDAENLGKenfKKPVPPNP--EDLSVICFTSGTTGDPKGAML-----THQNIVSNMAAFL--KFLEPIFQptpEDVT 296
Cdd:PTZ00297 575 IPYEFVEQKGR---LCPVPLKEhvTTDTVFTYVVDNTTSASGDGLavvrvTHADVLRDISTLVmtGVLPSSFK---KHLM 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 297 ISYLPLAHMFERLVQGVIFSCGGKIGffQGDIRLLPDDMKALKPTVFPTVPRLL--NRVYDKVQNEAKTPLKKFLLNLAI 374
Cdd:PTZ00297 649 VHFTPFAMLFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSLFstSRLQLSRANERYSAVYSWLFERAF 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 375 iskfnEVRNGII---RRNSLWDKLVFSK-IQSSLGGKVRLMITGAAPISTpvltffraamgcwvfeAYGQTECTAGCSit 450
Cdd:PTZ00297 727 -----QLRSRLInihRRDSSLLRFIFFRaTQELLGGCVEKIVLCVSEEST----------------SFSLLEHISVCY-- 783
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 451 spgdwtaghvgTPVSCNFvkledvadmnyFSVNNEGEICIKGN-----NVFKGYLKDPEKT----QEVLDKDGWL-HTGD 520
Cdd:PTZ00297 784 -----------VPCLREV-----------FFLPSEGVFCVDGTpapslQVDLEPFDEPSDGagigQLVLAKKGEPrRTLP 841
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 521 I-GRWLPNGTLKIIDRKKNIFKLAQGEYIAPEKIENVYSRSRPILQVFVHGESLRSfLIGVVVPDPESLP-----SFAAK 594
Cdd:PTZ00297 842 IaAQWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEfewrqSHCMG 920
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 595 IGVKGSfEELCQNQCVKKA---ILEDLQKVGKEGGLKSfEQVKSiFVHPEP--FSIENGLLTPTLKAKRVELAKFFQTQI 669
Cdd:PTZ00297 921 EGGGPA-RQLGWTELVAYAsslLTADFACIAKENGLHP-SNVPE-YVHLHPhaFKDHSTFLTPYGKIRRDAVHSYFSSVI 997
|
....*...
gi 1958650325 670 KSLYESIE 677
Cdd:PTZ00297 998 ERFYSDVE 1005
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
101-586 |
1.59e-26 |
|
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: 112.96 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKpsQDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIC 180
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVR--KGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 DTPQkatmlienvekdltpglktvilmdpfdddlmkrgekcgiemlslhdaenlgkenfkkpvppnpEDLSVICFTSGTT 260
Cdd:cd05935 80 GSEL---------------------------------------------------------------DDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 261 GDPKGAMLTHQNIVSNMAAFLKFlepiFQPTPEDVTISYLPLAHM--FERLVQGVIFSCGGKIGFFQGDIRLLPDDMKAL 338
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQSAVW----TGLTPSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMARWDRETALELIEKY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 339 KPTVFPTVPRLLNRVYDKVQNEAKTplkkfllnlaiiskfnevrngiirrnslWDKLVfskiqsSLGGkvrlmitGAAPI 418
Cdd:cd05935 173 KVTFWTNIPTMLVDLLATPEFKTRD----------------------------LSSLK------VLTG-------GGAPM 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 419 STPVLTFFRAAMGCWVFEAYGQTECTAGCSITSPGDWTAGHVGTPVSCNFVKLEDVADMNYFSVNNEGEICIKGNNVFKG 498
Cdd:cd05935 212 PPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKG 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 499 YLKDPEKTQEVLDKDG---WLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENVYSRSRPILQVFV------- 568
Cdd:cd05935 292 YWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVisvpder 370
|
490
....*....|....*...
gi 1958650325 569 HGESLRSFligvVVPDPE 586
Cdd:cd05935 371 VGEEVKAF----IVLRPE 384
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
243-606 |
7.04e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 112.43 E-value: 7.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 243 VPPNPE-DLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFLEPIFQPtpEDVTISYLPLAHMF-ERLVQGVIFSCGGK 320
Cdd:PRK06710 200 VPCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEG--EEVVLGVLPFFHVYgMTAVMNLSIMQGYK 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 321 IGFF-QGDIRLLPDDMKALKPTVFPTVPRLLNRvydkvqneaktplkkfLLNLAIISKFNevrngiirrnslwdklvfsk 399
Cdd:PRK06710 278 MVLIpKFDMKMVFEAIKKHKVTLFPGAPTIYIA----------------LLNSPLLKEYD-------------------- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 400 IQSslggkVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAgcSITSPGDW---TAGHVGTPVSCNFVKLEDVAD 476
Cdd:PRK06710 322 ISS-----IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSP--VTHSNFLWekrVPGSIGVPWPDTEAMIMSLET 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 477 MNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENV 556
Cdd:PRK06710 395 GEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREVEEV 472
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1958650325 557 YSRSRPILQVFVHGeslrsfligvvVPDP---ESLPSFAA-KIGVKGSFEELCQ 606
Cdd:PRK06710 473 LYEHEKVQEVVTIG-----------VPDPyrgETVKAFVVlKEGTECSEEELNQ 515
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
136-555 |
1.47e-25 |
|
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: 110.12 E-value: 1.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 136 NRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVICDTpqkatmlienvekdltpglktvilmdpfdddlm 215
Cdd:cd05972 34 RVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA--------------------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 216 krgekcgiemlslhdaenlgkenfkkpvppnpEDLSVICFTSGTTGDPKGAMLTHqnivSNMAAFLKFLEPIFQPTPEDV 295
Cdd:cd05972 81 --------------------------------EDPALIYFTSGTTGLPKGVLHTH----SYPLGHIPTAAYWLGLRPDDI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 296 --TIS-----YLPLAHMFERLVQGV-IFSCGGKiGFfqgDIRLLPDDMKALKPTVF---PTVPRLLNRVydkvqneaktp 364
Cdd:cd05972 125 hwNIAdpgwaKGAWSSFFGPWLLGAtVFVYEGP-RF---DAERILELLERYGVTSFcgpPTAYRMLIKQ----------- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 365 lkkfllnlaiiskfnevrngiirrnsLWDKLVFSKiqsslggkVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECT 444
Cdd:cd05972 190 --------------------------DLSSYKFSH--------LRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETG 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 445 AGCSITSPGDWTAGHVGTPVSCNFVKLEDvADMNYFSVNNEGEICIKGNNV--FKGYLKDPEKTQEVLdKDGWLHTGDIG 522
Cdd:cd05972 236 LTVGNFPDMPVKPGSMGRPTPGYDVAIID-DDGRELPPGEEGDIAIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDRA 313
|
410 420 430
....*....|....*....|....*....|...
gi 1958650325 523 RWLPNGTLKIIDRKKNIFKlAQGEYIAPEKIEN 555
Cdd:cd05972 314 YRDEDGYFWFVGRADDIIK-SSGYRIGPFEVES 345
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
102-556 |
4.68e-25 |
|
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: 108.12 E-value: 4.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 102 SYKQVSDRAEYLGSCLL-HKGYKPsqDQFIGIFAQNRPEWVISELACY----TYsmvaVPLYDTLGAEAIIYVINRADIS 176
Cdd:TIGR01733 1 TYRELDERANRLARHLRaAGGVGP--GDRVAVLLERSAELVVAILAVLkagaAY----VPLDPAYPAERLAFILEDAGAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 177 VVICDTPqkatmlienvEKDLTPGLKTVILMDPFDDDLmkrgekcgiemlsLHDAENLGkenFKKPVPPNPEDLSVICFT 256
Cdd:TIGR01733 75 LLLTDSA----------LASRLAGLVLPVILLDPLELA-------------ALDDAPAP---PPPDAPSGPDDLAYVIYT 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 257 SGTTGDPKGAMLTHQNIVSNMAAFLKFlepiFQPTPEDVTISYLPLAH---MFErlvqgvIFSCggkigFFQGDIRLLPD 333
Cdd:TIGR01733 129 SGSTGRPKGVVVTHRSLVNLLAWLARR----YGLDPDDRVLQFASLSFdasVEE------IFGA-----LLAGATLVVPP 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 334 DmKALKPTvfptvPRLLNRVYDKVQneaktplkkfllnlaiISKFNEVRngiirrnSLWDKLVFSKIQSSLGgkVRLMIT 413
Cdd:TIGR01733 194 E-DEERDD-----AALLAALIAEHP----------------VTVLNLTP-------SLLALLAAALPPALAS--LRLVIL 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 414 GAAPISTPVLTFFRAAMG-CWVFEAYGQTECTAGCSITS-PGDWTAGHV----GTPVSCNFVKLEDvADMNYFSVNNEGE 487
Cdd:TIGR01733 243 GGEALTPALVDRWRARGPgARLINLYGPTETTVWSTATLvDPDDAPRESpvpiGRPLANTRLYVLD-DDLRPVPVGVVGE 321
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958650325 488 ICIKGNNVFKGYLKDPEKTQEVL--------DKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIENV 556
Cdd:TIGR01733 322 LYIGGPGVARGYLNRPELTAERFvpdpfaggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAA 397
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
101-556 |
5.09e-25 |
|
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: 108.95 E-value: 5.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIC 180
Cdd:cd17655 23 LTYRELNERANQLARTLREKGVGP--DTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 DTPQKAtmlienvekdLTPGLKTVILMDpfDDDLMKRgekcgiemlslhDAENLgkenfkkPVPPNPEDLSVICFTSGTT 260
Cdd:cd17655 101 QSHLQP----------PIAFIGLIDLLD--EDTIYHE------------ESENL-------EPVSKSDDLAYVIYTSGST 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 261 GDPKGAMLTHQNIVSNMAAFLKFlepIFQPTPEDVtISYLPLAhmFERLVQGvIFS---CGGKIgffqgdirllpddmka 337
Cdd:cd17655 150 GKPKGVMIEHRGVVNLVEWANKV---IYQGEHLRV-ALFASIS--FDASVTE-IFAsllSGNTL---------------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 338 lkptvfptvprllnRVYDKVQNEAKTPLKKFllnlaiiskFNEVRNGIIRRNSLWDKLVfSKIQSSLGGKVRLMITGAAP 417
Cdd:cd17655 207 --------------YIVRKETVLDGQALTQY---------IRQNRITIIDLTPAHLKLL-DAADDSEGLSLKHLIVGGEA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 418 ISTPVLTFF--RAAMGCWVFEAYGQTECTAGCSI--TSPGDWTAGHV--GTPVSCNFVKLEDvADMNYFSVNNEGEICIK 491
Cdd:cd17655 263 LSTELAKKIieLFGTNPTITNAYGPTETTVDASIyqYEPETDQQVSVpiGKPLGNTRIYILD-QYGRPQPVGVAGELYIG 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958650325 492 GNNVFKGYLKDPEKTQEVLDKDGWL------HTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIENV 556
Cdd:cd17655 342 GEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-RGYRIELGEIEAR 411
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
77-604 |
5.16e-25 |
|
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: 108.93 E-value: 5.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 77 QRGLAVSDNGPCLGYRKPnqpykWISYKQVSDRAEYLGSCLLHKGYKPSQdqFIGIFAQNRPEWVISELACYTYSMVAVP 156
Cdd:cd12118 11 ERAAAVYPDRTSIVYGDR-----RYTWRQTYDRCRRLASALAALGISRGD--TVAVLAPNTPAMYELHFGVPMAGAVLNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 157 LYDTLGAEAIIYVINRADISVVICDTPqkatmlienvekdltpglktvilmdpFD-DDLMKRGEKcgiemlslhdaenlg 235
Cdd:cd12118 84 LNTRLDAEEIAFILRHSEAKVLFVDRE--------------------------FEyEDLLAEGDP--------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 236 keNFKkPVPPNPE-DLSVICFTSGTTGDPKGAMLTHQ----NIVSNMAAFLKFLEPIFQPTpedvtisyLPLAHM----F 306
Cdd:cd12118 123 --DFE-WIPPADEwDPIALNYTSGTTGRPKGVVYHHRgaylNALANILEWEMKQHPVYLWT--------LPMFHCngwcF 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 307 erlVQGVIFSCGGKIGFFQGDIRLLPDDMKALKPTVFPTVPRLLNrvydkvqneaktplkkFLLNLAiiskfnevrngii 386
Cdd:cd12118 192 ---PWTVAAVGGTNVCLRKVDAKAIYDLIEKHKVTHFCGAPTVLN----------------MLANAP------------- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 387 rrnslwdklvfSKIQSSLGGKVRLMITGAAPistPVLTFFRA-AMGCWVFEAYGQTEcTAGCSITSPgdWTAGHVGTPVS 465
Cdd:cd12118 240 -----------PSDARPLPHRVHVMTAGAPP---PAAVLAKMeELGFDVTHVYGLTE-TYGPATVCA--WKPEWDELPTE 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 466 ----------CNFVKLE--DVADMNYF-SVNNE----GEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNG 528
Cdd:cd12118 303 erarlkarqgVRYVGLEevDVLDPETMkPVPRDgktiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDG 381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 529 TLKIIDRKKNIFkLAQGEYIAPEKIENVYSRSRPILQVFVhgeslrsfligVVVPDP---ESLPSFAA-KIGVKGSFEEL 604
Cdd:cd12118 382 YIEIKDRSKDII-ISGGENISSVEVEGVLYKHPAVLEAAV-----------VARPDEkwgEVPCAFVElKEGAKVTEEEI 449
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
249-665 |
9.57e-25 |
|
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: 105.49 E-value: 9.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 249 DLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFLepifQPTPEDVTISYLPLAHM--FERLVQGVIfsCGGKIGFFQG 326
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRL----GFGGGDSWLLSLPLYHVggLAILVRSLL--AGAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 327 DiRLLPDDMKALKPTVFPTVPRLLNRVYDKVQNEAktPLKKFllnlaiiskfnevrngiirrnslwdKLVFSkiqsslgg 406
Cdd:cd17630 75 N-QALAEDLAPPGVTHVSLVPTQLQRLLDSGQGPA--ALKSL-------------------------RAVLL-------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 407 kvrlmitGAAPISTPVLTFFrAAMGCWVFEAYGQTEcTAGCSITS-PGDWTAGHVGTPvscnfvkLEDVAdmnyFSVNNE 485
Cdd:cd17630 119 -------GGAPIPPELLERA-ADRGIPLYTTYGMTE-TASQVATKrPDGFGRGGVGVL-------LPGRE----LRIVED 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 486 GEICIKGNNVFKGYLKDPEktQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENVYSRSRPILQ 565
Cdd:cd17630 179 GEIWVGGASLAMGYLRGQL--VPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAVRD 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 566 VFVHGESLRSF---LIGVVVPDPESLPsfaakigvkgsfEELcqNQCVKkailedlqkvgkeGGLKSFEQVKSIFVHPEP 642
Cdd:cd17630 256 AFVVGVPDEELgqrPVAVIVGRGPADP------------AEL--RAWLK-------------DKLARFKLPKRIYPVPEL 308
|
410 420
....*....|....*....|...
gi 1958650325 643 fsiengLLTPTLKAKRVELAKFF 665
Cdd:cd17630 309 ------PRTGGGKVDRRALRAWL 325
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
80-586 |
1.64e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 108.12 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 80 LAVSDNgpclgyRKPNQPYKW-----ISYKQVSDRAEYLGSCLLHK-GYKPSqDQfIGIFAQNRPEWVISELACYTYSMV 153
Cdd:PRK08314 16 LEVSAR------RYPDKTAIVfygraISYRELLEEAERLAGYLQQEcGVRKG-DR-VLLYMQNSPQFVIAYYAILRANAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 154 AVPLYDTLGAEAIIYVINRADISVVICdtpqkATMLIENVEKDL-TPGLKTVIL---MDPFDDD--------LMKRGEKC 221
Cdd:PRK08314 88 VVPVNPMNREEELAHYVTDSGARVAIV-----GSELAPKVAPAVgNLRLRHVIVaqySDYLPAEpeiavpawLRAEPPLQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 222 GIEMLSLHD-AENLGKENFKKPVPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFlepiFQPTPEDVTISYL 300
Cdd:PRK08314 163 ALAPGGVVAwKEALAAGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLW----SNSTPESVVLAVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 301 PLAHmferlVQGVIFSCGGKIgFFQGDIRLLPD-DMKAlkptvfptVPRLLNRVYDKVQNEAKTPLKKFLLNlaiiskfn 379
Cdd:PRK08314 239 PLFH-----VTGMVHSMNAPI-YAGATVVLMPRwDREA--------AARLIERYRVTHWTNIPTMVVDFLAS-------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 380 evrNGIIRRN--SLWdklvfskiqsSLGGkvrlmitGAAPISTPVLTFFRAAMGCWVFEAYGQTEcTAGCSITSPGDWTA 457
Cdd:PRK08314 297 ---PGLAERDlsSLR----------YIGG-------GGAAMPEAVAERLKELTGLDYVEGYGLTE-TMAQTHSNPPDRPK 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 458 -GHVGTPV------SCNFVKLEDVAdmnyfsVNNEGEICIKGNNVFKGYLKDPEKTQEV---LDKDGWLHTGDIGRWLPN 527
Cdd:PRK08314 356 lQCLGIPTfgvdarVIDPETLEELP------PGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEE 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958650325 528 GTLKIIDRKKNIFKlAQGEYIAPEKIENVYSRSRPILQVFV-------HGESLRSfligVVVPDPE 586
Cdd:PRK08314 430 GYFFITDRLKRMIN-ASGFKVWPAEVENLLYKHPAIQEACViatpdprRGETVKA----VVVLRPE 490
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
244-595 |
2.55e-24 |
|
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: 106.24 E-value: 2.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 244 PPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSnmaaFLKFLEPIFQPTPEDVTISYLPLAhmFERLVqGVIFS--CGGKI 321
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLN----YVSQPPARLDVGPGSRVAQVLSIA--FDACI-GEIFStlCNGGT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 322 GFFQGDIRLLPDDMKALkpTVFPTVPRLLnrvydkvqneaktplkkfllnlaiiskfnevrnGIIRRNSLwdklvfskiq 401
Cdd:cd17653 174 LVLADPSDPFAHVARTV--DALMSTPSIL---------------------------------STLSPQDF---------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 402 sslgGKVRLMITGAAPISTPVLTffRAAMGCWVFEAYGQTECTAGCSITSPGDWTAGHVGTPVSCNFVKLEDvADMNYFS 481
Cdd:cd17653 209 ----PNLKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTCYILD-ADLQPVP 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 482 VNNEGEICIKGNNVFKGYLKDPEKTQE----VLDKDGWLH--TGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIEN 555
Cdd:cd17653 282 EGVVGEICISGVQVARGYLGNPALTASkfvpDPFWPGSRMyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEIEE 360
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1958650325 556 VYSRSRPILQ---VFVHGEslrsFLIGVVVP---DPESLPSFAAKI 595
Cdd:cd17653 361 VVLQSQPEVTqaaAIVVNG----RLVAFVTPetvDVDGLRSELAKH 402
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
101-530 |
6.14e-24 |
|
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: 108.02 E-value: 6.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEWVISELA------CYtysmvaVPLYDTLGAEAIIYVINRAD 174
Cdd:COG1020 502 LTYAELNARANRLAHHLRALGVGP--GDLVGVCLERSLEMVVALLAvlkagaAY------VPLDPAYPAERLAYMLEDAG 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 175 ISVVICDTPQKATMLIENVEkdltpglktVILMDPfdddlmkrgekcgiEMLSLHDAENLgkenfkkPVPPNPEDLSVIC 254
Cdd:COG1020 574 ARLVLTQSALAARLPELGVP---------VLALDA--------------LALAAEPATNP-------PVPVTPDDLAYVI 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 255 FTSGTTGDPKGAMLTHQNIVSNMAAFLKFlepiFQPTPEDVTISYLPLAH---MFErlvqgvIFS---CGGKIGFFQGDI 328
Cdd:COG1020 624 YTSGSTGRPKGVMVEHRALVNLLAWMQRR----YGLGPGDRVLQFASLSFdasVWE------IFGallSGATLVLAPPEA 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 329 RLLPDDMKAL----KPTVFPTVPrllnrvydkvqneaktplkkfllnlaiiskfnevrngiirrnSLWDKLVFSKIQSSL 404
Cdd:COG1020 694 RRDPAALAELlarhRVTVLNLTP------------------------------------------SLLRALLDAAPEALP 731
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 405 GgkVRLMITG--AAPISTpVLTFFRAAMGCWVFEAYGQTECTAGCSI--TSPGDWTAGHV--GTPVScN---FV---KLE 472
Cdd:COG1020 732 S--LRLVLVGgeALPPEL-VRRWRARLPGARLVNLYGPTETTVDSTYyeVTPPDADGGSVpiGRPIA-NtrvYVldaHLQ 807
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958650325 473 DVAdmnyfsVNNEGEICIKGNNVFKGYLKDPEKTQEV-----LDKDG--WLHTGDIGRWLPNGTL 530
Cdd:COG1020 808 PVP------VGVPGELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNL 866
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
191-556 |
1.05e-23 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 105.69 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 191 ENVEKDLTPGLKTVILMDPFDDDlMKRGEKCGIEMLSLHDAENLgkenfkkPVPP-NPEDLSVICFTSGTTGDPKGAMLT 269
Cdd:PLN02574 148 ENVEKLSPLGVPVIGVPENYDFD-SKRIEFPKFYELIKEDFDFV-------PKPViKQDDVAAIMYSSGTTGASKGVVLT 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 270 HQNIVSNMAAFLKFLEPIFQ-PTPEDVTISYLPLAHMF--ERLVQGVIfSCGGKIGFFQgdiRLLPDDM-KAL---KPTV 342
Cdd:PLN02574 220 HRNLIAMVELFVRFEASQYEyPGSDNVYLAALPMFHIYglSLFVVGLL-SLGSTIVVMR---RFDASDMvKVIdrfKVTH 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 343 FPTVPRLLNRVYDKVQNEAKTPLKKfllnlaiiskfnevrngiirrnslwdklvfskiqsslggkVRLMITGAAPISTPV 422
Cdd:PLN02574 296 FPVVPPILMALTKKAKGVCGEVLKS----------------------------------------LKQVSCGAAPLSGKF 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 423 LTFFRAAMGCWVF-EAYGQTECTA----GCSITSPGDWTAghVGTPVSCNFVKLEDVADMNYFSVNNEGEICIKGNNVFK 497
Cdd:PLN02574 336 IQDFVQTLPHVDFiQGYGMTESTAvgtrGFNTEKLSKYSS--VGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMK 413
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958650325 498 GYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIENV 556
Cdd:PLN02574 414 GYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQIAPADLEAV 471
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
245-593 |
1.31e-23 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 105.14 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 245 PNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFLEPifqpTPEDVTISYLPLAHMferlvqgvifscggkIGFF 324
Cdd:PRK13295 194 PGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGL----GADDVILMASPMAHQ---------------TGFM 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 325 QGdiRLLPDDMKA---LKPTVFPTvprllnRVYDKVQNE------AKTPlkkFLLNLAiiskfNEVRNGiiRRNSlwdkl 395
Cdd:PRK13295 255 YG--LMMPVMLGAtavLQDIWDPA------RAAELIRTEgvtftmASTP---FLTDLT-----RAVKES--GRPV----- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 396 vfskiqSSLggkvRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAgCSITSPGD---WTAGHVGTPVSCNFVKLE 472
Cdd:PRK13295 312 ------SSL----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA-VTLTKLDDpdeRASTTDGCPLPGVEVRVV 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 473 DvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEvlDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEK 552
Cdd:PRK13295 381 D-ADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGT--DADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVE 456
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1958650325 553 IENVYSRSRPILQVFVHG---ESLRSFLIGVVVPDPESLPSFAA 593
Cdd:PRK13295 457 IEALLYRHPAIAQVAIVAypdERLGERACAFVVPRPGQSLDFEE 500
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
99-572 |
1.39e-23 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 104.66 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 99 KWISYKQVSDRAEYLGSCLLHKGYKpsQDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVV 178
Cdd:PRK03640 26 KKVTFMELHEAVVSVAGKLAALGVK--KGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 179 ICDtpqkatmlienvekdltpglktvilmDPFDDDLmkrgeKCGIEMlslhDAENLGKENFKKPVPPNPEDLS---VICF 255
Cdd:PRK03640 104 ITD--------------------------DDFEAKL-----IPGISV----KFAELMNGPKEEAEIQEEFDLDevaTIMY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 256 TSGTTGDPKGAMLTHQN-IVSNMAAFLKF-LepifqpTPEDVTISYLPLAHM--FERLVQGVIFSCggkigffqgDIRLL 331
Cdd:PRK03640 149 TSGTTGKPKGVIQTYGNhWWSAVGSALNLgL------TEDDCWLAAVPIFHIsgLSILMRSVIYGM---------RVVLV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 332 P--------DDMKALKPTVFPTVPRLLNRVYDKVQNEaktplkkfllnlaiiskfnevrngiiRRNSlwdklvfskiqss 403
Cdd:PRK03640 214 EkfdaekinKLLQTGGVTIISVVSTMLQRLLERLGEG--------------------------TYPS------------- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 404 lggKVRLMITGAAPISTPVLTFFRAAmGCWVFEAYGQTEcTAGCSITSPGDWTA---GHVGTPVSCNFVKLEDvaDMNYF 480
Cdd:PRK03640 255 ---SFRCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLFPCELKIEK--DGVVV 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 481 SVNNEGEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENVYSRS 560
Cdd:PRK03640 328 PPFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSH 405
|
490
....*....|..
gi 1958650325 561 RPILQVFVHGES 572
Cdd:PRK03640 406 PGVAEAGVVGVP 417
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
102-556 |
2.10e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 104.63 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 102 SYKQVSDRAEYLGSCLLHKGYKPSqDQfIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVICD 181
Cdd:PRK08316 38 TYAELDAAVNRVAAALLDLGLKKG-DR-VAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 182 TPqkatmLIENVEKDL-TPGLKTVILMDPFDDDLMKRGEKCGIEMLSLHDAENLGkenfkkpVPPNPEDLSVICFTSGTT 260
Cdd:PRK08316 116 PA-----LAPTAEAALaLLPVDTLILSLVLGGREAPGGWLDFADWAEAGSVAEPD-------VELADDDLAQILYTSGTE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 261 GDPKGAMLTHQNI----VSNMAAfLKFlepifqpTPEDVTISYLPLAHMFERLV-QGVIFSCGGKIGFFQG-DIRLLPDD 334
Cdd:PRK08316 184 SLPKGAMLTHRALiaeyVSCIVA-GDM-------SADDIPLHALPLYHCAQLDVfLGPYLYVGATNVILDApDPELILRT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 335 MKALKPTVF---PTV-PRLLNR-VYDKVqneaktplkkfllNLaiiskfnevrngiirrnslwdklvfskiqSSLggkvR 409
Cdd:PRK08316 256 IEAERITSFfapPTVwISLLRHpDFDTR-------------DL-----------------------------SSL----R 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 410 LMITGAAPISTPVLTFFRAAM-GCWVFEAYGQTECTAGCSITSPGDwtagHVGTPVSCN----FV--KLEDvADMNYFSV 482
Cdd:PRK08316 290 KGYYGASIMPVEVLKELRERLpGLRFYNCYGQTEIAPLATVLGPEE----HLRRPGSAGrpvlNVetRVVD-DDGNDVAP 364
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958650325 483 NNEGEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENV 556
Cdd:PRK08316 365 GEVGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEA 436
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
100-593 |
2.12e-23 |
|
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: 103.91 E-value: 2.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 100 WISYKQVSDRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVI 179
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGVGP--GDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 180 CDTPqkatmlienvekdltpglktviLMDPFDDDLMkrgekcgIEMLSLHDAENLGKEnfkKPVPPNPEDLSVICFTSGT 259
Cdd:cd12116 90 TDDA----------------------LPDRLPAGLP-------VLLLALAAAAAAPAA---PRTPVSPDDLAYVIYTSGS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 260 TGDPKGAMLTHQNIVSnmaaFLKFLEPIFQPTPED----VT-----IS----YLPLahmferlvqgvifSCGGKIGFFQG 326
Cdd:cd12116 138 TGRPKGVVVSHRNLVN----FLHSMRERLGLGPGDrllaVTtyafdISllelLLPL-------------LAGARVVIAPR 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 327 DIRLLPDDMKALKPTVFPTVprllnrvydkVQneaKTPlkkfllnlaiiskfnevrngiirrnSLWdKLVFSKIQSSLGG 406
Cdd:cd12116 201 ETQRDPEALARLIEAHSITV----------MQ---ATP-------------------------ATW-RMLLDAGWQGRAG 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 407 kVRLMITGAA-PistPVLTFFRAAMGCWVFEAYGQTECT--AGCSITSPGDwTAGHVGTPVSCNFVKLEDvADMNYFSVN 483
Cdd:cd12116 242 -LTALCGGEAlP---PDLAARLLSRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLD-AALRPVPPG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 484 NEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLH-------TGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIENV 556
Cdd:cd12116 316 VPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQVKI-RGHRIELGEIEAA 394
|
490 500 510
....*....|....*....|....*....|....*....
gi 1958650325 557 YSRSRPILQ--VFVHGESLRSFLIGVVVPDPESLPSFAA 593
Cdd:cd12116 395 LAAHPGVAQaaVVVREDGGDRRLVAYVVLKAGAAPDAAA 433
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
245-556 |
2.88e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 103.53 E-value: 2.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 245 PNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAflkfLEPIFQPTPEDVTISYLPLAHMfERLVQGVIFSC--GGKig 322
Cdd:PRK07787 125 PDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDA----LAEAWQWTADDVLVHGLPLFHV-HGLVLGVLGPLriGNR-- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 323 fFQGDIRLLPD---DMKALKPTVFPTVPRLLNRVYDkVQNEAKtplkkfllnlaiiskfnevrngiirrnslwdklvfsk 399
Cdd:PRK07787 198 -FVHTGRPTPEayaQALSEGGTLYFGVPTVWSRIAA-DPEAAR------------------------------------- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 400 iqsSLGGkVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCSITSPGDWTAGHVGTPVSCNFVKLEDVaDMNY 479
Cdd:PRK07787 239 ---ALRG-ARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDE-DGGP 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 480 FSVNNE--GEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDR------KKNIFKLAQGEyiape 551
Cdd:PRK07787 314 VPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGGYRIGAGE----- 388
|
....*
gi 1958650325 552 kIENV 556
Cdd:PRK07787 389 -IETA 392
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
101-587 |
4.61e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 103.70 E-value: 4.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPSqDQFIgIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIC 180
Cdd:PRK07786 43 TTWRELDDRVAALAGALSRRGVGFG-DRVL-ILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 DTPqkATMLIENVeKDLTPGLKTVILM-DPFDDDLMkrgekcgiemlslhDAENLGKENFKKPVPPN-PEDL-SVICFTS 257
Cdd:PRK07786 121 EAA--LAPVATAV-RDIVPLLSTVVVAgGSSDDSVL--------------GYEDLLAEAGPAHAPVDiPNDSpALIMYTS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 258 GTTGDPKGAMLTHQNIVSNMAAFLKFLEpifQPTPEDVTISYLPLAHmferlvqgvIFSCGGKIGFFQGDIRLLPDDMKA 337
Cdd:PRK07786 184 GTTGRPKGAVLTHANLTGQAMTCLRTNG---ADINSDVGFVGVPLFH---------IAGIGSMLPGLLLGAPTVIYPLGA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 338 LKPTvfptvprllnRVYDKVQNEAKTplkkfllnlaiiskfnevrnGIIRRNSLWDKLVFSKIQSSLGGKVRLMITGAAP 417
Cdd:PRK07786 252 FDPG----------QLLDVLEAEKVT--------------------GIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 418 ISTPVL-----TFFRAAmgcwVFEAYGQTECTAGCSITSPGDWTA--GHVGTPVSCNFVKLEDvADMNYFSVNNEGEICI 490
Cdd:PRK07786 302 ASDTLLrqmaaTFPEAQ----ILAAFGQTEMSPVTCMLLGEDAIRklGSVGKVIPTVAARVVD-ENMNDVPVGEVGEIVY 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 491 KGNNVFKGYLKDPEKTQEVLDkDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENVYSRSRPILQVFVHG 570
Cdd:PRK07786 377 RAPTLMSGYWNNPEATAEAFA-GGWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPDIVEVAVIG 454
|
490 500
....*....|....*....|
gi 1958650325 571 ESLRSF---LIGVVVPDPES 587
Cdd:PRK07786 455 RADEKWgevPVAVAAVRNDD 474
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
248-557 |
5.12e-23 |
|
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: 102.04 E-value: 5.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 248 EDLSVICFTSGTTGDPKGAMLTHQNI-------VSNMAAflkflepifqpTPEDVTISYLPLAHM--FERLVQGVIFSCG 318
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNHwwsaigsALNLGL-----------TEDDNWLCALPLFHIsgLSILMRSVIYGMT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 319 GKI--GFfqgDIRLLPDDMKALKPTVFPTVPRLLNRvydkvqneaktplkkfllnlaIISKFNEVRNgiirrNSLwdklv 396
Cdd:cd05912 146 VYLvdKF---DAEQVLHLINSGKVTIISVVPTMLQR---------------------LLEILGEGYP-----NNL----- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 397 fskiqsslggkvRLMITGAAPISTPVLTFFRAaMGCWVFEAYGQTEcTAGCSIT-SPGDWTA--GHVGTPVSCNFVKLED 473
Cdd:cd05912 192 ------------RCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTE-TCSQIVTlSPEDALNkiGSAGKPLFPVELKIED 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 474 vadmNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKI 553
Cdd:cd05912 258 ----DGQPPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEI 331
|
....
gi 1958650325 554 ENVY 557
Cdd:cd05912 332 EEVL 335
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
246-588 |
1.32e-22 |
|
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: 101.47 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 246 NPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKflepIFQPTPEDVTI---SYLPLAHMFErlvqgvIF---SCGG 319
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGR----ALGLTSESRVLqfaSYTFDVSILE------IFttlAAGG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 320 KIGFFQGDIRL--LPDDMKALKPT-VF--PTVPRLLNRvydkvqneAKTPLKKFLLnLAiiskfNE-VRNGIIRRnslWd 393
Cdd:cd05918 174 CLCIPSEEDRLndLAGFINRLRVTwAFltPSVARLLDP--------EDVPSLRTLV-LG-----GEaLTQSDVDT---W- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 394 klvfskiqsslGGKVRLMItgaapistpvltffraamgcwvfeAYGQTECTAGCSITSPG-DWTAGHVGTPVSCNF--Vk 470
Cdd:cd05918 236 -----------ADRVRLIN------------------------AYGPAECTIAATVSPVVpSTDPRNIGRPLGATCwvV- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 471 leDVADMNYFS-VNNEGEICIKGNNVFKGYLKDPEKTQEVLDKD-GWLH------------TGDIGRWLPNGTLKIIDRK 536
Cdd:cd05918 280 --DPDNHDRLVpIGAVGELLIEGPILARGYLNDPEKTAAAFIEDpAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRK 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958650325 537 KNIFKLaQGEYIAPEKIENVYSRSRP-----ILQVFVH-GESLRSFLIGVVVPDPESL 588
Cdd:cd05918 358 DTQVKI-RGQRVELGEIEHHLRQSLPgakevVVEVVKPkDGSSSPQLVAFVVLDGSSS 414
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
99-586 |
5.45e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 99.88 E-value: 5.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 99 KWiSYKQVSDRAEYLGSCLLHKGYKPSQDqfIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVV 178
Cdd:PRK09088 22 RW-TYAELDALVGRLAAVLRRRGCVDGER--LAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 179 IcdtpqkatmlienvekdltpglktvilmdpfDDDLMKRGEKCGIEMLSLHDAENLGKENFKKPVPPnpEDLSVICFTSG 258
Cdd:PRK09088 99 L-------------------------------GDDAVAAGRTDVEDLAAFIASADALEPADTPSIPP--ERVSLILFTSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 259 TTGDPKGAMLTHQNIVSNMAAFLKFlepifqpTPEDVTISYLPLAHMFErlVQGVIFSC------GGKI----GFFQG-D 327
Cdd:PRK09088 146 TSGQPKGVMLSERNLQQTAHNFGVL-------GRVDAHSSFLCDAPMFH--IIGLITSVrpvlavGGSIlvsnGFEPKrT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 328 IRLLPDdmKALKPTVFPTVPRLLNRvydkvqneaktplkkfllnlaiiskfnevrngiIRRNSLWDKlvfskiqSSLGgK 407
Cdd:PRK09088 217 LGRLGD--PALGITHYFCVPQMAQA---------------------------------FRAQPGFDA-------AALR-H 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 408 VRLMITGAAPISTPVLTFFRAAmGCWVFEAYGQTEctAGCSITSPGDWT-----AGHVGTPVSCNFVKLEDvADMNYFSV 482
Cdd:PRK09088 254 LTALFTGGAPHAAEDILGWLDD-GIPMVDGFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVVD-DQGNDCPA 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 483 NNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENVYSRSRP 562
Cdd:PRK09088 330 GVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIEAVLADHPG 408
|
490 500
....*....|....*....|....
gi 1958650325 563 ILQVFVHGeslrsfligvvVPDPE 586
Cdd:PRK09088 409 IRECAVVG-----------MADAQ 421
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
247-554 |
1.85e-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: 341266 [Multi-domain] Cd Length: 359 Bit Score: 96.40 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 247 PEDLSVICFTSGTTGDPKGAMLTHQNIVSN---MAAFLKFlepifqpTPEDVTISYLPLAHMFERLVQGVIFscggkigF 323
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNawmLALNSLF-------DPDDVLLCGLPLFHVNGSVVTLLTP-------L 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 324 FQGDIRLLPDDMKALKPTVFPTVPRLLNRVydKVQNEAKTPlkkfllnlAIISKFNEVRNGiirrnslwdklvfSKIqSS 403
Cdd:cd05944 67 ASGAHVVLAGPAGYRNPGLFDNFWKLVERY--RITSLSTVP--------TVYAALLQVPVN-------------ADI-SS 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 404 LggkvRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCSITSP-GDWTAGHVGTPVSCNFVKL--EDvADMNYF 480
Cdd:cd05944 123 L----RFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIkvLD-GVGRLL 197
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958650325 481 ---SVNNEGEICIKGNNVFKGYLKDpEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIE 554
Cdd:cd05944 198 rdcAPDEVGEICVAGPGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIE 272
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
68-537 |
1.96e-20 |
|
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: 95.43 E-value: 1.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 68 DAKTLYEVFQRglAVSdNGPCLG--YRKPNQPYKWISYKQVSDRAEYLGSCLLHKGYKPsQDQFIGIFAQNRpEWVISEL 145
Cdd:cd05906 8 APRTLLELLLR--AAE-RGPTKGitYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRP-GDSVILQFDDNE-DFIPAFW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 146 ACYTYSMVAVPLydtlgAEAIIYvinradisvvicDTPQKATMLIENVEKDLTpglKTVILMDP-FDDDLMKRGEKCGIE 224
Cdd:cd05906 83 ACVLAGFVPAPL-----TVPPTY------------DEPNARLRKLRHIWQLLG---SPVVLTDAeLVAEFAGLETLSGLP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 225 MLSLHDAENLGKENFKKPVPP-NPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAflkfLEPIFQPTPEDVTISYLPLA 303
Cdd:cd05906 143 GIRVLSIEELLDTAADHDLPQsRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG----KIQHNGLTPQDVFLNWVPLD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 304 HmferlVQGVIFscggkIGFFqgDIRLLPDDMKALKPTVFPTVPRLLNRVyDKVQnEAKTPLKKFLLNLaiiskfneVRN 383
Cdd:cd05906 219 H-----VGGLVE-----LHLR--AVYLGCQQVHVPTEEILADPLRWLDLI-DRYR-VTITWAPNFAFAL--------LND 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 384 GIIRRNSL-WDklvfskiQSSLggkvRLMITGAAPISTPVL--------------TFFRAAmgcwvfeaYGQTECTAGCS 448
Cdd:cd05906 277 LLEEIEDGtWD-------LSSL----RYLVNAGEAVVAKTIrrllrllepyglppDAIRPA--------FGMTETCSGVI 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 449 ITSP---GDWTAGH----VGTP---VSCNFVKLEDvadmNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHT 518
Cdd:cd05906 338 YSRSfptYDHSQALefvsLGRPipgVSMRIVDDEG----QLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRT 413
|
490
....*....|....*....
gi 1958650325 519 GDIGrWLPNGTLKIIDRKK 537
Cdd:cd05906 414 GDLG-FLDNGNLTITGRTK 431
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
247-586 |
3.11e-20 |
|
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: 93.85 E-value: 3.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 247 PEDLSVICFTSGTTGDPKGAMLTHQNIVSnmaaFLKFLEPIFQPTPEDVTISYLPLA---HMFErlvqgvIF---SCGGK 320
Cdd:cd05945 96 GDDNAYIIFTSGSTGRPKGVQISHDNLVS----FTNWMLSDFPLGPGDVFLNQAPFSfdlSVMD------LYpalASGAT 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 321 IgffqgdiRLLPDDMKALKPTVFPTVPRL-LNRVYdkvqneaKTPlkkfllnlaiiskfnevrngiirrnSLWDKLVFSK 399
Cdd:cd05945 166 L-------VPVPRDATADPKQLFRFLAEHgITVWV-------STP-------------------------SFAAMCLLSP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 400 --IQSSLGGkVRLMITGAAPISTPVL-TFFRAAMGCWVFEAYGQTECTAGCSITspgDWT----AGH----VGTPVSCNF 468
Cdd:cd05945 207 tfTPESLPS-LRHFLFCGEVLPHKTArALQQRFPDARIYNTYGPTEATVAVTYI---EVTpevlDGYdrlpIGYAKPGAK 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 469 VKLEDvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKD---GWLHTGDIGRWLPNGTLKIIDRKKNIFKLaQG 545
Cdd:cd05945 283 LVILD-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NG 360
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1958650325 546 EYIAPEKIENVYSRSRPILQVFV----HGESlRSFLIGVVVPDPE 586
Cdd:cd05945 361 YRIELEEIEAALRQVPGVKEAVVvpkyKGEK-VTELIAFVVPKPG 404
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
95-564 |
3.53e-20 |
|
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: 94.48 E-value: 3.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 95 NQPYKWISYKQVSDRA-EYLGScLLHKGYKPSQDQFIGIfaQNRPEWVISELACYTYSMVAVPlydtlgaeaiiyvinra 173
Cdd:cd05908 10 DKKEKFVSYRHLREEAlGYLGA-LQELGIKPGQEVVFQI--THNNKFLYLFWACLLGGMIAVP----------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 174 dISVVICDTPQKATMLIENvekdltpglktvILMDPF---DDDLMKRgekcgiemlslhdaenlgkenfkkpvppNPEDL 250
Cdd:cd05908 70 -VSIGSNEEHKLKLNKVWN------------TLKNPYlitEEEVLCE----------------------------LADEL 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 251 SVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFLEpifqPTPEDVTISYLPLAHmferlvqgvifscggKIGFFQGDIRL 330
Cdd:cd05908 109 AFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTE----WKTKDRILSWMPLTH---------------DMGLIAFHLAP 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 331 LPDDMKA-LKPT-VFPTVPRL-LNRVYDKVQNEAKTP--LKKFLLNLAIISKFNEvrngiirrnslWDklvfskiQSSlg 405
Cdd:cd05908 170 LIAGMNQyLMPTrLFIRRPILwLKKASEHKATIVSSPnfGYKYFLKTLKPEKAND-----------WD-------LSS-- 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 406 gkVRLMITGAAPISTPVLTFFRAAMGCW------VFEAYGQTECTAGCSI----------------------------TS 451
Cdd:cd05908 230 --IRMILNGAEPIDYELCHEFLDHMSKYglkrnaILPVYGLAEASVGASLpkaqspfktitlgrrhvthgepepevdkKD 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 452 PGDWTAGHVGTPVSCNFVKLEDVADmNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGrWLPNGTLK 531
Cdd:cd05908 308 SECLTFVEVGKPIDETDIRICDEDN-KILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIRNGRLV 385
|
490 500 510
....*....|....*....|....*....|...
gi 1958650325 532 IIDRKKNIFkLAQGEYIAPEKIENVYSRSRPIL 564
Cdd:cd05908 386 ITGREKDII-FVNGQNVYPHDIERIAEELEGVE 417
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
101-588 |
3.58e-20 |
|
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: 94.11 E-value: 3.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADI-SVVI 179
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRP--GQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMtAAVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 180 CDtpqkatmlienvEKDLTPGLKTVILMDPFDDDLMKRGEkcgiemlslhdAENLGKEnFKKPvPPNPEDLSVICFTSGT 259
Cdd:cd05923 107 AV------------DAQVMDAIFQSGVRVLALSDLVGLGE-----------PESAGPL-IEDP-PREPEQPAFVFYTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 260 TGDPKGAMLTHQNIVSNMAAFLKFLEPIFqpTPEDVTISYLPLAHMferlvqgvifscggkIGFFQgdirLLpddMKALK 339
Cdd:cd05923 162 TGLPKGAVIPQRAAESRVLFMSTQAGLRH--GRHNVVLGLMPLYHV---------------IGFFA----VL---VAALA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 340 PTVFPTVPRllnrvYDKVQNEaktplkkfllnLAIISKfnEVRNGIIRRNSLWDKLVFSKIQSSLGGK-VRLMITGAAPI 418
Cdd:cd05923 218 LDGTYVVVE-----EFDPADA-----------LKLIEQ--ERVTSLFATPTHLDALAAAAEFAGLKLSsLRHVTFAGATM 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 419 STPVLTFFRAAMGCWVFEAYGQTEctAGCSITSPgDWTAGHVGTPVSCNFVKLEDV--ADMNYFSVNNEGEICIK--GNN 494
Cdd:cd05923 280 PDAVLERVNQHLPGEKVNIYGTTE--AMNSLYMR-DARTGTEMRPGFFSEVRIVRIggSPDEALANGEEGELIVAaaADA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 495 VFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENVYSRSRPILQVFVHG---E 571
Cdd:cd05923 357 AFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIGvadE 434
|
490
....*....|....*..
gi 1958650325 572 SLRSFLIGVVVPDPESL 588
Cdd:cd05923 435 RWGQSVTACVVPREGTL 451
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
153-612 |
4.79e-20 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 93.98 E-value: 4.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 153 VAVPLYDTLGAEAIIYVINRADISVVICdTPQKATMLIENVEKDLTPgLKTVILMDPFDDDLmkRGEKCGIEMLSLHDAE 232
Cdd:PRK08008 88 IMVPINARLLREESAWILQNSQASLLVT-SAQFYPMYRQIQQEDATP-LRHICLTRVALPAD--DGVSSFTQLKAQQPAT 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 233 nlgkenFKKPVPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVsnMAAFLKFLEPIFqpTPEDVTISYLPLAHM-FERLVQ 311
Cdd:PRK08008 164 ------LCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYYSAWQCAL--RDDDVYLTVMPAFHIdCQCTAA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 312 GVIFSCGGKIGF--------FQGDIRllpdDMKALKPTVFPTVPRLLnRVYDKVQNEAKTPLKK--FLLNLAiiskfNEV 381
Cdd:PRK08008 234 MAAFSAGATFVLlekysaraFWGQVC----KYRATITECIPMMIRTL-MVQPPSANDRQHCLREvmFYLNLS-----DQE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 382 RNGIIRRnslwdklvFskiqsslggKVRLmitgaapistpvltffraamgcwvFEAYGQTECTAGCSITSPGD---WTAg 458
Cdd:PRK08008 304 KDAFEER--------F---------GVRL------------------------LTSYGMTETIVGIIGDRPGDkrrWPS- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 459 hVGTPVSCNFVKLEDvADMNYFSVNNEGEICIKG---NNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDR 535
Cdd:PRK08008 342 -IGRPGFCYEAEIRD-DHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDR 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 536 KKNIFKLAqGEYIAPEKIENVYSRSRPILQVFVHG-------ESLRSFLI---GVVVPDPESL------------PSFaa 593
Cdd:PRK08008 420 RCNMIKRG-GENVSCVELENIIATHPKIQDIVVVGikdsirdEAIKAFVVlneGETLSEEEFFafceqnmakfkvPSY-- 496
|
490
....*....|....*....
gi 1958650325 594 kIGVKGSFEELCQNQCVKK 612
Cdd:PRK08008 497 -LEIRKDLPRNCSGKIIKK 514
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
249-591 |
5.52e-20 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 93.80 E-value: 5.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 249 DLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKflepIFQPTPEDVTISYLPLAHMfERLVQGVI--FSCGGKIgffqg 326
Cdd:PRK05852 177 DDAMIMFTGGTTGLPKMVPWTHANIASSVRAIIT----GYRLSPRDATVAVMPLYHG-HGLIAALLatLASGGAV----- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 327 dirLLP-----------DDMKALKPTVFPTVPrllnrvydkvqneaktPLKKFLLNLAIISKFNEVRngiirrnslwdkl 395
Cdd:PRK05852 247 ---LLPargrfsahtfwDDIKAVGATWYTAVP----------------TIHQILLERAATEPSGRKP------------- 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 396 vfskiqsslgGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAgcSITSPGDWTAGHVGTP-VSCNFVKLEDV 474
Cdd:PRK05852 295 ----------AALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATH--QVTTTQIEGIGQTENPvVSTGLVGRSTG 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 475 ADMNYFSVNNE-------GEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEY 547
Cdd:PRK05852 363 AQIRIVGSDGLplpagavGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEK 440
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1958650325 548 IAPEKIENVYSRSRPILQVFV-------HGESLRSFLI--GVVVPDPESLPSF 591
Cdd:PRK05852 441 ISPERVEGVLASHPNVMEAAVfgvpdqlYGEAVAAVIVprESAPPTAEELVQF 493
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
248-558 |
1.07e-19 |
|
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: 90.78 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 248 EDLSVICFTSGTTGDPKGAMLTHQNIVsnmAAFLKFLEPIFQPTPEDVTISYLPLAHMFERLVQGVIFSCGGKIgffqgd 327
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFF---AVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLC------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 328 irllpddmkalkptvfptvprllnrvydkVQNEAKTPLKKFLLNLaiisKFNEVrNGIIRRNSLWDKLVF---SKIQSSl 404
Cdd:cd17635 72 -----------------------------VTGGENTTYKSLFKIL----TTNAV-TTTCLVPTLLSKLVSelkSANATV- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 405 gGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCSI-TSPGDWTAGHVGTPVSCNFVKLEDVADMNYFSvN 483
Cdd:cd17635 117 -PSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLpTDDDSIEINAVGRPYPGVDVYLAATDGIAGPS-A 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958650325 484 NEGEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENVYS 558
Cdd:cd17635 195 SFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERIAE 267
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
132-585 |
1.15e-19 |
|
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: 92.94 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 132 IFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVICDTPQKATMLIENVEKDLTPGLKTVILMDPFD 211
Cdd:cd05970 77 LTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDNIPEEIEKAAPECPSKPKLVWVGDPVP 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 212 DDLMKRGEKCgiemlslhdaENLGkENFKKP---VPPNPEDLSVICFTSGTTGDPKgaMLTHQN------IVSNMaaflk 282
Cdd:cd05970 157 EGWIDFRKLI----------KNAS-PDFERPtanSYPCGEDILLVYFSSGTTGMPK--MVEHDFtyplghIVTAK----- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 283 flepiFQPTPEDVTISYLPLAHMFERLVQGVIFS---CGGKIGFFQGDiRLLPDDM--KALK--PTVF---PTVPRLLNR 352
Cdd:cd05970 219 -----YWQNVREGGLHLTVADTGWGKAVWGKIYGqwiAGAAVFVYDYD-KFDPKALleKLSKygVTTFcapPTIYRFLIR 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 353 vydkvqneaktplkkfllnlAIISKFNevrngiirrnslwdklvFSKIqsslggkvRLMITGAAPISTPVLTFFRAAMGC 432
Cdd:cd05970 293 --------------------EDLSRYD-----------------LSSL--------RYCTTAGEALNPEVFNTFKEKTGI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 433 WVFEAYGQTECTAgCSITSPG-DWTAGHVGTPVSCNFVKLEDvADMNYFSVNNEGEICI---KGNNV--FKGYLKDPEKT 506
Cdd:cd05970 328 KLMEGFGQTETTL-TIATFPWmEPKPGSMGKPAPGYEIDLID-REGRSCEAGEEGEIVIrtsKGKPVglFGGYYKDAEKT 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958650325 507 QEVLdKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKlAQGEYIAPEKIENVYSRSRPILQVFVHGeslrsfligvvVPDP 585
Cdd:cd05970 406 AEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVESALIQHPAVLECAVTG-----------VPDP 471
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
249-586 |
1.85e-19 |
|
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: 90.02 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 249 DLSVICFTSGTTGDPKGAMLTHQNIV-SNMAaflkfLEPIFQPTPEDVTISYLPLAHmferlVQGVIFS-----CGGK-- 320
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIaANLQ-----LIHAMGLTEADVYLNMLPLFH-----IAGLNLAlatfhAGGAnv 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 321 -IGFFQGDIRLlpDDMKALKPTVFPTVPRLLNRVYDKVqneAKTPLKkfLLNLAIISkfnevrnGI-----IRRnslWDK 394
Cdd:cd17637 71 vMEKFDPAEAL--ELIEEEKVTLMGSFPPILSNLLDAA---EKSGVD--LSSLRHVL-------GLdapetIQR---FEE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 395 lvfskiqsslggkvrlmITGAapistpvlTFfraamgcWVfeAYGQTEcTAGCSITSPGDWTAGHVGTPVSCNFVKLEDV 474
Cdd:cd17637 134 -----------------TTGA--------TF-------WS--LYGQTE-TSGLVTLSPYRERPGSAGRPGPLVRVRIVDD 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 475 ADmNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIIDRK--KNIFKlAQGEYIAPEK 552
Cdd:cd17637 179 ND-RPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAE 255
|
330 340 350
....*....|....*....|....*....|....
gi 1958650325 553 IENVysrsrpILQvfvHGESLRSFLIGvvVPDPE 586
Cdd:cd17637 256 VEKV------ILE---HPAIAEVCVIG--VPDPK 278
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
81-593 |
3.50e-19 |
|
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: 91.25 E-value: 3.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 81 AVSDNGPCLGYRKPNQpykwisykqvsdRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDT 160
Cdd:cd17651 13 ALVAEGRRLTYAELDR------------RANRLAHRLRARGVGP--GDLVALCARRSAELVVALLAILKAGAAYVPLDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 161 LGAEAIIYVINRADISVVICDtpqkatmliENVEKDLTPGLKTVILMDPFDDdlmkrgekcgiemLSLHDAEnlgkenfk 240
Cdd:cd17651 79 YPAERLAFMLADAGPVLVLTH---------PALAGELAVELVAVTLLDQPGA-------------AAGADAE-------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 241 KPVPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSnmaaFLKFLEPIFQPTPEDVTISYLPLAhmFERLVQGvIFS---C 317
Cdd:cd17651 129 PDPALDADDLAYVIYTSGSTGRPKGVVMPHRSLAN----LVAWQARASSLGPGARTLQFAGLG--FDVSVQE-IFStlcA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 318 GGKIGFFQGDIRLLPDDMKALKPTvfptvpRLLNRVYdkvqneAKTPLKKFLLNLAiiskfnevrngiirrnslwdklvf 397
Cdd:cd17651 202 GATLVLPPEEVRTDPPALAAWLDE------QRISRVF------LPTVALRALAEHG------------------------ 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 398 sKIQSSLGGKVRLMITGAAPISTPVLT--FFRAAMGCWVFEAYGQTECTAGCSITSPGD---WTA-GHVGTPVSCNFVKL 471
Cdd:cd17651 246 -RPLGVRLAALRYLLTGGEQLVLTEDLreFCAGLPGLRLHNHYGPTETHVVTALSLPGDpaaWPApPPIGRPIDNTRVYV 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 472 EDvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWL------HTGDIGRWLPNGTLKIIDRKKNIFKLaQG 545
Cdd:cd17651 325 LD-AALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RG 402
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1958650325 546 EYIAPEKIENVYSRSRPILQVFVHGESLRS---FLIGVVVPDPESLPSFAA 593
Cdd:cd17651 403 FRIELGEIEAALARHPGVREAVVLAREDRPgekRLVAYVVGDPEAPVDAAE 453
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
101-594 |
9.77e-19 |
|
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: 89.57 E-value: 9.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEWVISELA------CYtysmvaVPLYDTLGAEAIIYVINRAD 174
Cdd:cd12117 23 LTYAELNERANRLARRLRAAGVGP--GDVVGVLAERSPELVVALLAvlkagaAY------VPLDPELPAERLAFMLADAG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 175 ISVVICDTPqkatmlienvEKDLTPGLKTVILMDPFDDDlmkrgekcgiemlslHDAENLgkenfkkPVPPNPEDLSVIC 254
Cdd:cd12117 95 AKVLLTDRS----------LAGRAGGLEVAVVIDEALDA---------------GPAGNP-------AVPVSPDDLAYVM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 255 FTSGTTGDPKGAMLTHQNIV-----SNMAAFlkflepifqpTPEDVTISYLPL---AHMFErlvqgvIFSC---GGKigf 323
Cdd:cd12117 143 YTSGSTGRPKGVAVTHRGVVrlvknTNYVTL----------GPDDRVLQTSPLafdASTFE------IWGAllnGAR--- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 324 fqgdIRLLPDDmkalkptvfptVPRLLNRVYDKVQNEAKTPLkkFLlnlaIISKFNevrngiirrnslwdkLVFSKIQSS 403
Cdd:cd12117 204 ----LVLAPKG-----------TLLDPDALGALIAEEGVTVL--WL----TAALFN---------------QLADEDPEC 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 404 LGGkVRLMITGAAPISTP-VLTFFRAAMGCWVFEAYGQTECT--AGCSITSPGDWTAGHV--GTPVSCNFVKLEDvADMN 478
Cdd:cd12117 248 FAG-LRELLTGGEVVSPPhVRRVLAACPGLRLVNGYGPTENTtfTTSHVVTELDEVAGSIpiGRPIANTRVYVLD-EDGR 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 479 YFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWL------HTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEK 552
Cdd:cd12117 326 PVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI-RGFRIELGE 404
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1958650325 553 IENVYSRSRPILQVFV---HGESLRSFLIGVVVP----DPESLPSFAAK 594
Cdd:cd12117 405 IEAALRAHPGVREAVVvvrEDAGGDKRLVAYVVAegalDAAELRAFLRE 453
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
101-570 |
1.05e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 90.10 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPSQDqfIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIC 180
Cdd:PRK06178 59 ITYAELDELSDRFAALLRQRGVGAGDR--VAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 -DT------PQKATMLIENVEK----DLTPGLKTVILMDPFDDdlmKRGEKCG-IEMLSLHDAEnlgkenfKKPVP---P 245
Cdd:PRK06178 137 lDQlapvveQVRAETSLRHVIVtslaDVLPAEPTLPLPDSLRA---PRLAAAGaIDLLPALRAC-------TAPVPlppP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 246 NPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLkflePIFQPTPED-VTISYLPlahMF----ERLvqGVIFscggk 320
Cdd:PRK06178 207 ALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAY----AVAVVGGEDsVFLSFLP---EFwiagENF--GLLF----- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 321 igffqgdirllpddmkalkPTVFPTVPRLLNRvYDKVQNEAKTPLKKFLLNLAIISKFNEVRN--GIIRRNslwdklvFS 398
Cdd:PRK06178 273 -------------------PLFSGATLVLLAR-WDAVAFMAAVERYRVTRTVMLVDNAVELMDhpRFAEYD-------LS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 399 KIQSslggkvrlmitgaapisTPVLTF-----------FRAAMGCWVFEA-YGQTEcTAGCSITSPGDWTAGH------- 459
Cdd:PRK06178 326 SLRQ-----------------VRVVSFvkklnpdyrqrWRALTGSVLAEAaWGMTE-THTCDTFTAGFQDDDFdllsqpv 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 460 -VGTPVSCNFVKLEDVADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIIDRKKN 538
Cdd:PRK06178 388 fVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKE 466
|
490 500 510
....*....|....*....|....*....|..
gi 1958650325 539 IFKLaQGEYIAPEKIENVYSRSRPILQVFVHG 570
Cdd:PRK06178 467 MLKV-NGMSVFPSEVEALLGQHPAVLGSAVVG 497
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
185-661 |
1.49e-18 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 89.47 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 185 KATMLI---------ENVEKDLTPGLKTVILMDPFDDDLmkrgekcGIEMLSLHDAENLGKENFKKPVPP---NPEDLSV 252
Cdd:PLN02860 104 RPVMLVtdetcsswyEELQNDRLPSLMWQVFLESPSSSV-------FIFLNSFLTTEMLKQRALGTTELDyawAPDDAVL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 253 ICFTSGTTGDPKGAMLTHQN-IVSNMA--AFLKFLEpifqptpEDVTISYLPLAHMferlvqGVIFSC------GGKIGF 323
Cdd:PLN02860 177 ICFTSGTTGRPKGVTISHSAlIVQSLAkiAIVGYGE-------DDVYLHTAPLCHI------GGLSSAlamlmvGACHVL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 324 F-QGDIRLLPDDMKALKPTVFPTVPRLLNRvydkvqneaktplkkfLLNLAIISKFNEVRNGIirrnslwdklvfSKIQS 402
Cdd:PLN02860 244 LpKFDAKAALQAIKQHNVTSMITVPAMMAD----------------LISLTRKSMTWKVFPSV------------RKILN 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 403 SLGGKVRLMITGAapistpVLTFFRAAmgcwVFEAYGQTE-C--------------TAGCSITSPGDWTAGHVGTPV-SC 466
Cdd:PLN02860 296 GGGSLSSRLLPDA------KKLFPNAK----LFSAYGMTEaCssltfmtlhdptleSPKQTLQTVNQTKSSSVHQPQgVC 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 467 -----NFVKLEDVADmnyfSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFK 541
Cdd:PLN02860 366 vgkpaPHVELKIGLD----ESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIK 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 542 lAQGEYIAPEKIENVYSRSRPILQVFVHG---ESLRSFLIGVVVPDPESLPSFAAKIGVKGSFeELCQnqcvkkailEDL 618
Cdd:PLN02860 442 -TGGENVYPEEVEAVLSQHPGVASVVVVGvpdSRLTEMVVACVRLRDGWIWSDNEKENAKKNL-TLSS---------ETL 510
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1958650325 619 QKVGKEGGLKSFEQVKSIFVHPEPFSienglLTPTLKAKRVEL 661
Cdd:PLN02860 511 RHHCREKNLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEV 548
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
172-554 |
1.99e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 89.28 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 172 RADISVVICDTPQKATMLienvekdltpGLKTVILMDPFD---DDLMKRGEKcGIEMLSLHDAENLgkenfkKPVPPNPE 248
Cdd:PRK07768 90 RTDLAVWAEDTLRVIGMI----------GAKAVVVGEPFLaaaPVLEEKGIR-VLTVADLLAADPI------DPVETGED 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 249 DLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFLEpiFQPTpEDVTISYLPLAH-MferlvqgvifscgGKIGFFqgd 327
Cdd:PRK07768 153 DLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAE--FDVE-TDVMVSWLPLFHdM-------------GMVGFL--- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 328 irLLPddMKALKPTVFPTVPRLLNRVydkvqneaktplkkfLLNLAIISKFnevRNGIIRR-N---SLWDKLVFSKIQ-- 401
Cdd:PRK07768 214 --TVP--MYFGAELVKVTPMDFLRDP---------------LLWAELISKY---RGTMTAApNfayALLARRLRRQAKpg 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 402 ----SSLggkvRLMITGAAPISTPVLTFFRAAMGCW------VFEAYGQTECTAGCSITSPGD-----------WTAGHV 460
Cdd:PRK07768 272 afdlSSL----RFALNGAEPIDPADVEDLLDAGARFglrpeaILPAYGMAEATLAVSFSPCGAglvvdevdadlLAALRR 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 461 GTPVSCN----FVKL-------------EDVADMNYFSVnneGEICIKGNNVFKGYLkDPEKTQEVLDKDGWLHTGDIGR 523
Cdd:PRK07768 348 AVPATKGntrrLATLgpplpglevrvvdEDGQVLPPRGV---GVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLGY 423
|
410 420 430
....*....|....*....|....*....|.
gi 1958650325 524 WLPNGTLKIIDRKKNIFKLAqGEYIAPEKIE 554
Cdd:PRK07768 424 LTEEGEVVVCGRVKDVIIMA-GRNIYPTDIE 453
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
100-565 |
2.21e-18 |
|
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: 88.83 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 100 WISYKQVSDRAEYLGSCLLHKGyKPSQDqfIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIY---VINRADIS 176
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAVG-KPGDR--VLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHAERlaaILADAGPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 177 VVICDTPQKATmLIENVEKDLTPGLKTVILMDPFDDDlmkrgekcgiemlslhDAENLGkenfkkPVPPNPEDLSVICFT 256
Cdd:cd05931 101 VVLTTAAALAA-VRAFAASRPAAGTPRLLVVDLLPDT----------------SAADWP------PPSPDPDDIAYLQYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 257 SGTTGDPKGAMLTHQNIVSNMAAFLKflepIFQPTPEDVTISYLPLAH-MfeRLVQGVIFSCggkigFFQGDIRLLPddm 335
Cdd:cd05931 158 SGSTGTPKGVVVTHRNLLANVRQIRR----AYGLDPGDVVVSWLPLYHdM--GLIGGLLTPL-----YSGGPSVLMS--- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 336 kalkPTVFPTVP----RLLNRV-----------YD----KVQNEAKTPlkkflLNLaiiskfnevrngiirrnslwdklv 396
Cdd:cd05931 224 ----PAAFLRRPlrwlRLISRYratisaapnfaYDlcvrRVRDEDLEG-----LDL------------------------ 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 397 fskiqsslgGKVRLMITGAAPISTPVLTFFRAAMGCW------VFEAYGQTECTAGCSITSPG----------DWTAGHV 460
Cdd:cd05931 271 ---------SSWRVALNGAEPVRPATLRRFAEAFAPFgfrpeaFRPSYGLAEATLFVSGGPPGtgpvvlrvdrDALAGRA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 461 GTP----------VSCNFVkledVADMNYFSVNNE----------GEICIKGNNVFKGYLKDPEKTQEV------LDKDG 514
Cdd:cd05931 342 VAVaaddpaarelVSCGRP----LPDQEVRIVDPEtgrelpdgevGEIWVRGPSVASGYWGRPEATAETfgalaaTDEGG 417
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958650325 515 WLHTGDIGRWLPN-----GTLK--IIDRKKNIFklaqgeyiaPEKIENVYSRSRPILQ 565
Cdd:cd05931 418 WLRTGDLGFLHDGelyitGRLKdlIIVRGRNHY---------PQDIEATAEEAHPALR 466
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
87-651 |
3.09e-18 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 88.64 E-value: 3.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 87 PCLGYRKPNQPYKWISYKQVSDRAEYLGSCLLhkGYKPSQDQFIGIFAQNRPEWVISELACYTYSMVAVPL---YDTLGA 163
Cdd:cd05921 12 TWLAEREGNGGWRRVTYAEALRQVRAIAQGLL--DLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVspaYSLMSQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 164 E--AIIYVINRADISVVICdtpQKATMLIENVEKDLTPGLKTVILmdpfdddlmkRGEKCGIEMLSLhdAENLGKENFKK 241
Cdd:cd05921 90 DlaKLKHLFELLKPGLVFA---QDAAPFARALAAIFPLGTPLVVS----------RNAVAGRGAISF--AELAATPPTAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 242 pVPP-----NPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKfLEPIFQPTPEdVTISYLPLAHMF-ERLVQGVIF 315
Cdd:cd05921 155 -VDAafaavGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQ-TYPFFGEEPP-VLVDWLPWNHTFgGNHNFNLVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 316 SCGGKI---------GFFQGDIRllpdDMKALKPTVFPTVPRLLNRVYDKVQNEAkTPLKKFLLNLAIIskfneVRNGII 386
Cdd:cd05921 232 YNGGTLyiddgkpmpGGFEETLR----NLREISPTVYFNVPAGWEMLVAALEKDE-ALRRRFFKRLKLM-----FYAGAG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 387 RRNSLWDKLVFSKIQSSlGGKVRlMITGaapistpvltffraamgcwvfeaYGQTEcTAGCSITSPGDWT-AGHVGTPVS 465
Cdd:cd05921 302 LSQDVWDRLQALAVATV-GERIP-MMAG-----------------------LGATE-TAPTATFTHWPTErSGLIGLPAP 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 466 CNFVKLedvadmnyFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWL----PNGTLKIIDRKKNIFK 541
Cdd:cd05921 356 GTELKL--------VPSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpddPAKGLVFDGRVAEDFK 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 542 LAQGEYIA--PEKIENVYSRSRPILQVFVHGESlRSFLIGVVVPDPESLPSFAAkiGVKGSFEELCQNQCVKKAILEDLQ 619
Cdd:cd05921 428 LASGTWVSvgPLRARAVAACAPLVHDAVVAGED-RAEVGALVFPDLLACRRLVG--LQEASDAEVLRHAKVRAAFRDRLA 504
|
570 580 590
....*....|....*....|....*....|..
gi 1958650325 620 KVGKEGGlKSFEQVKSIFVHPEPFSIENGLLT 651
Cdd:cd05921 505 ALNGEAT-GSSSRIARALLLDEPPSIDKGEIT 535
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
102-661 |
5.29e-18 |
|
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: 87.10 E-value: 5.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 102 SYKQVSDRAEYLGSCLLHKGYKPSQDqfIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVICD 181
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDR--VGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 182 TPqkatmlienvekdltpglktvilmdpfdddlmkrgekcgiemlslhdaenlgkenfkkpvppnpEDLSVICFTSGTTG 261
Cdd:cd05971 86 GS----------------------------------------------------------------DDPALIIYTSGTTG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 262 DPKGAMLTHQNIVSNmaafLKFLEPIFQPTPEDVTISYLP---------LAHMFERLVQGV-IFSCGGKiGFfqgDIRLL 331
Cdd:cd05971 102 PPKGALHAHRVLLGH----LPGVQFPFNLFPRDGDLYWTPadwawigglLDVLLPSLYFGVpVLAHRMT-KF---DPKAA 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 332 PDDMKALKPT-VF--PTVPRLLNRVYDkvqneaktPLKKFLLNLAIISkfnevrngiirrnslwdklvfskiqsslggkv 408
Cdd:cd05971 174 LDLMSRYGVTtAFlpPTALKMMRQQGE--------QLKHAQVKLRAIA-------------------------------- 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 409 rlmiTGAAPISTPVLTFFRAAMGCWVFEAYGQTEC---TAGCSITSPGDwtAGHVGTPVSCNFVKLEDvADMNYFSVNNE 485
Cdd:cd05971 214 ----TGGESLGEELLGWAREQFGVEVNEFYGQTECnlvIGNCSALFPIK--PGSMGKPIPGHRVAIVD-DNGTPLPPGEV 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 486 GEICIK--GNNVFKGYLKDPEKTqEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENVYSRSRPI 563
Cdd:cd05971 287 GEIAVElpDPVAFLGYWNNPSAT-EKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAEIEECLLKHPAV 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 564 LQVFVHGeslrsfligvvVPDPESLPSFAAKIGVKGSFEElcqnqcvKKAILEDLQkvgkegglksfEQVKSIF-VHPEP 642
Cdd:cd05971 365 LMAAVVG-----------IPDPIRGEIVKAFVVLNPGETP-------SDALAREIQ-----------ELVKTRLaAHEYP 415
|
570 580
....*....|....*....|..
gi 1958650325 643 FSIE--NGL-LTPTLKAKRVEL 661
Cdd:cd05971 416 REIEfvNELpRTATGKIRRREL 437
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
101-590 |
8.40e-18 |
|
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: 86.36 E-value: 8.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIC 180
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSS--GDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 DTpqkatmlienvekdltpglktvilmdpfdddlmkrgekcgiemlslhdaenlgkenfkkpvppnpEDLSVICFTSGTT 260
Cdd:cd05919 89 SA-----------------------------------------------------------------DDIAYLLYSSGTT 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 261 GDPKGAMLTHQNIVSNMAAFLKflePIFQPTPEDVTISylpLAHMF--ERLVQGVIF--SCGGKIGFFQGdiRLLPDDMK 336
Cdd:cd05919 104 GPPKGVMHAHRDPLLFADAMAR---EALGLTPGDRVFS---SAKMFfgYGLGNSLWFplAVGASAVLNPG--WPTAERVL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 337 AL----KPTVFPTVPRLLNRVydkvqneaktplkkfllnlaiiskfneVRNGIIRRNSLWDklvfskiqsslggkVRLMI 412
Cdd:cd05919 176 ATlarfRPTVLYGVPTFYANL---------------------------LDSCAGSPDALRS--------------LRLCV 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 413 TGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCSITSPGDWTAGHVGTPVSCNFVKLEDvADMNYFSVNNEGEICIKG 492
Cdd:cd05919 215 SAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD-EEGHTIPPGEEGDLLVRG 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 493 NNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENVYSRSRPILQVFV---- 568
Cdd:cd05919 294 PSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVESLIIQHPAVAEAAVvavp 371
|
490 500
....*....|....*....|....*
gi 1958650325 569 --HGES-LRSFligvVVPDPESLPS 590
Cdd:cd05919 372 esTGLSrLTAF----VVLKSPAAPQ 392
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
101-562 |
9.48e-18 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 88.10 E-value: 9.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGScLLHKGYKPsqDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIC 180
Cdd:PRK06814 659 LTYRKLLTGAFVLGR-KLKKNTPP--GENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 DTP--QKATM--LIENVEKdltpGLKTVILMDpfdddlMKRGEKCGIEMLSLhdaenLGKENFKKPVP-PNPEDLSVICF 255
Cdd:PRK06814 736 SRAfiEKARLgpLIEALEF----GIRIIYLED------VRAQIGLADKIKGL-----LAGRFPLVYFCnRDPDDPAVILF 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 256 TSGTTGDPKGAMLTHQNIVSNMA---AFLKFlepifqpTPEDVTISYLPLAHMFerlvqgvifscggkiGFFQGdiRLLP 332
Cdd:PRK06814 801 TSGSEGTPKGVVLSHRNLLANRAqvaARIDF-------SPEDKVFNALPVFHSF---------------GLTGG--LVLP 856
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 333 ddMKALKPTVF-PT------VPRLlnrVYDkvqneaktplkkflLNLAIISKFNEVRNGIIRRNSLWDklvFSKIqsslg 405
Cdd:PRK06814 857 --LLSGVKVFLyPSplhyriIPEL---IYD--------------TNATILFGTDTFLNGYARYAHPYD---FRSL----- 909
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 406 gkvRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCSITSPGDWTAGHVGTPVSCNFVKLEDVAdmnyfSVNNE 485
Cdd:PRK06814 910 ---RYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVP-----GIDEG 981
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958650325 486 GEICIKGNNVFKGYLKdPEKtQEVLD--KDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENVYSRSRP 562
Cdd:PRK06814 982 GRLFVRGPNVMLGYLR-AEN-PGVLEppADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAVEELAAELWP 1057
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
246-556 |
2.90e-17 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 85.25 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 246 NPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFlepiFQPTPEDVTISYLPLAHMFErlvqgviFSCGGkigffq 325
Cdd:PRK06334 181 DPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKF----FSPKEDDVMMSFLPPFHAYG-------FNSCT------ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 326 gdirLLPddMKALKPTVFPTVPRLLNRVYDKVQNEAKTplkkFLLNLAIIskFNEVRNGIIRRNSLWDKLVFSKIqsslG 405
Cdd:PRK06334 244 ----LFP--LLSGVPVVFAYNPLYPKKIVEMIDEAKVT----FLGSTPVF--FDYILKTAKKQESCLPSLRFVVI----G 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 406 GKV-RLMITGAAPISTPVLTffraamgcwVFEAYGQTECTAGCSIT---SPGDWTAghVGTPVSCNFVKLedVADMNYFS 481
Cdd:PRK06334 308 GDAfKDSLYQEALKTFPHIQ---------LRQGYGTTECSPVITINtvnSPKHESC--VGMPIRGMDVLI--VSEETKVP 374
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958650325 482 VNN--EGEICIKGNNVFKGYL-KDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENV 556
Cdd:PRK06334 375 VSSgeTGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSLEALESI 451
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
246-651 |
8.83e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 84.33 E-value: 8.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 246 NPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKfLEPiFQPTPE-DVTISYLPLAHMF--ERLVQGVIFSCG---- 318
Cdd:PRK12582 218 TPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQ-LRP-REPDPPpPVSLDWMPWNHTMggNANFNGLLWGGGtlyi 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 319 --GK--IGFFQGDIRLLPDdmkaLKPTVFPTVPRLLNRVYDKVQNEAKTpLKKFLLNLAIISkfnevRNGIIRRNSLWDK 394
Cdd:PRK12582 296 ddGKplPGMFEETIRNLRE----ISPTVYGNVPAGYAMLAEAMEKDDAL-RRSFFKNLRLMA-----YGGATLSDDLYER 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 395 LvfskiqsslgGKVRLMITGA-APISTpvltffraamgcwvfeAYGQTEcTAGcsITSPGDWTA---GHVGTPVSCNFVK 470
Cdd:PRK12582 366 M----------QALAVRTTGHrIPFYT----------------GYGATE-TAP--TTTGTHWDTervGLIGLPLPGVELK 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 471 LEDVADmNYfsvnnegEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWL----PNGTLKIIDRKKNIFKLAQGE 546
Cdd:PRK12582 417 LAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdpddPEKGLIFDGRVAEDFKLSTGT 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 547 Y--IAPEKIENVYSRSRPILQVFVHGESlRSFLIGVVVPDPESLPSFAAKIGvkGSFEELCQNQCVKKAILEDLQKVGKE 624
Cdd:PRK12582 489 WvsVGTLRPDAVAACSPVIHDAVVAGQD-RAFIGLLAWPNPAACRQLAGDPD--AAPEDVVKHPAVLAILREGLSAHNAE 565
|
410 420
....*....|....*....|....*..
gi 1958650325 625 GGLKSfEQVKSIFVHPEPFSIENGLLT 651
Cdd:PRK12582 566 AGGSS-SRIARALLMTEPPSIDAGEIT 591
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
247-524 |
1.38e-16 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 83.39 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 247 PEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFLePIFQPTPEdVTISYLPLAHMFE-----RLV---QGVIFSCG 318
Cdd:PRK08180 208 PDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTF-PFLAEEPP-VLVDWLPWNHTFGgnhnlGIVlynGGTLYIDD 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 319 GK--IGFFQGDIRLLpddmKALKPTVFPTVPRLlnrvydkvqneaktplkkfllnlaiiskFNEVRNGIIRRNSLWDKLv 396
Cdd:PRK08180 286 GKptPGGFDETLRNL----REISPTVYFNVPKG----------------------------WEMLVPALERDAALRRRF- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 397 FSKiqsslggkVRLMITGAAPISTPVLT----FFRAAMG--CWVFEAYGQTECT-AGCSITSPGDwTAGHVGTPVSCNFV 469
Cdd:PRK08180 333 FSR--------LKLLFYAGAALSQDVWDrldrVAEATCGerIRMMTGLGMTETApSATFTTGPLS-RAGNIGLPAPGCEV 403
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958650325 470 KLedvadmnyfsVNNEG--EICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRW 524
Cdd:PRK08180 404 KL----------VPVGGklEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRF 450
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
101-593 |
2.38e-16 |
|
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: 82.32 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIc 180
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVRP--GDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 dtpqkatmlienVEKDLTPGLKTVILMDPFDDDLMKRGEkcgiemlslhdaenlgkenFKKPVPPNPEDLSVICFTSGTT 260
Cdd:cd12114 90 ------------TDGPDAQLDVAVFDVLILDLDALAAPA-------------------PPPPVDVAPDDLAYVIFTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 261 GDPKGAMLTHQNIVSNMAAFLKflepIFQPTPEDVTISYLPLAH---MFErlvqgvIF---SCGGKIgffqgdirLLPDD 334
Cdd:cd12114 139 GTPKGVMISHRAALNTILDINR----RFAVGPDDRVLALSSLSFdlsVYD------IFgalSAGATL--------VLPDE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 335 MKALKP------------TVFPTVPRLLNRVYDKVQNEAKTPLKkflLNLAIISkfnevrngiirrnSLWdklvfskIQS 402
Cdd:cd12114 201 ARRRDPahwaelierhgvTLWNSVPALLEMLLDVLEAAQALLPS---LRLVLLS-------------GDW-------IPL 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 403 SLGGKVRLMITGAAPIStpvltffraaMGcwvfeayGQTECtagcSITS--------PGDWTAGHVGTPVscnfvkledv 474
Cdd:cd12114 258 DLPARLRALAPDARLIS----------LG-------GATEA----SIWSiyhpidevPPDWRSIPYGRPL---------- 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 475 ADMNYFSVNN---------EGEICIKGNNVFKGYLKDPEKTQE--VLDKDG--WLHTGDIGRWLPNGTLKIIDRKKNIFK 541
Cdd:cd12114 307 ANQRYRVLDPrgrdcpdwvPGELWIGGRGVALGYLGDPELTAArfVTHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVK 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1958650325 542 LaQGEYIAPEKIENVYSRSRPILQ--VFVHGESLRSFLIGVVVPDPESLPSFAA 593
Cdd:cd12114 387 V-RGYRIELGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPDNDGTPIAPD 439
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
247-584 |
2.96e-16 |
|
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: 81.74 E-value: 2.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 247 PEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFLEPIFQPTP--EDVTISYLPLAHMFER--LVQGVIFSCGGKIG 322
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRllQMASFSFDVFAGDFARslLNGGTLVICPDEVK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 323 FfqgDIRLLPDDMKALKPTVFPTVPRLLNRVYDKVQneaktplkkfllnlaiiskfnevrngiirrnslWDKLVFSKIqs 402
Cdd:cd17650 172 L---DPAALYDLILKSRITLMESTPALIRPVMAYVY---------------------------------RNGLDLSAM-- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 403 slggkvRLMITGA--APISTPVLTFFRAAMGCWVFEAYGQTECTAGCSITSPGDWTAGH-----VGTPVSCNFVKLEDvA 475
Cdd:cd17650 214 ------RLLIVGSdgCKAQDFKTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGDsanvpIGRPLPNTAMYVLD-E 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 476 DMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGW------LHTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIA 549
Cdd:cd17650 287 RLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI-RGFRIE 365
|
330 340 350
....*....|....*....|....*....|....*...
gi 1958650325 550 PEKIENVYSRSRPILQVFV---HGESLRSFLIGVVVPD 584
Cdd:cd17650 366 LGEIESQLARHPAIDEAVVavrEDKGGEARLCAYVVAA 403
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
161-568 |
3.63e-16 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 82.20 E-value: 3.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 161 LGAEAIIYVINRADISVVICD------TPQKATMLIENVEKDLTPGLKTVILMDPFDDDLMKRGEKCGI----EMLSLHD 230
Cdd:PLN02479 104 LNAPTIAFLLEHSKSEVVMVDqefftlAEEALKILAEKKKSSFKPPLLIVIGDPTCDPKSLQYALGKGAieyeKFLETGD 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 231 AENLGKenfkkpvPPNPEDLSV-ICFTSGTTGDPKGAMLTHQnivsnmAAFLKFLE-PIFQPTPED-VTISYLPLAHmfe 307
Cdd:PLN02479 184 PEFAWK-------PPADEWQSIaLGYTSGTTASPKGVVLHHR------GAYLMALSnALIWGMNEGaVYLWTLPMFH--- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 308 rlVQGVIFS------CGGKIGFFQGDIRLLPDDMKALKPTVFPTVPRLLNRVYDKVQNEAKTPLKKFllnlaiiskfnev 381
Cdd:PLN02479 248 --CNGWCFTwtlaalCGTNICLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETILPLPRV------------- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 382 rngiirrnslwdklvfskiqsslggkVRLMITGAAPisTPVLTFFRAAMGCWVFEAYGQTEcTAGCSIT---SPgDWTAG 458
Cdd:PLN02479 313 --------------------------VHVMTAGAAP--PPSVLFAMSEKGFRVTHTYGLSE-TYGPSTVcawKP-EWDSL 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 459 HVGTPVSCN------FVKLE--DVAD---MNYFSVNNE--GEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWL 525
Cdd:PLN02479 363 PPEEQARLNarqgvrYIGLEglDVVDtktMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKH 441
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1958650325 526 PNGTLKIIDRKKNIFkLAQGEYIAPEKIENVYSRSRPILQVFV 568
Cdd:PLN02479 442 PDGYIEIKDRSKDII-ISGGENISSLEVENVVYTHPAVLEASV 483
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
102-568 |
6.21e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 81.22 E-value: 6.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 102 SYKQVSDRAEYLGSCLLhkGYKPSQDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVICD 181
Cdd:PLN03102 41 TWPQTYDRCCRLAASLI--SLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 182 TP-----QKATMLIENVEKDLTPGLKTVILMD----PFDDD-----LMKRGEKCGI---EMLSLHDAENlgkenfkkPVP 244
Cdd:PLN03102 119 RSfeplaREVLHLLSSEDSNLNLPVIFIHEIDfpkrPSSEEldyecLIQRGEPTPSlvaRMFRIQDEHD--------PIS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 245 PNpedlsvicFTSGTTGDPKGAMLTHQnivsnmAAFLKFLEPI--FQPTPEDVTISYLPLAHmferlVQGVIFSCG-GKI 321
Cdd:PLN03102 191 LN--------YTSGTTADPKGVVISHR------GAYLSTLSAIigWEMGTCPVYLWTLPMFH-----CNGWTFTWGtAAR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 322 GFFQGDIRLLpddmkalkptvfpTVPRllnrVYDKVQneaktplkkfLLNLAIISKFNEVRNGIIRRNSLwdklvfskIQ 401
Cdd:PLN03102 252 GGTSVCMRHV-------------TAPE----IYKNIE----------MHNVTHMCCVPTVFNILLKGNSL--------DL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 402 SSLGGKVRLMITGAAPISTPVLTFFRaaMGCWVFEAYGQTECTAGCSITSPGD-WT------AGHVGTPVSCNFVKLEDV 474
Cdd:PLN03102 297 SPRSGPVHVLTGGSPPPAALVKKVQR--LGFQVMHAYGLTEATGPVLFCEWQDeWNrlpenqQMELKARQGVSILGLADV 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 475 ADMNYFSVNNE-------GEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEY 547
Cdd:PLN03102 375 DVKNKETQESVprdgktmGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGEN 452
|
490 500
....*....|....*....|.
gi 1958650325 548 IAPEKIENVYSRSRPILQVFV 568
Cdd:PLN03102 453 ISSVEVENVLYKYPKVLETAV 473
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
101-598 |
6.49e-16 |
|
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: 80.88 E-value: 6.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVI--NRADISVV 178
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVKR--EERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLedSRARVVVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 179 icdTPQKATMLIENVEKDlTPGLKTVILMDPfdddlmkrgekCGIEMLSLHDAENLGKE-NFKKPVPPNPEDLSVICFTS 257
Cdd:cd05959 108 ---SGELAPVLAAALTKS-EHTLVVLIVSGG-----------AGPEAGALLLAELVAAEaEQLKPAATHADDPAFWLYSS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 258 GTTGDPKGAMLTHQNIVSNMAAFLKflePIFQPTPEDVTISYLPLAHMFErLVQGVIF--SCGGKIGFFQGdiRLLPDDM 335
Cdd:cd05959 173 GSTGRPKGVVHLHADIYWTAELYAR---NVLGIREDDVCFSAAKLFFAYG-LGNSLTFplSVGATTVLMPE--RPTPAAV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 336 KAL----KPTVFPTVPRLLNRvydkvqneaktplkkfLLNLAIISKFNEVRngiirrnslwdklvfskiqsslggkVRLM 411
Cdd:cd05959 247 FKRirryRPTVFFGVPTLYAA----------------MLAAPNLPSRDLSS-------------------------LRLC 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 412 ITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCSITSPGDWTAGHVGTPVSCNFVKL-----EDVADmnyfsvNNEG 486
Cdd:cd05959 286 VSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELrdedgGDVAD------GEPG 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 487 EICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKlAQGEYIAPEKIENVYSRSRPILQV 566
Cdd:cd05959 360 ELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSPFEVESALVQHPAVLEA 437
|
490 500 510
....*....|....*....|....*....|....*
gi 1958650325 567 FVHGESLRSFLI---GVVVPDPESLPSFAAKIGVK 598
Cdd:cd05959 438 AVVGVEDEDGLTkpkAFVVLRPGYEDSEALEEELK 472
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
101-570 |
6.83e-16 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 81.37 E-value: 6.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLlHKGYKPSQDQFIGIFAQNRPEWVISELAcyTYSMVAV--PLYDTLGAEAIIYVINRADISVV 178
Cdd:PRK05620 39 TTFAAIGARAAALAHAL-HDELGITGDQRVGSMMYNCAEHLEVLFA--VACMGAVfnPLNKQLMNDQIVHIINHAEDEVI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 179 ICD---TPQKATMLIEnvekdlTPGLKTVILMDPFDDDLMKRGEKCGIEMLSLHDAENLGKENFKKPVPPNpEDLSVICF 255
Cdd:PRK05620 116 VADprlAEQLGEILKE------CPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALLDGRSTVYDWPELDE-TTAAAICY 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 256 TSGTTGDPKGAMLTHQNIvsnmaaflkFLEPIFQPTPEDVTI----SYL---PLAHMferLVQGVIFScggkiGFFQGdi 328
Cdd:PRK05620 189 STGTTGAPKGVVYSHRSL---------YLQSLSLRTTDSLAVthgeSFLccvPIYHV---LSWGVPLA-----AFMSG-- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 329 rllpddmkalKPTVFP----TVPRLlnrvydkvqneAKTplkkfllnlaIISKFNEVRNGIirrNSLWDKLVFSKIQS-- 402
Cdd:PRK05620 250 ----------TPLVFPgpdlSAPTL-----------AKI----------IATAMPRVAHGV---PTLWIQLMVHYLKNpp 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 403 ---SLggkvRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCSITSPGDWTAGHVGT---------PVSCNFVK 470
Cdd:PRK05620 296 ermSL----QEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEARWayrvsqgrfPASLEYRI 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 471 LEDVADMNYFSvNNEGEICIKGNNVFKGYLKDP----------------EKTQEVLDKDGWLHTGDIGRWLPNGTLKIID 534
Cdd:PRK05620 372 VNDGQVMESTD-RNEGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHD 450
|
490 500 510
....*....|....*....|....*....|....*.
gi 1958650325 535 RKKNIFKlAQGEYIAPEKIENVYSRSRPILQVFVHG 570
Cdd:PRK05620 451 RARDVIR-SGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
100-559 |
1.55e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 79.99 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 100 WISYKQVSDRAEYLGSCLLHKGYKPSQDqfIGIFAQNRPEwviselacytysMV----AVP--------LYDTLGAEAII 167
Cdd:PRK08162 43 RRTWAETYARCRRLASALARRGIGRGDT--VAVLLPNIPA------------MVeahfGVPmagavlntLNTRLDAASIA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 168 YVINRADISVVICDTP-----QKATMLIenvekdltPGLKtVILMDpFDDDLMKRGEKcgIEMLSLHDAENLGKENFKKP 242
Cdd:PRK08162 109 FMLRHGEAKVLIVDTEfaevaREALALL--------PGPK-PLVID-VDDPEYPGGRF--IGALDYEAFLASGDPDFAWT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 243 VPPNPEDLSVICFTSGTTGDPKGAMLTHQ----NIVSNMAAFlkflepifQPTPEDVTISYLPLAHmferlVQGVIF--- 315
Cdd:PRK08162 177 LPADEWDAIALNYTSGTTGNPKGVVYHHRgaylNALSNILAW--------GMPKHPVYLWTLPMFH-----CNGWCFpwt 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 316 ---SCGGKIGFFQGDIRLLPDDMKALKPTVFPTVPRLLNrvydkvqneaktplkkfllnlAIISKFNEVRNGIirrnslw 392
Cdd:PRK08162 244 vaaRAGTNVCLRKVDPKLIFDLIREHGVTHYCGAPIVLS---------------------ALINAPAEWRAGI------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 393 dklvfskiqsslGGKVRLMITGAAPISTpVLTFFrAAMGCWVFEAYGQTEcTAG----CsitspgDWTAGHVGTPVS--- 465
Cdd:PRK08162 296 ------------DHPVHAMVAGAAPPAA-VIAKM-EEIGFDLTHVYGLTE-TYGpatvC------AWQPEWDALPLDera 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 466 -------CNFVKLED--VAD---MNYFSVNNE--GEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLK 531
Cdd:PRK08162 355 qlkarqgVRYPLQEGvtVLDpdtMQPVPADGEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIK 433
|
490 500
....*....|....*....|....*...
gi 1958650325 532 IIDRKKNIFkLAQGEYIAPEKIENVYSR 559
Cdd:PRK08162 434 IKDRSKDII-ISGGENISSIEVEDVLYR 460
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
130-586 |
1.62e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 79.72 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 130 IGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVICDTPQKATMlienveKDLTPGLKTVILMDP 209
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELL------DGLDPGVRVINVDSP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 210 FDDDLMkrgekcgiemlslhdAENLGKEnfKKPVPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAflkfLEPIFQ 289
Cdd:PRK07867 131 AWADEL---------------AAHRDAE--PPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVM----LAQRFG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 290 PTPEDVTISYLPLAHMfERLVQG--VIFSCGGKIGF---FQGDiRLLPdDMKALKPTVFPTVPRLLNRVY--DKVQNEAK 362
Cdd:PRK07867 190 LGPDDVCYVSMPLFHS-NAVMAGwaVALAAGASIALrrkFSAS-GFLP-DVRRYGATYANYVGKPLSYVLatPERPDDAD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 363 TPLKkfllnlaiISKFNEVRNGIIRRnslwdklvfskiqsslggkvrlmitgaapistpvltfFRAAMGCWVFEAYGQTE 442
Cdd:PRK07867 267 NPLR--------IVYGNEGAPGDIAR-------------------------------------FARRFGCVVVDGFGSTE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 443 ctAGCSITSPGDWTAGHVGTPVSCnfVKLEDVA----------DMNYFSVNNE--GEIC-IKGNNVFKGYLKDPEKTQEV 509
Cdd:PRK07867 302 --GGVAITRTPDTPPGALGPLPPG--VAIVDPDtgtecppaedADGRLLNADEaiGELVnTAGPGGFEGYYNDPEADAER 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958650325 510 LdKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIENVYSRSRPILQVFVHGeslrsfligvvVPDPE 586
Cdd:PRK07867 378 M-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPIERILLRYPDATEVAVYA-----------VPDPV 441
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
246-593 |
3.72e-15 |
|
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: 78.50 E-value: 3.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 246 NPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAflkfLEPIFQPTPEDVTI---SY----------LPLAHmferlvqg 312
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA----TQRWFGFNEDDVWTlfhSYafdfsvweiwGALLH-------- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 313 vifscGGKIGFFQGDIRLLPDDMkalkptvfptvPRLLNRVYDKVQNEakTPlkkfllnlaiiSKFnevrngiiRRNSLW 392
Cdd:cd17643 159 -----GGRLVVVPYEVARSPEDF-----------ARLLRDEGVTVLNQ--TP-----------SAF--------YQLVEA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 393 DkLVFSKIQSSLggkvRLMITGAAPISTPVLTFFRAAMGCW---VFEAYGQTECTAGCSIT--SPGDW---TAGHVGTPV 464
Cdd:cd17643 202 A-DRDGRDPLAL----RYVIFGGEALEAAMLRPWAGRFGLDrpqLVNMYGITETTVHVTFRplDAADLpaaAASPIGRPL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 465 SCNFVKLEDvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQE--VLDKDG-----WLHTGDIGRWLPNGTLKIIDRKK 537
Cdd:cd17643 277 PGLRVYVLD-ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfVANPFGgpgsrMYRTGDLARRLPDGELEYLGRAD 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958650325 538 NIFKLaQGEYIAPEKIENVYSRSRPILQVFV---HGESLRSFLIGVVVPDPESLPSFAA 593
Cdd:cd17643 356 EQVKI-RGFRIELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVADDGAAADIAE 413
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
101-584 |
4.33e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 79.82 E-value: 4.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIC 180
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGVGP--DVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLT 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 DTPQKATMlienvekDLTPGLKTVILMDPFDddlmkrgekcgieMLSLHDAENlgkenfkKPVPPNPEDLSVICFTSGTT 260
Cdd:PRK12467 616 QSHLLAQL-------PVPAGLRSLCLDEPAD-------------LLCGYSGHN-------PEVALDPDNLAYVIYTSGST 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 261 GDPKGAMLTHQNIVSnmaaFLKFLEPIFQPTPEDVTISYLPLA------HMFERLVQGvifscggkigffqGDIRLLPDD 334
Cdd:PRK12467 669 GQPKGVAISHGALAN----YVCVIAERLQLAADDSMLMVSTFAfdlgvtELFGALASG-------------ATLHLLPPD 731
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 335 MkALKPTVFptvprllnrvYDKVQNEAKTPLKKFllnlaiiskfnevrngiirrNSLWDKLVFSKIQSSLGGKVRLMITG 414
Cdd:PRK12467 732 C-ARDAEAF----------AALMADQGVTVLKIV--------------------PSHLQALLQASRVALPRPQRALVCGG 780
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 415 AA-PISTPVLtFFRAAMGCWVFEAYGQTECTAGCSI----TSPGDWTAGHVGTPVSCNFVKLEDvADMNYFSVNNEGEIC 489
Cdd:PRK12467 781 EAlQVDLLAR-VRALGPGARLINHYGPTETTVGVSTyelsDEERDFGNVPIGQPLANLGLYILD-HYLNPVPVGVVGELY 858
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 490 IKGNNVFKGYLKDPEKTQE--VLDKDG-----WLHTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIENVYSRSRP 562
Cdd:PRK12467 859 IGGAGLARGYHRRPALTAErfVPDPFGadggrLYRTGDLARYRADGVIEYLGRMDHQVKI-RGFRIELGEIEARLLAQPG 937
|
490 500
....*....|....*....|....
gi 1958650325 563 ILQVFV--HGESLRSFLIGVVVPD 584
Cdd:PRK12467 938 VREAVVlaQPGDAGLQLVAYLVPA 961
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
101-585 |
6.08e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 78.16 E-value: 6.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPSqDQfIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIC 180
Cdd:PRK07470 33 WTWREIDARVDALAAALAARGVRKG-DR-ILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMIC 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 --DTPQKATMLienveKDLTPGLKTVILMDPfdddlmKRGEkcgiemlslHDAENLGKENFKKPVPPNPEDLSVIC---F 255
Cdd:PRK07470 111 haDFPEHAAAV-----RAASPDLTHVVAIGG------ARAG---------LDYEALVARHLGARVANAAVDHDDPCwffF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 256 TSGTTGDPKGAMLTHQN---IVSNMAAFLkflepifQP--TPEDVTISYLPLAHM--FERLVQgviFSCGGKIGFFQGDi 328
Cdd:PRK07470 171 TSGTTGRPKAAVLTHGQmafVITNHLADL-------MPgtTEQDASLVVAPLSHGagIHQLCQ---VARGAATVLLPSE- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 329 RLLPDDMKAL----KPTVFPTVPRLLnrvydkvqneaktplkKFLLNLAIISKFNevrngiirrnslwdklvfskiQSSL 404
Cdd:PRK07470 240 RFDPAEVWALverhRVTNLFTVPTIL----------------KMLVEHPAVDRYD---------------------HSSL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 405 ggkvRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTaGCsIT-------SPGDWTAGHVGTpvsCNF------VKL 471
Cdd:PRK07470 283 ----RYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVT-GN-ITvlppalhDAEDGPDARIGT---CGFertgmeVQI 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 472 EDvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPE 551
Cdd:PRK07470 354 QD-DEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPR 430
|
490 500 510
....*....|....*....|....*....|....
gi 1958650325 552 KIENVYSRSRPILQVFVHGeslrsfligvvVPDP 585
Cdd:PRK07470 431 EIEEKLLTHPAVSEVAVLG-----------VPDP 453
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
243-575 |
9.65e-15 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 77.83 E-value: 9.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 243 VPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAflkfLEPIFQPTPEDVTISYLPLAHMFerlvqgvifscGGKIG 322
Cdd:PRK08043 360 VKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQ----IKTIADFTPNDRFMSALPLFHSF-----------GLTVG 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 323 FFQ-----GDIRLLPddmkalKPTVFPTVPRLlnrVYDK---VQNEAKTplkkFLLNLAiiskfnevrngiiRRNSLWDk 394
Cdd:PRK08043 425 LFTplltgAEVFLYP------SPLHYRIVPEL---VYDRnctVLFGTST----FLGNYA-------------RFANPYD- 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 395 lvFskiqsslgGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCSITSPGDWTAGHVGTPVSCNFVKLEDV 474
Cdd:PRK08043 478 --F--------ARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSV 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 475 AdmnyfSVNNEGEICIKGNNVFKGYLK--DP--------EKTQEVLDKdGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAq 544
Cdd:PRK08043 548 P-----GIEQGGRLQLKGPNIMNGYLRveKPgvlevptaENARGEMER-GWYDTGDIVRFDEQGFVQIQGRAKRFAKIA- 620
|
330 340 350
....*....|....*....|....*....|.
gi 1958650325 545 GEYIAPEKIENVYSRSRPILQvfvHGESLRS 575
Cdd:PRK08043 621 GEMVSLEMVEQLALGVSPDKQ---HATAIKS 648
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
246-590 |
1.02e-14 |
|
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: 77.09 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 246 NPEDLSVICFTSGTTGDPKGAMLTHQNIVSnmaaFLKFLEPIFQPTPEDVTISYLPLAhmFERLVQGVIFS-CGGkigff 324
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMIEHQSLVN----LSHGLIKEYGITSSDRVLQFASIA--FDVAAEEIYVTlLSG----- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 325 qGDIRLLPDDMkalkptvFPTVPRLLnrvyDKVQNEAKTplkkfLLNLAiiskfnevrngiirrNSLWDKLVFSKIQSSL 404
Cdd:cd17644 173 -ATLVLRPEEM-------RSSLEDFV----QYIQQWQLT-----VLSLP---------------PAYWHLLVLELLLSTI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 405 GG--KVRLMITGAAPISTPVLTFFRAAMGCWV--FEAYGQTECTAGCSITSPGDWTAGH-----VGTPVSCNFVKLEDvA 475
Cdd:cd17644 221 DLpsSLRLVIVGGEAVQPELVRQWQKNVGNFIqlINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIANTQVYILD-E 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 476 DMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLH--------TGDIGRWLPNGTLKIIDRKKNIFKLaQGEY 547
Cdd:cd17644 300 NLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKI-RGFR 378
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1958650325 548 IAPEKIENVYSRSRPILQVFV---HGESLRSFLIGVVVPDPESLPS 590
Cdd:cd17644 379 IELGEIEAVLSQHNDVKTAVVivrEDQPGNKRLVAYIVPHYEESPS 424
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
101-589 |
2.02e-14 |
|
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: 76.20 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIC 180
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVGP--ESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 DtpqkatmlienvekdltpglktvilmdpfdddlmkrgekcgiemlslhdaenlgkenfkkpvppnPEDLSVICFTSGTT 260
Cdd:cd12115 103 D-----------------------------------------------------------------PDDLAYVIYTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 261 GDPKGAMLTHqnivSNMAAFLKFLEPIFqpTPEDVT-------ISY-LPLAHMFERLvqgvifSCGGKIgFFQGDIRLLP 332
Cdd:cd12115 118 GRPKGVAIEH----RNAAAFLQWAAAAF--SAEELAgvlastsICFdLSVFELFGPL------ATGGKV-VLADNVLALP 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 333 DDMKALKPTVFPTVP----RLLNrvYDKVQNEAKTplkkflLNLAiiskfnevrnGIIRRNSLWDKlvfskIQSSLGGKV 408
Cdd:cd12115 185 DLPAAAEVTLINTVPsaaaELLR--HDALPASVRV------VNLA----------GEPLPRDLVQR-----LYARLQVER 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 409 rlmitgaapistpvltffraamgcwVFEAYGQTECTA---GCSITsPGDWTAGHVGTPVSCNFVKLEDvADMNYFSVNNE 485
Cdd:cd12115 242 -------------------------VVNLYGPSEDTTystVAPVP-PGASGEVSIGRPLANTQAYVLD-RALQPVPLGVP 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 486 GEICIKGNNVFKGYLKDPEKTQEVLDKDGWL------HTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIENVYsR 559
Cdd:cd12115 295 GELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAAL-R 372
|
490 500 510
....*....|....*....|....*....|....
gi 1958650325 560 SRPILQ---VFVHGESLRS-FLIGVVVPDPESLP 589
Cdd:cd12115 373 SIPGVReavVVAIGDAAGErRLVAYIVAEPGAAG 406
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
243-589 |
7.15e-14 |
|
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: 74.62 E-value: 7.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 243 VPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAaflkFLEPIFQPTPEDVTISYLPLA------HMFERLVQG---V 313
Cdd:cd17646 133 VPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLL----WMQDEYPLGPGDRVLQKTPLSfdvsvwELFWPLVAGarlV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 314 IFSCGGkigffQGDIRLLPDDMKALKPTVFPTVPRLLnRVydkvqneaktplkkFLlnlaiiskfNEVRNGiiRRNSLwd 393
Cdd:cd17646 209 VARPGG-----HRDPAYLAALIREHGVTTCHFVPSML-RV--------------FL---------AEPAAG--SCASL-- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 394 klvfskiqsslggkvRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCS-ITSPGDWTAGHV--GTPVSCNFVK 470
Cdd:cd17646 256 ---------------RRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVThWPVRGPAETPSVpiGRPVPNTRLY 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 471 LEDvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQE--VLDKDG----WLHTGDIGRWLPNGTLKIIDRKKNIFKLaQ 544
Cdd:cd17646 321 VLD-DALRPVPVGVPGELYLGGVQLARGYLGRPALTAErfVPDPFGpgsrMYRTGDLARWRPDGALEFLGRSDDQVKI-R 398
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1958650325 545 GEYIAPEKIENVYSRSRPILQVFV---HGESLRSFLIGVVVPDPESLP 589
Cdd:cd17646 399 GFRVEPGEIEAALAAHPAVTHAVVvarAAPAGAARLVGYVVPAAGAAG 446
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
101-554 |
1.41e-13 |
|
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: 73.66 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIC 180
Cdd:cd17656 14 LTYRELNERSNQLARFLREKGVKK--DSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 DTpQKATMLIENvekdltpglKTVILMDpfdDDLMKRGekcgiemlslhDAENLGKENfkkpvppNPEDLSVICFTSGTT 260
Cdd:cd17656 92 QR-HLKSKLSFN---------KSTILLE---DPSISQE-----------DTSNIDYIN-------NSDDLLYIIYTSGTT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 261 GDPKGAMLTHQNIVsNMAAF------LKFLEPIFQPTPEDVTISYlplAHMFERLVQGvifscggkigffqGDIRLLPDD 334
Cdd:cd17656 141 GKPKGVQLEHKNMV-NLLHFerektnINFSDKVLQFATCSFDVCY---QEIFSTLLSG-------------GTLYIIREE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 335 MKAlkptvfpTVPRLLNRVydkvqneAKTPLKKFLLNLAIIskfnevrngiirrnslwdKLVFSKIQ--SSLGGKVRLMI 412
Cdd:cd17656 204 TKR-------DVEQLFDLV-------KRHNIEVVFLPVAFL------------------KFIFSEREfiNRFPTCVKHII 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 413 TGAAP--ISTPVLTFFRAAmGCWVFEAYG--QTECTAGCSITSPGDWTA-GHVGTPVSCNFVKLEDvADMNYFSVNNEGE 487
Cdd:cd17656 252 TAGEQlvITNEFKEMLHEH-NVHLHNHYGpsETHVVTTYTINPEAEIPElPPIGKPISNTWIYILD-QEQQLQPQGIVGE 329
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958650325 488 ICIKGNNVFKGYLKDPEKTQEVLDKDGW------LHTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIE 554
Cdd:cd17656 330 LYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-RGYRIELGEIE 401
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
402-586 |
2.68e-13 |
|
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: 72.80 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 402 SSLggkvRLMITGAAPISTPVltffRAAMGCW----VFEAYGQTECTAGCSITSPgDWTA--GHVGTPVSCNfVKLEDvA 475
Cdd:cd05929 244 SSL----KRVIHAAAPCPPWV----KEQWIDWggpiIWEYYGGTEGQGLTIINGE-EWLThpGSVGRAVLGK-VHILD-E 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 476 DMNYFSVNNEGEICIKGNNVFKgYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIEN 555
Cdd:cd05929 313 DGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMI-ISGGVNIYPQEIEN 390
|
170 180 190
....*....|....*....|....*....|.
gi 1958650325 556 VYSRSRPILQVFVHGeslrsfligvvVPDPE 586
Cdd:cd05929 391 ALIAHPKVLDAAVVG-----------VPDEE 410
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
242-586 |
3.02e-13 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 72.21 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 242 PVPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFlepiFQPTPEDVTISYLPLAHmferlV--QGVIF---S 316
Cdd:PRK09029 129 AVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSL----MPFTAQDSWLLSLPLFH-----VsgQGIVWrwlY 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 317 CGGKIGFfqGDIRLLPDDMK-----ALKPTvfpTVPRLLNrvydkvQNEAKTPLKKFLLnlaiiskfnevrngiirrnsl 391
Cdd:PRK09029 200 AGATLVV--RDKQPLEQALAgcthaSLVPT---QLWRLLD------NRSEPLSLKAVLL--------------------- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 392 wdklvfskiqsslggkvrlmitGAAPISTpVLTFFRAAMG--CWVfeAYGQTEctAGCSITS-PGDWTAGhVGTPVSCNF 468
Cdd:PRK09029 248 ----------------------GGAAIPV-ELTEQAEQQGirCWC--GYGLTE--MASTVCAkRADGLAG-VGSPLPGRE 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 469 VKLEDvadmnyfsvnneGEICIKGNNVFKGYLKDpEKTQEVLDKDGWLHTGDIGRWLpNGTLKIIDRKKNIFkLAQGEYI 548
Cdd:PRK09029 300 VKLVD------------GEIWLRGASLALGYWRQ-GQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGI 364
|
330 340 350
....*....|....*....|....*....|....*...
gi 1958650325 549 APEKIENVYSRSRPILQVFVhgeslrsfligVVVPDPE 586
Cdd:PRK09029 365 QPEEIERVINQHPLVQQVFV-----------VPVADAE 391
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
226-561 |
3.92e-13 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 72.49 E-value: 3.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 226 LSLHDAENLGKENFKKPVPPNP-EDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLkflEPIFQPTPEDVTISYLPLAH 304
Cdd:PRK05851 129 VTVHDLATAAHTNRSASLTPPDsGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLN---ARVGLDAATDVGCSWLPLYH 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 305 -MferlvqGVIFSCGGKIGffQGDIRLLPDdmkalkpTVFPTVP-RLLNRVYDKVQNEAKTPlkkfllNLA--IISKFNe 380
Cdd:PRK05851 206 dM------GLAFLLTAALA--GAPLWLAPT-------TAFSASPfRWLSWLSDSRATLTAAP------NFAynLIGKYA- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 381 vrngiiRRNSLWDKlvfskiqsslgGKVRLMITGAAPISTPVLTFFRAAMGCWVFEA------YGQTECTagCSITSP-- 452
Cdd:PRK05851 264 ------RRVSDVDL-----------GALRVALNGGEPVDCDGFERFATAMAPFGFDAgaaapsYGLAEST--CAVTVPvp 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 453 -------------GDWTAGH--VGTPVSCNFVKL---EDVADMNYFSVnneGEICIKGNNVFKGYLKdpektQEVLDKDG 514
Cdd:PRK05851 325 giglrvdevttddGSGARRHavLGNPIPGMEVRIspgDGAAGVAGREI---GEIEIRGASMMSGYLG-----QAPIDPDD 396
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1958650325 515 WLHTGDIGrWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENVYSRSR 561
Cdd:PRK05851 397 WFPTGDLG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERVAAQVR 441
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
87-590 |
5.46e-13 |
|
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: 71.36 E-value: 5.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 87 PCLgyRKPNQPYkwiSYKQVSDRAEYLGSCLLHKGYKPSQDQfIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAI 166
Cdd:cd05958 2 TCL--RSPEREW---TYRDLLALANRIANVLVGELGIVPGNR-VLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 167 IYVINRADISVVICDTPQKATmlienvekdltpglktvilmdpfdddlmkrgekcgiemlslhdaenlgkenfkkpvppn 246
Cdd:cd05958 76 AYILDKARITVALCAHALTAS----------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 247 pEDLSVICFTSGTTGDPKGAMLTHQNIvsnMAAFLKFLEPIFQPTPEDVTISYLPLAHMFER-LVQGVIFSCGGKIGFFQ 325
Cdd:cd05958 97 -DDICILAFTSGTTGAPKATMHFHRDP---LASADRYAVNVLRLREDDRFVGSPPLAFTFGLgGVLLFPFGVGASGVLLE 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 326 GDIrllPDDMKAL----KPTVFPTVPRLLNrvydkvqneaktplkkfllnlAIISKFNEvrngiirrnslwdklvfskiQ 401
Cdd:cd05958 173 EAT---PDLLLSAiaryKPTVLFTAPTAYR---------------------AMLAHPDA--------------------A 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 402 SSLGGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCSITSPGDWTAGHVGTPVSCNFVKLEDvADMNYFS 481
Cdd:cd05958 209 GPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD-DEGNPVP 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 482 VNNEGEICIKGNNvfkGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENVYSRSR 561
Cdd:cd05958 288 DGTIGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQHP 363
|
490 500 510
....*....|....*....|....*....|..
gi 1958650325 562 PILQVFVHGESLRSFLIGV---VVPDPESLPS 590
Cdd:cd05958 364 AVAECAVVGHPDESRGVVVkafVVLRPGVIPG 395
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
246-589 |
6.41e-13 |
|
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: 71.28 E-value: 6.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 246 NPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFLepiFQPTPEDVTISYLPlAHMFERLVQGVIFSCGGkigffq 325
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERY---FGRDNGDEAVLFFS-NYVFDFFVEQMTLALLN------ 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 326 GDIRLLPDDMKALKPtvfPTVPRLLNRvyDKVQNEAKTPlkkfllnlAIISKFNevrngIIRRNSLwdklvfskiqsslg 405
Cdd:cd17648 162 GQKLVVPPDEMRFDP---DRFYAYINR--EKVTYLSGTP--------SVLQQYD-----LARLPHL-------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 406 gkvRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCSIT--SPGDWTAGHVGTPVSCNFVKLEDvADMNYFSVN 483
Cdd:cd17648 210 ---KRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRffPGDQRFDKSLGRPVRNTKCYVLN-DAMKRVPVG 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 484 NEGEICIKGNNVFKGYLKDPEKTQEVL-------DKDGWL-------HTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIA 549
Cdd:cd17648 286 AVGELYLGGDGVARGYLNRPELTAERFlpnpfqtEQERARgrnarlyKTGDLVRWLPSGELEYLGRNDFQVKI-RGQRIE 364
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1958650325 550 PEKIENVYSRSRPILQVFV--------HGESLRSFLIGVVVPDPESLP 589
Cdd:cd17648 365 PGEVEAALASYPGVRECAVvakedasqAQSRIQKYLVGYYLPEPGHVP 412
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
246-594 |
8.15e-13 |
|
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: 71.05 E-value: 8.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 246 NPEDLSVICFTSGTTGDPKGAMLTHQNIVSnmaaFLKFLEPIFQPTPEDVTISYlplahmferlvqgvifscgGKIGFFQ 325
Cdd:cd17645 102 NPDDLAYVIYTSGSTGLPKGVMIEHHNLVN----LCEWHRPYFGVTPADKSLVY-------------------ASFSFDA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 326 GDIRLLPDDMKALKPTVFPTVPRL-LNRVYDKVQNEAKTPLkkfLLNLAIISKFNEVRNgiirrnslwdklvfskiqSSL 404
Cdd:cd17645 159 SAWEIFPHLTAGAALHVVPSERRLdLDALNDYFNQEGITIS---FLPTGAAEQFMQLDN------------------QSL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 405 ggkvRLMITGAAPISTPVLTFFRaamgcwVFEAYGQTECTAgCSITSPGDWTAGH--VGTPVSCNFVKLEDvADMNYFSV 482
Cdd:cd17645 218 ----RVLLTGGDKLKKIERKGYK------LVNNYGPTENTV-VATSFEIDKPYANipIGKPIDNTRVYILD-EALQLQPI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 483 NNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWL------HTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIENV 556
Cdd:cd17645 286 GVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIEPF 364
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1958650325 557 ---YSRSRPILQVFVHGESLRSFLIGVVVP----DPESLPSFAAK 594
Cdd:cd17645 365 lmnHPLIELAAVLAKEDADGRKYLVAYVTApeeiPHEELREWLKN 409
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
100-568 |
9.88e-13 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 70.94 E-value: 9.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 100 WISYKQVSDRAEYLGSCLLHKGYKPSqDQfIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVI 179
Cdd:PRK06155 46 RWTYAEAARAAAAAAHALAAAGVKRG-DR-VALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 180 CDTPQKAtmLIENVEKDLTPgLKTVILMDPFDDDLMKRGEKCgIEMLSLHDAENlgkenfkkPVPPNPEDLSVICFTSGT 259
Cdd:PRK06155 124 VEAALLA--ALEAADPGDLP-LPAVWLLDAPASVSVPAGWST-APLPPLDAPAP--------AAAVQPGDTAAILYTSGT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 260 TGDPKGAMLTHQNIV---SNMAAFLKFlepifqpTPEDVTISYLPLAH------MFERLVQGVIFSCGGKI---GFFqgd 327
Cdd:PRK06155 192 TGPSKGVCCPHAQFYwwgRNSAEDLEI-------GADDVLYTTLPLFHtnalnaFFQALLAGATYVLEPRFsasGFW--- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 328 irllpDDMKALKPTVFptvprllnrvydkvqneaktplkkFLLNlAIISkfnevrngIIrrnslwdkLVFSKIQSSLGGK 407
Cdd:PRK06155 262 -----PAVRRHGATVT------------------------YLLG-AMVS--------IL--------LSQPARESDRAHR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 408 VRLMITGAAPIStpVLTFFRAAMGCWVFEAYGQTECTAGCSITSPGD--WTAGHVGTPVSCNFVKLEDVAdmnyFSVNNE 485
Cdd:PRK06155 296 VRVALGPGVPAA--LHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQrpGSMGRLAPGFEARVVDEHDQE----LPDGEP 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 486 GEICIKGNNVF---KGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKlAQGEYIAPEKIENVYSRSRP 562
Cdd:PRK06155 370 GELLLRADEPFafaTGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIKDAIR-RRGENISSFEVEQVLLSHPA 447
|
....*.
gi 1958650325 563 ILQVFV 568
Cdd:PRK06155 448 VAAAAV 453
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
101-587 |
1.81e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 70.34 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEWVISELACyTYSMVAVPLYDT-LGAEAIIYVINRADISVVI 179
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRA--GDGVAVLARNHRGFVLALYAA-GKVGARIILLNTgFSGPQLAEVAAREGVKALV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 180 CDtpQKATMLIENVEKDLtPGLKTVIlMDPFDDDLMKRGEKCGIEMLSLHDAENLgkenfkkPVPPNPEdlSVICFTSGT 259
Cdd:PRK07788 152 YD--DEFTDLLSALPPDL-GRLRAWG-GNPDDDEPSGSTDETLDDLIAGSSTAPL-------PKPPKPG--GIVILTSGT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 260 TGDPKGAMLTHQNIVSNMAAFLKFLepifqPTPEDVTISyLPlAHMFERLvqGviFSCGGkIGFFQG---------DIRL 330
Cdd:PRK07788 219 TGTPKGAPRPEPSPLAPLAGLLSRV-----PFRAGETTL-LP-APMFHAT--G--WAHLT-LAMALGstvvlrrrfDPEA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 331 LPDDMKALKPTVFPTVPRLLNRVYDKVQNeaktplkkfllnlaIISKFNevrngiirrnslwdklvfskiQSSLggkvRL 410
Cdd:PRK07788 287 TLEDIAKHKATALVVVPVMLSRILDLGPE--------------VLAKYD---------------------TSSL----KI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 411 MITGAAPISTPVLTFFRAAMGCWVFEAYGQTECtAGCSITSPGDWTA--GHVGTPVSCNFVKLEDvADMNYFSVNNEGEI 488
Cdd:PRK07788 328 IFVSGSALSPELATRALEAFGPVLYNLYGSTEV-AFATIATPEDLAEapGTVGRPPKGVTVKILD-ENGNEVPRGVVGRI 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 489 CIKGNNVFKGYLKDPEKtQEVldkDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENVYSRSRPILQVFV 568
Cdd:PRK07788 406 FVGNGFPFEGYTDGRDK-QII---DGLLSSGDVGYFDEDGLLFVDGRDDDMI-VSGGENVFPAEVEDLLAGHPDVVEAAV 480
|
490 500
....*....|....*....|....*.
gi 1958650325 569 -------HGESLRSFligvVVPDPES 587
Cdd:PRK07788 481 igvddeeFGQRLRAF----VVKAPGA 502
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
102-593 |
2.08e-12 |
|
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: 69.59 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 102 SYKQVSDRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIcd 181
Cdd:cd17652 14 TYAELNARANRLARLLAARGVGP--ERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLL-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 182 tpqkaTMlienvekdltpglktvilmdpfdddlmkrgekcgiemlslhdaenlgkenfkkpvppnPEDLSVICFTSGTTG 261
Cdd:cd17652 90 -----TT----------------------------------------------------------PDNLAYVIYTSGSTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 262 DPKGAMLTHQNIVSNMAAFLKFlepiFQPTPEDVTISYLPL---AHMFERLVqgvIFSCGGkigffqgdiRLlpddmkal 338
Cdd:cd17652 107 RPKGVVVTHRGLANLAAAQIAA----FDVGPGSRVLQFASPsfdASVWELLM---ALLAGA---------TL-------- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 339 kptVFPTVPRLLnrvydkvqneAKTPLKKFLlnlaiiskfnevRNGIIRRNSLWDKLVFSKIQSSLGGKVRLMITGAAPi 418
Cdd:cd17652 163 ---VLAPAEELL----------PGEPLADLL------------REHRITHVTLPPAALAALPPDDLPDLRTLVVAGEAC- 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 419 sTPVLTFfRAAMGCWVFEAYGQTECTAGCSITSP-GDWTAGHVGTPVSCNFVKLEDvADMNYFSVNNEGEICIKGNNVFK 497
Cdd:cd17652 217 -PAELVD-RWAPGRRMINAYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYVLD-ARLRPVPPGVPGELYIAGAGLAR 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 498 GYLKDPEKTQE--VLDKDGWL-----HTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIENVYSRSRPILQ--VFV 568
Cdd:cd17652 294 GYLNRPGLTAErfVADPFGAPgsrmyRTGDLARWRADGQLEFLGRADDQVKI-RGFRIELGEVEAALTEHPGVAEavVVV 372
|
490 500
....*....|....*....|....*.
gi 1958650325 569 HGESL-RSFLIGVVVPDPESLPSFAA 593
Cdd:cd17652 373 RDDRPgDKRLVAYVVPAPGAAPTAAE 398
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
101-542 |
2.29e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 70.76 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIC 180
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGVGP--EVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLT 2106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 DTPQKATMLIenvekdltPGlktvilmdpfdddlmkrgekcGIEMLSLHDAENLGKENFKKPVPP-NPEDLSVICFTSGT 259
Cdd:PRK12316 2107 QRHLLERLPL--------PA---------------------GVARLPLDRDAEWADYPDTAPAVQlAGENLAYVIYTSGS 2157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 260 TGDPKGAMLTHqnivSNMAAFLKFLEPIFQPTPEDVTISYLPLAhmFERLVQGVIFS-CGGKIGFFQGDIRLLP----DD 334
Cdd:PRK12316 2158 TGLPKGVAVSH----GALVAHCQAAGERYELSPADCELQFMSFS--FDGAHEQWFHPlLNGARVLIRDDELWDPeqlyDE 2231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 335 MKALKPTVFPTVPRLLNRVYDKVQNEAKTPlkkfllnlaiiskfnevrngiirrnslwdklvfskiqsslggKVRLMITG 414
Cdd:PRK12316 2232 MERHGVTILDFPPVYLQQLAEHAERDGRPP------------------------------------------AVRVYCFG 2269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 415 AAPISTPVLTFFRAAMGC-WVFEAYGQTEctagcSITSPGDWTAGH----------VGTPVSCNFVKLEDvADMNYFSVN 483
Cdd:PRK12316 2270 GEAVPAASLRLAWEALRPvYLFNGYGPTE-----AVVTPLLWKCRPqdpcgaayvpIGRALGNRRAYILD-ADLNLLAPG 2343
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958650325 484 NEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLH-------TGDIGRWLPNGTLKIIDRKKNIFKL 542
Cdd:PRK12316 2344 MAGELYLGGEGLARGYLNRPGLTAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKI 2409
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
101-556 |
2.48e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 69.77 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPSQDqfIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIC 180
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGVRRGDR--VAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 DTPQKATML---IENVEKDLTPGLKTVILMDPFDDDLMKRGEKCGIEMLSLHDAENLGKenfkKPVPPNPEDLSVICFT- 256
Cdd:PRK06164 114 WPGFKGIDFaaiLAAVPPDALPPLRAIAVVDDAADATPAPAPGARVQLFALPDPAPPAA----AGERAADPDAGALLFTt 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 257 SGTTGDPK------GAMLTHQNIVSNMAAFlkflepifqpTPEDVTISYLPlahmferlVQGViFSCGGKIGFFQGDIRL 330
Cdd:PRK06164 190 SGTTSGPKlvlhrqATLLRHARAIARAYGY----------DPGAVLLAALP--------FCGV-FGFSTLLGALAGGAPL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 331 LPDDmkalkptVFPTvPRLLNRVYD-KV-----QNEAKTPLkkflLNLAIISK-FNEVRngiirrnslwdKLVFSKIQSS 403
Cdd:PRK06164 251 VCEP-------VFDA-ARTARALRRhRVthtfgNDEMLRRI----LDTAGERAdFPSAR-----------LFGFASFAPA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 404 LGGKVRLMITGAAPISTpvltffraamgcwvfeAYGQTECTAGCSI-TSPGDWTAGHV--GTPVSCNF-VKLEDVADMNY 479
Cdd:PRK06164 308 LGELAALARARGVPLTG----------------LYGSSEVQALVALqPATDPVSVRIEggGRPASPEArVRARDPQDGAL 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958650325 480 FSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENV 556
Cdd:PRK06164 372 LPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNPAEIEHA 447
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
101-556 |
3.45e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 69.14 E-value: 3.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPsQDQfIGIFAQNRPEWVISELACYTYSMVAVPL-YDTLGAEaIIYVINRADISVVI 179
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGP-GDH-VGIYARNRIEYVEAMLGAFKARAVPVNVnYRYVEDE-LRYLLDDSDAVALV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 180 CD---TPQKATMLienvekDLTPGLKTVILMDpfdDDLMKRGEKCGI---EMLSLHDAENLgkenfkkPVPPNPEDLSVI 253
Cdd:PRK07798 106 YErefAPRVAEVL------PRLPKLRTLVVVE---DGSGNDLLPGAVdyeDALAAGSPERD-------FGERSPDDLYLL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 254 CfTSGTTGDPKGAMLTHQNIVsnMAAF--LKFLEPIFQPTPEDVT--------ISYLPLAHMFERLVQGVIFScggkiGF 323
Cdd:PRK07798 170 Y-TGGTTGMPKGVMWRQEDIF--RVLLggRDFATGEPIEDEEELAkraaagpgMRRFPAPPLMHGAGQWAAFA-----AL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 324 FQGDirllpddmkalkPTVFPTVPRL-LNRVYDKVQNE------------AKtPLKKFLLNlaiiskfnevRNGiirrns 390
Cdd:PRK07798 242 FSGQ------------TVVLLPDVRFdADEVWRTIEREkvnvitivgdamAR-PLLDALEA----------RGP------ 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 391 lWDklvfskiQSSLggkvRLMITGAAPISTPVLTFFRAAM-GCWVFEAYGQTECTAGCSITSPGDwtAGHVGTPV----- 464
Cdd:PRK07798 293 -YD-------LSSL----FAIASGGALFSPSVKEALLELLpNVVLTDSIGSSETGFGGSGTVAKG--AVHTGGPRftigp 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 465 SCnFVKLEDvadmNYFSVNNEGEICI--KGNNVFKGYLKDPEKTQEVL-DKDG--WLHTGDIGRWLPNGTLKIIDRKKNI 539
Cdd:PRK07798 359 RT-VVLDED----GNPVEPGSGEIGWiaRRGHIPLGYYKDPEKTAETFpTIDGvrYAIPGDRARVEADGTITLLGRGSVC 433
|
490
....*....|....*..
gi 1958650325 540 FKLAqGEYIAPEKIENV 556
Cdd:PRK07798 434 INTG-GEKVFPEEVEEA 449
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
103-554 |
3.90e-12 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 69.26 E-value: 3.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 103 YKQVSDRAEYLGSCLLHKGYKPsQDQfIGIFAQNRPEWVISELACYTYSMVAVPLY--DTLGAEAIiYVinrADISVVIc 180
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKP-GDR-VALIAETDGDFVEAFFACQYAGLVPVPLPlpMGFGGRES-YI---AQLRGML- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 dTPQKATMLIENVE-----KDLTPGLKTVILMDPfdddlmkrgekcgiEMLSLHDAENLgkenfkkPVPPN-PEDLSVIC 254
Cdd:PRK09192 125 -ASAQPAAIITPDEllpwvNEATHGNPLLHVLSH--------------AWFKALPEADV-------ALPRPtPDDIAYLQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 255 FTSGTTGDPKGAMLTHQNIVSNMAAF----LKFLepifqptPEDVTISYLPLAH-MferlvqgvifscgGKIGFFqgdir 329
Cdd:PRK09192 183 YSSGSTRFPRGVIITHRALMANLRAIshdgLKVR-------PGDRCVSWLPFYHdM-------------GLVGFL----- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 330 llpddmkaLKPtvfptvprLLNRV---YDKVQNEAKTPLkkflLNLAIISKfNEvrnGII------------RRNSLWDK 394
Cdd:PRK09192 238 --------LTP--------VATQLsvdYLPTRDFARRPL----QWLDLISR-NR---GTIsysppfgyelcaRRVNSKDL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 395 LVFSkiQSSLggkvRLMITGAAPISTPVLTFFRAAMGCWVFEA------YGQTECTAGCSITSPG--------------- 453
Cdd:PRK09192 294 AELD--LSCW----RVAGIGADMIRPDVLHQFAEAFAPAGFDDkafmpsYGLAEATLAVSFSPLGsgivveevdrdrley 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 454 -------DWTAGHVGTPVSC------NFVKLEDVADmnyfSVNNE---GEICIKGNNVFKGYLKDPEkTQEVLDKDGWLH 517
Cdd:PRK09192 368 qgkavapGAETRRVRTFVNCgkalpgHEIEIRNEAG----MPLPErvvGHICVRGPSLMSGYFRDEE-SQDVLAADGWLD 442
|
490 500 510
....*....|....*....|....*....|....*..
gi 1958650325 518 TGDIGrWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIE 554
Cdd:PRK09192 443 TGDLG-YLLDGYLYITGRAKDLI-IINGRNIWPQDIE 477
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
242-583 |
4.29e-12 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 69.16 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 242 PVPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAfLKFLEPIfqpTPEDVTISYLPLahmFerlvqgVIFS--CGG 319
Cdd:PRK09274 168 MADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEA-LREDYGI---EPGEIDLPTFPL---F------ALFGpaLGM 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 320 KigffqgdiRLLPDdMKALKP-TVFPtvprllNRVYDKVQNEAKTPLkkFLlNLAIISKfnevrngiIRRNSLWDKLVFS 398
Cdd:PRK09274 235 T--------SVIPD-MDPTRPaTVDP------AKLFAAIERYGVTNL--FG-SPALLER--------LGRYGEANGIKLP 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 399 KiqsslggkVRLMITGAAPISTPVLTFFRAAM--GCWVFEAYGQTECTAGCSITS------PGDWT---AGH-VGTPVSC 466
Cdd:PRK09274 289 S--------LRRVISAGAPVPIAVIERFRAMLppDAEILTPYGATEALPISSIESreilfaTRAATdngAGIcVGRPVDG 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 467 NFVKLEDVAD--MNYFS------VNNEGEICIKGNNVFKGYLKDPEKTQE--VLDKDG--WLHTGDIGRWLPNGTLKIID 534
Cdd:PRK09274 361 VEVRIIAISDapIPEWDdalrlaTGEIGEIVVAGPMVTRSYYNRPEATRLakIPDGQGdvWHRMGDLGYLDAQGRLWFCG 440
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1958650325 535 RKKNIFKLAQGEY--IAPEKIENVYSrsrpilQVFvhgeslRSFLIGVVVP 583
Cdd:PRK09274 441 RKAHRVETAGGTLytIPCERIFNTHP------GVK------RSALVGVGVP 479
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
102-556 |
4.51e-12 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 69.01 E-value: 4.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 102 SYKQVSDRAEYLGSCLLHKGYKPSqDQfIGIFAQNRPEwvisELACYTYSMVAVPLYDTLG----AEAIIYVINRADISV 177
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLG-DR-VATIAWNTWR----HLEAWYGIMGIGAICHTVNprlfPEQIAWIINHAEDRV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 178 VICDT---PqkatmLIENVeKDLTPGLKTVILMDpfDDDLMKR----GEKCGIEMLSLHDAenlgkeNFK-KPVPPNPEd 249
Cdd:PRK06018 115 VITDLtfvP-----ILEKI-ADKLPSVERYVVLT--DAAHMPQttlkNAVAYEEWIAEADG------DFAwKTFDENTA- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 250 lSVICFTSGTTGDPKGAMLTHQ-NIVSNMAAFLKflePIFQPTPEDVTisyLPLAHMFERLVQGVIFSC---GGKI---- 321
Cdd:PRK06018 180 -AGMCYTSGTTGDPKGVLYSHRsNVLHALMANNG---DALGTSAADTM---LPVVPLFHANSWGIAFSApsmGTKLvmpg 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 322 ----GffqGDIRLLPDDMKALKPTVFPTVPRLLnrvydkVQNEAKTPLKKFLLNLAIIskfnevrngiirrnslwdklvf 397
Cdd:PRK06018 253 akldG---ASVYELLDTEKVTFTAGVPTVWLML------LQYMEKEGLKLPHLKMVVC---------------------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 398 skiqsslGGkvrlmitGAAPIStpVLTFFRAaMGCWVFEAYGQTEctagcsiTSPgdwtAGHVGTpVSCNFVKLEDVADM 477
Cdd:PRK06018 302 -------GG-------SAMPRS--MIKAFED-MGVEVRHAWGMTE-------MSP----LGTLAA-LKPPFSKLPGDARL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 478 NY--------FSV--------NNE--------GEICIKGNNVFKGYLKdpeKTQEVLDKDGWLHTGDIGRWLPNGTLKII 533
Cdd:PRK06018 353 DVlqkqgyppFGVemkitddaGKElpwdgktfGRLKVRGPAVAAAYYR---VDGEILDDDGFFDTGDVATIDAYGYMRIT 429
|
490 500
....*....|....*....|...
gi 1958650325 534 DRKKNIFKlAQGEYIAPEKIENV 556
Cdd:PRK06018 430 DRSKDVIK-SGGEWISSIDLENL 451
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
247-554 |
5.37e-12 |
|
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: 68.55 E-value: 5.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 247 PEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFlepiFQPTPEDVTISYLPL----AHmfERLVQGVIfsCGGKIg 322
Cdd:cd17649 93 PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAER----YGLTPGDRELQFASFnfdgAH--EQLLPPLI--CGACV- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 323 ffqgdirLLPDDMKALKPtvfptvprllNRVYDKVQNEAKTplkkfLLNLAiiskfnevrngiirrNSLWDKLV--FSKI 400
Cdd:cd17649 164 -------VLRPDELWASA----------DELAEMVRELGVT-----VLDLP---------------PAYLQQLAeeADRT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 401 QSSLGGKVRLMITGAAPISTPVLTffRAAM-GCWVFEAYGQTECTagcsITS------PGDWTAGH---VGTPVSCNFVK 470
Cdd:cd17649 207 GDGRPPSLRLYIFGGEALSPELLR--RWLKaPVRLFNAYGPTEAT----VTPlvwkceAGAARAGAsmpIGRPLGGRSAY 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 471 LEDvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQE--VLDKDG-----WLHTGDIGRWLPNGTLKIIDRKKNIFKLa 543
Cdd:cd17649 281 ILD-ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAErfVPDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI- 358
|
330
....*....|.
gi 1958650325 544 QGEYIAPEKIE 554
Cdd:cd17649 359 RGFRIELGEIE 369
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
255-586 |
8.71e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 68.18 E-value: 8.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 255 FTSGTTGDPKG--AMLTHQNIVSNMAAFlKFLEPIFQPTPEDVTISYLPLAHMFERLVQGVIFSCGGKIGFFQgdiRLLP 332
Cdd:PRK13391 161 YSSGTTGRPKGikRPLPEQPPDTPLPLT-AFLQRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVME---HFDA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 333 DDMKAL----KPTVFPTVPRLLNRVYdkvqneaKTPlkkfllnlaiiskfNEVRNgiirRNSLwdklvfskiqSSLggkv 408
Cdd:PRK13391 237 EQYLALieeyGVTHTQLVPTMFSRML-------KLP--------------EEVRD----KYDL----------SSL---- 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 409 RLMITGAAPisTPVLTffRAAMGCW----VFEAYGQTECTAGCSITSPgDWTA--GHVGTPVSCNFVKLEDvaDMNYFSV 482
Cdd:PRK13391 278 EVAIHAAAP--CPPQV--KEQMIDWwgpiIHEYYAATEGLGFTACDSE-EWLAhpGTVGRAMFGDLHILDD--DGAELPP 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 483 NNEGEICIKGNNVFKgYLKDPEKTQEVLDKDG-WLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENVysrsr 561
Cdd:PRK13391 351 GEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMI-ISGGVNIYPQEAENL----- 423
|
330 340
....*....|....*....|....*
gi 1958650325 562 pilqVFVHGESLRSFLIGvvVPDPE 586
Cdd:PRK13391 424 ----LITHPKVADAAVFG--VPNED 442
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
252-585 |
9.85e-12 |
|
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: 66.56 E-value: 9.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 252 VICFTSGTTGDPKGAMLTHQNIVSnMAAFLKFLEPIfqpTPEDVTISYLPLAHMFERLVQGVIFSCGGKigffqgdirll 331
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALLA-QALVLAVLQAI---DEGTVFLNSGPLFHIGTLMFTLATFHAGGT----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 332 pddmkalkpTVFptVPRL-LNRVYDKVQNEAKTplKKFLLNLAI--ISKFNevrngiirRNSLWDklvFSKIQSSLGGKV 408
Cdd:cd17636 69 ---------NVF--VRRVdAEEVLELIEAERCT--HAFLLPPTIdqIVELN--------ADGLYD---LSSLRSSPAAPE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 409 RLMitgAAPISTPvlTFFRAAMGcwvfeaYGQTECTAGCSITSPGDWTAGHVGTPVSCNFVKLEDvADMNYFSVNNEGEI 488
Cdd:cd17636 125 WND---MATVDTS--PWGRKPGG------YGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILD-EDGREVPDGEVGEI 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 489 CIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENVYsRSRP-ILQVF 567
Cdd:cd17636 193 VARGPTVMAGYWNRPEVNARRT-RGGWHHTNDLGRREPDGSLSFVGPKTRMIKSG-AENIYPAEVERCL-RQHPaVADAA 269
|
330
....*....|....*...
gi 1958650325 568 VhgeslrsflIGvvVPDP 585
Cdd:cd17636 270 V---------IG--VPDP 276
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
436-556 |
1.20e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 67.60 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 436 EAYGQTECTAGCSITSPGDWTA--GHVGTPVSCNFVKLEDvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLdKD 513
Cdd:PRK06145 295 DAYGLTETCSGDTLMEAGREIEkiGSTGRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YG 372
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1958650325 514 GWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENV 556
Cdd:PRK06145 373 DWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERV 414
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
255-586 |
5.65e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 65.31 E-value: 5.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 255 FTSGTTGDPKGAM--LTHQNIVSNMAAFLKFLEPIFQPTPEDVTISYLPLAHMFERLVQGVIFSCGGKIGFFQgdiRLLP 332
Cdd:PRK08276 147 YSSGTTGRPKGIKrpLPGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAPLRFGMSALALGGTVVVME---KFDA 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 333 DDMKAL----KPTVFPTVPRLLNRvydkvqneaktplkkfLLNLAiiskfNEVRNgiirRNSLwdklvfskiqSSLggkv 408
Cdd:PRK08276 224 EEALALieryRVTHSQLVPTMFVR----------------MLKLP-----EEVRA----RYDV----------SSL---- 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 409 RLMITGAAPISTPVltffRAAMGCW----VFEAYGQTEcTAGCSITSPGDWTA--GHVGTPVSCNFVKLEDvaDMNYFSV 482
Cdd:PRK08276 265 RVAIHAAAPCPVEV----KRAMIDWwgpiIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGEVRILDE--DGNELPP 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 483 NNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGrWL-PNGTLKIIDRKKNIFkLAQGEYIAPEKIENVYSRSR 561
Cdd:PRK08276 338 GEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVG-YLdEDGYLYLTDRKSDMI-ISGGVNIYPQEIENLLVTHP 415
|
330 340
....*....|....*....|....*
gi 1958650325 562 PILQVFVHGeslrsfligvvVPDPE 586
Cdd:PRK08276 416 KVADVAVFG-----------VPDEE 429
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
230-556 |
5.67e-11 |
|
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: 65.53 E-value: 5.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 230 DAENLGKENFKKPVPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFLEPIFQPTPedVTISYLPLAHMFERL 309
Cdd:cd05915 135 LAYEEALGEEADPVRVPERAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKD--VVLPVVPMFHVNAWC 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 310 VQGVIFSCGGKIGFfqgdIRLLPDDmkalkPTVFPTVprllnrVYDKVQNEAKTPlkkfllnlaiiSKFNEVRNGiirRN 389
Cdd:cd05915 213 LPYAATLVGAKQVL----PGPRLDP-----ASLVELF------DGEGVTFTAGVP-----------TVWLALADY---LE 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 390 SlwdklvfskIQSSLGGKVRLMITGAAP----ISTPVLTFFRAAMGCWVFEAYG-QTECTAGCSITSPGDWTAGHVGTPV 464
Cdd:cd05915 264 S---------TGHRLKTLRRLVVGGSAAprslIARFERMGVEVRQGYGLTETSPvVVQNFVKSHLESLSEEEKLTLKAKT 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 465 SCN-FVKLEDVADMNYFSVNNEGE----ICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNI 539
Cdd:cd05915 335 GLPiPLVRLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDL 414
|
330
....*....|....*..
gi 1958650325 540 FKLAqGEYIAPEKIENV 556
Cdd:cd05915 415 IKSG-GEWISSVDLENA 430
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
245-583 |
6.07e-11 |
|
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: 65.17 E-value: 6.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 245 PNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAflkfLEPIFQPTPEDVTISYLPLAHMFERLVqgvifscggkigff 324
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDA----LRQLYGIRPGEVDLATFPLFALFGPAL-------------- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 325 qGDIRLLPDdMKALKPTvfPTVPRLLnrvydkVQneaktPLKKFLLNLAIISKfnevrnGIIRRNSLWDKLVFSKIQSsl 404
Cdd:cd05910 144 -GLTSVIPD-MDPTRPA--RADPQKL------VG-----AIRQYGVSIVFGSP------ALLERVARYCAQHGITLPS-- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 405 ggkVRLMITGAAPISTPVLTFFRAAM--GCWVFEAYGQTECTAGCSI------TSPGDWTAGH----VGTPVSCNFVKLE 472
Cdd:cd05910 201 ---LRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSIgsrellATTTAATSGGagtcVGRPIPGVRVRII 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 473 DVADMNYFSVNNE--------GEICIKGNNVFKGYLKDPEKTQ--EVLDKDG--WLHTGDIGRWLPNGTLKIIDRKKNIF 540
Cdd:cd05910 278 EIDDEPIAEWDDTlelprgeiGEITVTGPTVTPTYVNRPVATAlaKIDDNSEgfWHRMGDLGYLDDEGRLWFCGRKAHRV 357
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1958650325 541 KLAQGEYIApEKIENVYSrsrpilqvfVHGESLRSFLIGVVVP 583
Cdd:cd05910 358 ITTGGTLYT-EPVERVFN---------THPGVRRSALVGVGKP 390
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
102-602 |
8.37e-11 |
|
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: 64.45 E-value: 8.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 102 SYKQVSDRAEYLGSCLLHKGYKPSQDQFIgiFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIcd 181
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFV--LSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 182 tpqkatmlienvekdLTPGLKtvilmdpfdddlmkrgEKCgiemlslhdaenlgkenfkkpvppNPEDLSVICFTSGTTG 261
Cdd:cd05969 78 ---------------TTEELY----------------ERT------------------------DPEDPTLLHYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 262 DPKGAMLTHqnivsnmaaflkflepifqptpEDVTISYLPLAHMFErLVQGVIFSCGGKIGFFQGdirllpddmkalkpT 341
Cdd:cd05969 103 TPKGVLHVH----------------------DAMIFYYFTGKYVLD-LHPDDIYWCTADPGWVTG--------------T 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 342 VFPTVPRLLNRVyDKVQNEAKTPLKKFLLNLA--IISKFNEVRNGIIRRNSLWDKLVFSKIQSSLggkvRLMITGAAPIS 419
Cdd:cd05969 146 VYGIWAPWLNGV-TNVVYEGRFDAESWYGIIErvKVTVWYTAPTAIRMLMKEGDELARKYDLSSL----RFIHSVGEPLN 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 420 TPVLTFFRAAMGCWVFEAYGQTEcTAGCSITS-PG-DWTAGHVGTPVSCnfVKLEDV-ADMNYFSVNNEGEICIKGN--N 494
Cdd:cd05969 221 PEAIRWGMEVFGVPIHDTWWQTE-TGSIMIANyPCmPIKPGSMGKPLPG--VKAAVVdENGNELPPGTKGILALKPGwpS 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 495 VFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENVYSRSRPILQVFVHGeslr 574
Cdd:cd05969 298 MFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHRVGPFEVESALMEHPAVAEAGVIG---- 371
|
490 500
....*....|....*....|....*...
gi 1958650325 575 sfligvvVPDPESLPSFAAKIGVKGSFE 602
Cdd:cd05969 372 -------KPDPLRGEIIKAFISLKEGFE 392
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
402-556 |
2.18e-10 |
|
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: 63.63 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 402 SSLggkvRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTEctaG-CSITSPGD---WTAGHVGTPVSC-NFVKL----- 471
Cdd:COG1021 300 SSL----RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---GlVNYTRLDDpeeVILTTQGRPISPdDEVRIvdedg 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 472 EDVADmnyfsvNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNifklaQ----GEY 547
Cdd:COG1021 373 NPVPP------GEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKD-----QinrgGEK 441
|
....*....
gi 1958650325 548 IAPEKIENV 556
Cdd:COG1021 442 IAAEEVENL 450
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
101-271 |
4.43e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 62.61 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPSQDQFIgiFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIC 180
Cdd:PRK04319 74 YTYKELKELSNKFANVLKELGVEKGDRVFI--FMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLIT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 dTPQkatmLIENVEKDLTPGLKTVILMDPFDDDlmkrGEKCgiemLSLHDAENLGKENFKkPVPPNPEDLSVICFTSGTT 260
Cdd:PRK04319 152 -TPA----LLERKPADDLPSLKHVLLVGEDVEE----GPGT----LDFNALMEQASDEFD-IEWTDREDGAILHYTSGST 217
|
170
....*....|.
gi 1958650325 261 GDPKGAMLTHQ 271
Cdd:PRK04319 218 GKPKGVLHVHN 228
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
249-555 |
1.14e-09 |
|
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: 61.19 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 249 DLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKflepIFQPTPEDVTISYLPLAHMFERLVQGVI--FSCGGKIgffqg 326
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAE----VCGLDQDTVYLAVLPAAHNFPLACPGVLgtLLAGGRV----- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 327 dirLLPDDMKALKptVFPTVPRllnrvyDKVQNEAKTPlkkfllnlAIISkfnevrngiirrnsLW-DKLVFSKIQ-SSL 404
Cdd:cd05920 211 ---VLAPDPSPDA--AFPLIER------EGVTVTALVP--------ALVS--------------LWlDAAASRRADlSSL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 405 ggkvRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTE----CTAgcsITSPGDWTAGHVGTPVSC-NFVKLEDvADMNY 479
Cdd:cd05920 258 ----RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEgllnYTR---LDDPDEVIIHTQGRPMSPdDEIRVVD-EEGNP 329
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958650325 480 FSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIEN 555
Cdd:cd05920 330 VPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVEN 404
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
412-588 |
1.43e-09 |
|
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: 60.94 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 412 ITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCSITSPGDWTAGHVGTPVSCNFVKLEDVaDMNYFSVNNEGEICIK 491
Cdd:cd05928 297 VTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDD-NGNVLPPGTEGDIGIR 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 492 GNNV-----FKGYLKDPEKTQEVLDKDGWLhTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIEN----------- 555
Cdd:cd05928 376 VKPIrpfglFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYRIGPFEVESaliehpavves 453
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958650325 556 -VYSRSRPIlqvfvHGESLRSFLigVVVP-----DPESL 588
Cdd:cd05928 454 aVVSSPDPI-----RGEVVKAFV--VLAPqflshDPEQL 485
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
101-606 |
1.61e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 60.79 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPSQdqFIGIFAQNRPEWVIselacYTYSMVAVPLYDTlgaeAIIYVINRADISVVIC 180
Cdd:PRK13390 25 VSYRQLDDDSAALARVLYDAGLRTGD--VVALLSDNSPEALV-----VLWAALRSGLYIT----AINHHLTAPEADYIVG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 DTpqkatmlienvekdltpGLKTVILMDPFDDDLMKRGEKCGIEMLSLHDAENLG--KENFKKPVPPNPEDL--SVICFT 256
Cdd:PRK13390 94 DS-----------------GARVLVASAALDGLAAKVGADLPLRLSFGGEIDGFGsfEAALAGAGPRLTEQPcgAVMLYS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 257 SGTTGDPKGAM--LTHQNIVSNMAAFLKFLEPIFQPTPEDVTISYLPLAHMFERLVQGVIFSCGGKIGFFQG-DIRLLPD 333
Cdd:PRK13390 157 SGTTGFPKGIQpdLPGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHAAPLRWCSMVHALGGTVVLAKRfDAQATLG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 334 DMKALKPTVFPTVPRLLNRVydkvqneaktpLKkflLNLAIISKFNevrngiirrnslwdklvfskiQSSLggkvRLMIT 413
Cdd:PRK13390 237 HVERYRITVTQMVPTMFVRL-----------LK---LDADVRTRYD---------------------VSSL----RAVIH 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 414 GAAPISTPVltffRAAMGCW----VFEAYGQTEcTAGCSITSPGDWTA--GHVGTPVSCNFVKLEDvaDMNYFSVNNEGE 487
Cdd:PRK13390 278 AAAPCPVDV----KHAMIDWlgpiVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGRSVLGDLHICDD--DGNELPAGRIGT 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 488 ICIKGNNVFKGYLKDPEKTQEVLDKDG--WLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENVYSRSRPILQ 565
Cdd:PRK13390 351 VYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQETENALTMHPAVHD 429
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1958650325 566 VFVHGeslrsfligvvVPDPESLPSFAAKI----GVKGSfEELCQ 606
Cdd:PRK13390 430 VAVIG-----------VPDPEMGEQVKAVIqlveGIRGS-DELAR 462
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
400-588 |
1.94e-09 |
|
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: 60.27 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 400 IQSSLGG---KVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCSiTSPGD-WTAGHVGTPVSCNFVKLEDVA 475
Cdd:cd05974 191 IQQDLASfdvKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVG-NSPGQpVKAGSMGRPLPGYRVALLDPD 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 476 DmnyfSVNNEGEICIK-GNN----VFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKlAQGEYIAP 550
Cdd:cd05974 270 G----APATEGEVALDlGDTrpvgLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SSDYRISP 343
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958650325 551 EKIENVYSRSRPILQVFVhgeslrsfligVVVPDPESL 588
Cdd:cd05974 344 FELESVLIEHPAVAEAAV-----------VPSPDPVRL 370
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
164-556 |
3.04e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 60.11 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 164 EAIIYVINRADISVVICDT---PqkatmLIENVEKDLtPGLKTVILMDpfDDDLMKRGEkcgIEMLSLHDAenLGKENFK 240
Cdd:PRK07008 101 EQIAYIVNHAEDRYVLFDLtflP-----LVDALAPQC-PNVKGWVAMT--DAAHLPAGS---TPLLCYETL--VGAQDGD 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 241 KPVPPNPEDL-SVICFTSGTTGDPKGAMLTHQNIVsnMAAFLKFLEPIFQPTPEDVTisyLPLAHMFERLVQGVIFSC-- 317
Cdd:PRK07008 168 YDWPRFDENQaSSLCYTSGTTGNPKGALYSHRSTV--LHAYGAALPDAMGLSARDAV---LPVVPMFHVNAWGLPYSApl 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 318 -GGKIgffqgdirllpddmkalkptVFPTvPRLLNR-VYDKVQNE-----AKTPLKKFLLnlaiiskFNEVRNGiirrns 390
Cdd:PRK07008 243 tGAKL--------------------VLPG-PDLDGKsLYELIEAErvtfsAGVPTVWLGL-------LNHMREA------ 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 391 lwdKLVFSKIQsslggkvRLMITGAA-PIStpVLTFFRAAMGCWVFEAYGQTECT---AGCSITS-----PGD------W 455
Cdd:PRK07008 289 ---GLRFSTLR-------RTVIGGSAcPPA--MIRTFEDEYGVEVIHAWGMTEMSplgTLCKLKWkhsqlPLDeqrkllE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 456 TAGHVGTPVSCNFVKlEDVADMNYFSVNnEGEICIKGNNVFKGYLKdpeKTQEVLDkDGWLHTGDIGRWLPNGTLKIIDR 535
Cdd:PRK07008 357 KQGRVIYGVDMKIVG-DDGRELPWDGKA-FGDLQVRGPWVIDRYFR---GDASPLV-DGWFPTGDVATIDADGFMQITDR 430
|
410 420
....*....|....*....|.
gi 1958650325 536 KKNIFKlAQGEYIAPEKIENV 556
Cdd:PRK07008 431 SKDVIK-SGGEWISSIDIENV 450
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
95-568 |
4.52e-09 |
|
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: 59.02 E-value: 4.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 95 NQPYKWISYKQVSDRAEYLGSCLLHKGYKPSQdqfigifaqnrpewviselacytysmvAVPLYDTLGAEAIIYVINrad 174
Cdd:cd17654 11 TTSDTTVSYADLAEKISNLSNFLRKKFQTEER---------------------------AIGLRCDRGTESPVAILA--- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 175 ISVVICD-TPQKATMLienvekdltPGLKTVILMDPFDDDLMKRGEKCgIEMLSLHDAenlgKENFKKPVPpnpEDLSVI 253
Cdd:cd17654 61 ILFLGAAyAPIDPASP---------EQRSLTVMKKCHVSYLLQNKELD-NAPLSFTPE----HRHFNIRTD---ECLAYV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 254 CFTSGTTGDPKGAMLTHQNIVSNMAAFLKflepIFQPTPEDVTISYLPLahMFERLVQGVI--FSCGGKIGFFQGDIRLL 331
Cdd:cd17654 124 IHTSGTTGTPKIVAVPHKCILPNIQHFRS----LFNITSEDILFLTSPL--TFDPSVVEIFlsLSSGATLLIVPTSVKVL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 332 PD-----DMKALKPTVFPTVPRLLNRVYDKVqneaktpLKKFLLnlaiiskfnevrngiirrnslwdklvfSKIQSslgg 406
Cdd:cd17654 198 PSkladiLFKRHRITVLQATPTLFRRFGSQS-------IKSTVL---------------------------SATSS---- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 407 kVRLMITGAAPisTPVLTFFRAAMGCW----VFEAYGQTECTAGCSITSPGDWTAG-HVGTPVscnFVKLEDVADMNYFS 481
Cdd:cd17654 240 -LRVLALGGEP--FPSLVILSSWRGKGnrtrIFNIYGITEVSCWALAYKVPEEDSPvQLGSPL---LGTVIEVRDQNGSE 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 482 VnnEGEICIKGNNVfKGYLKDPEKTQEVLdkdgWLHTGDIGRwLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENVYSRSR 561
Cdd:cd17654 314 G--TGQVFLGGLNR-VCILDDEVTVPKGT----MRATGDFVT-VKDGELFFLGRKDSQIKRR-GKRINLDLIQQVIESCL 384
|
....*..
gi 1958650325 562 PILQVFV 568
Cdd:cd17654 385 GVESCAV 391
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
101-604 |
4.73e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 59.97 E-value: 4.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIC 180
Cdd:PRK12316 4577 LTYAELNRRANRLAHALIARGVGP--EVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLT 4654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 DTpqkatmlienvekDLTPGLktvilmdPFDDdlmkrgekcGIEMLSLHDAENL-GKENFKKPVPPNPEDLSVICFTSGT 259
Cdd:PRK12316 4655 QS-------------HLLQRL-------PIPD---------GLASLALDRDEDWeGFPAHDPAVRLHPDNLAYVIYTSGS 4705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 260 TGDPKGAMLTHQNIVSNMAAFLKFlepiFQPTPEDVTISYLPLAhmFERLVQGVI--FSCGGKIgffqgdirLLPDDMKA 337
Cdd:PRK12316 4706 TGRPKGVAVSHGSLVNHLHATGER----YELTPDDRVLQFMSFS--FDGSHEGLYhpLINGASV--------VIRDDSLW 4771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 338 LKPTVFptvpRLLNRVYDKVQNEAKTPLKKFLlnlaiiskfnevrNGIIRRNSLwdklvfskiqsslgGKVRLMITGAAP 417
Cdd:PRK12316 4772 DPERLY----AEIHEHRVTVLVFPPVYLQQLA-------------EHAERDGEP--------------PSLRVYCFGGEA 4820
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 418 ISTPVLT-FFRAAMGCWVFEAYGQTECTAGCSI-TSPGDWTAG----HVGTPVSCNFVKLEDVAdMNYFSVNNEGEICIK 491
Cdd:PRK12316 4821 VAQASYDlAWRALKPVYLFNGYGPTETTVTVLLwKARDGDACGaaymPIGTPLGNRSGYVLDGQ-LNPLPVGVAGELYLG 4899
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 492 GNNVFKGYLKDPEKTQE-----VLDKDG--WLHTGDIGRWLPNGTLKIIDR-----KKNIFKLAQGEYIAPEKIENVYSR 559
Cdd:PRK12316 4900 GEGVARGYLERPALTAErfvpdPFGAPGgrLYRTGDLARYRADGVIDYLGRvdhqvKIRGFRIELGEIEARLREHPAVRE 4979
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1958650325 560 SRPILQVFVHGESlrsfLIGVVVP-DPESLPSFAAKIGVKGSFEEL 604
Cdd:PRK12316 4980 AVVIAQEGAVGKQ----LVGYVVPqDPALADADEAQAELRDELKAA 5021
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
101-587 |
6.15e-09 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 59.00 E-value: 6.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKpsQDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIC 180
Cdd:PRK13382 69 LTWRELDERSDALAAALQALPIG--EPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIY 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 DTPqkatmLIENVEKDL--TPGLKTVILMDPFDDDLMkrgekcgIEMLSlhdAENLGKEnfkkpVPPNPEDLSVICFTSG 258
Cdd:PRK13382 147 DEE-----FSATVDRALadCPQATRIVAWTDEDHDLT-------VEVLI---AAHAGQR-----PEPTGRKGRVILLTSG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 259 TTGDPKGAmlTHQNIVSNMAaflkfLEPIFQPTP---EDVTISYLPLAHM--FERLVQGVIFSCggkigffqgDI----R 329
Cdd:PRK13382 207 TTGTPKGA--RRSGPGGIGT-----LKAILDRTPwraEEPTVIVAPMFHAwgFSQLVLAASLAC---------TIvtrrR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 330 LLPDDMKAL----KPTVFPTVPRLLNRVYDKVQneaktplkkfllnlaiiskfnEVRNgiirrnslwdklvfskiqSSLG 405
Cdd:PRK13382 271 FDPEATLDLidrhRATGLAVVPVMFDRIMDLPA---------------------EVRN------------------RYSG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 406 GKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTEctAG-CSITSPGDWTAG--HVGTPVSCNFVKLEDvADMNYFSV 482
Cdd:PRK13382 312 RSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATE--AGmIATATPADLRAApdTAGRPAEGTEIRILD-QDFREVPT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 483 NNEGEICIKGNNVFKGYlkDPEKTQEVldKDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENVYSRSRP 562
Cdd:PRK13382 389 GEVGTIFVRNDTQFDGY--TSGSTKDF--HDGFMASGDVGYLDENGRLFVVGRDDEMI-VSGGENVYPIEVEKTLATHPD 463
|
490 500
....*....|....*....|....*...
gi 1958650325 563 ILQVFVHG---ESLRSFLIGVVVPDPES 587
Cdd:PRK13382 464 VAEAAVIGvddEQYGQRLAAFVVLKPGA 491
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
244-556 |
1.05e-08 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 58.17 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 244 PPNPEDLSVIcFTSGTTGDPKGAMLthqnivsnmaaflkflepiFQPTPEdvtisylpLAHMFERLVqGVIFscggkiGF 323
Cdd:PRK12406 149 PPVPQPQSMI-YTSGTTGHPKGVRR-------------------AAPTPE--------QAAAAEQMR-ALIY------GL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 324 FQGDIRLLPDDMKALKPTVFPtvpRLLNRVYDKVQNEAKTPLKKFLLNLAI--ISKFNEVRNGIIRRNSLWDKLVFSKIQ 401
Cdd:PRK12406 194 KPGIRALLTGPLYHSAPNAYG---LRAGRLGGVLVLQPRFDPEELLQLIERhrITHMHMVPTMFIRLLKLPEEVRAKYDV 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 402 SSLggkvRLMITGAAPISTPVLtffRAAMGCW---VFEAYGQTECTAGCSITSPgDWTA--GHVGTPVSCNFVKLEDvAD 476
Cdd:PRK12406 271 SSL----RHVIHAAAPCPADVK---RAMIEWWgpvIYEYYGSTESGAVTFATSE-DALShpGTVGKAAPGAELRFVD-ED 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 477 MNYFSVNNEGEIC--IKGNNVFKgYLKDPEKTQEVlDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIE 554
Cdd:PRK12406 342 GRPLPQGEIGEIYsrIAGNPDFT-YHNKPEKRAEI-DRGGFITSGDVGYLDADGYLFLCDRKRDMV-ISGGVNIYPAEIE 418
|
..
gi 1958650325 555 NV 556
Cdd:PRK12406 419 AV 420
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
101-596 |
1.52e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 58.25 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIC 180
Cdd:PRK12467 1600 LTYGELNRRANRLAHRLIALGVGP--EVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLT 1677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 DTPQKATMLIENvekdltpGLKTVILmDPFDDdlmkrgekcgieMLSLHDAENLGkenfkkpVPPNPEDLSVICFTSGTT 260
Cdd:PRK12467 1678 QSHLQARLPLPD-------GLRSLVL-DQEDD------------WLEGYSDSNPA-------VNLAPQNLAYVIYTSGST 1730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 261 GDPKGAMLTHQNIVsnmaAFLKFLEPIFQPTPEDVTISYLPLAhmFERLVQGVIFSC--GGKIGFFQGDIRLLPDDMKAL 338
Cdd:PRK12467 1731 GRPKGAGNRHGALV----NRLCATQEAYQLSAADVVLQFTSFA--FDVSVWELFWPLinGARLVIAPPGAHRDPEQLIQL 1804
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 339 ----KPTVFPTVPRLLNRVYDKVQNEAKtPLKkfllnlaiiskfnevrngiIRRnslwdkLVFskiqsslGGKvrlmitg 414
Cdd:PRK12467 1805 ierqQVTTLHFVPSMLQQLLQMDEQVEH-PLS-------------------LRR------VVC-------GGE------- 1844
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 415 AAPISTPVLTFfrAAMG-CWVFEAYGQTECTAG-----CSITSPGDWTAGHVGTPVSCNFVKLEDvADMNYFSVNNEGEI 488
Cdd:PRK12467 1845 ALEVEALRPWL--ERLPdTGLFNLYGPTETAVDvthwtCRRKDLEGRDSVPIGQPIANLSTYILD-ASLNPVPIGVAGEL 1921
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 489 CIKGNNVFKGYLKDPEKTQE--VLDKDGWL-----HTGDIGRWLPNGTLKI---IDRKKNI--FKLAQGEyiapekIEnV 556
Cdd:PRK12467 1922 YLGGVGLARGYLNRPALTAErfVADPFGTVgsrlyRTGDLARYRADGVIEYlgrIDHQVKIrgFRIELGE------IE-A 1994
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1958650325 557 YSRSRPILQ---VFVHGESLRSFLIGVVVPDPESLPSFAAKIG 596
Cdd:PRK12467 1995 RLREQGGVReavVIAQDGANGKQLVAYVVPTDPGLVDDDEAQV 2037
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
253-576 |
2.56e-08 |
|
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: 56.26 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 253 ICFTSGTTGDPKGAMLTHQNivsnMAAFLKFLEPIFQPTPEDVTISYLPLAH-MFERLVQGVIFSCGGKIGFFQGDIRLL 331
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERS----WIESFVCNEDLFNISGEDAILAPGPLSHsLFLYGAISALYLGGTFIGQRKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 332 PDDMKALKPTVFPTVPrllnrvydkvqneakTPLKKFLLNLAIISKFNEVRNGiirrNSLWDKLVFSKIQSslggkvrlm 411
Cdd:cd17633 81 IRKINQYNATVIYLVP---------------TMLQALARTLEPESKIKSIFSS----GQKLFESTKKKLKN--------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 412 itgAAPISTpvltffraamgcwVFEAYGQTE---CTAGCSITSPgdwTAGHVGTPVSCNFVKLEDVADmnyfsvNNEGEI 488
Cdd:cd17633 133 ---IFPKAN-------------LIEFYGTSElsfITYNFNQESR---PPNSVGRPFPNVEIEIRNADG------GEIGKI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 489 CIKGNNVFKGYLKdpektQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENVYSRSRPILQVFV 568
Cdd:cd17633 188 FVKSEMVFSGYVR-----GGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIEEAIV 261
|
....*...
gi 1958650325 569 HGESLRSF 576
Cdd:cd17633 262 VGIPDARF 269
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
66-554 |
2.82e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 57.66 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 66 FSDAKTLYEVFQRGLAVSDNGPCLGYRKPNqpykwISYKQVSDRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEWVISEL 145
Cdd:PRK12316 507 YPLQRGVHRLFEEQVERTPEAPALAFGEET-----LDYAELNRRANRLAHALIERGVGP--DVLVGVAMERSIEMVVALL 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 146 ACYTYSMVAVPLYDTLGAEAIIYVINRADISVVICDTPQKATMlienvekDLTPGLKTVILMDPfdddlmkrgekcgIEM 225
Cdd:PRK12316 580 AILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKL-------PLAAGVQVLDLDRP-------------AAW 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 226 LSLHDAENLGKEnfkkpvpPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFL-----EPIFQPTPEDVTIS-- 298
Cdd:PRK12316 640 LEGYSEENPGTE-------LNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYglgvgDTVLQKTPFSFDVSvw 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 299 --YLPLAHMfERLVQGVifscggkigffQGDIR---LLPDDMKALKPTVFPTVPRLLNRVYDKVQNEAKTPLKkfllnla 373
Cdd:PRK12316 713 efFWPLMSG-ARLVVAA-----------PGDHRdpaKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLR------- 773
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 374 iiskfnevrngiirrnslwdklvfskiqsslggkvRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCSITSPG 453
Cdd:PRK12316 774 -----------------------------------RIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCV 818
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 454 DWTAGHV--GTPVSCNFVKLEDvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQE------VLDKDGWLHTGDIGRWL 525
Cdd:PRK12316 819 EEGGDSVpiGRPIANLACYILD-ANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAErfvpspFVAGERMYRTGDLARYR 897
|
490 500
....*....|....*....|....*....
gi 1958650325 526 PNGTLKIIDRKKNIFKLaQGEYIAPEKIE 554
Cdd:PRK12316 898 ADGVIEYAGRIDHQVKL-RGLRIELGEIE 925
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
93-620 |
2.98e-07 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 53.36 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 93 KPNQP-YKW----ISYKQVSDRAEYLGSCLLHKgyKPSQDQFIGIFAQNRPEWVISELAC----YTYsmvaVPLYDTLGA 163
Cdd:PRK04813 15 QPDFPaYDYlgekLTYGQLKEDSDALAAFIDSL--KLPDKSPIIVFGHMSPEMLATFLGAvkagHAY----IPVDVSSPA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 164 EAIIYVINRADISVVICDTPQkatmlienvekdltpglktvilmdPFDDDLMKRgekcgiemlslHDAENLgKENFKKPV 243
Cdd:PRK04813 89 ERIEMIIEVAKPSLIIATEEL------------------------PLEILGIPV-----------ITLDEL-KDIFATGN 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 244 PPNPE------DLSVICFTSGTTGDPKGAMLTHQNIVSnmaaFLKFLEPIFqPTPE------------DVTISYLPLAhm 305
Cdd:PRK04813 133 PYDFDhavkgdDNYYIIFTSGTTGKPKGVQISHDNLVS----FTNWMLEDF-ALPEgpqflnqapysfDLSVMDLYPT-- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 306 ferLVQGvifscggkigffqGDIRLLPDDMKALKPTVFPTVPRLlnrvydKVQNEAKTPlkKF----LLNlaiiSKFNEv 381
Cdd:PRK04813 206 ---LASG-------------GTLVALPKDMTANFKQLFETLPQL------PINVWVSTP--SFadmcLLD----PSFNE- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 382 rngiirrnslwdklvfskiqSSLGGKVRLMITGAA-PISTP--VLTFFRAAMgcwVFEAYGQTECT-AGCSITSPGDWTA 457
Cdd:PRK04813 257 --------------------EHLPNLTHFLFCGEElPHKTAkkLLERFPSAT---IYNTYGPTEATvAVTSIEITDEMLD 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 458 GHVGTPVScnFVK-----LEDVADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVL-DKDGW--LHTGDIGRwLPNGT 529
Cdd:PRK04813 314 QYKRLPIG--YAKpdsplLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGY-LEDGL 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 530 LKI---IDrkkniF--KLAqGEYIAPEKIENVYSRSRPILQ---VFVHGESLRSFLIGVVVPDpeslpsfaakigvKGSF 601
Cdd:PRK04813 391 LFYqgrID-----FqiKLN-GYRIELEEIEQNLRQSSYVESavvVPYNKDHKVQYLIAYVVPK-------------EEDF 451
|
570
....*....|....*....
gi 1958650325 602 EElcqNQCVKKAILEDLQK 620
Cdd:PRK04813 452 ER---EFELTKAIKKELKE 467
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
249-595 |
4.07e-07 |
|
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: 53.13 E-value: 4.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 249 DLSVICFTSGTTGDPKGAMLTHQNIVsNMAAFLKFLepiFQPTPEDVTISYLPLAHmferlvqgvifSCGGKIGFFQGDI 328
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAW-RGGAFFAGS---GGALPSDVLYTCLPLYH-----------STALIVGWSACLA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 329 -------------RLLPDDMKALKPTVFPTVPRLLnrvydkvqneaktplkKFLLNL--AIISKFNEVR----NGIirRN 389
Cdd:cd05940 147 sgatlvirkkfsaSNFWDDIRKYQATIFQYIGELC----------------RYLLNQppKPTERKHKVRmifgNGL--RP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 390 SLWDKLvfskiqsslggKVRLMITGaapistpvltffraamgcwVFEAYGQTECTAGcSITSPG-DWTAGHVGTPVSCNF 468
Cdd:cd05940 209 DIWEEF-----------KERFGVPR-------------------IAEFYAATEGNSG-FINFFGkPGAIGRNPSLLRKVA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 469 ----VKLeDVADMNyfSVNNEGEICIKGN--------------NVFKGYLkDPEKTQEVL------DKDGWLHTGDIGRW 524
Cdd:cd05940 258 plalVKY-DLESGE--PIRDAEGRCIKVPrgepgllisrinplEPFDGYT-DPAATEKKIlrdvfkKGDAWFNTGDLMRL 333
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958650325 525 LPNGTLKIIDRKKNIFKLaQGEYIAPEKIENVYSRSRPILQVFVHGESL-----RSFLIGVVVPDPES--LPSFAAKI 595
Cdd:cd05940 334 DGEGFWYFVDRLGDTFRW-KGENVSTTEVAAVLGAFPGVEEANVYGVQVpgtdgRAGMAAIVLQPNEEfdLSALAAHL 410
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
125-556 |
1.53e-06 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 51.16 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 125 SQDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVICDTPQKatmlienVEKDLTPGLKTV 204
Cdd:PRK05857 64 SRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVAPGSK-------MASSAVPEALHS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 205 ILMDPFDDDLMKRGEKCGIEMLSLHDAENLGKEnfkkpvppnpEDLSVIcFTSGTTGDPKGAMLTHQ------NIVSNMA 278
Cdd:PRK05857 137 IPVIAVDIAAVTRESEHSLDAASLAGNADQGSE----------DPLAMI-FTSGTTGEPKAVLLANRtffavpDILQKEG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 279 afLKFLEPIFQPTpedvTISYLPLAHM------FERLVQGVIFSCGGKIGffqGDIRLLPDDMKALKPTVFPTvprLLNR 352
Cdd:PRK05857 206 --LNWVTWVVGET----TYSPLPATHIgglwwiLTCLMHGGLCVTGGENT---TSLLEILTTNAVATTCLVPT---LLSK 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 353 -VYDKVQNEAKTPlkkfllnlaiiskfnevrngiirrnslwdklvfskiqsslggKVRLMITGAAPISTPVLTFFRAAmG 431
Cdd:PRK05857 274 lVSELKSANATVP------------------------------------------SLRLVGYGGSRAIAADVRFIEAT-G 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 432 CWVFEAYG--QTECTAGCSITSPGDWT---AGHVGTPVSCNFVKL--EDVADMNYFSVNNE---GEICIKGNNVFKGYLK 501
Cdd:PRK05857 311 VRTAQVYGlsETGCTALCLPTDDGSIVkieAGAVGRPYPGVDVYLaaTDGIGPTAPGAGPSasfGTLWIKSPANMLGYWN 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1958650325 502 DPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENV 556
Cdd:PRK05857 391 NPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGGVNIAPDEVDRI 443
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
224-565 |
1.54e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 51.71 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 224 EMLSLHDAENLGKENFKKPVPPnPEDLSVICFTSGTTGDPKGAMLTHQNIVSNmaaflkflEPIFQ------PTPEDVTI 297
Cdd:PRK05691 143 ELLCVDTLDPALAEAWQEPALQ-PDDIAFLQYTSGSTALPKGVQVSHGNLVAN--------EQLIRhgfgidLNPDDVIV 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 298 SYLPLAH-MferlvqGVIfscGGkigffqgdirllpddmkALKPtVFPTVPRLLnrvydkvqneaKTP---LKKFLLNLA 373
Cdd:PRK05691 214 SWLPLYHdM------GLI---GG-----------------LLQP-IFSGVPCVL-----------MSPayfLERPLRWLE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 374 IISKFNEVRNGiirRNSLWDKLVFSKI-QSSLGG----KVRLMITGAAPISTPVL-TFFRAAMGCWV-----FEAYGQTE 442
Cdd:PRK05691 256 AISEYGGTISG---GPDFAYRLCSERVsESALERldlsRWRVAYSGSEPIRQDSLeRFAEKFAACGFdpdsfFASYGLAE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 443 CTAGCSITSPG----------DWTAGHVGTP------VSCNF------VKLEDVADMNYFSVNNEGEICIKGNNVFKGYL 500
Cdd:PRK05691 333 ATLFVSGGRRGqgipaleldaEALARNRAEPgtgsvlMSCGRsqpghaVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYW 412
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958650325 501 KDPEKTQEV-LDKDG--WLHTGDIGrWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENVYSRSRPILQ 565
Cdd:PRK05691 413 RNPEASAKTfVEHDGrtWLRTGDLG-FLRDGELFVTGRLKDML-IVRGHNLYPQDIEKTVEREVEVVR 478
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
255-555 |
1.54e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 51.48 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 255 FTSGTTGDPKGAMLTHQNIVSN----MAAFlkFLEPIFQPTPEDVTISYLPLAH-MfeRLVQGVIFS--CG------GKI 321
Cdd:PRK05850 167 YTSGSTRTPAGVMVSHRNVIANfeqlMSDY--FGDTGGVPPPDTTVVSWLPFYHdM--GLVLGVCAPilGGcpavltSPV 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 322 GFFQGDIRLLpdDMKALKPTVFPTVPrllnrvydkvqneaktplkKFLLNLAiiskfnevrngiIRRNSLWDklvfskiq 401
Cdd:PRK05850 243 AFLQRPARWM--QLLASNPHAFSAAP-------------------NFAFELA------------VRKTSDDD-------- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 402 ssLGGK----VRLMITGAAPISTPVLTFF---------RAAMgcwVFEAYGQTECTAGCSITSPGD-----------WTA 457
Cdd:PRK05850 282 --MAGLdlggVLGIISGSERVHPATLKRFadrfapfnlRETA---IRPSYGLAEATVYVATREPGQppesvrfdyekLSA 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 458 GHV-------GTP-VSCN-----FVKLEDVADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLD----------KDG 514
Cdd:PRK05850 357 GHAkrcetggGTPlVSYGsprspTVRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGatlvdpspgtPEG 436
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1958650325 515 -WLHTGDIGrWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIEN 555
Cdd:PRK05850 437 pWLRTGDLG-FISEGELFIVGRIKDLL-IVDGRNHYPDDIEA 476
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
102-570 |
1.90e-06 |
|
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: 50.89 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 102 SYKQVSDRAEYLGScLLHKGYKPSQDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVICD 181
Cdd:cd05937 7 TYSETYDLVLRYAH-WLHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVIVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 182 tpqkatmlienvekdltpglktvilmdpfdddlmkrgekcgiemlslhdaenlgkenfkkpvppnPEDLSVICFTSGTTG 261
Cdd:cd05937 86 -----------------------------------------------------------------PDDPAILIYTSGTTG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 262 DPKGAmlthqnIVSNMAAFL--KFLEPIFQPTPEDVTISYLPLAHMFERLVQGV-IFSCGGKIGF---FQgdIRLLPDDM 335
Cdd:cd05937 101 LPKAA------AISWRRTLVtsNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACnCLMSGGTLALsrkFS--ASQFWKDV 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 336 KALKPTVFPTVPRLLnrvydkvqneaktplkKFLLNlAIISKFNE---VR----NGIirRNSLWDKLvfskiqsslggKV 408
Cdd:cd05937 173 RDSGATIIQYVGELC----------------RYLLS-TPPSPYDRdhkVRvawgNGL--RPDIWERF-----------RE 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 409 RLMItgaaPIstpvltffraamgcwVFEAYGQTECTAGCSITSPGDWTAGHVGTPVSCNFVKLEDV---------ADMNY 479
Cdd:cd05937 223 RFNV----PE---------------IGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKFENQvvlvkmdpeTDDPI 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 480 FS----------VNNEGEIC--IKGNNV--FKGYLKDPEKTQ-----EVLDK-DGWLHTGDIGRWLPNGTLKIIDRKKNI 539
Cdd:cd05937 284 RDpktgfcvrapVGEPGEMLgrVPFKNReaFQGYLHNEDATEsklvrDVFRKgDIYFRTGDLLRQDADGRWYFLDRLGDT 363
|
490 500 510
....*....|....*....|....*....|.
gi 1958650325 540 FKLaQGEYIAPEKIENVYSRSRPILQVFVHG 570
Cdd:cd05937 364 FRW-KSENVSTTEVADVLGAHPDIAEANVYG 393
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
99-270 |
3.08e-06 |
|
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: 50.27 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 99 KWISYKQVSDRAEYLGSCLLHKGYKpsQDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVV 178
Cdd:cd17634 83 RTISYRELHREVCRFAGTLLDLGVK--KGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 179 ICDT----PQKATMLIENVEKDLT---PGLKTVILMD----PFDDDlmkrgekcGIEMLSLHDAENLGKENFKkPVPPNP 247
Cdd:cd17634 161 ITADggvrAGRSVPLKKNVDDALNpnvTSVEHVIVLKrtgsDIDWQ--------EGRDLWWRDLIAKASPEHQ-PEAMNA 231
|
170 180
....*....|....*....|...
gi 1958650325 248 EDLSVICFTSGTTGDPKGAMLTH 270
Cdd:cd17634 232 EDPLFILYTSGTTGKPKGVLHTT 254
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
444-555 |
4.10e-06 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 49.99 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 444 TAGCSItSPGD--WTAGHVGTPVScnfvkledvadmnyfsVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDI 521
Cdd:PRK10946 354 TQGRPM-SPDDevWVADADGNPLP----------------QGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDL 416
|
90 100 110
....*....|....*....|....*....|....*...
gi 1958650325 522 GRWLPNGTLKIIDRKKNifklaQ----GEYIAPEKIEN 555
Cdd:PRK10946 417 VSIDPDGYITVVGREKD-----QinrgGEKIAAEEIEN 449
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
242-305 |
4.16e-06 |
|
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: 49.98 E-value: 4.16e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958650325 242 PVPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSnMAAFLkflePIFQPTPEDVTISYLPLAHM 305
Cdd:cd05938 138 RAHVTIKSPALYIYTSGTTGLPKAARISHLRVLQ-CSGFL----SLCGVTADDVIYITLPLYHS 196
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
101-304 |
9.05e-06 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 48.72 E-value: 9.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPSQdqFIGIFAQNRPEWVISELACyTYSMVAVPLYDT-LGAEAIIYVINRADISVVI 179
Cdd:PRK08279 63 ISYAELNARANRYAHWAAARGVGKGD--VVALLMENRPEYLAAWLGL-AKLGAVVALLNTqQRGAVLAHSLNLVDAKHLI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 180 CDTPQKATmlIENVEKDLTPGLKTVILMDPFDDDLMkrgekcgiemlslhDAENLGKENFKKPvPPNP--------EDLS 251
Cdd:PRK08279 140 VGEELVEA--FEEARADLARPPRLWVAGGDTLDDPE--------------GYEDLAAAAAGAP-TTNPasrsgvtaKDTA 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958650325 252 VICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFLEpifqPTPEDVTISYLPLAH 304
Cdd:PRK08279 203 FYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLR----LTPDDVLYCCLPLYH 251
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
255-585 |
9.51e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 48.62 E-value: 9.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 255 FTSGTTGDPKGAMLTHQNIVSNmaaflkflepiFQPTPEDVTISylplaHMFERLVQGVIFSCG---GKIG--FFQGDIR 329
Cdd:PRK07638 150 FTSGSTGKPKAFLRAQQSWLHS-----------FDCNVHDFHMK-----REDSVLIAGTLVHSLflyGAIStlYVGQTVH 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 330 LLP--------DDMKALKPTVFPTVPRLLNRVYdKVQNEAKTPLKkfllnlaiiskfnevrngIIRRNSLWDKLVFSKIQ 401
Cdd:PRK07638 214 LMRkfipnqvlDKLETENISVMYTVPTMLESLY-KENRVIENKMK------------------IISSGAKWEAEAKEKIK 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 402 SSLggkvrlmitgaapistPVLTFFraamgcwvfEAYGQTECTAgCSITSPGDWT--AGHVGTPvsCNFVKLEDV-ADMN 478
Cdd:PRK07638 275 NIF----------------PYAKLY---------EFYGASELSF-VTALVDEESErrPNSVGRP--FHNVQVRICnEAGE 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 479 YFSVNNEGEICIKGNNVFKGYLKDPEKTQEvLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENVYS 558
Cdd:PRK07638 327 EVQKGEIGTVYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIESVLH 404
|
330 340
....*....|....*....|....*..
gi 1958650325 559 RsrpilqvfvHGESLRSFLIGvvVPDP 585
Cdd:PRK07638 405 E---------HPAVDEIVVIG--VPDS 420
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
242-565 |
3.28e-05 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 47.04 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 242 PVPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMaafLKFLEPIFQPTPEDVTISYLPLAHMFERLVQGVIFSCGGKI 321
Cdd:PRK12476 187 PVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNL---VQMILSIDLLDRNTHGVSWLPLYHDMGLSMIGFPAVYGGHS 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 322 GFfqgdirllpddmkaLKPTVFPTVP----RLLNRVYDKVQNEAKTPlkKFLLNLAiiskfneVRNGIIRRNslwDKLVF 397
Cdd:PRK12476 264 TL--------------MSPTAFVRRPqrwiKALSEGSRTGRVVTAAP--NFAYEWA-------AQRGLPAEG---DDIDL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 398 SKIqsslggkvrLMITGAAPISTPVLTFFRAAMGCW------VFEAYGQTECTAGCSITSPG-----------DWTAGHV 460
Cdd:PRK12476 318 SNV---------VLIIGSEPVSIDAVTTFNKAFAPYglprtaFKPSYGIAEATLFVATIAPDaepsvvyldreQLGAGRA 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 461 -----GTP-----VSCNFVKLEDVADMNYFSVNNE------GEICIKGNNVFKGYLKDPEKTQEVL-------------- 510
Cdd:PRK12476 389 vrvaaDAPnavahVSCGQVARSQWAVIVDPDTGAElpdgevGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegsha 468
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 511 ----DKDGWLHTGDIGRWLpNGTLKIIDRKKNIFKL-AQGEYiaPEKIENVYSRSRPILQ 565
Cdd:PRK12476 469 dgaaDDGTWLRTGDLGVYL-DGELYITGRIADLIVIdGRNHY--PQDIEATVAEASPMVR 525
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
241-539 |
6.59e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 46.26 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 241 KPVPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMaafLKFLEPIfQPTPEDVTISYLPLAHMFERLVqgVIFS--CG 318
Cdd:PRK07769 173 VPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNV---LQVIDAL-EGQEGDRGVSWLPFFHDMGLIT--VLLPalLG 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 319 GKIGFfqgdirllpddmkaLKPTVFPTVP----RLLNRVYDKVQNE-AKTPlkKFLLNLAIIskfnevrNGIIRRNSL-W 392
Cdd:PRK07769 247 HYITF--------------MSPAAFVRRPgrwiRELARKPGGTGGTfSAAP--NFAFEHAAA-------RGLPKDGEPpL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 393 DklvFSKIQSslggkvrlMITGAAPISTPVLTFFRAAMGCWVFE------AYGQTECTAGCSiTSPGD------------ 454
Cdd:PRK07769 304 D---LSNVKG--------LLNGSEPVSPASMRKFNEAFAPYGLPptaikpSYGMAEATLFVS-TTPMDeeptviyvdrde 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 455 WTAGHV-----GTP-----VSCNFVKLEDVADMnyfsVNNE----------GEICIKGNNVFKGYLKDPEKTQEVL---- 510
Cdd:PRK07769 372 LNAGRFvevpaDAPnavaqVSAGKVGVSEWAVI----VDPEtaselpdgqiGEIWLHGNNIGTGYWGKPEETAATFqnil 447
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1958650325 511 -------------DKDGWLHTGDIGRWLpNGTLKIIDRKKNI 539
Cdd:PRK07769 448 ksrlseshaegapDDALWVRTGDYGVYF-DGELYITGRVKDL 488
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
245-554 |
8.85e-05 |
|
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: 45.45 E-value: 8.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 245 PNPEDLSVICfTSGTTGDPKGAMLTHQNIVSNMAAFLKFLEPIFQPTPEDV--------TISYL--PLAHMFERLVQGVI 314
Cdd:cd05924 1 RSADDLYILY-TGGTTGMPKGVMWRQEDIFRMLMGGADFGTGEFTPSEDAHkaaaaaagTVMFPapPLMHGTGSWTAFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 315 FSCGGKIgfFQGDIRLLPDDmkalkptVFPTVPR----LLNRVYDKVqneAKtPLKKFLlnlaiiskfnevrngiiRRNS 390
Cdd:cd05924 80 LLGGQTV--VLPDDRFDPEE-------VWRTIEKhkvtSMTIVGDAM---AR-PLIDAL-----------------RDAG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 391 LWDklvfskiQSSLggkvRLMITGAAPISTPVLTFFRAAM-GCWVFEAYGQTECTAGCSITSPGDWTAGHVGTPVSCNFV 469
Cdd:cd05924 130 PYD-------LSSL----FAISSGGALLSPEVKQGLLELVpNITLVDAFGSSETGFTGSGHSAGSGPETGPFTRANPDTV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 470 KLEDvaDMNYFSVNNEGE--ICIKGNnVFKGYLKDPEKTQEVL-DKDG--WLHTGDIGRWLPNGTLKIIDRKKNIFKLAq 544
Cdd:cd05924 199 VLDD--DGRVVPPGSGGVgwIARRGH-IPLGYYGDEAKTAETFpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTG- 274
|
330
....*....|
gi 1958650325 545 GEYIAPEKIE 554
Cdd:cd05924 275 GEKVFPEEVE 284
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
243-274 |
1.02e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 45.81 E-value: 1.02e-04
10 20 30
....*....|....*....|....*....|..
gi 1958650325 243 VPPNPEDLSVICFTSGTTGDPKGAMLTHQNIV 274
Cdd:PRK10252 593 QLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIV 624
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
248-593 |
1.64e-04 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 44.27 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 248 EDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFLepifqpTPEDVTISYLPLAHM--FERLVQGVIfscGGKI---- 321
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTASADATHDRL------GGPGQWLLALPAHHIagLQVLVRSVI---AGSEpvel 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 322 ----GFfqgDIRLLPDDMKALKPtvfptvprllNRVYDKVqneAKTPLKKFLLNLAIISKFNEvrngiirrnslwdklvF 397
Cdd:PRK07824 106 dvsaGF---DPTALPRAVAELGG----------GRRYTSL---VPMQLAKALDDPAATAALAE----------------L 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 398 SKIqsslggkvrlmITGAAPISTPVLTFFRAAmGCWVFEAYGQTECTAGCSitspgdwtagHVGTPVSCNFVKLEDvadm 477
Cdd:PRK07824 154 DAV-----------LVGGGPAPAPVLDAAAAA-GINVVRTYGMSETSGGCV----------YDGVPLDGVRVRVED---- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 478 nyfsvnneGEICIKGNNVFKGY--LKDPEKTQEvldkDGWLHTGDIGRwLPNGTLKIIDRKKNIFKLAqGEYIAPEKIEN 555
Cdd:PRK07824 208 --------GRIALGGPTLAKGYrnPVDPDPFAE----PGWFRTDDLGA-LDDGVLTVLGRADDAISTG-GLTVLPQVVEA 273
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1958650325 556 VYSRSRPILQVFVHG---ESLRSFLIGVVVPDPESLPSFAA 593
Cdd:PRK07824 274 ALATHPAVADCAVFGlpdDRLGQRVVAAVVGDGGPAPTLEA 314
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
101-554 |
2.21e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.77 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 101 ISYKQVSDRAEYLGSCLLHKGYKPsqDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVIc 180
Cdd:PRK05691 1157 LDYAELHAQANRLAHYLRDKGVGP--DVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLL- 1233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 181 dtpqKATMLIENVEKdlTPGLKTVILmdpfdDDLMKRGEKCGIEMLSLHDaenlgkenfkkpvppnpEDLSVICFTSGTT 260
Cdd:PRK05691 1234 ----TQSHLLERLPQ--AEGVSAIAL-----DSLHLDSWPSQAPGLHLHG-----------------DNLAYVIYTSGST 1285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 261 GDPKGAMLTHqnivSNMAAFLKFLEPIFQPTPEDVTISYLPLA------HMFERLVQG---VIFSCGGkigffQGDIRLL 331
Cdd:PRK05691 1286 GQPKGVGNTH----AALAERLQWMQATYALDDSDVLMQKAPISfdvsvwECFWPLITGcrlVLAGPGE-----HRDPQRI 1356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 332 PDDMKALKPTVFPTVPRLLNRVYDKVQNEAKTPLKkfllnlaiiskfnevrngiirrnslwdkLVFSkiqsslGGKVRlm 411
Cdd:PRK05691 1357 AELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLR----------------------------RLFS------GGEAL-- 1400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 412 itgAAPISTPVLTFFRAAMgcwVFEAYGQTE---------CTAGCSITSPgdwtaghVGTPVSCNFVKLEDvADMNYFSV 482
Cdd:PRK05691 1401 ---PAELRNRVLQRLPQVQ---LHNRYGPTEtainvthwqCQAEDGERSP-------IGRPLGNVLCRVLD-AELNLLPP 1466
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958650325 483 NNEGEICIKGNNVFKGYLKDPEKTQE--VLDKDG-----WLHTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIE 554
Cdd:PRK05691 1467 GVAGELCIGGAGLARGYLGRPALTAErfVPDPLGedgarLYRTGDRARWNADGALEYLGRLDQQVKL-RGFRVEPEEIQ 1544
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
438-556 |
4.12e-04 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 43.44 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 438 YGQTECTAGCSITSPGDWTAG--HVGTPVSCNFVKLEDvadmnyfsvNNEGEICIKGNNVFKGYLkdpektQEVLDKDGW 515
Cdd:PRK07445 261 YGMTETASQIATLKPDDFLAGnnSSGQVLPHAQITIPA---------NQTGNITIQAQSLALGYY------PQILDSQGI 325
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1958650325 516 LHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENV 556
Cdd:PRK07445 326 FETDDLGYLDAQGYLHILGRNSQKI-ITGGENVYPAEVEAA 365
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
138-307 |
1.37e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 42.05 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 138 PEWVISELACY----TYSMVavplydtLG---AEAIIYVINRADISVVICDTPQ----KATMLIENVEKDL--TPGLKTV 204
Cdd:PRK00174 134 PEAAVAMLACArigaVHSVV-------FGgfsAEALADRIIDAGAKLVITADEGvrggKPIPLKANVDEALanCPSVEKV 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 205 ILMdpfdddlmKR-GEKcgIEM-----LSLHDAENLGKENFKkPVPPNPEDLSVICFTSGTTGDPKG-----------AM 267
Cdd:PRK00174 207 IVV--------RRtGGD--VDWvegrdLWWHELVAGASDECE-PEPMDAEDPLFILYTSGSTGKPKGvlhttggylvyAA 275
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958650325 268 LTHQNivsnmaaflkflepIFQPTPED----------VT----ISYLPLAH-----MFE 307
Cdd:PRK00174 276 MTMKY--------------VFDYKDGDvywctadvgwVTghsyIVYGPLANgattlMFE 320
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
99-304 |
1.42e-03 |
|
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: 41.64 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 99 KWiSYKQVSDRAEYLGSCLLHKGYKpSQDqFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRAdisvv 178
Cdd:cd05939 3 HW-TFRELNEYSNKVANFFQAQGYR-SGD-VVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVS----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650325 179 icdtpqKATMLIENVEKDLTPGLKTvilmdpfdddlmkrgekcgiemlslhdaenlgkenfKKPVPPNPEDLSVICF--T 256
Cdd:cd05939 75 ------KAKALIFNLLDPLLTQSST------------------------------------EPPSQDDVNFRDKLFYiyT 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958650325 257 SGTTGDPKGAMLTHQNIVSnMAAFLKFLepiFQPTPEDVTISYLPLAH 304
Cdd:cd05939 113 SGTTGLPKAAVIVHSRYYR-IAAGAYYA---FGMRPEDVVYDCLPLYH 156
|
|
| |
